CNRS Nantes University UFIP UFIP
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***  job_1  ***

elNémo ID: 21022118583984647

Job options:

ID        	=	 21022118583984647
JOBID     	=	 job_1
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER job_1

HEADER    MEMBRANE PROTEIN                        01-MAY-19   6OS1              
TITLE     STRUCTURE OF SYNTHETIC NANOBODY-STABILIZED ANGIOTENSIN II TYPE 1      
TITLE    2 RECEPTOR BOUND TO TRV023                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE-1 ANGIOTENSIN II RECEPTOR,SOLUBLE CYTOCHROME B562 BRIL
COMPND   3 FUSION PROTEIN;                                                      
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: AT1AR,AT1BR,ANGIOTENSIN II TYPE-1 RECEPTOR,AT1,CYTOCHROME B-
COMPND   6 562;                                                                 
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NANOBODY NB.AT110I1_LE;                                    
COMPND  10 CHAIN: D;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: TRV023 PEPTIDE;                                            
COMPND  14 CHAIN: B;                                                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: AGTR1, AGTR1A, AGTR1B, AT2R1, AT2R1B, CYBC;                    
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: EXPI293;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PCDNA-ZEO-TETO;                           
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630;                                               
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 SYNTHETIC: YES;                                                      
SOURCE  20 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  21 ORGANISM_TAXID: 32630                                                
KEYWDS    GPCR, MEMBRANE PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.M.WINGLER,D.P.STAUS,M.A.SKIBA,C.MCMAHON,A.L.W.KLEINHENZ,            
AUTHOR   2 R.J.LEFKOWITZ,A.C.KRUSE                                              
REVDAT   2   04-MAR-20 6OS1    1       JRNL                                     
REVDAT   1   19-FEB-20 6OS1    0                                                
JRNL        AUTH   L.M.WINGLER,M.A.SKIBA,C.MCMAHON,D.P.STAUS,A.L.W.KLEINHENZ,   
JRNL        AUTH 2 C.M.SUOMIVUORI,N.R.LATORRACA,R.O.DROR,R.J.LEFKOWITZ,         
JRNL        AUTH 3 A.C.KRUSE                                                    
JRNL        TITL   ANGIOTENSIN AND BIASED ANALOGS INDUCE STRUCTURALLY DISTINCT  
JRNL        TITL 2 ACTIVE CONFORMATIONS WITHIN A GPCR.                          
JRNL        REF    SCIENCE                       V. 367   888 2020              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   32079768                                                     
JRNL        DOI    10.1126/SCIENCE.AAY9813                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.14_3260)                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 17764                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 888                             
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 47.4094 -  5.0745    0.98     2936   156  0.2143 0.2579        
REMARK   3     2  5.0745 -  4.0285    1.00     2858   150  0.1972 0.2223        
REMARK   3     3  4.0285 -  3.5195    1.00     2822   149  0.2655 0.3147        
REMARK   3     4  3.5195 -  3.1977    1.00     2798   147  0.2984 0.3994        
REMARK   3     5  3.1977 -  2.9686    1.00     2800   147  0.3249 0.3735        
REMARK   3     6  2.9686 -  2.7936    0.95     2662   139  0.3539 0.4040        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.690           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 85.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 92.55                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 225 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9126 -13.4647 -57.0137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4776 T22:   0.5117                                     
REMARK   3      T33:   0.4377 T12:  -0.0090                                     
REMARK   3      T13:  -0.0138 T23:  -0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5778 L22:   1.2809                                     
REMARK   3      L33:   2.1088 L12:  -0.1309                                     
REMARK   3      L13:  -0.4309 L23:  -0.7555                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0076 S12:   0.1737 S13:   0.1566                       
REMARK   3      S21:  -0.0682 S22:  -0.1514 S23:  -0.1924                       
REMARK   3      S31:  -0.1547 S32:   0.0806 S33:   0.1529                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 266 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.0178 -47.8622 -16.9204              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0985 T22:   1.1405                                     
REMARK   3      T33:   0.9498 T12:   0.0079                                     
REMARK   3      T13:   0.1233 T23:   0.1346                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3521 L22:   9.8076                                     
REMARK   3      L33:   7.1062 L12:  -0.9664                                     
REMARK   3      L13:   1.2020 L23:  -4.6234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5003 S12:  -0.1448 S13:  -0.7505                       
REMARK   3      S21:  -0.9366 S22:   0.4577 S23:  -0.2350                       
REMARK   3      S31:   1.2556 S32:  -0.4712 S33:   0.0123                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 267 THROUGH 1318 )                
REMARK   3    ORIGIN FOR THE GROUP (A): -17.6911 -29.6058 -43.3914              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6222 T22:   0.5369                                     
REMARK   3      T33:   0.5517 T12:  -0.0060                                     
REMARK   3      T13:  -0.0053 T23:   0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9525 L22:   1.2424                                     
REMARK   3      L33:   3.7121 L12:  -0.1873                                     
REMARK   3      L13:  -0.2761 L23:  -0.5638                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1617 S12:  -0.3018 S13:  -0.1782                       
REMARK   3      S21:   0.1320 S22:  -0.0553 S23:  -0.1347                       
REMARK   3      S31:   0.5260 S32:   0.1711 S33:   0.3064                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 32 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -11.1454 -14.5006 -10.3740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9423 T22:   1.1991                                     
REMARK   3      T33:   0.6260 T12:   0.0096                                     
REMARK   3      T13:   0.1558 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5313 L22:   6.7257                                     
REMARK   3      L33:   8.1230 L12:   5.2363                                     
REMARK   3      L13:   5.6903 L23:   5.7904                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4726 S12:  -0.8324 S13:   0.0148                       
REMARK   3      S21:   0.6658 S22:  -0.6492 S23:   0.3675                       
REMARK   3      S31:   1.3302 S32:  -0.0253 S33:   0.4216                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 33 THROUGH 59 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5126 -16.0348 -17.9898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8868 T22:   0.7113                                     
REMARK   3      T33:   0.6067 T12:   0.0456                                     
REMARK   3      T13:  -0.0853 T23:  -0.0885                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9509 L22:   5.8410                                     
REMARK   3      L33:   7.2088 L12:  -0.6490                                     
REMARK   3      L13:  -1.5876 L23:  -5.3036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0176 S12:  -0.0901 S13:  -0.3875                       
REMARK   3      S21:  -0.6406 S22:  -0.1577 S23:   0.1390                       
REMARK   3      S31:  -0.1298 S32:  -0.2357 S33:   0.0138                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 60 THROUGH 98 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7737 -16.3493 -11.3948              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7446 T22:   0.9190                                     
REMARK   3      T33:   0.4839 T12:  -0.0136                                     
REMARK   3      T13:  -0.0220 T23:  -0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1029 L22:   7.8770                                     
REMARK   3      L33:   6.0764 L12:   3.1687                                     
REMARK   3      L13:   2.6628 L23:   0.8485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3710 S12:   0.1587 S13:  -0.3672                       
REMARK   3      S21:   0.5379 S22:  -0.1126 S23:  -0.2323                       
REMARK   3      S31:  -0.0154 S32:   0.1693 S33:  -0.1614                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 99 THROUGH 113 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -20.2127 -19.6490 -29.3444              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4002 T22:   0.9587                                     
REMARK   3      T33:   0.5547 T12:   0.0425                                     
REMARK   3      T13:  -0.1136 T23:   0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7003 L22:   6.1850                                     
REMARK   3      L33:   6.9757 L12:  -3.9507                                     
REMARK   3      L13:   4.0737 L23:  -4.2168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1095 S12:   1.4167 S13:   0.1435                       
REMARK   3      S21:   0.1042 S22:  -0.4415 S23:   0.0668                       
REMARK   3      S31:  -0.4567 S32:  -0.9878 S33:   0.2336                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 114 THROUGH 127 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7202  -7.3726 -12.4364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9456 T22:   0.6384                                     
REMARK   3      T33:   0.6763 T12:  -0.0573                                     
REMARK   3      T13:  -0.2052 T23:   0.0216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7014 L22:   7.0889                                     
REMARK   3      L33:   3.4648 L12:   5.7552                                     
REMARK   3      L13:   3.8717 L23:   4.8537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6325 S12:   0.0598 S13:   0.6214                       
REMARK   3      S21:  -0.0276 S22:  -0.1264 S23:   0.4778                       
REMARK   3      S31:  -0.9627 S32:  -0.0519 S33:   1.0703                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 8 )                     
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8409 -16.7070 -72.5748              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7828 T22:   0.8411                                     
REMARK   3      T33:   0.3804 T12:   0.1457                                     
REMARK   3      T13:  -0.0472 T23:   0.1540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8309 L22:   7.6897                                     
REMARK   3      L33:   1.9998 L12:   1.2839                                     
REMARK   3      L13:   1.0868 L23:  -6.0400                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7180 S12:  -1.4146 S13:  -0.7297                       
REMARK   3      S21:   1.4270 S22:   1.1584 S23:   1.0731                       
REMARK   3      S31:  -1.1315 S32:  -0.9407 S33:  -0.4899                       
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 6OS1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000241240.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-NOV-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17795                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.403                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 10.54                              
REMARK 200  R MERGE                    (I) : 0.20600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.61                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.88200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.850                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 6OS2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN COMPLEX WAS RECONSTITUTED WITH   
REMARK 280  A 10:1 (W/W) MIXTURE OF MONOOLEIN AND CHOLESTEROL. CRYSTALS WERE    
REMARK 280  GROWN IN 100 MM TRIS PH 8, 50-70 MM MGCL2, 30% PEG 300, 2-4% 1,3-   
REMARK 280  BUTANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE 293K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
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+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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       30.33500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.99500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      113.79500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.33500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.99500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      113.79500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.33500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.99500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      113.79500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.33500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.99500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      113.79500            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     LYS A     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     THR A   269                                                      
REMARK 465     PRO A   270                                                      
REMARK 465     PRO A   271                                                      
REMARK 465     LYS A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     GLU A   274                                                      
REMARK 465     ASP A   275                                                      
REMARK 465     LYS A   276                                                      
REMARK 465     SER A   277                                                      
REMARK 465     PRO A   278                                                      
REMARK 465     ASP A   279                                                      
REMARK 465     SER A   280                                                      
REMARK 465     PRO A   281                                                      
REMARK 465     GLU A   282                                                      
REMARK 465     MET A   283                                                      
REMARK 465     LYS A   284                                                      
REMARK 465     ASP A   285                                                      
REMARK 465     PHE A   286                                                      
REMARK 465     THR A  1222                                                      
REMARK 465     THR A  1223                                                      
REMARK 465     ARG A  1224                                                      
REMARK 465     ASN A  1225                                                      
REMARK 465     ALA A  1226                                                      
REMARK 465     GLU A  1227                                                      
REMARK 465     ILE A  1228                                                      
REMARK 465     GLN A  1229                                                      
REMARK 465     TYR A  1319                                                      
REMARK 465     GLU D   128                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  12    CG   CD   CE   NZ                                   
REMARK 470     ARG A  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  20    CG   CD   CE   NZ                                   
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     ARG A 139    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 173    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 176    CG   OD1  ND2                                       
REMARK 470     GLU A 185    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 191    CG   CD1  CD2                                       
REMARK 470     ILE A 193    CG1  CG2  CD1                                       
REMARK 470     ILE A 201    CD1                                                 
REMARK 470     LYS A 220    CG   CD   CE   NZ                                   
REMARK 470     LYS A 224    CG   CD   CE   NZ                                   
REMARK 470     GLU A 233    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 239    CG   CD1  CD2                                       
REMARK 470     LYS A 240    CG   CD   CE   NZ                                   
REMARK 470     GLU A 243    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     ASP A 253    CG   OD1  OD2                                       
REMARK 470     LEU A 255    CG   CD1  CD2                                       
REMARK 470     ARG A 259    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 266    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 267    CG   CD   CE   NZ                                   
REMARK 470     ARG A 287    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 291    CG   OD1  OD2                                       
REMARK 470     ILE A 292    CG1  CG2  CD1                                       
REMARK 470     VAL A 294    CG1  CG2                                            
REMARK 470     ASP A 298    CG   OD1  OD2                                       
REMARK 470     ASP A 299    CG   OD1  OD2                                       
REMARK 470     LYS A 302    CG   CD   CE   NZ                                   
REMARK 470     LEU A 303    CG   CD1  CD2                                       
REMARK 470     ASN A 305    CG   OD1  ND2                                       
REMARK 470     GLU A 306    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 308    CG   CD   CE   NZ                                   
REMARK 470     VAL A 309    CG1  CG2                                            
REMARK 470     LYS A 310    CG   CD   CE   NZ                                   
REMARK 470     GLU A 311    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 313    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 317    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 318    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 320    CG   CD   CE   NZ                                   
REMARK 470     LYS A1230    CG   CD   CE   NZ                                   
REMARK 470     LYS A1232    CG   CD   CE   NZ                                   
REMARK 470     ARG A1272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1275    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1307    CG   CD   CE   NZ                                   
REMARK 470     LYS A1308    CG   CD   CE   NZ                                   
REMARK 470     ARG A1311    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1318    CG   CD   CE   NZ                                   
REMARK 470     GLN D   5    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  44    CG   CD   OE1  OE2                                  
REMARK 470     ASN D  58    CG   OD1  ND2                                       
REMARK 470     LYS D  64    CG   CD   CE   NZ                                   
REMARK 470     LYS D  75    CG   CD   CE   NZ                                   
REMARK 470     GLN D 118    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  59       87.73     55.95                                   
REMARK 500    TYR A  92       70.32     57.19                                   
REMARK 500    PHE A 204      -58.08   -151.27                                   
REMARK 500    LYS A 267       58.21    -92.37                                   
REMARK 500    LEU A 319      -71.59    -71.32                                   
REMARK 500    PRO B   7       89.61    -68.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A 1401                                                       
REMARK 610     OLC A 1402                                                       
REMARK 610     OLC A 1403                                                       
REMARK 610     OLC A 1404                                                       
REMARK 610     OLC A 1405                                                       
REMARK 610     OLC A 1406                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1402                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1403                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1404                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1405                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1406                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1407                
DBREF  6OS1 A    2   226  UNP    P30556   AGTR1_HUMAN      2    226             
DBREF  6OS1 A  227  1226  UNP    P0ABE7   C562_ECOLX      24    122             
DBREF  6OS1 A 1227  1319  UNP    P30556   AGTR1_HUMAN    227    319             
DBREF  6OS1 D    1   128  PDB    6OS1     6OS1             1    128             
DBREF  6OS1 B    1     8  PDB    6OS1     6OS1             1      8             
SEQADV 6OS1 ASP A   -6  UNP  P30556              EXPRESSION TAG                 
SEQADV 6OS1 TYR A   -5  UNP  P30556              EXPRESSION TAG                 
SEQADV 6OS1 LYS A   -4  UNP  P30556              EXPRESSION TAG                 
SEQADV 6OS1 ASP A   -3  UNP  P30556              EXPRESSION TAG                 
SEQADV 6OS1 ASP A   -2  UNP  P30556              EXPRESSION TAG                 
SEQADV 6OS1 ASP A   -1  UNP  P30556              EXPRESSION TAG                 
SEQADV 6OS1 ASP A    0  UNP  P30556              EXPRESSION TAG                 
SEQADV 6OS1 LYS A    1  UNP  P30556              EXPRESSION TAG                 
SEQADV 6OS1 TRP A  232  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQRES   1 A  425  ASP TYR LYS ASP ASP ASP ASP LYS ILE LEU ASN SER SER          
SEQRES   2 A  425  THR GLU ASP GLY ILE LYS ARG ILE GLN ASP ASP CYS PRO          
SEQRES   3 A  425  LYS ALA GLY ARG HIS ASN TYR ILE PHE VAL MET ILE PRO          
SEQRES   4 A  425  THR LEU TYR SER ILE ILE PHE VAL VAL GLY ILE PHE GLY          
SEQRES   5 A  425  ASN SER LEU VAL VAL ILE VAL ILE TYR PHE TYR MET LYS          
SEQRES   6 A  425  LEU LYS THR VAL ALA SER VAL PHE LEU LEU ASN LEU ALA          
SEQRES   7 A  425  LEU ALA ASP LEU CYS PHE LEU LEU THR LEU PRO LEU TRP          
SEQRES   8 A  425  ALA VAL TYR THR ALA MET GLU TYR ARG TRP PRO PHE GLY          
SEQRES   9 A  425  ASN TYR LEU CYS LYS ILE ALA SER ALA SER VAL SER PHE          
SEQRES  10 A  425  ASN LEU TYR ALA SER VAL PHE LEU LEU THR CYS LEU SER          
SEQRES  11 A  425  ILE ASP ARG TYR LEU ALA ILE VAL HIS PRO MET LYS SER          
SEQRES  12 A  425  ARG LEU ARG ARG THR MET LEU VAL ALA LYS VAL THR CYS          
SEQRES  13 A  425  ILE ILE ILE TRP LEU LEU ALA GLY LEU ALA SER LEU PRO          
SEQRES  14 A  425  ALA ILE ILE HIS ARG ASN VAL PHE PHE ILE GLU ASN THR          
SEQRES  15 A  425  ASN ILE THR VAL CYS ALA PHE HIS TYR GLU SER GLN ASN          
SEQRES  16 A  425  SER THR LEU PRO ILE GLY LEU GLY LEU THR LYS ASN ILE          
SEQRES  17 A  425  LEU GLY PHE LEU PHE PRO PHE LEU ILE ILE LEU THR SER          
SEQRES  18 A  425  TYR THR LEU ILE TRP LYS ALA LEU LYS LYS ALA TYR ASP          
SEQRES  19 A  425  LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS          
SEQRES  20 A  425  VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP          
SEQRES  21 A  425  ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN          
SEQRES  22 A  425  LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP          
SEQRES  23 A  425  SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE          
SEQRES  24 A  425  LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN          
SEQRES  25 A  425  GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN          
SEQRES  26 A  425  LEU LYS THR THR ARG ASN ALA GLU ILE GLN LYS ASN LYS          
SEQRES  27 A  425  PRO ARG ASN ASP ASP ILE PHE LYS ILE ILE MET ALA ILE          
SEQRES  28 A  425  VAL LEU PHE PHE PHE PHE SER TRP ILE PRO HIS GLN ILE          
SEQRES  29 A  425  PHE THR PHE LEU ASP VAL LEU ILE GLN LEU GLY ILE ILE          
SEQRES  30 A  425  ARG ASP CYS ARG ILE ALA ASP ILE VAL ASP THR ALA MET          
SEQRES  31 A  425  PRO ILE THR ILE CYS ILE ALA TYR PHE ASN ASN CYS LEU          
SEQRES  32 A  425  ASN PRO LEU PHE TYR GLY PHE LEU GLY LYS LYS PHE LYS          
SEQRES  33 A  425  ARG TYR PHE LEU GLN LEU LEU LYS TYR                          
SEQRES   1 D  128  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL ALA          
SEQRES   2 D  128  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 D  128  ASN ILE PHE ASP VAL ASP ILE MET GLY TRP TYR ARG GLN          
SEQRES   4 D  128  ALA PRO GLY LYS GLU ARG GLU LEU VAL ALA SER ILE THR          
SEQRES   5 D  128  ASP GLY GLY SER THR ASN TYR ALA ASP SER VAL LYS GLY          
SEQRES   6 D  128  ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL          
SEQRES   7 D  128  TYR LEU ALA MET ALA SER LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 D  128  VAL TYR TYR CYS ALA ALA VAL ALA TYR PRO ASP ILE PRO          
SEQRES   9 D  128  THR TYR PHE ASP TYR ASP SER ASP ASN PHE TYR TRP GLY          
SEQRES  10 D  128  GLN GLY THR GLN VAL THR VAL SER SER LEU GLU                  
SEQRES   1 B    8  SAR ARG VAL TYR LYS HIS PRO ALA                              
HET    SAR  B   1       5                                                       
HET    OLC  A1401      10                                                       
HET    OLC  A1402      15                                                       
HET    OLC  A1403      10                                                       
HET    OLC  A1404       8                                                       
HET    OLC  A1405      13                                                       
HET    OLC  A1406      10                                                       
HET    CLR  A1407      28                                                       
HETNAM     SAR SARCOSINE                                                        
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     CLR CHOLESTEROL                                                      
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   3  SAR    C3 H7 N O2                                                   
FORMUL   4  OLC    6(C21 H40 O4)                                                
FORMUL  10  CLR    C27 H46 O                                                    
FORMUL  11  HOH   *17(H2 O)                                                     
HELIX    1 AA1 HIS A   24  MET A   57  1                                  34    
HELIX    2 AA2 THR A   61  THR A   80  1                                  20    
HELIX    3 AA3 THR A   80  MET A   90  1                                  11    
HELIX    4 AA4 PHE A   96  HIS A  132  1                                  37    
HELIX    5 AA5 THR A  141  SER A  160  1                                  20    
HELIX    6 AA6 LEU A  161  HIS A  166  1                                   6    
HELIX    7 AA7 GLY A  194  LEU A  202  1                                   9    
HELIX    8 AA8 PHE A  204  LYS A  244  1                                  41    
HELIX    9 AA9 ASN A  247  LYS A  267  1                                  21    
HELIX   10 AB1 GLY A  289  ASN A  305  1                                  17    
HELIX   11 AB2 VAL A  309  LYS A  320  1                                  12    
HELIX   12 AB3 ASP A 1237  LEU A 1268  1                                  32    
HELIX   13 AB4 ASP A 1273  LEU A 1297  1                                  25    
HELIX   14 AB5 LEU A 1297  GLY A 1306  1                                  10    
HELIX   15 AB6 GLY A 1306  LYS A 1318  1                                  13    
HELIX   16 AB7 LYS D   86  THR D   90  5                                   5    
SHEET    1 AA1 4 LYS A  12  ILE A  14  0                                        
SHEET    2 AA1 4 ASN A 168  ILE A 172  1  O  PHE A 171   N  LYS A  12           
SHEET    3 AA1 4 ILE A 177  TYR A 184 -1  O  VAL A 179   N  PHE A 170           
SHEET    4 AA1 4 ARG B   2  TYR B   4 -1  O  TYR B   4   N  PHE A 182           
SHEET    1 AA2 4 GLN D   3  SER D   7  0                                        
SHEET    2 AA2 4 SER D  17  SER D  25 -1  O  SER D  21   N  SER D   7           
SHEET    3 AA2 4 THR D  77  ALA D  83 -1  O  LEU D  80   N  LEU D  20           
SHEET    4 AA2 4 THR D  68  ASP D  72 -1  N  THR D  68   O  ALA D  81           
SHEET    1 AA3 6 GLY D  10  ALA D  13  0                                        
SHEET    2 AA3 6 THR D 120  SER D 125  1  O  THR D 123   N  VAL D  12           
SHEET    3 AA3 6 ALA D  91  VAL D  98 -1  N  TYR D  93   O  THR D 120           
SHEET    4 AA3 6 ILE D  33  GLN D  39 -1  N  TYR D  37   O  TYR D  94           
SHEET    5 AA3 6 ARG D  45  THR D  52 -1  O  ALA D  49   N  TRP D  36           
SHEET    6 AA3 6 THR D  57  TYR D  59 -1  O  ASN D  58   N  SER D  50           
SHEET    1 AA4 4 GLY D  10  ALA D  13  0                                        
SHEET    2 AA4 4 THR D 120  SER D 125  1  O  THR D 123   N  VAL D  12           
SHEET    3 AA4 4 ALA D  91  VAL D  98 -1  N  TYR D  93   O  THR D 120           
SHEET    4 AA4 4 PHE D 114  TRP D 116 -1  O  TYR D 115   N  ALA D  97           
SSBOND   1 CYS A   18    CYS A 1274                          1555   1555  2.03  
SSBOND   2 CYS A  101    CYS A  180                          1555   1555  2.03  
SSBOND   3 CYS D   22    CYS D   95                          1555   1555  2.03  
LINK         C   SAR B   1                 N   ARG B   2     1555   1555  1.33  
SITE     1 AC1  2 CYS A 121  OLC A1406                                          
SITE     1 AC2  5 MET A1243  ALA A1244  LEU A1247  ASN A1294                    
SITE     2 AC2  5 OLC A1405                                                     
SITE     1 AC3  3 LEU A1268  PHE A1304  LYS A1310                               
SITE     1 AC4  1 TRP A 219                                                     
SITE     1 AC5  2 GLY A 194  OLC A1402                                          
SITE     1 AC6  3 THR A 120  ILE A 151  OLC A1401                               
SITE     1 AC7  2 ILE A  51  LEU A1316                                          
CRYST1   60.670  101.990  227.590  90.00  90.00  90.00 I 2 2 2       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      0.016483  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009805  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004394        0.00000                         
ATOM      1  N   ILE A  11     -12.235  -0.342 -82.681  1.00115.12           N  
ANISOU    1  N   ILE A  11    14749  16307  12684   1003    992   2634       N  
ATOM      2  CA  ILE A  11     -11.735  -1.460 -81.892  1.00114.32           C  
ANISOU    2  CA  ILE A  11    14616  16180  12642    921    979   2427       C  
ATOM      3  C   ILE A  11     -10.982  -2.440 -82.784  1.00117.57           C  
ANISOU    3  C   ILE A  11    15011  16777  12884    956   1081   2405       C  
ATOM      4  O   ILE A  11     -10.666  -2.130 -83.933  1.00126.23           O  
ANISOU    4  O   ILE A  11    16113  18003  13843   1026   1173   2568       O  
ATOM      5  CB  ILE A  11     -12.880  -2.165 -81.143  1.00103.87           C  
ANISOU    5  CB  ILE A  11    13316  14852  11297    921    843   2196       C  
ATOM      6  CG1 ILE A  11     -13.961  -2.621 -82.125  1.00107.87           C  
ANISOU    6  CG1 ILE A  11    13859  15578  11548   1026    792   2151       C  
ATOM      7  CG2 ILE A  11     -13.468  -1.246 -80.083  1.00 90.94           C  
ANISOU    7  CG2 ILE A  11    11693  13010   9851    885    762   2205       C  
ATOM      8  CD1 ILE A  11     -15.146  -3.287 -81.462  1.00107.07           C  
ANISOU    8  CD1 ILE A  11    13769  15490  11423   1019    657   1941       C  
ATOM      9  N   LYS A  12     -10.696  -3.623 -82.250  1.00104.25           N  
ANISOU    9  N   LYS A  12    13309  15098  11202    916   1072   2208       N  
ATOM     10  CA  LYS A  12      -9.941  -4.643 -82.962  1.00 90.35           C  
ANISOU   10  CA  LYS A  12    11543  13486   9298    956   1179   2163       C  
ATOM     11  C   LYS A  12     -10.885  -5.640 -83.621  1.00 95.14           C  
ANISOU   11  C   LYS A  12    12228  14267   9656   1029   1127   1991       C  
ATOM     12  O   LYS A  12     -11.918  -6.006 -83.052  1.00 98.23           O  
ANISOU   12  O   LYS A  12    12647  14630  10044   1008    998   1828       O  
ATOM     13  CB  LYS A  12      -8.990  -5.376 -82.013  1.00 71.10           C  
ANISOU   13  CB  LYS A  12     9047  10950   7017    878   1214   2062       C  
ATOM     14  N   ARG A  13     -10.523  -6.074 -84.826  1.00 92.16           N  
ANISOU   14  N   ARG A  13    11884  14071   9063   1110   1228   2028       N  
ATOM     15  CA  ARG A  13     -11.282  -7.065 -85.579  1.00 88.14           C  
ANISOU   15  CA  ARG A  13    11460  13738   8290   1169   1190   1861       C  
ATOM     16  C   ARG A  13     -10.511  -8.378 -85.566  1.00 84.36           C  
ANISOU   16  C   ARG A  13    11006  13282   7765   1173   1283   1704       C  
ATOM     17  O   ARG A  13      -9.366  -8.433 -86.027  1.00 85.82           O  
ANISOU   17  O   ARG A  13    11165  13504   7939   1213   1438   1811       O  
ATOM     18  CB  ARG A  13     -11.528  -6.594 -87.012  1.00 95.72           C  
ANISOU   18  CB  ARG A  13    12464  14900   9006   1268   1234   2009       C  
ATOM     19  N   ILE A  14     -11.137  -9.431 -85.039  1.00 82.25           N  
ANISOU   19  N   ILE A  14    10788  12989   7475   1136   1197   1461       N  
ATOM     20  CA  ILE A  14     -10.490 -10.724 -84.868  1.00 83.21           C  
ANISOU   20  CA  ILE A  14    10944  13094   7578   1140   1278   1297       C  
ATOM     21  C   ILE A  14     -11.329 -11.798 -85.549  1.00 80.23           C  
ANISOU   21  C   ILE A  14    10692  12846   6947   1166   1232   1086       C  
ATOM     22  O   ILE A  14     -12.452 -11.560 -85.994  1.00 71.45           O  
ANISOU   22  O   ILE A  14     9618  11835   5694   1162   1114   1058       O  
ATOM     23  CB  ILE A  14     -10.271 -11.077 -83.382  1.00 84.43           C  
ANISOU   23  CB  ILE A  14    11040  13052   7986   1053   1231   1198       C  
ATOM     24  CG1 ILE A  14     -11.615 -11.252 -82.672  1.00 91.05           C  
ANISOU   24  CG1 ILE A  14    11906  13838   8851    987   1053   1040       C  
ATOM     25  CG2 ILE A  14      -9.435 -10.008 -82.697  1.00 70.65           C  
ANISOU   25  CG2 ILE A  14     9177  11183   6484   1008   1264   1396       C  
ATOM     26  CD1 ILE A  14     -11.495 -11.778 -81.259  1.00 91.91           C  
ANISOU   26  CD1 ILE A  14    11977  13775   9171    909   1007    918       C  
ATOM     27  N   GLN A  15     -10.758 -12.999 -85.619  1.00 89.33           N  
ANISOU   27  N   GLN A  15    11906  13991   8042   1190   1326    938       N  
ATOM     28  CA  GLN A  15     -11.412 -14.168 -86.190  1.00100.67           C  
ANISOU   28  CA  GLN A  15    13482  15517   9252   1198   1297    710       C  
ATOM     29  C   GLN A  15     -11.566 -15.227 -85.110  1.00 98.17           C  
ANISOU   29  C   GLN A  15    13187  15043   9069   1128   1252    500       C  
ATOM     30  O   GLN A  15     -10.619 -15.500 -84.364  1.00102.90           O  
ANISOU   30  O   GLN A  15    13732  15514   9851   1133   1342    520       O  
ATOM     31  CB  GLN A  15     -10.610 -14.727 -87.370  1.00107.26           C  
ANISOU   31  CB  GLN A  15    14408  16478   9867   1307   1472    710       C  
ATOM     32  CG  GLN A  15     -10.584 -13.831 -88.597  1.00113.23           C  
ANISOU   32  CG  GLN A  15    15167  17422  10433   1382   1516    899       C  
ATOM     33  CD  GLN A  15     -11.736 -14.105 -89.545  1.00123.01           C  
ANISOU   33  CD  GLN A  15    16524  18839  11375   1381   1408    780       C  
ATOM     34  OE1 GLN A  15     -12.213 -15.235 -89.649  1.00135.76           O  
ANISOU   34  OE1 GLN A  15    18257  20464  12859   1350   1368    537       O  
ATOM     35  NE2 GLN A  15     -12.190 -13.070 -90.242  1.00116.12           N  
ANISOU   35  NE2 GLN A  15    15619  18107  10393   1412   1357    955       N  
ATOM     36  N   ASP A  16     -12.754 -15.819 -85.025  1.00 84.55           N  
ANISOU   36  N   ASP A  16    11535  13337   7252   1060   1113    310       N  
ATOM     37  CA  ASP A  16     -13.029 -16.865 -84.050  1.00 87.21           C  
ANISOU   37  CA  ASP A  16    11905  13530   7701    986   1066    108       C  
ATOM     38  C   ASP A  16     -12.814 -18.229 -84.693  1.00 90.01           C  
ANISOU   38  C   ASP A  16    12417  13909   7872   1019   1157    -88       C  
ATOM     39  O   ASP A  16     -13.368 -18.512 -85.761  1.00 99.02           O  
ANISOU   39  O   ASP A  16    13669  15200   8756   1028   1133   -172       O  
ATOM     40  CB  ASP A  16     -14.458 -16.744 -83.517  1.00 94.11           C  
ANISOU   40  CB  ASP A  16    12758  14400   8597    883    866     18       C  
ATOM     41  CG  ASP A  16     -14.712 -17.632 -82.313  1.00105.79           C  
ANISOU   41  CG  ASP A  16    14242  15715  10240    799    816   -148       C  
ATOM     42  OD1 ASP A  16     -13.760 -18.287 -81.837  1.00106.65           O  
ANISOU   42  OD1 ASP A  16    14364  15702  10456    826    932   -182       O  
ATOM     43  OD2 ASP A  16     -15.867 -17.672 -81.840  1.00108.68           O  
ANISOU   43  OD2 ASP A  16    14591  16077  10626    712    665   -233       O  
ATOM     44  N   ASP A  17     -12.005 -19.069 -84.043  1.00 87.62           N  
ANISOU   44  N   ASP A  17    12130  13460   7700   1038   1263   -158       N  
ATOM     45  CA  ASP A  17     -11.723 -20.395 -84.583  1.00 82.97           C  
ANISOU   45  CA  ASP A  17    11706  12859   6959   1083   1372   -344       C  
ATOM     46  C   ASP A  17     -12.984 -21.251 -84.619  1.00 87.31           C  
ANISOU   46  C   ASP A  17    12379  13405   7388    974   1234   -586       C  
ATOM     47  O   ASP A  17     -13.339 -21.811 -85.663  1.00 96.77           O  
ANISOU   47  O   ASP A  17    13728  14711   8330    982   1244   -718       O  
ATOM     48  CB  ASP A  17     -10.631 -21.078 -83.758  1.00 89.42           C  
ANISOU   48  CB  ASP A  17    12497  13509   7968   1135   1509   -348       C  
ATOM     49  CG  ASP A  17      -9.311 -20.333 -83.808  1.00 98.00           C  
ANISOU   49  CG  ASP A  17    13457  14619   9158   1236   1655   -110       C  
ATOM     50  OD1 ASP A  17      -9.084 -19.588 -84.784  1.00 98.39           O  
ANISOU   50  OD1 ASP A  17    13494  14819   9072   1296   1705     26       O  
ATOM     51  OD2 ASP A  17      -8.499 -20.497 -82.873  1.00 97.36           O  
ANISOU   51  OD2 ASP A  17    13284  14416   9293   1253   1718    -50       O  
ATOM     52  N   CYS A  18     -13.674 -21.365 -83.484  1.00 84.47           N  
ANISOU   52  N   CYS A  18    11959  12930   7208    865   1103   -648       N  
ATOM     53  CA  CYS A  18     -14.926 -22.110 -83.383  1.00 90.14           C  
ANISOU   53  CA  CYS A  18    12762  13641   7845    740    959   -858       C  
ATOM     54  C   CYS A  18     -16.054 -21.117 -83.132  1.00 82.23           C  
ANISOU   54  C   CYS A  18    11640  12731   6872    658    769   -778       C  
ATOM     55  O   CYS A  18     -16.387 -20.828 -81.974  1.00 88.82           O  
ANISOU   55  O   CYS A  18    12366  13462   7921    599    687   -745       O  
ATOM     56  CB  CYS A  18     -14.858 -23.152 -82.263  1.00101.59           C  
ANISOU   56  CB  CYS A  18    14243  14882   9474    685    973   -995       C  
ATOM     57  SG  CYS A  18     -13.298 -24.068 -82.153  1.00110.76           S  
ANISOU   57  SG  CYS A  18    15481  15898  10706    819   1217  -1008       S  
ATOM     58  N   PRO A  19     -16.672 -20.563 -84.179  1.00 79.48           N  
ANISOU   58  N   PRO A  19    11306  12582   6311    662    696   -739       N  
ATOM     59  CA  PRO A  19     -17.696 -19.532 -83.950  1.00 85.95           C  
ANISOU   59  CA  PRO A  19    11997  13493   7166    612    530   -631       C  
ATOM     60  C   PRO A  19     -19.000 -20.082 -83.399  1.00 89.15           C  
ANISOU   60  C   PRO A  19    12398  13888   7588    472    362   -790       C  
ATOM     61  O   PRO A  19     -19.737 -19.340 -82.739  1.00 85.89           O  
ANISOU   61  O   PRO A  19    11856  13482   7296    435    244   -703       O  
ATOM     62  CB  PRO A  19     -17.887 -18.916 -85.342  1.00 65.40           C  
ANISOU   62  CB  PRO A  19     9424  11120   4304    672    519   -541       C  
ATOM     63  CG  PRO A  19     -17.533 -20.017 -86.281  1.00 77.26           C  
ANISOU   63  CG  PRO A  19    11108  12669   5578    688    611   -713       C  
ATOM     64  CD  PRO A  19     -16.431 -20.798 -85.613  1.00 85.13           C  
ANISOU   64  CD  PRO A  19    12151  13456   6738    727    771   -774       C  
ATOM     65  N   LYS A  20     -19.311 -21.351 -83.645  1.00 81.72           N  
ANISOU   65  N   LYS A  20    11595  12926   6529    393    353  -1015       N  
ATOM     66  CA  LYS A  20     -20.555 -21.948 -83.178  1.00 91.46           C  
ANISOU   66  CA  LYS A  20    12824  14155   7771    242    195  -1168       C  
ATOM     67  C   LYS A  20     -20.441 -22.555 -81.784  1.00100.70           C  
ANISOU   67  C   LYS A  20    13967  15099   9196    186    213  -1236       C  
ATOM     68  O   LYS A  20     -21.407 -23.161 -81.307  1.00108.50           O  
ANISOU   68  O   LYS A  20    14954  16061  10209     55    100  -1365       O  
ATOM     69  CB  LYS A  20     -21.028 -23.020 -84.166  1.00 89.61           C  
ANISOU   69  CB  LYS A  20    12763  14010   7275    159    163  -1387       C  
ATOM     70  N   ALA A  21     -19.298 -22.403 -81.121  1.00 81.77           N  
ANISOU   70  N   ALA A  21    11539  12548   6983    277    348  -1143       N  
ATOM     71  CA  ALA A  21     -19.088 -23.005 -79.810  1.00 79.96           C  
ANISOU   71  CA  ALA A  21    11287  12111   6982    236    375  -1197       C  
ATOM     72  C   ALA A  21     -19.801 -22.186 -78.741  1.00 84.12           C  
ANISOU   72  C   ALA A  21    11650  12623   7689    189    253  -1097       C  
ATOM     73  O   ALA A  21     -19.543 -20.986 -78.593  1.00 90.78           O  
ANISOU   73  O   ALA A  21    12381  13503   8608    259    250   -913       O  
ATOM     74  CB  ALA A  21     -17.595 -23.106 -79.505  1.00 82.33           C  
ANISOU   74  CB  ALA A  21    11599  12280   7404    354    556  -1120       C  
ATOM     75  N   GLY A  22     -20.698 -22.833 -77.999  1.00 80.13           N  
ANISOU   75  N   GLY A  22    11137  12057   7252     70    159  -1216       N  
ATOM     76  CA  GLY A  22     -21.377 -22.202 -76.888  1.00 70.65           C  
ANISOU   76  CA  GLY A  22     9793  10829   6224     30     60  -1139       C  
ATOM     77  C   GLY A  22     -22.554 -21.325 -77.250  1.00 72.98           C  
ANISOU   77  C   GLY A  22     9989  11307   6435      1    -86  -1070       C  
ATOM     78  O   GLY A  22     -23.142 -20.710 -76.351  1.00 81.82           O  
ANISOU   78  O   GLY A  22    10987  12409   7693    -13   -159   -995       O  
ATOM     79  N   ARG A  23     -22.924 -21.244 -78.526  1.00 83.07           N  
ANISOU   79  N   ARG A  23    11313  12765   7484      1   -129  -1088       N  
ATOM     80  CA  ARG A  23     -24.022 -20.386 -78.971  1.00 87.58           C  
ANISOU   80  CA  ARG A  23    11782  13536   7959    -10   -267  -1001       C  
ATOM     81  C   ARG A  23     -25.269 -21.253 -79.107  1.00 80.18           C  
ANISOU   81  C   ARG A  23    10856  12689   6918   -164   -401  -1163       C  
ATOM     82  O   ARG A  23     -25.582 -21.765 -80.183  1.00 82.52           O  
ANISOU   82  O   ARG A  23    11241  13120   6991   -218   -444  -1266       O  
ATOM     83  CB  ARG A  23     -23.669 -19.685 -80.276  1.00 97.32           C  
ANISOU   83  CB  ARG A  23    13043  14932   9000     87   -240   -896       C  
ATOM     84  CG  ARG A  23     -22.266 -19.104 -80.298  1.00110.26           C  
ANISOU   84  CG  ARG A  23    14700  16474  10721    217    -83   -763       C  
ATOM     85  CD  ARG A  23     -22.154 -17.938 -81.264  1.00112.95           C  
ANISOU   85  CD  ARG A  23    15002  16975  10940    321    -80   -579       C  
ATOM     86  NE  ARG A  23     -22.655 -16.696 -80.683  1.00115.32           N  
ANISOU   86  NE  ARG A  23    15160  17283  11374    362   -148   -406       N  
ATOM     87  CZ  ARG A  23     -23.878 -16.215 -80.879  1.00119.16           C  
ANISOU   87  CZ  ARG A  23    15564  17923  11789    343   -285   -361       C  
ATOM     88  NH1 ARG A  23     -24.737 -16.869 -81.649  1.00118.74           N  
ANISOU   88  NH1 ARG A  23    15544  18043  11527    267   -386   -478       N  
ATOM     89  NH2 ARG A  23     -24.241 -15.076 -80.308  1.00121.67           N  
ANISOU   89  NH2 ARG A  23    15766  18220  12242    401   -322   -200       N  
ATOM     90  N   HIS A  24     -25.988 -21.415 -77.999  1.00 78.04           N  
ANISOU   90  N   HIS A  24    10496  12349   6808   -241   -469  -1186       N  
ATOM     91  CA  HIS A  24     -27.195 -22.226 -77.953  1.00 72.82           C  
ANISOU   91  CA  HIS A  24     9820  11762   6086   -403   -596  -1325       C  
ATOM     92  C   HIS A  24     -28.345 -21.393 -77.409  1.00 77.76           C  
ANISOU   92  C   HIS A  24    10256  12504   6784   -411   -720  -1206       C  
ATOM     93  O   HIS A  24     -28.159 -20.587 -76.493  1.00 75.07           O  
ANISOU   93  O   HIS A  24     9823  12076   6624   -322   -685  -1076       O  
ATOM     94  CB  HIS A  24     -26.989 -23.473 -77.088  1.00 62.09           C  
ANISOU   94  CB  HIS A  24     8544  10194   4855   -503   -542  -1483       C  
ATOM     95  CG  HIS A  24     -25.925 -24.394 -77.599  1.00 82.11           C  
ANISOU   95  CG  HIS A  24    11271  12605   7322   -489   -412  -1607       C  
ATOM     96  ND1 HIS A  24     -26.198 -25.661 -78.067  1.00 92.24           N  
ANISOU   96  ND1 HIS A  24    12699  13862   8487   -621   -426  -1812       N  
ATOM     97  CD2 HIS A  24     -24.587 -24.228 -77.722  1.00 87.50           C  
ANISOU   97  CD2 HIS A  24    12026  13183   8038   -354   -260  -1551       C  
ATOM     98  CE1 HIS A  24     -25.074 -26.238 -78.452  1.00 91.01           C  
ANISOU   98  CE1 HIS A  24    12706  13582   8294   -552   -279  -1881       C  
ATOM     99  NE2 HIS A  24     -24.081 -25.389 -78.253  1.00 89.62           N  
ANISOU   99  NE2 HIS A  24    12478  13367   8208   -388   -176  -1719       N  
ATOM    100  N   ASN A  25     -29.536 -21.599 -77.976  1.00 90.63           N  
ANISOU  100  N   ASN A  25    11831  14337   8268   -517   -865  -1253       N  
ATOM    101  CA  ASN A  25     -30.686 -20.789 -77.590  1.00 97.96           C  
ANISOU  101  CA  ASN A  25    12566  15411   9243   -508   -982  -1125       C  
ATOM    102  C   ASN A  25     -31.134 -21.073 -76.162  1.00 95.92           C  
ANISOU  102  C   ASN A  25    12223  15018   9203   -566   -985  -1144       C  
ATOM    103  O   ASN A  25     -31.597 -20.158 -75.471  1.00106.06           O  
ANISOU  103  O   ASN A  25    13365  16326  10606   -486  -1006  -1001       O  
ATOM    104  CB  ASN A  25     -31.840 -21.017 -78.567  1.00 95.06           C  
ANISOU  104  CB  ASN A  25    12146  15315   8658   -618  -1144  -1168       C  
ATOM    105  CG  ASN A  25     -31.570 -20.421 -79.933  1.00 90.74           C  
ANISOU  105  CG  ASN A  25    11641  14948   7886   -529  -1157  -1095       C  
ATOM    106  OD1 ASN A  25     -31.631 -21.113 -80.950  1.00110.90           O  
ANISOU  106  OD1 ASN A  25    14301  17612  10224   -621  -1203  -1223       O  
ATOM    107  ND2 ASN A  25     -31.267 -19.128 -79.964  1.00 78.72           N  
ANISOU  107  ND2 ASN A  25    10046  13453   6410   -351  -1114   -888       N  
ATOM    108  N   TYR A  26     -31.010 -22.320 -75.699  1.00 94.80           N  
ANISOU  108  N   TYR A  26    12173  14732   9116   -698   -956  -1313       N  
ATOM    109  CA  TYR A  26     -31.393 -22.621 -74.324  1.00105.60           C  
ANISOU  109  CA  TYR A  26    13465  15971  10687   -750   -948  -1322       C  
ATOM    110  C   TYR A  26     -30.451 -21.979 -73.316  1.00100.15           C  
ANISOU  110  C   TYR A  26    12774  15089  10191   -607   -826  -1219       C  
ATOM    111  O   TYR A  26     -30.838 -21.787 -72.158  1.00104.03           O  
ANISOU  111  O   TYR A  26    13169  15514  10842   -603   -826  -1171       O  
ATOM    112  CB  TYR A  26     -31.463 -24.137 -74.102  1.00118.33           C  
ANISOU  112  CB  TYR A  26    15188  17463  12310   -927   -940  -1520       C  
ATOM    113  CG  TYR A  26     -30.146 -24.874 -74.237  1.00131.47           C  
ANISOU  113  CG  TYR A  26    17051  18920  13982   -900   -800  -1623       C  
ATOM    114  CD1 TYR A  26     -29.775 -25.458 -75.441  1.00136.44           C  
ANISOU  114  CD1 TYR A  26    17835  19587  14420   -939   -789  -1743       C  
ATOM    115  CD2 TYR A  26     -29.285 -25.005 -73.153  1.00131.15           C  
ANISOU  115  CD2 TYR A  26    17041  18654  14134   -832   -679  -1599       C  
ATOM    116  CE1 TYR A  26     -28.579 -26.141 -75.565  1.00137.32           C  
ANISOU  116  CE1 TYR A  26    18126  19511  14540   -895   -647  -1830       C  
ATOM    117  CE2 TYR A  26     -28.087 -25.682 -73.269  1.00127.19           C  
ANISOU  117  CE2 TYR A  26    16705  17976  13644   -793   -547  -1677       C  
ATOM    118  CZ  TYR A  26     -27.738 -26.247 -74.476  1.00132.09           C  
ANISOU  118  CZ  TYR A  26    17475  18632  14081   -819   -526  -1790       C  
ATOM    119  OH  TYR A  26     -26.546 -26.924 -74.596  1.00129.71           O  
ANISOU  119  OH  TYR A  26    17336  18157  13792   -762   -381  -1860       O  
ATOM    120  N   ILE A  27     -29.228 -21.642 -73.728  1.00 85.79           N  
ANISOU  120  N   ILE A  27    11054  13188   8356   -495   -722  -1183       N  
ATOM    121  CA  ILE A  27     -28.324 -20.904 -72.853  1.00 79.61           C  
ANISOU  121  CA  ILE A  27    10257  12247   7745   -368   -621  -1072       C  
ATOM    122  C   ILE A  27     -28.711 -19.433 -72.800  1.00 81.35           C  
ANISOU  122  C   ILE A  27    10352  12566   7991   -250   -660   -890       C  
ATOM    123  O   ILE A  27     -28.739 -18.825 -71.725  1.00 83.33           O  
ANISOU  123  O   ILE A  27    10533  12726   8403   -194   -639   -810       O  
ATOM    124  CB  ILE A  27     -26.866 -21.094 -73.314  1.00 70.02           C  
ANISOU  124  CB  ILE A  27     9177  10917   6509   -299   -494  -1088       C  
ATOM    125  CG1 ILE A  27     -26.334 -22.453 -72.856  1.00 84.36           C  
ANISOU  125  CG1 ILE A  27    11108  12561   8383   -378   -421  -1239       C  
ATOM    126  CG2 ILE A  27     -25.981 -19.961 -72.804  1.00 56.66           C  
ANISOU  126  CG2 ILE A  27     7446   9136   4945   -161   -418   -931       C  
ATOM    127  CD1 ILE A  27     -24.863 -22.650 -73.130  1.00 89.05           C  
ANISOU  127  CD1 ILE A  27    11815  13033   8985   -292   -281  -1238       C  
ATOM    128  N   PHE A  28     -29.033 -18.844 -73.953  1.00 90.01           N  
ANISOU  128  N   PHE A  28    11427  13847   8925   -207   -715   -822       N  
ATOM    129  CA  PHE A  28     -29.397 -17.434 -74.017  1.00 89.11           C  
ANISOU  129  CA  PHE A  28    11206  13824   8827    -81   -744   -637       C  
ATOM    130  C   PHE A  28     -30.719 -17.128 -73.328  1.00 82.18           C  
ANISOU  130  C   PHE A  28    10179  13035   8013    -97   -837   -591       C  
ATOM    131  O   PHE A  28     -31.036 -15.950 -73.133  1.00 94.52           O  
ANISOU  131  O   PHE A  28    11654  14632   9625     23   -843   -436       O  
ATOM    132  CB  PHE A  28     -29.458 -16.981 -75.477  1.00 96.19           C  
ANISOU  132  CB  PHE A  28    12118  14913   9517    -31   -782   -571       C  
ATOM    133  CG  PHE A  28     -28.171 -17.179 -76.225  1.00 92.93           C  
ANISOU  133  CG  PHE A  28    11844  14435   9029      4   -680   -595       C  
ATOM    134  CD1 PHE A  28     -26.955 -16.940 -75.609  1.00 86.30           C  
ANISOU  134  CD1 PHE A  28    11060  13391   8340     69   -554   -559       C  
ATOM    135  CD2 PHE A  28     -28.177 -17.614 -77.540  1.00 98.61           C  
ANISOU  135  CD2 PHE A  28    12637  15308   9522    -28   -708   -654       C  
ATOM    136  CE1 PHE A  28     -25.769 -17.123 -76.292  1.00 89.91           C  
ANISOU  136  CE1 PHE A  28    11628  13803   8733    108   -451   -567       C  
ATOM    137  CE2 PHE A  28     -26.992 -17.800 -78.229  1.00 91.51           C  
ANISOU  137  CE2 PHE A  28    11865  14355   8548     18   -598   -671       C  
ATOM    138  CZ  PHE A  28     -25.787 -17.554 -77.604  1.00 88.83           C  
ANISOU  138  CZ  PHE A  28    11565  13815   8370     90   -466   -622       C  
ATOM    139  N   VAL A  29     -31.492 -18.146 -72.958  1.00 67.29           N  
ANISOU  139  N   VAL A  29     8260  11179   6128   -238   -899   -714       N  
ATOM    140  CA  VAL A  29     -32.769 -17.961 -72.288  1.00 63.67           C  
ANISOU  140  CA  VAL A  29     7645  10818   5729   -261   -980   -669       C  
ATOM    141  C   VAL A  29     -32.688 -18.325 -70.810  1.00 80.44           C  
ANISOU  141  C   VAL A  29     9759  12756   8047   -290   -922   -713       C  
ATOM    142  O   VAL A  29     -33.253 -17.626 -69.965  1.00 83.40           O  
ANISOU  142  O   VAL A  29    10028  13131   8528   -218   -923   -617       O  
ATOM    143  CB  VAL A  29     -33.878 -18.770 -72.997  1.00 67.98           C  
ANISOU  143  CB  VAL A  29     8130  11578   6123   -413  -1112   -754       C  
ATOM    144  CG1 VAL A  29     -35.190 -18.674 -72.233  1.00 70.52           C  
ANISOU  144  CG1 VAL A  29     8270  12004   6519   -447  -1187   -703       C  
ATOM    145  CG2 VAL A  29     -34.056 -18.278 -74.425  1.00 66.96           C  
ANISOU  145  CG2 VAL A  29     7991  11663   5786   -370  -1182   -690       C  
ATOM    146  N   MET A  30     -31.977 -19.403 -70.476  1.00 86.91           N  
ANISOU  146  N   MET A  30    10696  13416   8911   -384   -863   -850       N  
ATOM    147  CA  MET A  30     -31.941 -19.869 -69.093  1.00 83.62           C  
ANISOU  147  CA  MET A  30    10270  12838   8662   -422   -813   -891       C  
ATOM    148  C   MET A  30     -30.898 -19.126 -68.266  1.00 76.79           C  
ANISOU  148  C   MET A  30     9451  11791   7937   -295   -709   -816       C  
ATOM    149  O   MET A  30     -31.164 -18.764 -67.113  1.00 75.56           O  
ANISOU  149  O   MET A  30     9233  11568   7908   -257   -689   -770       O  
ATOM    150  CB  MET A  30     -31.676 -21.374 -69.053  1.00 86.61           C  
ANISOU  150  CB  MET A  30    10754  13119   9034   -575   -793  -1060       C  
ATOM    151  CG  MET A  30     -31.589 -21.950 -67.648  1.00 88.49           C  
ANISOU  151  CG  MET A  30    10993  13190   9439   -616   -736  -1096       C  
ATOM    152  SD  MET A  30     -31.429 -23.745 -67.634  1.00 94.16           S  
ANISOU  152  SD  MET A  30    11834  13790  10152   -797   -713  -1282       S  
ATOM    153  CE  MET A  30     -29.891 -23.960 -68.524  1.00104.34           C  
ANISOU  153  CE  MET A  30    13307  14966  11370   -731   -618  -1335       C  
ATOM    154  N   ILE A  31     -29.709 -18.894 -68.831  1.00 69.46           N  
ANISOU  154  N   ILE A  31     8627  10787   6979   -233   -642   -804       N  
ATOM    155  CA  ILE A  31     -28.634 -18.260 -68.062  1.00 72.54           C  
ANISOU  155  CA  ILE A  31     9057  11004   7500   -138   -550   -739       C  
ATOM    156  C   ILE A  31     -29.006 -16.855 -67.596  1.00 80.85           C  
ANISOU  156  C   ILE A  31    10027  12073   8619    -21   -561   -597       C  
ATOM    157  O   ILE A  31     -28.740 -16.530 -66.425  1.00 89.35           O  
ANISOU  157  O   ILE A  31    11099  13020   9831     13   -518   -574       O  
ATOM    158  CB  ILE A  31     -27.319 -18.293 -68.864  1.00 67.63           C  
ANISOU  158  CB  ILE A  31     8546  10324   6828   -100   -476   -740       C  
ATOM    159  CG1 ILE A  31     -26.913 -19.736 -69.160  1.00 63.29           C  
ANISOU  159  CG1 ILE A  31     8095   9722   6229   -201   -444   -888       C  
ATOM    160  CG2 ILE A  31     -26.210 -17.577 -68.106  1.00 52.87           C  
ANISOU  160  CG2 ILE A  31     6700   8295   5092    -17   -394   -660       C  
ATOM    161  CD1 ILE A  31     -26.660 -20.564 -67.919  1.00 69.21           C  
ANISOU  161  CD1 ILE A  31     8867  10312   7117   -255   -399   -958       C  
ATOM    162  N   PRO A  32     -29.594 -15.983 -68.423  1.00 85.65           N  
ANISOU  162  N   PRO A  32    10576  12829   9137     50   -611   -498       N  
ATOM    163  CA  PRO A  32     -30.035 -14.682 -67.889  1.00 78.70           C  
ANISOU  163  CA  PRO A  32     9625  11944   8332    170   -611   -366       C  
ATOM    164  C   PRO A  32     -31.067 -14.803 -66.782  1.00 83.05           C  
ANISOU  164  C   PRO A  32    10083  12507   8965    155   -638   -380       C  
ATOM    165  O   PRO A  32     -31.086 -13.966 -65.871  1.00 85.67           O  
ANISOU  165  O   PRO A  32    10401  12745   9404    243   -600   -314       O  
ATOM    166  CB  PRO A  32     -30.611 -13.974 -69.123  1.00 67.74           C  
ANISOU  166  CB  PRO A  32     8185  10742   6810    239   -668   -262       C  
ATOM    167  CG  PRO A  32     -29.918 -14.605 -70.268  1.00 76.04           C  
ANISOU  167  CG  PRO A  32     9321  11838   7732    182   -664   -322       C  
ATOM    168  CD  PRO A  32     -29.755 -16.041 -69.888  1.00 79.16           C  
ANISOU  168  CD  PRO A  32     9765  12172   8140     41   -659   -490       C  
ATOM    169  N   THR A  33     -31.931 -15.819 -66.835  1.00 78.80           N  
ANISOU  169  N   THR A  33     9484  12079   8376     41   -701   -464       N  
ATOM    170  CA  THR A  33     -32.891 -16.030 -65.756  1.00 79.49           C  
ANISOU  170  CA  THR A  33     9475  12183   8544     17   -717   -472       C  
ATOM    171  C   THR A  33     -32.185 -16.404 -64.459  1.00 79.19           C  
ANISOU  171  C   THR A  33     9506  11942   8641     -4   -639   -532       C  
ATOM    172  O   THR A  33     -32.566 -15.935 -63.380  1.00 81.17           O  
ANISOU  172  O   THR A  33     9712  12146   8984     55   -612   -491       O  
ATOM    173  CB  THR A  33     -33.898 -17.111 -66.154  1.00 70.62           C  
ANISOU  173  CB  THR A  33     8273  11220   7339   -127   -802   -550       C  
ATOM    174  OG1 THR A  33     -34.669 -16.659 -67.275  1.00 71.53           O  
ANISOU  174  OG1 THR A  33     8301  11554   7323   -100   -888   -477       O  
ATOM    175  CG2 THR A  33     -34.835 -17.429 -64.997  1.00 58.50           C  
ANISOU  175  CG2 THR A  33     6632   9699   5894   -164   -807   -554       C  
ATOM    176  N   LEU A  34     -31.147 -17.238 -64.546  1.00 71.18           N  
ANISOU  176  N   LEU A  34     8602  10810   7632    -79   -599   -624       N  
ATOM    177  CA  LEU A  34     -30.402 -17.622 -63.352  1.00 69.16           C  
ANISOU  177  CA  LEU A  34     8408  10374   7497    -95   -529   -669       C  
ATOM    178  C   LEU A  34     -29.666 -16.431 -62.750  1.00 81.74           C  
ANISOU  178  C   LEU A  34    10037  11850   9172     24   -476   -585       C  
ATOM    179  O   LEU A  34     -29.609 -16.286 -61.524  1.00 87.91           O  
ANISOU  179  O   LEU A  34    10818  12534  10048     44   -443   -585       O  
ATOM    180  CB  LEU A  34     -29.425 -18.748 -63.683  1.00 61.57           C  
ANISOU  180  CB  LEU A  34     7553   9322   6518   -182   -492   -770       C  
ATOM    181  CG  LEU A  34     -30.068 -20.099 -63.997  1.00 68.72           C  
ANISOU  181  CG  LEU A  34     8455  10286   7369   -324   -531   -880       C  
ATOM    182  CD1 LEU A  34     -29.015 -21.126 -64.379  1.00 76.72           C  
ANISOU  182  CD1 LEU A  34     9597  11188   8366   -382   -475   -974       C  
ATOM    183  CD2 LEU A  34     -30.877 -20.577 -62.805  1.00 71.18           C  
ANISOU  183  CD2 LEU A  34     8697  10582   7766   -381   -536   -897       C  
ATOM    184  N   TYR A  35     -29.097 -15.567 -63.596  1.00 79.55           N  
ANISOU  184  N   TYR A  35     9794  11577   8853     98   -468   -515       N  
ATOM    185  CA  TYR A  35     -28.442 -14.366 -63.089  1.00 77.62           C  
ANISOU  185  CA  TYR A  35     9588  11215   8688    197   -423   -432       C  
ATOM    186  C   TYR A  35     -29.429 -13.451 -62.376  1.00 64.90           C  
ANISOU  186  C   TYR A  35     7912   9625   7120    284   -434   -367       C  
ATOM    187  O   TYR A  35     -29.041 -12.707 -61.469  1.00 64.00           O  
ANISOU  187  O   TYR A  35     7840   9384   7094    341   -393   -339       O  
ATOM    188  CB  TYR A  35     -27.753 -13.615 -64.231  1.00 87.94           C  
ANISOU  188  CB  TYR A  35    10938  12535   9941    253   -411   -354       C  
ATOM    189  CG  TYR A  35     -26.526 -14.309 -64.782  1.00 84.96           C  
ANISOU  189  CG  TYR A  35    10636  12105   9538    196   -371   -402       C  
ATOM    190  CD1 TYR A  35     -25.895 -15.321 -64.069  1.00 80.22           C  
ANISOU  190  CD1 TYR A  35    10075  11408   8996    122   -337   -492       C  
ATOM    191  CD2 TYR A  35     -25.996 -13.948 -66.014  1.00 81.33           C  
ANISOU  191  CD2 TYR A  35    10208  11697   8997    229   -359   -345       C  
ATOM    192  CE1 TYR A  35     -24.772 -15.955 -64.570  1.00 75.11           C  
ANISOU  192  CE1 TYR A  35     9494  10715   8330     90   -289   -526       C  
ATOM    193  CE2 TYR A  35     -24.874 -14.576 -66.522  1.00 76.34           C  
ANISOU  193  CE2 TYR A  35     9642  11024   8339    192   -308   -382       C  
ATOM    194  CZ  TYR A  35     -24.267 -15.578 -65.796  1.00 73.08           C  
ANISOU  194  CZ  TYR A  35     9264  10513   7990    127   -271   -473       C  
ATOM    195  OH  TYR A  35     -23.150 -16.206 -66.299  1.00 78.03           O  
ANISOU  195  OH  TYR A  35     9952  11100   8594    109   -209   -500       O  
ATOM    196  N   SER A  36     -30.704 -13.492 -62.768  1.00 72.26           N  
ANISOU  196  N   SER A  36     8743  10722   7989    298   -487   -341       N  
ATOM    197  CA  SER A  36     -31.716 -12.705 -62.071  1.00 72.16           C  
ANISOU  197  CA  SER A  36     8657  10744   8017    395   -486   -273       C  
ATOM    198  C   SER A  36     -32.024 -13.296 -60.702  1.00 75.20           C  
ANISOU  198  C   SER A  36     9024  11071   8477    352   -461   -340       C  
ATOM    199  O   SER A  36     -32.230 -12.557 -59.732  1.00 76.28           O  
ANISOU  199  O   SER A  36     9168  11135   8680    439   -420   -307       O  
ATOM    200  CB  SER A  36     -32.986 -12.616 -62.917  1.00 69.68           C  
ANISOU  200  CB  SER A  36     8216  10648   7611    424   -553   -211       C  
ATOM    201  OG  SER A  36     -32.718 -12.033 -64.180  1.00 74.92           O  
ANISOU  201  OG  SER A  36     8897  11376   8193    474   -575   -137       O  
ATOM    202  N   ILE A  37     -32.061 -14.626 -60.604  1.00 73.47           N  
ANISOU  202  N   ILE A  37     8791  10878   8245    219   -480   -435       N  
ATOM    203  CA  ILE A  37     -32.307 -15.271 -59.318  1.00 77.01           C  
ANISOU  203  CA  ILE A  37     9225  11272   8762    172   -450   -489       C  
ATOM    204  C   ILE A  37     -31.147 -15.017 -58.364  1.00 78.42           C  
ANISOU  204  C   ILE A  37     9515  11260   9020    194   -390   -512       C  
ATOM    205  O   ILE A  37     -31.351 -14.754 -57.173  1.00 80.37           O  
ANISOU  205  O   ILE A  37     9765  11450   9324    234   -354   -510       O  
ATOM    206  CB  ILE A  37     -32.560 -16.777 -59.518  1.00 68.22           C  
ANISOU  206  CB  ILE A  37     8085  10214   7620     17   -481   -579       C  
ATOM    207  CG1 ILE A  37     -33.733 -16.996 -60.476  1.00 65.74           C  
ANISOU  207  CG1 ILE A  37     7654  10104   7218    -24   -557   -559       C  
ATOM    208  CG2 ILE A  37     -32.824 -17.458 -58.184  1.00 56.59           C  
ANISOU  208  CG2 ILE A  37     6596   8685   6220    -31   -444   -618       C  
ATOM    209  CD1 ILE A  37     -34.011 -18.452 -60.780  1.00 57.36           C  
ANISOU  209  CD1 ILE A  37     6580   9090   6122   -196   -595   -657       C  
ATOM    210  N   ILE A  38     -29.913 -15.089 -58.869  1.00 73.33           N  
ANISOU  210  N   ILE A  38     8961  10526   8375    166   -378   -531       N  
ATOM    211  CA  ILE A  38     -28.748 -14.797 -58.038  1.00 58.05           C  
ANISOU  211  CA  ILE A  38     7117   8428   6512    179   -332   -541       C  
ATOM    212  C   ILE A  38     -28.759 -13.337 -57.603  1.00 71.49           C  
ANISOU  212  C   ILE A  38     8847  10067   8250    292   -313   -473       C  
ATOM    213  O   ILE A  38     -28.353 -13.002 -56.483  1.00 82.62           O  
ANISOU  213  O   ILE A  38    10309  11366   9717    308   -284   -487       O  
ATOM    214  CB  ILE A  38     -27.453 -15.154 -58.793  1.00 53.81           C  
ANISOU  214  CB  ILE A  38     6649   7833   5964    132   -320   -558       C  
ATOM    215  CG1 ILE A  38     -27.445 -16.636 -59.173  1.00 56.06           C  
ANISOU  215  CG1 ILE A  38     6930   8157   6214     29   -325   -637       C  
ATOM    216  CG2 ILE A  38     -26.228 -14.811 -57.957  1.00 42.14           C  
ANISOU  216  CG2 ILE A  38     5243   6207   4560    137   -283   -554       C  
ATOM    217  CD1 ILE A  38     -26.247 -17.045 -60.004  1.00 45.01           C  
ANISOU  217  CD1 ILE A  38     5597   6713   4792      0   -300   -653       C  
ATOM    218  N   PHE A  39     -29.235 -12.447 -58.476  1.00 71.52           N  
ANISOU  218  N   PHE A  39     8824  10135   8214    371   -329   -397       N  
ATOM    219  CA  PHE A  39     -29.227 -11.021 -58.166  1.00 71.46           C  
ANISOU  219  CA  PHE A  39     8861  10045   8245    485   -302   -328       C  
ATOM    220  C   PHE A  39     -30.195 -10.695 -57.035  1.00 71.75           C  
ANISOU  220  C   PHE A  39     8868  10082   8309    556   -278   -330       C  
ATOM    221  O   PHE A  39     -29.823 -10.035 -56.058  1.00 70.55           O  
ANISOU  221  O   PHE A  39     8797   9798   8210    595   -241   -342       O  
ATOM    222  CB  PHE A  39     -29.565 -10.213 -59.419  1.00 66.10           C  
ANISOU  222  CB  PHE A  39     8157   9444   7515    564   -319   -230       C  
ATOM    223  CG  PHE A  39     -29.513  -8.726 -59.214  1.00 69.05           C  
ANISOU  223  CG  PHE A  39     8592   9709   7933    685   -283   -150       C  
ATOM    224  CD1 PHE A  39     -28.300  -8.056 -59.217  1.00 67.83           C  
ANISOU  224  CD1 PHE A  39     8546   9399   7829    672   -257   -133       C  
ATOM    225  CD2 PHE A  39     -30.675  -7.996 -59.026  1.00 54.95           C  
ANISOU  225  CD2 PHE A  39     6759   7976   6144    812   -270    -86       C  
ATOM    226  CE1 PHE A  39     -28.248  -6.688 -59.031  1.00 57.97           C  
ANISOU  226  CE1 PHE A  39     7371   8029   6627    769   -221    -64       C  
ATOM    227  CE2 PHE A  39     -30.629  -6.627 -58.839  1.00 58.91           C  
ANISOU  227  CE2 PHE A  39     7338   8356   6691    931   -224    -15       C  
ATOM    228  CZ  PHE A  39     -29.413  -5.973 -58.842  1.00 60.33           C  
ANISOU  228  CZ  PHE A  39     7640   8362   6921    903   -201     -8       C  
ATOM    229  N   VAL A  40     -31.443 -11.153 -57.147  1.00 74.13           N  
ANISOU  229  N   VAL A  40     9055  10539   8572    569   -298   -318       N  
ATOM    230  CA  VAL A  40     -32.449 -10.827 -56.140  1.00 75.13           C  
ANISOU  230  CA  VAL A  40     9137  10690   8720    652   -264   -304       C  
ATOM    231  C   VAL A  40     -32.101 -11.477 -54.805  1.00 84.81           C  
ANISOU  231  C   VAL A  40    10406  11832   9986    588   -234   -387       C  
ATOM    232  O   VAL A  40     -32.165 -10.836 -53.750  1.00 84.28           O  
ANISOU  232  O   VAL A  40    10395  11678   9949    662   -185   -393       O  
ATOM    233  CB  VAL A  40     -33.849 -11.247 -56.623  1.00 64.19           C  
ANISOU  233  CB  VAL A  40     7591   9513   7284    665   -297   -260       C  
ATOM    234  CG1 VAL A  40     -34.893 -10.932 -55.565  1.00 52.17           C  
ANISOU  234  CG1 VAL A  40     6008   8028   5785    762   -248   -233       C  
ATOM    235  CG2 VAL A  40     -34.187 -10.553 -57.934  1.00 80.27           C  
ANISOU  235  CG2 VAL A  40     9582  11649   9269    739   -333   -165       C  
ATOM    236  N   VAL A  41     -31.725 -12.756 -54.832  1.00 75.65           N  
ANISOU  236  N   VAL A  41     9231  10693   8821    455   -257   -451       N  
ATOM    237  CA  VAL A  41     -31.384 -13.455 -53.596  1.00 54.26           C  
ANISOU  237  CA  VAL A  41     6557   7914   6146    395   -229   -515       C  
ATOM    238  C   VAL A  41     -30.082 -12.916 -53.017  1.00 68.90           C  
ANISOU  238  C   VAL A  41     8541   9599   8037    398   -210   -540       C  
ATOM    239  O   VAL A  41     -29.938 -12.782 -51.795  1.00 81.73           O  
ANISOU  239  O   VAL A  41    10216  11155   9682    414   -179   -569       O  
ATOM    240  CB  VAL A  41     -31.314 -14.972 -53.846  1.00 49.40           C  
ANISOU  240  CB  VAL A  41     5898   7350   5520    257   -253   -567       C  
ATOM    241  CG1 VAL A  41     -30.855 -15.702 -52.594  1.00 49.36           C  
ANISOU  241  CG1 VAL A  41     5937   7266   5552    203   -219   -616       C  
ATOM    242  CG2 VAL A  41     -32.668 -15.495 -54.301  1.00 58.39           C  
ANISOU  242  CG2 VAL A  41     6903   8658   6624    232   -279   -547       C  
ATOM    243  N   GLY A  42     -29.117 -12.589 -53.879  1.00 73.79           N  
ANISOU  243  N   GLY A  42     9213  10162   8660    377   -231   -526       N  
ATOM    244  CA  GLY A  42     -27.845 -12.082 -53.390  1.00 58.23           C  
ANISOU  244  CA  GLY A  42     7349   8045   6729    361   -222   -540       C  
ATOM    245  C   GLY A  42     -27.959 -10.704 -52.767  1.00 61.14           C  
ANISOU  245  C   GLY A  42     7792   8321   7118    457   -197   -520       C  
ATOM    246  O   GLY A  42     -27.379 -10.443 -51.709  1.00 70.24           O  
ANISOU  246  O   GLY A  42     9023   9372   8292    442   -186   -559       O  
ATOM    247  N   ILE A  43     -28.695  -9.800 -53.416  1.00 61.73           N  
ANISOU  247  N   ILE A  43     7849   8426   7180    558   -188   -457       N  
ATOM    248  CA  ILE A  43     -28.882  -8.463 -52.860  1.00 59.06           C  
ANISOU  248  CA  ILE A  43     7596   7981   6863    664   -151   -438       C  
ATOM    249  C   ILE A  43     -29.696  -8.531 -51.573  1.00 70.78           C  
ANISOU  249  C   ILE A  43     9080   9477   8337    719   -111   -479       C  
ATOM    250  O   ILE A  43     -29.438  -7.789 -50.620  1.00 77.13           O  
ANISOU  250  O   ILE A  43     9994  10158   9154    757    -80   -515       O  
ATOM    251  CB  ILE A  43     -29.536  -7.537 -53.903  1.00 56.03           C  
ANISOU  251  CB  ILE A  43     7187   7634   6469    777   -141   -343       C  
ATOM    252  CG1 ILE A  43     -28.581  -7.289 -55.073  1.00 67.55           C  
ANISOU  252  CG1 ILE A  43     8672   9057   7935    728   -169   -296       C  
ATOM    253  CG2 ILE A  43     -29.946  -6.214 -53.275  1.00 52.18           C  
ANISOU  253  CG2 ILE A  43     6789   7032   6004    910    -86   -322       C  
ATOM    254  CD1 ILE A  43     -27.322  -6.542 -54.688  1.00 65.77           C  
ANISOU  254  CD1 ILE A  43     8578   8646   7764    683   -161   -312       C  
ATOM    255  N   PHE A  44     -30.678  -9.433 -51.517  1.00 82.03           N  
ANISOU  255  N   PHE A  44    10384  11051   9732    717   -109   -477       N  
ATOM    256  CA  PHE A  44     -31.495  -9.566 -50.316  1.00 87.22           C  
ANISOU  256  CA  PHE A  44    11024  11739  10375    772    -61   -503       C  
ATOM    257  C   PHE A  44     -30.684 -10.125 -49.152  1.00 90.24           C  
ANISOU  257  C   PHE A  44    11481  12044  10761    685    -60   -581       C  
ATOM    258  O   PHE A  44     -30.680  -9.555 -48.055  1.00103.41           O  
ANISOU  258  O   PHE A  44    13239  13634  12418    740    -20   -618       O  
ATOM    259  CB  PHE A  44     -32.706 -10.455 -50.604  1.00 89.34           C  
ANISOU  259  CB  PHE A  44    11130  12196  10619    768    -64   -469       C  
ATOM    260  CG  PHE A  44     -33.374 -10.994 -49.370  1.00105.67           C  
ANISOU  260  CG  PHE A  44    13162  14314  12675    778    -17   -495       C  
ATOM    261  CD1 PHE A  44     -33.124 -12.288 -48.939  1.00111.18           C  
ANISOU  261  CD1 PHE A  44    13826  15044  13373    651    -32   -539       C  
ATOM    262  CD2 PHE A  44     -34.252 -10.209 -48.641  1.00115.19           C  
ANISOU  262  CD2 PHE A  44    14371  15531  13867    924     53   -470       C  
ATOM    263  CE1 PHE A  44     -33.735 -12.788 -47.805  1.00112.06           C  
ANISOU  263  CE1 PHE A  44    13903  15204  13471    660     17   -550       C  
ATOM    264  CE2 PHE A  44     -34.867 -10.704 -47.506  1.00120.91           C  
ANISOU  264  CE2 PHE A  44    15058  16310  14571    939    106   -486       C  
ATOM    265  CZ  PHE A  44     -34.608 -11.994 -47.087  1.00116.43           C  
ANISOU  265  CZ  PHE A  44    14453  15781  14003    802     86   -523       C  
ATOM    266  N   GLY A  45     -29.989 -11.241 -49.375  1.00 81.69           N  
ANISOU  266  N   GLY A  45    10368  10984   9686    556   -100   -607       N  
ATOM    267  CA  GLY A  45     -29.301 -11.901 -48.277  1.00 84.78           C  
ANISOU  267  CA  GLY A  45    10808  11328  10077    481    -99   -662       C  
ATOM    268  C   GLY A  45     -28.099 -11.121 -47.778  1.00 83.43           C  
ANISOU  268  C   GLY A  45    10770  11012   9919    462   -116   -695       C  
ATOM    269  O   GLY A  45     -27.933 -10.918 -46.572  1.00 96.79           O  
ANISOU  269  O   GLY A  45    12534  12653  11588    471    -99   -739       O  
ATOM    270  N   ASN A  46     -27.244 -10.673 -48.699  1.00 69.79           N  
ANISOU  270  N   ASN A  46     9073   9223   8222    428   -150   -673       N  
ATOM    271  CA  ASN A  46     -26.011 -10.001 -48.303  1.00 67.35           C  
ANISOU  271  CA  ASN A  46     8873   8784   7933    380   -175   -697       C  
ATOM    272  C   ASN A  46     -26.257  -8.617 -47.715  1.00 71.66           C  
ANISOU  272  C   ASN A  46     9535   9221   8473    462   -149   -718       C  
ATOM    273  O   ASN A  46     -25.409  -8.120 -46.968  1.00 83.40           O  
ANISOU  273  O   ASN A  46    11124  10603   9961    413   -170   -762       O  
ATOM    274  CB  ASN A  46     -25.060  -9.903 -49.496  1.00 74.49           C  
ANISOU  274  CB  ASN A  46     9767   9660   8876    321   -209   -654       C  
ATOM    275  CG  ASN A  46     -24.534 -11.257 -49.931  1.00 88.43           C  
ANISOU  275  CG  ASN A  46    11452  11500  10646    235   -228   -649       C  
ATOM    276  OD1 ASN A  46     -24.211 -12.106 -49.100  1.00 99.36           O  
ANISOU  276  OD1 ASN A  46    12828  12900  12024    184   -232   -681       O  
ATOM    277  ND2 ASN A  46     -24.453 -11.468 -51.239  1.00 94.58           N  
ANISOU  277  ND2 ASN A  46    12181  12325  11430    227   -233   -608       N  
ATOM    278  N   SER A  47     -27.389  -7.983 -48.031  1.00 67.44           N  
ANISOU  278  N   SER A  47     8986   8708   7929    586   -104   -686       N  
ATOM    279  CA  SER A  47     -27.687  -6.686 -47.431  1.00 68.29           C  
ANISOU  279  CA  SER A  47     9220   8698   8031    683    -61   -709       C  
ATOM    280  C   SER A  47     -28.068  -6.836 -45.964  1.00 73.22           C  
ANISOU  280  C   SER A  47     9897   9323   8602    713    -27   -780       C  
ATOM    281  O   SER A  47     -27.630  -6.046 -45.120  1.00 84.47           O  
ANISOU  281  O   SER A  47    11465  10620  10009    714    -20   -843       O  
ATOM    282  CB  SER A  47     -28.803  -5.984 -48.202  1.00 69.28           C  
ANISOU  282  CB  SER A  47     9307   8854   8163    829    -13   -637       C  
ATOM    283  OG  SER A  47     -28.439  -5.783 -49.557  1.00 87.00           O  
ANISOU  283  OG  SER A  47    11513  11101  10442    807    -44   -565       O  
ATOM    284  N   LEU A  48     -28.883  -7.844 -45.642  1.00 69.04           N  
ANISOU  284  N   LEU A  48     9254   8936   8040    731     -3   -772       N  
ATOM    285  CA  LEU A  48     -29.267  -8.070 -44.254  1.00 67.60           C  
ANISOU  285  CA  LEU A  48     9112   8774   7799    762     38   -827       C  
ATOM    286  C   LEU A  48     -28.070  -8.454 -43.394  1.00 68.71           C  
ANISOU  286  C   LEU A  48     9328   8861   7918    638    -14   -890       C  
ATOM    287  O   LEU A  48     -28.032  -8.118 -42.205  1.00 77.95           O  
ANISOU  287  O   LEU A  48    10603   9987   9028    660      7   -953       O  
ATOM    288  CB  LEU A  48     -30.346  -9.150 -44.176  1.00 58.41           C  
ANISOU  288  CB  LEU A  48     7796   7781   6617    787     74   -787       C  
ATOM    289  CG  LEU A  48     -31.670  -8.829 -44.871  1.00 71.82           C  
ANISOU  289  CG  LEU A  48     9393   9570   8325    913    123   -716       C  
ATOM    290  CD1 LEU A  48     -32.629 -10.003 -44.768  1.00 79.28           C  
ANISOU  290  CD1 LEU A  48    10176  10690   9257    898    144   -677       C  
ATOM    291  CD2 LEU A  48     -32.292  -7.572 -44.283  1.00 78.99           C  
ANISOU  291  CD2 LEU A  48    10402  10404   9206   1077    203   -727       C  
ATOM    292  N   VAL A  49     -27.089  -9.151 -43.972  1.00 64.47           N  
ANISOU  292  N   VAL A  49     8740   8336   7420    514    -81   -870       N  
ATOM    293  CA  VAL A  49     -25.888  -9.506 -43.222  1.00 66.88           C  
ANISOU  293  CA  VAL A  49     9098   8605   7710    400   -136   -910       C  
ATOM    294  C   VAL A  49     -25.132  -8.251 -42.803  1.00 71.88           C  
ANISOU  294  C   VAL A  49     9886   9091   8334    379   -165   -965       C  
ATOM    295  O   VAL A  49     -24.624  -8.160 -41.678  1.00 84.92           O  
ANISOU  295  O   VAL A  49    11623  10712   9930    333   -190  -1026       O  
ATOM    296  CB  VAL A  49     -25.001 -10.454 -44.052  1.00 60.97           C  
ANISOU  296  CB  VAL A  49     8256   7898   7013    293   -188   -864       C  
ATOM    297  CG1 VAL A  49     -23.690 -10.730 -43.334  1.00 69.68           C  
ANISOU  297  CG1 VAL A  49     9399   8970   8105    185   -248   -886       C  
ATOM    298  CG2 VAL A  49     -25.738 -11.754 -44.336  1.00 54.48           C  
ANISOU  298  CG2 VAL A  49     7306   7202   6193    297   -160   -828       C  
ATOM    299  N   VAL A  50     -25.057  -7.260 -43.693  1.00 61.44           N  
ANISOU  299  N   VAL A  50     8606   7675   7063    405   -164   -942       N  
ATOM    300  CA  VAL A  50     -24.375  -6.014 -43.359  1.00 62.64           C  
ANISOU  300  CA  VAL A  50     8916   7665   7219    373   -187   -994       C  
ATOM    301  C   VAL A  50     -25.179  -5.222 -42.334  1.00 69.90           C  
ANISOU  301  C   VAL A  50     9970   8519   8072    482   -125  -1068       C  
ATOM    302  O   VAL A  50     -24.613  -4.592 -41.433  1.00 73.15           O  
ANISOU  302  O   VAL A  50    10527   8827   8441    431   -151  -1151       O  
ATOM    303  CB  VAL A  50     -24.115  -5.193 -44.636  1.00 55.98           C  
ANISOU  303  CB  VAL A  50     8082   6734   6455    377   -191   -934       C  
ATOM    304  CG1 VAL A  50     -23.402  -3.891 -44.300  1.00 59.30           C  
ANISOU  304  CG1 VAL A  50     8674   6967   6891    327   -213   -984       C  
ATOM    305  CG2 VAL A  50     -23.304  -6.006 -45.632  1.00 56.35           C  
ANISOU  305  CG2 VAL A  50     8002   6855   6553    278   -241   -863       C  
ATOM    306  N   ILE A  51     -26.509  -5.248 -42.448  1.00 67.49           N  
ANISOU  306  N   ILE A  51     9616   8278   7751    632    -41  -1040       N  
ATOM    307  CA  ILE A  51     -27.352  -4.479 -41.538  1.00 78.52           C  
ANISOU  307  CA  ILE A  51    11134   9616   9083    765     40  -1100       C  
ATOM    308  C   ILE A  51     -27.271  -5.040 -40.123  1.00 78.03           C  
ANISOU  308  C   ILE A  51    11114   9611   8923    733     38  -1175       C  
ATOM    309  O   ILE A  51     -27.251  -4.286 -39.142  1.00 91.70           O  
ANISOU  309  O   ILE A  51    13014  11245  10583    766     63  -1267       O  
ATOM    310  CB  ILE A  51     -28.801  -4.448 -42.059  1.00 76.29           C  
ANISOU  310  CB  ILE A  51    10754   9420   8812    938    132  -1028       C  
ATOM    311  CG1 ILE A  51     -28.871  -3.689 -43.385  1.00 67.62           C  
ANISOU  311  CG1 ILE A  51     9642   8253   7795    985    135   -952       C  
ATOM    312  CG2 ILE A  51     -29.733  -3.818 -41.035  1.00 66.08           C  
ANISOU  312  CG2 ILE A  51     9567   8094   7446   1094    234  -1081       C  
ATOM    313  CD1 ILE A  51     -30.241  -3.690 -44.015  1.00 49.05           C  
ANISOU  313  CD1 ILE A  51     7169   6012   5455   1148    208   -862       C  
ATOM    314  N   VAL A  52     -27.212  -6.365 -39.991  1.00 67.96           N  
ANISOU  314  N   VAL A  52     9699   8487   7636    670     11  -1138       N  
ATOM    315  CA  VAL A  52     -27.180  -6.975 -38.665  1.00 65.47           C  
ANISOU  315  CA  VAL A  52     9410   8241   7222    649     15  -1188       C  
ATOM    316  C   VAL A  52     -25.803  -6.826 -38.027  1.00 81.49           C  
ANISOU  316  C   VAL A  52    11544  10202   9217    503    -82  -1254       C  
ATOM    317  O   VAL A  52     -25.689  -6.540 -36.831  1.00 89.12           O  
ANISOU  317  O   VAL A  52    12635  11147  10080    503    -81  -1337       O  
ATOM    318  CB  VAL A  52     -27.609  -8.450 -38.753  1.00 59.69           C  
ANISOU  318  CB  VAL A  52     8497   7683   6499    631     26  -1114       C  
ATOM    319  CG1 VAL A  52     -27.428  -9.138 -37.410  1.00 69.05           C  
ANISOU  319  CG1 VAL A  52     9709   8941   7587    598     25  -1148       C  
ATOM    320  CG2 VAL A  52     -29.055  -8.553 -39.212  1.00 58.23           C  
ANISOU  320  CG2 VAL A  52     8208   7583   6333    767    118  -1055       C  
ATOM    321  N   ILE A  53     -24.739  -7.005 -38.807  1.00 83.98           N  
ANISOU  321  N   ILE A  53    11807  10493   9609    377   -168  -1216       N  
ATOM    322  CA  ILE A  53     -23.391  -7.007 -38.244  1.00 83.05           C  
ANISOU  322  CA  ILE A  53    11745  10344   9465    227   -269  -1256       C  
ATOM    323  C   ILE A  53     -22.928  -5.589 -37.932  1.00 85.72           C  
ANISOU  323  C   ILE A  53    12274  10512   9784    192   -298  -1346       C  
ATOM    324  O   ILE A  53     -22.549  -5.276 -36.797  1.00 90.87           O  
ANISOU  324  O   ILE A  53    13052  11137  10339    143   -334  -1435       O  
ATOM    325  CB  ILE A  53     -22.412  -7.719 -39.195  1.00 77.97           C  
ANISOU  325  CB  ILE A  53    10967   9745   8914    114   -339  -1172       C  
ATOM    326  CG1 ILE A  53     -22.724  -9.214 -39.261  1.00 81.75           C  
ANISOU  326  CG1 ILE A  53    11290  10377   9397    128   -317  -1102       C  
ATOM    327  CG2 ILE A  53     -20.977  -7.493 -38.751  1.00 76.31           C  
ANISOU  327  CG2 ILE A  53    10806   9497   8691    -39   -446  -1198       C  
ATOM    328  CD1 ILE A  53     -21.801  -9.984 -40.171  1.00 97.93           C  
ANISOU  328  CD1 ILE A  53    13217  12464  11528     37   -368  -1024       C  
ATOM    329  N   TYR A  54     -22.948  -4.710 -38.935  1.00 87.07           N  
ANISOU  329  N   TYR A  54    12477  10562  10043    212   -282  -1324       N  
ATOM    330  CA  TYR A  54     -22.357  -3.387 -38.784  1.00 91.05           C  
ANISOU  330  CA  TYR A  54    13162  10880  10554    150   -316  -1399       C  
ATOM    331  C   TYR A  54     -23.214  -2.434 -37.961  1.00110.61           C  
ANISOU  331  C   TYR A  54    15830  13247  12949    272   -235  -1502       C  
ATOM    332  O   TYR A  54     -22.673  -1.489 -37.376  1.00122.96           O  
ANISOU  332  O   TYR A  54    17579  14663  14476    200   -271  -1602       O  
ATOM    333  CB  TYR A  54     -22.086  -2.774 -40.161  1.00 77.53           C  
ANISOU  333  CB  TYR A  54    11421   9069   8966    134   -317  -1325       C  
ATOM    334  CG  TYR A  54     -21.320  -1.470 -40.115  1.00 75.75           C  
ANISOU  334  CG  TYR A  54    11371   8642   8770     37   -359  -1384       C  
ATOM    335  CD1 TYR A  54     -19.944  -1.457 -39.929  1.00 69.48           C  
ANISOU  335  CD1 TYR A  54    10579   7831   7991   -164   -475  -1396       C  
ATOM    336  CD2 TYR A  54     -21.972  -0.252 -40.264  1.00 75.26           C  
ANISOU  336  CD2 TYR A  54    11468   8403   8726    143   -281  -1420       C  
ATOM    337  CE1 TYR A  54     -19.239  -0.268 -39.886  1.00 70.61           C  
ANISOU  337  CE1 TYR A  54    10877   7785   8165   -276   -519  -1450       C  
ATOM    338  CE2 TYR A  54     -21.275   0.942 -40.224  1.00 87.63           C  
ANISOU  338  CE2 TYR A  54    13208   9761  10326     43   -316  -1476       C  
ATOM    339  CZ  TYR A  54     -19.909   0.927 -40.035  1.00 85.50           C  
ANISOU  339  CZ  TYR A  54    12937   9478  10071   -177   -439  -1494       C  
ATOM    340  OH  TYR A  54     -19.211   2.113 -39.994  1.00 92.87           O  
ANISOU  340  OH  TYR A  54    14041  10202  11044   -299   -478  -1549       O  
ATOM    341  N   PHE A  55     -24.527  -2.656 -37.891  1.00109.75           N  
ANISOU  341  N   PHE A  55    15684  13206  12812    453   -124  -1481       N  
ATOM    342  CA  PHE A  55     -25.421  -1.730 -37.206  1.00100.53           C  
ANISOU  342  CA  PHE A  55    14689  11934  11572    602    -23  -1565       C  
ATOM    343  C   PHE A  55     -26.007  -2.272 -35.912  1.00 90.11           C  
ANISOU  343  C   PHE A  55    13395  10729  10114    671     25  -1624       C  
ATOM    344  O   PHE A  55     -26.352  -1.481 -35.032  1.00 86.39           O  
ANISOU  344  O   PHE A  55    13115  10160   9550    747     83  -1731       O  
ATOM    345  CB  PHE A  55     -26.569  -1.314 -38.136  1.00 87.44           C  
ANISOU  345  CB  PHE A  55    12981  10255   9988    788     88  -1484       C  
ATOM    346  CG  PHE A  55     -26.116  -0.567 -39.360  1.00 85.72           C  
ANISOU  346  CG  PHE A  55    12773   9904   9891    751     61  -1426       C  
ATOM    347  CD1 PHE A  55     -25.965   0.811 -39.330  1.00 80.25           C  
ANISOU  347  CD1 PHE A  55    12291   8982   9219    774     90  -1487       C  
ATOM    348  CD2 PHE A  55     -25.840  -1.241 -40.538  1.00 81.48           C  
ANISOU  348  CD2 PHE A  55    12047   9467   9446    693     14  -1309       C  
ATOM    349  CE1 PHE A  55     -25.548   1.502 -40.454  1.00 81.84           C  
ANISOU  349  CE1 PHE A  55    12503   9059   9535    739     72  -1418       C  
ATOM    350  CE2 PHE A  55     -25.422  -0.555 -41.665  1.00 72.81           C  
ANISOU  350  CE2 PHE A  55    10958   8257   8449    663     -4  -1245       C  
ATOM    351  CZ  PHE A  55     -25.276   0.817 -41.623  1.00 68.67           C  
ANISOU  351  CZ  PHE A  55    10634   7508   7949    686     26  -1293       C  
ATOM    352  N   TYR A  56     -26.133  -3.593 -35.768  1.00 85.41           N  
ANISOU  352  N   TYR A  56    12622  10331   9500    650     10  -1557       N  
ATOM    353  CA  TYR A  56     -26.686  -4.182 -34.557  1.00 83.31           C  
ANISOU  353  CA  TYR A  56    12364  10185   9103    713     60  -1593       C  
ATOM    354  C   TYR A  56     -25.651  -4.889 -33.691  1.00 91.08           C  
ANISOU  354  C   TYR A  56    13351  11250  10006    555    -47  -1626       C  
ATOM    355  O   TYR A  56     -25.973  -5.264 -32.559  1.00106.35           O  
ANISOU  355  O   TYR A  56    15325  13273  11810    596    -13  -1665       O  
ATOM    356  CB  TYR A  56     -27.813  -5.167 -34.908  1.00 83.90           C  
ANISOU  356  CB  TYR A  56    12240  10431   9208    827    145  -1481       C  
ATOM    357  CG  TYR A  56     -29.126  -4.503 -35.270  1.00 88.62           C  
ANISOU  357  CG  TYR A  56    12843  11000   9828   1027    277  -1456       C  
ATOM    358  CD1 TYR A  56     -29.348  -3.161 -34.991  1.00102.22           C  
ANISOU  358  CD1 TYR A  56    14769  12552  11517   1127    338  -1542       C  
ATOM    359  CD2 TYR A  56     -30.147  -5.221 -35.881  1.00 92.10           C  
ANISOU  359  CD2 TYR A  56    13086  11586  10323   1117    340  -1342       C  
ATOM    360  CE1 TYR A  56     -30.546  -2.550 -35.315  1.00112.45           C  
ANISOU  360  CE1 TYR A  56    16063  13825  12836   1331    466  -1504       C  
ATOM    361  CE2 TYR A  56     -31.349  -4.619 -36.209  1.00 98.10           C  
ANISOU  361  CE2 TYR A  56    13829  12343  11103   1305    456  -1303       C  
ATOM    362  CZ  TYR A  56     -31.543  -3.283 -35.924  1.00111.41           C  
ANISOU  362  CZ  TYR A  56    15711  13861  12757   1421    523  -1378       C  
ATOM    363  OH  TYR A  56     -32.737  -2.678 -36.247  1.00117.68           O  
ANISOU  363  OH  TYR A  56    16484  14657  13574   1629    646  -1324       O  
ATOM    364  N   MET A  57     -24.424  -5.078 -34.184  1.00 88.79           N  
ANISOU  364  N   MET A  57    13012  10941   9784    385   -170  -1600       N  
ATOM    365  CA  MET A  57     -23.356  -5.679 -33.398  1.00 84.91           C  
ANISOU  365  CA  MET A  57    12513  10529   9219    236   -281  -1618       C  
ATOM    366  C   MET A  57     -22.097  -4.830 -33.317  1.00 95.75           C  
ANISOU  366  C   MET A  57    14008  11779  10595     71   -401  -1691       C  
ATOM    367  O   MET A  57     -21.303  -5.032 -32.392  1.00117.01           O  
ANISOU  367  O   MET A  57    16744  14528  13188    -41   -493  -1737       O  
ATOM    368  CB  MET A  57     -22.985  -7.062 -33.956  1.00 88.85           C  
ANISOU  368  CB  MET A  57    12789  11176   9794    177   -320  -1489       C  
ATOM    369  CG  MET A  57     -24.058  -8.115 -33.749  1.00 95.28           C  
ANISOU  369  CG  MET A  57    13484  12133  10584    293   -224  -1421       C  
ATOM    370  SD  MET A  57     -23.492  -9.776 -34.158  1.00 98.25           S  
ANISOU  370  SD  MET A  57    13644  12657  11028    208   -273  -1291       S  
ATOM    371  CE  MET A  57     -24.893 -10.745 -33.613  1.00 89.42           C  
ANISOU  371  CE  MET A  57    12442  11675   9857    339   -149  -1239       C  
ATOM    372  N   LYS A  58     -21.880  -3.912 -34.260  1.00 83.10           N  
ANISOU  372  N   LYS A  58    12452  10020   9101     47   -407  -1694       N  
ATOM    373  CA  LYS A  58     -20.816  -2.911 -34.172  1.00 84.21           C  
ANISOU  373  CA  LYS A  58    12734  10014   9250   -110   -506  -1771       C  
ATOM    374  C   LYS A  58     -19.424  -3.536 -34.213  1.00 96.32           C  
ANISOU  374  C   LYS A  58    14147  11641  10808   -305   -650  -1716       C  
ATOM    375  O   LYS A  58     -18.456  -2.933 -33.743  1.00108.74           O  
ANISOU  375  O   LYS A  58    15822  13151  12345   -464   -756  -1786       O  
ATOM    376  CB  LYS A  58     -20.974  -2.043 -32.919  1.00 64.79           C  
ANISOU  376  CB  LYS A  58    10519   7458   6639   -104   -500  -1933       C  
ATOM    377  N   LEU A  59     -19.320  -4.746 -34.769  1.00 86.50           N  
ANISOU  377  N   LEU A  59    12689  10550   9628   -295   -651  -1589       N  
ATOM    378  CA  LEU A  59     -18.041  -5.416 -34.990  1.00 84.81           C  
ANISOU  378  CA  LEU A  59    12334  10430   9459   -448   -765  -1508       C  
ATOM    379  C   LEU A  59     -17.231  -5.556 -33.705  1.00 86.36           C  
ANISOU  379  C   LEU A  59    12583  10707   9525   -568   -874  -1565       C  
ATOM    380  O   LEU A  59     -16.400  -4.697 -33.395  1.00 86.89           O  
ANISOU  380  O   LEU A  59    12756  10691   9569   -713   -972  -1635       O  
ATOM    381  CB  LEU A  59     -17.217  -4.662 -36.039  1.00 78.81           C  
ANISOU  381  CB  LEU A  59    11564   9550   8828   -558   -815  -1474       C  
ATOM    382  CG  LEU A  59     -17.718  -4.688 -37.483  1.00 70.11           C  
ANISOU  382  CG  LEU A  59    10370   8406   7862   -468   -732  -1384       C  
ATOM    383  CD1 LEU A  59     -16.882  -3.761 -38.347  1.00 72.22           C  
ANISOU  383  CD1 LEU A  59    10663   8541   8236   -582   -780  -1359       C  
ATOM    384  CD2 LEU A  59     -17.677  -6.103 -38.025  1.00 68.19           C  
ANISOU  384  CD2 LEU A  59     9917   8329   7665   -433   -716  -1265       C  
ATOM    385  N   LYS A  60     -17.453  -6.637 -32.958  1.00 90.95           N  
ANISOU  385  N   LYS A  60    13087  11451  10017   -517   -864  -1529       N  
ATOM    386  CA  LYS A  60     -16.757  -6.850 -31.698  1.00 90.14           C  
ANISOU  386  CA  LYS A  60    13026  11452   9771   -613   -966  -1569       C  
ATOM    387  C   LYS A  60     -15.772  -8.010 -31.729  1.00 98.42           C  
ANISOU  387  C   LYS A  60    13878  12669  10848   -690  -1047  -1436       C  
ATOM    388  O   LYS A  60     -15.020  -8.183 -30.763  1.00105.39           O  
ANISOU  388  O   LYS A  60    14770  13654  11619   -786  -1152  -1447       O  
ATOM    389  CB  LYS A  60     -17.769  -7.079 -30.565  1.00 72.53           C  
ANISOU  389  CB  LYS A  60    10894   9283   7382   -488   -889  -1635       C  
ATOM    390  CG  LYS A  60     -18.719  -5.915 -30.335  1.00 60.97           C  
ANISOU  390  CG  LYS A  60     9641   7661   5864   -395   -801  -1773       C  
ATOM    391  CD  LYS A  60     -19.726  -6.236 -29.244  1.00 73.72           C  
ANISOU  391  CD  LYS A  60    11332   9360   7320   -256   -709  -1820       C  
ATOM    392  CE  LYS A  60     -20.687  -5.080 -29.019  1.00 93.28           C  
ANISOU  392  CE  LYS A  60    14019  11680   9744   -141   -605  -1952       C  
ATOM    393  NZ  LYS A  60     -19.978  -3.844 -28.585  1.00101.63           N  
ANISOU  393  NZ  LYS A  60    15292  12588  10735   -269   -695  -2100       N  
ATOM    394  N   THR A  61     -15.750  -8.803 -32.797  1.00 91.81           N  
ANISOU  394  N   THR A  61    12869  11865  10149   -647  -1000  -1311       N  
ATOM    395  CA  THR A  61     -14.878  -9.964 -32.892  1.00 85.82           C  
ANISOU  395  CA  THR A  61    11927  11252   9428   -690  -1052  -1178       C  
ATOM    396  C   THR A  61     -14.146  -9.954 -34.228  1.00 80.62           C  
ANISOU  396  C   THR A  61    11146  10551   8934   -747  -1067  -1090       C  
ATOM    397  O   THR A  61     -14.437  -9.153 -35.121  1.00 91.29           O  
ANISOU  397  O   THR A  61    12545  11769  10370   -740  -1028  -1123       O  
ATOM    398  CB  THR A  61     -15.665 -11.274 -32.732  1.00 88.90           C  
ANISOU  398  CB  THR A  61    12226  11747   9804   -556   -954  -1101       C  
ATOM    399  OG1 THR A  61     -16.772 -11.283 -33.642  1.00 86.91           O  
ANISOU  399  OG1 THR A  61    11969  11415   9639   -441   -832  -1103       O  
ATOM    400  CG2 THR A  61     -16.180 -11.419 -31.308  1.00101.34           C  
ANISOU  400  CG2 THR A  61    13899  13400  11205   -511   -947  -1158       C  
ATOM    401  N   VAL A  62     -13.180 -10.866 -34.354  1.00 75.48           N  
ANISOU  401  N   VAL A  62    10334  10021   8323   -793  -1118   -969       N  
ATOM    402  CA  VAL A  62     -12.417 -10.980 -35.593  1.00 71.07           C  
ANISOU  402  CA  VAL A  62     9647   9445   7911   -836  -1122   -873       C  
ATOM    403  C   VAL A  62     -13.273 -11.597 -36.693  1.00 80.48           C  
ANISOU  403  C   VAL A  62    10781  10599   9198   -705   -992   -828       C  
ATOM    404  O   VAL A  62     -13.210 -11.179 -37.856  1.00 94.98           O  
ANISOU  404  O   VAL A  62    12594  12355  11139   -710   -962   -809       O  
ATOM    405  CB  VAL A  62     -11.130 -11.790 -35.351  1.00 61.19           C  
ANISOU  405  CB  VAL A  62     8238   8343   6668   -906  -1205   -749       C  
ATOM    406  CG1 VAL A  62     -10.398 -12.043 -36.660  1.00 69.60           C  
ANISOU  406  CG1 VAL A  62     9161   9403   7882   -921  -1183   -638       C  
ATOM    407  CG2 VAL A  62     -10.227 -11.065 -34.366  1.00 73.13           C  
ANISOU  407  CG2 VAL A  62     9797   9903   8087  -1061  -1353   -793       C  
ATOM    408  N   ALA A  63     -14.091 -12.593 -36.344  1.00 78.97           N  
ANISOU  408  N   ALA A  63    10567  10470   8968   -594   -917   -809       N  
ATOM    409  CA  ALA A  63     -14.931 -13.247 -37.343  1.00 87.13           C  
ANISOU  409  CA  ALA A  63    11545  11478  10083   -488   -804   -772       C  
ATOM    410  C   ALA A  63     -15.978 -12.298 -37.912  1.00 82.06           C  
ANISOU  410  C   ALA A  63    11001  10717   9460   -436   -744   -856       C  
ATOM    411  O   ALA A  63     -16.415 -12.476 -39.055  1.00 83.88           O  
ANISOU  411  O   ALA A  63    11182  10913   9776   -384   -679   -826       O  
ATOM    412  CB  ALA A  63     -15.605 -14.479 -36.738  1.00 98.47           C  
ANISOU  412  CB  ALA A  63    12944  12999  11472   -400   -740   -736       C  
ATOM    413  N   SER A  64     -16.392 -11.292 -37.139  1.00 72.70           N  
ANISOU  413  N   SER A  64     9958   9472   8192   -442   -763   -960       N  
ATOM    414  CA  SER A  64     -17.367 -10.331 -37.644  1.00 76.54           C  
ANISOU  414  CA  SER A  64    10542   9842   8699   -376   -700  -1030       C  
ATOM    415  C   SER A  64     -16.765  -9.433 -38.716  1.00 72.19           C  
ANISOU  415  C   SER A  64     9996   9185   8246   -441   -729  -1017       C  
ATOM    416  O   SER A  64     -17.474  -9.007 -39.635  1.00 66.90           O  
ANISOU  416  O   SER A  64     9341   8443   7635   -371   -663  -1016       O  
ATOM    417  CB  SER A  64     -17.922  -9.491 -36.495  1.00 77.63           C  
ANISOU  417  CB  SER A  64    10846   9931   8718   -354   -700  -1146       C  
ATOM    418  OG  SER A  64     -16.895  -8.743 -35.866  1.00 92.08           O  
ANISOU  418  OG  SER A  64    12759  11727  10500   -485   -809  -1199       O  
ATOM    419  N   VAL A  65     -15.468  -9.134 -38.619  1.00 69.06           N  
ANISOU  419  N   VAL A  65     9582   8790   7868   -576   -827   -995       N  
ATOM    420  CA  VAL A  65     -14.816  -8.318 -39.639  1.00 71.54           C  
ANISOU  420  CA  VAL A  65     9889   9010   8281   -651   -851   -965       C  
ATOM    421  C   VAL A  65     -14.728  -9.081 -40.954  1.00 86.55           C  
ANISOU  421  C   VAL A  65    11645  10957  10283   -603   -795   -857       C  
ATOM    422  O   VAL A  65     -14.957  -8.518 -42.031  1.00 95.07           O  
ANISOU  422  O   VAL A  65    12733  11956  11434   -578   -753   -837       O  
ATOM    423  CB  VAL A  65     -13.427  -7.866 -39.152  1.00 78.20           C  
ANISOU  423  CB  VAL A  65    10730   9863   9119   -822   -974   -959       C  
ATOM    424  CG1 VAL A  65     -12.776  -6.949 -40.177  1.00 69.64           C  
ANISOU  424  CG1 VAL A  65     9643   8675   8142   -909   -993   -922       C  
ATOM    425  CG2 VAL A  65     -13.537  -7.177 -37.804  1.00 83.07           C  
ANISOU  425  CG2 VAL A  65    11505  10443   9614   -876  -1035  -1082       C  
ATOM    426  N   PHE A  66     -14.397 -10.373 -40.889  1.00 90.44           N  
ANISOU  426  N   PHE A  66    12013  11575  10777   -585   -790   -785       N  
ATOM    427  CA  PHE A  66     -14.337 -11.183 -42.101  1.00 82.76           C  
ANISOU  427  CA  PHE A  66    10920  10641   9886   -535   -729   -697       C  
ATOM    428  C   PHE A  66     -15.722 -11.373 -42.706  1.00 74.50           C  
ANISOU  428  C   PHE A  66     9896   9567   8842   -414   -635   -725       C  
ATOM    429  O   PHE A  66     -15.887 -11.294 -43.929  1.00 83.37           O  
ANISOU  429  O   PHE A  66    10984  10664  10027   -383   -591   -689       O  
ATOM    430  CB  PHE A  66     -13.697 -12.537 -41.797  1.00 77.69           C  
ANISOU  430  CB  PHE A  66    10159  10120   9241   -533   -735   -619       C  
ATOM    431  CG  PHE A  66     -12.266 -12.446 -41.354  1.00 79.86           C  
ANISOU  431  CG  PHE A  66    10372  10451   9521   -646   -829   -561       C  
ATOM    432  CD1 PHE A  66     -11.447 -11.426 -41.811  1.00 83.58           C  
ANISOU  432  CD1 PHE A  66    10845  10868  10043   -749   -884   -547       C  
ATOM    433  CD2 PHE A  66     -11.738 -13.382 -40.479  1.00 78.57           C  
ANISOU  433  CD2 PHE A  66    10140  10400   9314   -650   -863   -511       C  
ATOM    434  CE1 PHE A  66     -10.129 -11.342 -41.404  1.00 89.36           C  
ANISOU  434  CE1 PHE A  66    11501  11669  10783   -865   -977   -486       C  
ATOM    435  CE2 PHE A  66     -10.421 -13.303 -40.069  1.00 82.41           C  
ANISOU  435  CE2 PHE A  66    10549  10960   9802   -752   -957   -445       C  
ATOM    436  CZ  PHE A  66      -9.615 -12.281 -40.532  1.00 87.75           C  
ANISOU  436  CZ  PHE A  66    11217  11593  10530   -865  -1017   -434       C  
ATOM    437  N   LEU A  67     -16.730 -11.620 -41.866  1.00 69.42           N  
ANISOU  437  N   LEU A  67     9305   8944   8127   -347   -603   -783       N  
ATOM    438  CA  LEU A  67     -18.079 -11.833 -42.377  1.00 72.71           C  
ANISOU  438  CA  LEU A  67     9723   9357   8546   -239   -519   -800       C  
ATOM    439  C   LEU A  67     -18.670 -10.553 -42.954  1.00 67.72           C  
ANISOU  439  C   LEU A  67     9174   8622   7932   -202   -498   -838       C  
ATOM    440  O   LEU A  67     -19.507 -10.614 -43.862  1.00 82.64           O  
ANISOU  440  O   LEU A  67    11033  10515   9851   -128   -440   -820       O  
ATOM    441  CB  LEU A  67     -18.978 -12.388 -41.272  1.00 68.76           C  
ANISOU  441  CB  LEU A  67     9248   8913   7965   -180   -486   -839       C  
ATOM    442  CG  LEU A  67     -20.294 -13.021 -41.730  1.00 60.70           C  
ANISOU  442  CG  LEU A  67     8180   7932   6952    -86   -402   -832       C  
ATOM    443  CD1 LEU A  67     -20.024 -14.143 -42.719  1.00 65.05           C  
ANISOU  443  CD1 LEU A  67     8619   8529   7568    -98   -381   -763       C  
ATOM    444  CD2 LEU A  67     -21.089 -13.535 -40.541  1.00 51.41           C  
ANISOU  444  CD2 LEU A  67     7022   6815   5696    -38   -366   -857       C  
ATOM    445  N   LEU A  68     -18.253  -9.392 -42.445  1.00 55.41           N  
ANISOU  445  N   LEU A  68     7725   6971   6356   -255   -544   -889       N  
ATOM    446  CA  LEU A  68     -18.709  -8.129 -43.018  1.00 58.56           C  
ANISOU  446  CA  LEU A  68     8216   7250   6784   -218   -518   -914       C  
ATOM    447  C   LEU A  68     -18.124  -7.919 -44.408  1.00 76.68           C  
ANISOU  447  C   LEU A  68    10447   9518   9170   -251   -520   -835       C  
ATOM    448  O   LEU A  68     -18.854  -7.631 -45.364  1.00 77.27           O  
ANISOU  448  O   LEU A  68    10513   9570   9275   -170   -465   -807       O  
ATOM    449  CB  LEU A  68     -18.336  -6.966 -42.099  1.00 52.98           C  
ANISOU  449  CB  LEU A  68     7662   6431   6038   -280   -567   -996       C  
ATOM    450  CG  LEU A  68     -18.625  -5.572 -42.663  1.00 57.97           C  
ANISOU  450  CG  LEU A  68     8409   6904   6712   -254   -540  -1017       C  
ATOM    451  CD1 LEU A  68     -20.122  -5.356 -42.829  1.00 65.49           C  
ANISOU  451  CD1 LEU A  68     9398   7842   7643    -86   -443  -1036       C  
ATOM    452  CD2 LEU A  68     -18.015  -4.490 -41.785  1.00 57.78           C  
ANISOU  452  CD2 LEU A  68     8544   6753   6656   -354   -600  -1103       C  
ATOM    453  N   ASN A  69     -16.803  -8.059 -44.539  1.00 73.75           N  
ANISOU  453  N   ASN A  69    10022   9162   8838   -367   -581   -788       N  
ATOM    454  CA  ASN A  69     -16.161  -7.906 -45.837  1.00 71.64           C  
ANISOU  454  CA  ASN A  69     9687   8883   8651   -399   -574   -702       C  
ATOM    455  C   ASN A  69     -16.534  -9.021 -46.804  1.00 82.93           C  
ANISOU  455  C   ASN A  69    11001  10413  10096   -325   -516   -644       C  
ATOM    456  O   ASN A  69     -16.422  -8.831 -48.020  1.00104.98           O  
ANISOU  456  O   ASN A  69    13757  13196  12935   -310   -487   -584       O  
ATOM    457  CB  ASN A  69     -14.643  -7.845 -45.667  1.00 69.13           C  
ANISOU  457  CB  ASN A  69     9321   8577   8369   -540   -648   -655       C  
ATOM    458  CG  ASN A  69     -14.180  -6.547 -45.033  1.00 80.58           C  
ANISOU  458  CG  ASN A  69    10892   9906   9819   -643   -712   -707       C  
ATOM    459  OD1 ASN A  69     -13.462  -6.552 -44.034  1.00 85.83           O  
ANISOU  459  OD1 ASN A  69    11569  10594  10449   -744   -790   -738       O  
ATOM    460  ND2 ASN A  69     -14.594  -5.426 -45.612  1.00 86.00           N  
ANISOU  460  ND2 ASN A  69    11674  10461  10542   -621   -680   -717       N  
ATOM    461  N   LEU A  70     -16.971 -10.176 -46.296  1.00 67.45           N  
ANISOU  461  N   LEU A  70     8992   8544   8095   -284   -498   -661       N  
ATOM    462  CA  LEU A  70     -17.433 -11.238 -47.182  1.00 60.36           C  
ANISOU  462  CA  LEU A  70     8004   7723   7206   -223   -443   -624       C  
ATOM    463  C   LEU A  70     -18.745 -10.864 -47.858  1.00 58.18           C  
ANISOU  463  C   LEU A  70     7753   7434   6918   -130   -393   -642       C  
ATOM    464  O   LEU A  70     -18.980 -11.249 -49.009  1.00 79.92           O  
ANISOU  464  O   LEU A  70    10450  10227   9687    -98   -360   -604       O  
ATOM    465  CB  LEU A  70     -17.587 -12.544 -46.401  1.00 70.59           C  
ANISOU  465  CB  LEU A  70     9253   9101   8468   -212   -434   -636       C  
ATOM    466  CG  LEU A  70     -17.729 -13.821 -47.230  1.00 78.02           C  
ANISOU  466  CG  LEU A  70    10108  10109   9426   -180   -384   -599       C  
ATOM    467  CD1 LEU A  70     -16.459 -14.086 -48.023  1.00 83.10           C  
ANISOU  467  CD1 LEU A  70    10690  10764  10120   -223   -388   -528       C  
ATOM    468  CD2 LEU A  70     -18.067 -15.005 -46.339  1.00 87.33           C  
ANISOU  468  CD2 LEU A  70    11263  11344  10575   -166   -367   -612       C  
ATOM    469  N   ALA A  71     -19.604 -10.115 -47.165  1.00 69.53           N  
ANISOU  469  N   ALA A  71     9274   8823   8321    -81   -386   -698       N  
ATOM    470  CA  ALA A  71     -20.853  -9.662 -47.764  1.00 80.63           C  
ANISOU  470  CA  ALA A  71    10693  10226   9718     20   -338   -700       C  
ATOM    471  C   ALA A  71     -20.656  -8.420 -48.623  1.00 81.18           C  
ANISOU  471  C   ALA A  71    10814  10202   9827     31   -336   -663       C  
ATOM    472  O   ALA A  71     -21.351  -8.256 -49.632  1.00 82.59           O  
ANISOU  472  O   ALA A  71    10961  10407  10010    102   -303   -622       O  
ATOM    473  CB  ALA A  71     -21.891  -9.386 -46.674  1.00 76.62           C  
ANISOU  473  CB  ALA A  71    10247   9709   9157     91   -313   -763       C  
ATOM    474  N   LEU A  72     -19.726  -7.540 -48.243  1.00 74.33           N  
ANISOU  474  N   LEU A  72    10025   9231   8987    -44   -375   -670       N  
ATOM    475  CA  LEU A  72     -19.450  -6.360 -49.056  1.00 67.24           C  
ANISOU  475  CA  LEU A  72     9182   8228   8137    -47   -369   -624       C  
ATOM    476  C   LEU A  72     -18.832  -6.744 -50.394  1.00 81.24           C  
ANISOU  476  C   LEU A  72    10860  10059   9950    -74   -363   -533       C  
ATOM    477  O   LEU A  72     -19.141  -6.134 -51.425  1.00 88.95           O  
ANISOU  477  O   LEU A  72    11842  11010  10944    -21   -332   -474       O  
ATOM    478  CB  LEU A  72     -18.532  -5.400 -48.301  1.00 68.60           C  
ANISOU  478  CB  LEU A  72     9460   8272   8334   -149   -418   -657       C  
ATOM    479  CG  LEU A  72     -19.103  -4.716 -47.058  1.00 70.34           C  
ANISOU  479  CG  LEU A  72     9818   8402   8508   -119   -417   -756       C  
ATOM    480  CD1 LEU A  72     -18.075  -3.777 -46.447  1.00 47.61           C  
ANISOU  480  CD1 LEU A  72     7048   5391   5650   -250   -477   -793       C  
ATOM    481  CD2 LEU A  72     -20.382  -3.967 -47.398  1.00 80.64           C  
ANISOU  481  CD2 LEU A  72    11189   9647   9806     29   -345   -758       C  
ATOM    482  N   ALA A  73     -17.955  -7.750 -50.398  1.00 79.32           N  
ANISOU  482  N   ALA A  73    10530   9896   9713   -146   -386   -514       N  
ATOM    483  CA  ALA A  73     -17.345  -8.192 -51.647  1.00 84.50           C  
ANISOU  483  CA  ALA A  73    11101  10612  10395   -160   -366   -433       C  
ATOM    484  C   ALA A  73     -18.378  -8.824 -52.572  1.00 79.60           C  
ANISOU  484  C   ALA A  73    10430  10081   9734    -65   -321   -424       C  
ATOM    485  O   ALA A  73     -18.296  -8.674 -53.797  1.00 83.14           O  
ANISOU  485  O   ALA A  73    10850  10554  10186    -42   -296   -359       O  
ATOM    486  CB  ALA A  73     -16.208  -9.172 -51.360  1.00 85.22           C  
ANISOU  486  CB  ALA A  73    11112  10767  10499   -238   -389   -414       C  
ATOM    487  N   ASP A  74     -19.356  -9.535 -52.005  1.00 68.63           N  
ANISOU  487  N   ASP A  74     9028   8748   8302    -16   -313   -484       N  
ATOM    488  CA  ASP A  74     -20.396 -10.141 -52.829  1.00 63.63           C  
ANISOU  488  CA  ASP A  74     8340   8207   7627     54   -282   -481       C  
ATOM    489  C   ASP A  74     -21.321  -9.092 -53.429  1.00 69.36           C  
ANISOU  489  C   ASP A  74     9100   8912   8343    140   -265   -451       C  
ATOM    490  O   ASP A  74     -21.821  -9.276 -54.544  1.00 90.20           O  
ANISOU  490  O   ASP A  74    11692  11628  10953    183   -250   -412       O  
ATOM    491  CB  ASP A  74     -21.199 -11.150 -52.008  1.00 57.12           C  
ANISOU  491  CB  ASP A  74     7487   7447   6769     69   -277   -544       C  
ATOM    492  CG  ASP A  74     -20.380 -12.363 -51.611  1.00 76.81           C  
ANISOU  492  CG  ASP A  74     9939   9973   9271      3   -282   -556       C  
ATOM    493  OD1 ASP A  74     -19.174 -12.401 -51.933  1.00 85.73           O  
ANISOU  493  OD1 ASP A  74    11057  11085  10433    -48   -290   -516       O  
ATOM    494  OD2 ASP A  74     -20.944 -13.279 -50.978  1.00 81.23           O  
ANISOU  494  OD2 ASP A  74    10476  10580   9809      7   -272   -596       O  
ATOM    495  N   LEU A  75     -21.558  -7.989 -52.714  1.00 65.04           N  
ANISOU  495  N   LEU A  75     8638   8262   7812    169   -266   -466       N  
ATOM    496  CA  LEU A  75     -22.429  -6.943 -53.240  1.00 70.77           C  
ANISOU  496  CA  LEU A  75     9400   8953   8534    270   -239   -425       C  
ATOM    497  C   LEU A  75     -21.791  -6.238 -54.432  1.00 79.29           C  
ANISOU  497  C   LEU A  75    10490   9993   9643    261   -233   -334       C  
ATOM    498  O   LEU A  75     -22.491  -5.843 -55.371  1.00 87.69           O  
ANISOU  498  O   LEU A  75    11535  11098  10686    347   -211   -272       O  
ATOM    499  CB  LEU A  75     -22.771  -5.939 -52.140  1.00 70.30           C  
ANISOU  499  CB  LEU A  75     9453   8772   8487    311   -229   -471       C  
ATOM    500  CG  LEU A  75     -23.708  -6.439 -51.039  1.00 70.03           C  
ANISOU  500  CG  LEU A  75     9412   8787   8409    360   -215   -545       C  
ATOM    501  CD1 LEU A  75     -23.912  -5.368 -49.978  1.00 67.13           C  
ANISOU  501  CD1 LEU A  75     9178   8285   8043    403   -195   -597       C  
ATOM    502  CD2 LEU A  75     -25.041  -6.872 -51.628  1.00 70.48           C  
ANISOU  502  CD2 LEU A  75     9375   8975   8428    461   -186   -514       C  
ATOM    503  N   CYS A  76     -20.466  -6.070 -54.412  1.00 77.40           N  
ANISOU  503  N   CYS A  76    10271   9687   9450    159   -252   -315       N  
ATOM    504  CA  CYS A  76     -19.788  -5.439 -55.541  1.00 82.81           C  
ANISOU  504  CA  CYS A  76    10957  10341  10165    141   -238   -216       C  
ATOM    505  C   CYS A  76     -19.881  -6.303 -56.792  1.00 80.76           C  
ANISOU  505  C   CYS A  76    10601  10226   9856    167   -222   -169       C  
ATOM    506  O   CYS A  76     -20.011  -5.781 -57.906  1.00 90.53           O  
ANISOU  506  O   CYS A  76    11835  11482  11080    215   -198    -83       O  
ATOM    507  CB  CYS A  76     -18.327  -5.159 -55.187  1.00 91.60           C  
ANISOU  507  CB  CYS A  76    12093  11370  11342     13   -263   -200       C  
ATOM    508  SG  CYS A  76     -18.095  -4.009 -53.813  1.00 97.64           S  
ANISOU  508  SG  CYS A  76    12994  11951  12155    -44   -294   -263       S  
ATOM    509  N   PHE A  77     -19.814  -7.626 -56.629  1.00 67.17           N  
ANISOU  509  N   PHE A  77     8813   8606   8102    135   -231   -223       N  
ATOM    510  CA  PHE A  77     -19.968  -8.521 -57.771  1.00 78.83           C  
ANISOU  510  CA  PHE A  77    10219  10213   9520    155   -214   -202       C  
ATOM    511  C   PHE A  77     -21.394  -8.496 -58.304  1.00 76.63           C  
ANISOU  511  C   PHE A  77     9918  10020   9178    248   -213   -202       C  
ATOM    512  O   PHE A  77     -21.611  -8.572 -59.520  1.00 75.22           O  
ANISOU  512  O   PHE A  77     9707   9928   8944    282   -203   -150       O  
ATOM    513  CB  PHE A  77     -19.562  -9.942 -57.376  1.00 85.72           C  
ANISOU  513  CB  PHE A  77    11043  11146  10382     99   -217   -266       C  
ATOM    514  CG  PHE A  77     -20.253 -11.016 -58.169  1.00 88.44           C  
ANISOU  514  CG  PHE A  77    11337  11613  10652    126   -206   -296       C  
ATOM    515  CD1 PHE A  77     -19.829 -11.336 -59.447  1.00 88.29           C  
ANISOU  515  CD1 PHE A  77    11297  11660  10590    129   -180   -253       C  
ATOM    516  CD2 PHE A  77     -21.324 -11.711 -57.629  1.00 90.94           C  
ANISOU  516  CD2 PHE A  77    11633  11981  10939    141   -220   -367       C  
ATOM    517  CE1 PHE A  77     -20.464 -12.324 -60.176  1.00 91.20           C  
ANISOU  517  CE1 PHE A  77    11636  12137  10880    141   -175   -296       C  
ATOM    518  CE2 PHE A  77     -21.963 -12.700 -58.353  1.00 87.08           C  
ANISOU  518  CE2 PHE A  77    11103  11600  10385    142   -218   -401       C  
ATOM    519  CZ  PHE A  77     -21.532 -13.007 -59.628  1.00 86.72           C  
ANISOU  519  CZ  PHE A  77    11048  11611  10289    139   -199   -372       C  
ATOM    520  N   LEU A  78     -22.381  -8.389 -57.412  1.00 77.43           N  
ANISOU  520  N   LEU A  78    10030  10111   9277    291   -224   -253       N  
ATOM    521  CA  LEU A  78     -23.776  -8.374 -57.835  1.00 81.74           C  
ANISOU  521  CA  LEU A  78    10533  10757   9768    380   -225   -243       C  
ATOM    522  C   LEU A  78     -24.142  -7.105 -58.593  1.00 90.88           C  
ANISOU  522  C   LEU A  78    11718  11888  10922    472   -210   -144       C  
ATOM    523  O   LEU A  78     -25.124  -7.111 -59.343  1.00 98.85           O  
ANISOU  523  O   LEU A  78    12672  13014  11872    545   -217   -103       O  
ATOM    524  CB  LEU A  78     -24.691  -8.539 -56.621  1.00 71.74           C  
ANISOU  524  CB  LEU A  78     9264   9488   8506    410   -227   -310       C  
ATOM    525  CG  LEU A  78     -24.617  -9.895 -55.916  1.00 71.37           C  
ANISOU  525  CG  LEU A  78     9177   9490   8451    334   -238   -394       C  
ATOM    526  CD1 LEU A  78     -25.178  -9.793 -54.511  1.00 75.30           C  
ANISOU  526  CD1 LEU A  78     9699   9947   8965    358   -230   -448       C  
ATOM    527  CD2 LEU A  78     -25.353 -10.959 -56.714  1.00 69.83           C  
ANISOU  527  CD2 LEU A  78     8895   9444   8194    323   -251   -407       C  
ATOM    528  N   LEU A  79     -23.382  -6.021 -58.417  1.00 83.82           N  
ANISOU  528  N   LEU A  79    10909  10847  10093    465   -193    -99       N  
ATOM    529  CA  LEU A  79     -23.667  -4.796 -59.157  1.00 88.74           C  
ANISOU  529  CA  LEU A  79    11570  11424  10722    555   -169      8       C  
ATOM    530  C   LEU A  79     -23.377  -4.959 -60.643  1.00 93.25           C  
ANISOU  530  C   LEU A  79    12092  12099  11240    557   -166     96       C  
ATOM    531  O   LEU A  79     -24.080  -4.379 -61.478  1.00 99.64           O  
ANISOU  531  O   LEU A  79    12886  12964  12008    656   -156    186       O  
ATOM    532  CB  LEU A  79     -22.860  -3.632 -58.584  1.00 89.52           C  
ANISOU  532  CB  LEU A  79    11785  11320  10910    525   -149     29       C  
ATOM    533  CG  LEU A  79     -23.187  -3.222 -57.147  1.00 91.21           C  
ANISOU  533  CG  LEU A  79    12079  11414  11163    537   -146    -57       C  
ATOM    534  CD1 LEU A  79     -22.339  -2.035 -56.720  1.00 95.33           C  
ANISOU  534  CD1 LEU A  79    12728  11726  11765    488   -134    -41       C  
ATOM    535  CD2 LEU A  79     -24.669  -2.909 -57.000  1.00 84.18           C  
ANISOU  535  CD2 LEU A  79    11177  10568  10239    686   -122    -49       C  
ATOM    536  N   THR A  80     -22.355  -5.739 -60.990  1.00 95.25           N  
ANISOU  536  N   THR A  80    12320  12386  11484    461   -169     78       N  
ATOM    537  CA  THR A  80     -22.041  -6.034 -62.380  1.00 95.42           C  
ANISOU  537  CA  THR A  80    12300  12518  11437    463   -158    147       C  
ATOM    538  C   THR A  80     -22.858  -7.190 -62.939  1.00 79.93           C  
ANISOU  538  C   THR A  80    10263  10739   9370    476   -185     93       C  
ATOM    539  O   THR A  80     -22.774  -7.464 -64.142  1.00 84.77           O  
ANISOU  539  O   THR A  80    10848  11462   9899    486   -180    139       O  
ATOM    540  CB  THR A  80     -20.549  -6.353 -62.530  1.00103.94           C  
ANISOU  540  CB  THR A  80    13385  13555  12552    365   -136    158       C  
ATOM    541  OG1 THR A  80     -20.231  -7.539 -61.789  1.00101.52           O  
ANISOU  541  OG1 THR A  80    13050  13270  12253    293   -151     48       O  
ATOM    542  CG2 THR A  80     -19.706  -5.199 -62.008  1.00105.27           C  
ANISOU  542  CG2 THR A  80    13622  13550  12827    326   -120    214       C  
ATOM    543  N   LEU A  81     -23.644  -7.866 -62.100  1.00 75.38           N  
ANISOU  543  N   LEU A  81     9656  10196   8791    468   -212     -2       N  
ATOM    544  CA  LEU A  81     -24.414  -9.015 -62.566  1.00 79.12           C  
ANISOU  544  CA  LEU A  81    10059  10830   9173    453   -243    -62       C  
ATOM    545  C   LEU A  81     -25.483  -8.658 -63.597  1.00 83.78           C  
ANISOU  545  C   LEU A  81    10599  11562   9671    536   -268      9       C  
ATOM    546  O   LEU A  81     -25.640  -9.425 -64.564  1.00 85.22           O  
ANISOU  546  O   LEU A  81    10744  11882   9754    507   -291     -8       O  
ATOM    547  CB  LEU A  81     -25.029  -9.738 -61.360  1.00 80.41           C  
ANISOU  547  CB  LEU A  81    10198  10988   9366    421   -261   -164       C  
ATOM    548  CG  LEU A  81     -25.542 -11.160 -61.595  1.00 70.09           C  
ANISOU  548  CG  LEU A  81     8833   9806   7992    359   -288   -249       C  
ATOM    549  CD1 LEU A  81     -24.425 -12.049 -62.118  1.00 68.66           C  
ANISOU  549  CD1 LEU A  81     8680   9617   7792    283   -266   -286       C  
ATOM    550  CD2 LEU A  81     -26.119 -11.721 -60.310  1.00 61.31           C  
ANISOU  550  CD2 LEU A  81     7699   8673   6924    332   -295   -327       C  
ATOM    551  N   PRO A  82     -26.241  -7.559 -63.472  1.00 78.02           N  
ANISOU  551  N   PRO A  82     9868  10815   8962    640   -267     89       N  
ATOM    552  CA  PRO A  82     -27.196  -7.229 -64.545  1.00 82.31           C  
ANISOU  552  CA  PRO A  82    10350  11516   9410    727   -294    179       C  
ATOM    553  C   PRO A  82     -26.537  -6.981 -65.890  1.00 91.40           C  
ANISOU  553  C   PRO A  82    11521  12716  10490    733   -283    266       C  
ATOM    554  O   PRO A  82     -27.186  -7.160 -66.928  1.00 94.59           O  
ANISOU  554  O   PRO A  82    11868  13296  10778    766   -320    310       O  
ATOM    555  CB  PRO A  82     -27.895  -5.967 -64.019  1.00 65.88           C  
ANISOU  555  CB  PRO A  82     8283   9358   7389    854   -271    262       C  
ATOM    556  CG  PRO A  82     -27.774  -6.057 -62.550  1.00 60.77           C  
ANISOU  556  CG  PRO A  82     7679   8575   6838    821   -251    168       C  
ATOM    557  CD  PRO A  82     -26.429  -6.680 -62.303  1.00 66.83           C  
ANISOU  557  CD  PRO A  82     8500   9252   7642    693   -242     93       C  
ATOM    558  N   LEU A  83     -25.269  -6.566 -65.904  1.00 85.26           N  
ANISOU  558  N   LEU A  83    10818  11801   9774    698   -234    297       N  
ATOM    559  CA  LEU A  83     -24.568  -6.378 -67.171  1.00 68.06           C  
ANISOU  559  CA  LEU A  83     8657   9676   7528    702   -211    386       C  
ATOM    560  C   LEU A  83     -24.361  -7.706 -67.889  1.00 75.09           C  
ANISOU  560  C   LEU A  83     9518  10708   8307    628   -229    302       C  
ATOM    561  O   LEU A  83     -24.565  -7.799 -69.105  1.00 75.65           O  
ANISOU  561  O   LEU A  83     9569  10924   8250    658   -241    354       O  
ATOM    562  CB  LEU A  83     -23.229  -5.680 -66.933  1.00 60.30           C  
ANISOU  562  CB  LEU A  83     7746   8514   6649    667   -151    441       C  
ATOM    563  CG  LEU A  83     -23.204  -4.153 -67.042  1.00 62.27           C  
ANISOU  563  CG  LEU A  83     8049   8647   6964    749   -117    584       C  
ATOM    564  CD1 LEU A  83     -24.164  -3.506 -66.055  1.00 51.69           C  
ANISOU  564  CD1 LEU A  83     6726   7223   5692    821   -129    570       C  
ATOM    565  CD2 LEU A  83     -21.789  -3.629 -66.839  1.00 67.68           C  
ANISOU  565  CD2 LEU A  83     8798   9168   7751    674    -66    627       C  
ATOM    566  N   TRP A  84     -23.959  -8.746 -67.155  1.00 79.78           N  
ANISOU  566  N   TRP A  84    10116  11258   8939    536   -228    172       N  
ATOM    567  CA  TRP A  84     -23.771 -10.056 -67.766  1.00 76.36           C  
ANISOU  567  CA  TRP A  84     9675  10931   8408    469   -235     79       C  
ATOM    568  C   TRP A  84     -25.093 -10.728 -68.113  1.00 71.83           C  
ANISOU  568  C   TRP A  84     9042  10523   7726    462   -306     18       C  
ATOM    569  O   TRP A  84     -25.123 -11.587 -69.001  1.00 59.18           O  
ANISOU  569  O   TRP A  84     7443   9038   6003    420   -321    -37       O  
ATOM    570  CB  TRP A  84     -22.959 -10.962 -66.838  1.00 80.06           C  
ANISOU  570  CB  TRP A  84    10168  11293   8959    383   -207    -28       C  
ATOM    571  CG  TRP A  84     -21.622 -10.401 -66.468  1.00 74.29           C  
ANISOU  571  CG  TRP A  84     9475  10419   8331    370   -149     30       C  
ATOM    572  CD1 TRP A  84     -21.258  -9.883 -65.260  1.00 60.72           C  
ANISOU  572  CD1 TRP A  84     7772   8556   6742    351   -145     30       C  
ATOM    573  CD2 TRP A  84     -20.472 -10.292 -67.314  1.00 76.54           C  
ANISOU  573  CD2 TRP A  84     9782  10705   8593    368    -90    100       C  
ATOM    574  NE1 TRP A  84     -19.951  -9.463 -65.299  1.00 66.15           N  
ANISOU  574  NE1 TRP A  84     8484   9156   7493    324    -97     96       N  
ATOM    575  CE2 TRP A  84     -19.445  -9.702 -66.550  1.00 72.27           C  
ANISOU  575  CE2 TRP A  84     9257  10020   8183    338    -57    146       C  
ATOM    576  CE3 TRP A  84     -20.209 -10.638 -68.643  1.00 79.25           C  
ANISOU  576  CE3 TRP A  84    10134  11166   8812    388    -60    128       C  
ATOM    577  CZ2 TRP A  84     -18.177  -9.451 -67.070  1.00 77.46           C  
ANISOU  577  CZ2 TRP A  84     9920  10651   8860    323      5    231       C  
ATOM    578  CZ3 TRP A  84     -18.950 -10.387 -69.158  1.00 87.84           C  
ANISOU  578  CZ3 TRP A  84    11237  12224   9915    388     14    211       C  
ATOM    579  CH2 TRP A  84     -17.950  -9.800 -68.373  1.00 88.38           C  
ANISOU  579  CH2 TRP A  84    11303  12151  10125    354     46    267       C  
ATOM    580  N   ALA A  85     -26.181 -10.360 -67.433  1.00 77.58           N  
ANISOU  580  N   ALA A  85     9717  11266   8492    500   -348     25       N  
ATOM    581  CA  ALA A  85     -27.477 -10.965 -67.720  1.00 70.81           C  
ANISOU  581  CA  ALA A  85     8781  10581   7541    484   -421    -20       C  
ATOM    582  C   ALA A  85     -27.977 -10.565 -69.102  1.00 76.24           C  
ANISOU  582  C   ALA A  85     9435  11447   8086    542   -460     73       C  
ATOM    583  O   ALA A  85     -28.300 -11.424 -69.930  1.00 67.38           O  
ANISOU  583  O   ALA A  85     8295  10476   6832    480   -508     11       O  
ATOM    584  CB  ALA A  85     -28.488 -10.573 -66.643  1.00 74.29           C  
ANISOU  584  CB  ALA A  85     9161  11004   8063    528   -442    -11       C  
ATOM    585  N   VAL A  86     -28.050  -9.258 -69.370  1.00 90.55           N  
ANISOU  585  N   VAL A  86    11245  13242   9916    659   -441    223       N  
ATOM    586  CA  VAL A  86     -28.474  -8.793 -70.685  1.00 91.34           C  
ANISOU  586  CA  VAL A  86    11313  13514   9877    729   -475    336       C  
ATOM    587  C   VAL A  86     -27.428  -9.094 -71.748  1.00 77.80           C  
ANISOU  587  C   VAL A  86     9669  11825   8068    694   -439    339       C  
ATOM    588  O   VAL A  86     -27.761  -9.178 -72.936  1.00 83.89           O  
ANISOU  588  O   VAL A  86    10420  12777   8677    712   -478    382       O  
ATOM    589  CB  VAL A  86     -28.795  -7.287 -70.648  1.00 95.80           C  
ANISOU  589  CB  VAL A  86    11868  14032  10500    876   -449    510       C  
ATOM    590  CG1 VAL A  86     -29.945  -7.014 -69.691  1.00 98.59           C  
ANISOU  590  CG1 VAL A  86    12146  14388  10925    933   -477    512       C  
ATOM    591  CG2 VAL A  86     -27.564  -6.492 -70.246  1.00 86.97           C  
ANISOU  591  CG2 VAL A  86    10851  12685   9508    893   -359    562       C  
ATOM    592  N   TYR A  87     -26.164  -9.257 -71.352  1.00 73.99           N  
ANISOU  592  N   TYR A  87     9264  11175   7673    647   -363    299       N  
ATOM    593  CA  TYR A  87     -25.129  -9.640 -72.306  1.00 57.81           C  
ANISOU  593  CA  TYR A  87     7276   9153   5538    618   -314    298       C  
ATOM    594  C   TYR A  87     -25.368 -11.049 -72.832  1.00 70.77           C  
ANISOU  594  C   TYR A  87     8923  10922   7043    529   -353    149       C  
ATOM    595  O   TYR A  87     -25.316 -11.289 -74.044  1.00 75.38           O  
ANISOU  595  O   TYR A  87     9530  11650   7463    535   -360    161       O  
ATOM    596  CB  TYR A  87     -23.752  -9.528 -71.650  1.00 71.25           C  
ANISOU  596  CB  TYR A  87     9036  10656   7379    586   -226    295       C  
ATOM    597  CG  TYR A  87     -22.645 -10.199 -72.425  1.00 73.32           C  
ANISOU  597  CG  TYR A  87     9351  10940   7568    549   -163    267       C  
ATOM    598  CD1 TYR A  87     -22.305  -9.765 -73.696  1.00 82.95           C  
ANISOU  598  CD1 TYR A  87    10590  12260   8667    604   -129    376       C  
ATOM    599  CD2 TYR A  87     -21.932 -11.259 -71.880  1.00 77.56           C  
ANISOU  599  CD2 TYR A  87     9917  11399   8155    472   -126    141       C  
ATOM    600  CE1 TYR A  87     -21.295 -10.371 -74.408  1.00 80.89           C  
ANISOU  600  CE1 TYR A  87    10377  12025   8331    584    -57    354       C  
ATOM    601  CE2 TYR A  87     -20.915 -11.871 -72.585  1.00 77.71           C  
ANISOU  601  CE2 TYR A  87     9983  11436   8107    457    -54    122       C  
ATOM    602  CZ  TYR A  87     -20.602 -11.422 -73.850  1.00 79.92           C  
ANISOU  602  CZ  TYR A  87    10283  11820   8264    515    -16    226       C  
ATOM    603  OH  TYR A  87     -19.592 -12.023 -74.564  1.00 81.38           O  
ANISOU  603  OH  TYR A  87    10515  12031   8376    514     70    210       O  
ATOM    604  N   THR A  88     -25.634 -11.997 -71.931  1.00 81.56           N  
ANISOU  604  N   THR A  88    10280  12236   8472    443   -376      6       N  
ATOM    605  CA  THR A  88     -25.955 -13.355 -72.357  1.00 71.75           C  
ANISOU  605  CA  THR A  88     9055  11093   7112    346   -414   -144       C  
ATOM    606  C   THR A  88     -27.326 -13.421 -73.020  1.00 74.37           C  
ANISOU  606  C   THR A  88     9315  11639   7305    338   -523   -141       C  
ATOM    607  O   THR A  88     -27.562 -14.286 -73.871  1.00 75.39           O  
ANISOU  607  O   THR A  88     9470  11896   7278    269   -563   -233       O  
ATOM    608  CB  THR A  88     -25.891 -14.306 -71.160  1.00 67.03           C  
ANISOU  608  CB  THR A  88     8467  10369   6634    258   -404   -279       C  
ATOM    609  OG1 THR A  88     -24.667 -14.094 -70.445  1.00 68.62           O  
ANISOU  609  OG1 THR A  88     8714  10386   6972    275   -316   -257       O  
ATOM    610  CG2 THR A  88     -25.951 -15.757 -71.618  1.00 66.94           C  
ANISOU  610  CG2 THR A  88     8506  10409   6517    153   -418   -437       C  
ATOM    611  N   ALA A  89     -28.233 -12.511 -72.656  1.00 72.47           N  
ANISOU  611  N   ALA A  89     8982  11444   7111    410   -570    -36       N  
ATOM    612  CA  ALA A  89     -29.571 -12.523 -73.239  1.00 70.08           C  
ANISOU  612  CA  ALA A  89     8581  11364   6681    409   -679    -12       C  
ATOM    613  C   ALA A  89     -29.540 -12.138 -74.712  1.00 90.63           C  
ANISOU  613  C   ALA A  89    11198  14141   9098    462   -703     78       C  
ATOM    614  O   ALA A  89     -30.303 -12.684 -75.518  1.00101.53           O  
ANISOU  614  O   ALA A  89    12539  15727  10310    405   -795     33       O  
ATOM    615  CB  ALA A  89     -30.493 -11.587 -72.459  1.00 76.91           C  
ANISOU  615  CB  ALA A  89     9342  12230   7651    500   -705     97       C  
ATOM    616  N   MET A  90     -28.666 -11.201 -75.086  1.00 89.62           N  
ANISOU  616  N   MET A  90    11123  13939   8990    563   -623    207       N  
ATOM    617  CA  MET A  90     -28.534 -10.767 -76.471  1.00 82.22           C  
ANISOU  617  CA  MET A  90    10205  13158   7876    626   -630    313       C  
ATOM    618  C   MET A  90     -27.564 -11.630 -77.268  1.00 82.27           C  
ANISOU  618  C   MET A  90    10322  13175   7763    560   -579    212       C  
ATOM    619  O   MET A  90     -26.938 -11.136 -78.216  1.00 89.03           O  
ANISOU  619  O   MET A  90    11225  14080   8521    627   -528    315       O  
ATOM    620  CB  MET A  90     -28.108  -9.299 -76.526  1.00 74.45           C  
ANISOU  620  CB  MET A  90     9224  12089   6973    768   -561    520       C  
ATOM    621  CG  MET A  90     -29.118  -8.340 -75.919  1.00 82.22           C  
ANISOU  621  CG  MET A  90    10114  13076   8052    865   -601    639       C  
ATOM    622  SD  MET A  90     -28.717  -6.613 -76.247  1.00 93.58           S  
ANISOU  622  SD  MET A  90    11577  14428   9552   1037   -523    892       S  
ATOM    623  CE  MET A  90     -27.057  -6.520 -75.583  1.00 90.52           C  
ANISOU  623  CE  MET A  90    11309  13752   9335    985   -395    852       C  
ATOM    624  N   GLU A  91     -27.424 -12.907 -76.904  1.00 76.78           N  
ANISOU  624  N   GLU A  91     9672  12429   7071    436   -582     19       N  
ATOM    625  CA  GLU A  91     -26.569 -13.855 -77.620  1.00 70.98           C  
ANISOU  625  CA  GLU A  91     9054  11696   6220    379   -526    -97       C  
ATOM    626  C   GLU A  91     -25.118 -13.372 -77.655  1.00 72.07           C  
ANISOU  626  C   GLU A  91     9261  11686   6437    451   -387    -13       C  
ATOM    627  O   GLU A  91     -24.480 -13.318 -78.708  1.00 81.85           O  
ANISOU  627  O   GLU A  91    10563  12999   7539    492   -332     29       O  
ATOM    628  CB  GLU A  91     -27.103 -14.115 -79.031  1.00 69.02           C  
ANISOU  628  CB  GLU A  91     8822  11695   5707    365   -599   -110       C  
ATOM    629  CG  GLU A  91     -28.571 -14.508 -79.065  1.00 85.26           C  
ANISOU  629  CG  GLU A  91    10788  13929   7680    284   -751   -173       C  
ATOM    630  CD  GLU A  91     -29.053 -14.860 -80.457  1.00105.18           C  
ANISOU  630  CD  GLU A  91    13334  16704   9924    249   -835   -205       C  
ATOM    631  OE1 GLU A  91     -28.240 -14.797 -81.403  1.00117.56           O  
ANISOU  631  OE1 GLU A  91    15001  18308  11359    298   -765   -181       O  
ATOM    632  OE2 GLU A  91     -30.245 -15.200 -80.604  1.00114.07           O  
ANISOU  632  OE2 GLU A  91    14378  18005  10960    168   -972   -253       O  
ATOM    633  N   TYR A  92     -24.602 -13.019 -76.475  1.00 63.36           N  
ANISOU  633  N   TYR A  92     8141  10381   5552    462   -332     14       N  
ATOM    634  CA  TYR A  92     -23.229 -12.546 -76.290  1.00 67.46           C  
ANISOU  634  CA  TYR A  92     8703  10748   6181    508   -211     96       C  
ATOM    635  C   TYR A  92     -22.949 -11.315 -77.159  1.00 66.60           C  
ANISOU  635  C   TYR A  92     8587  10704   6016    613   -177    296       C  
ATOM    636  O   TYR A  92     -22.196 -11.356 -78.131  1.00 77.49           O  
ANISOU  636  O   TYR A  92    10019  12143   7281    644   -107    341       O  
ATOM    637  CB  TYR A  92     -22.215 -13.661 -76.578  1.00 71.89           C  
ANISOU  637  CB  TYR A  92     9354  11266   6696    462   -125    -22       C  
ATOM    638  CG  TYR A  92     -22.280 -14.833 -75.623  1.00 83.94           C  
ANISOU  638  CG  TYR A  92    10899  12684   8309    369   -134   -198       C  
ATOM    639  CD1 TYR A  92     -22.125 -14.650 -74.255  1.00 81.99           C  
ANISOU  639  CD1 TYR A  92    10610  12273   8268    351   -128   -196       C  
ATOM    640  CD2 TYR A  92     -22.476 -16.125 -76.093  1.00 91.35           C  
ANISOU  640  CD2 TYR A  92    11909  13680   9120    298   -144   -365       C  
ATOM    641  CE1 TYR A  92     -22.179 -15.720 -73.380  1.00 74.96           C  
ANISOU  641  CE1 TYR A  92     9738  11290   7455    272   -131   -340       C  
ATOM    642  CE2 TYR A  92     -22.529 -17.200 -75.226  1.00 90.76           C  
ANISOU  642  CE2 TYR A  92    11860  13493   9132    215   -143   -514       C  
ATOM    643  CZ  TYR A  92     -22.381 -16.992 -73.871  1.00 83.79           C  
ANISOU  643  CZ  TYR A  92    10923  12458   8455    205   -136   -493       C  
ATOM    644  OH  TYR A  92     -22.434 -18.061 -73.006  1.00 90.49           O  
ANISOU  644  OH  TYR A  92    11797  13200   9387    128   -131   -626       O  
ATOM    645  N   ARG A  93     -23.577 -10.207 -76.769  1.00 60.39           N  
ANISOU  645  N   ARG A  93     7735   9896   5312    674   -218    423       N  
ATOM    646  CA  ARG A  93     -23.361  -8.913 -77.406  1.00 63.24           C  
ANISOU  646  CA  ARG A  93     8090  10279   5659    778   -181    632       C  
ATOM    647  C   ARG A  93     -23.146  -7.863 -76.327  1.00 73.34           C  
ANISOU  647  C   ARG A  93     9351  11355   7162    811   -150    726       C  
ATOM    648  O   ARG A  93     -23.965  -7.733 -75.413  1.00 71.78           O  
ANISOU  648  O   ARG A  93     9109  11107   7057    808   -209    687       O  
ATOM    649  CB  ARG A  93     -24.540  -8.524 -78.305  1.00 65.95           C  
ANISOU  649  CB  ARG A  93     8384  10842   5834    844   -271    715       C  
ATOM    650  CG  ARG A  93     -24.650  -9.350 -79.576  1.00 62.00           C  
ANISOU  650  CG  ARG A  93     7917  10558   5081    818   -300    649       C  
ATOM    651  CD  ARG A  93     -25.776  -8.851 -80.466  1.00 83.04           C  
ANISOU  651  CD  ARG A  93    10521  13457   7575    886   -397    757       C  
ATOM    652  NE  ARG A  93     -25.876  -9.619 -81.704  1.00101.09           N  
ANISOU  652  NE  ARG A  93    12850  15960   9599    853   -432    687       N  
ATOM    653  CZ  ARG A  93     -26.642 -10.693 -81.858  1.00106.92           C  
ANISOU  653  CZ  ARG A  93    13581  16832  10211    752   -534    512       C  
ATOM    654  NH1 ARG A  93     -27.382 -11.132 -80.848  1.00106.85           N  
ANISOU  654  NH1 ARG A  93    13511  16766  10322    678   -605    404       N  
ATOM    655  NH2 ARG A  93     -26.670 -11.330 -83.020  1.00105.56           N  
ANISOU  655  NH2 ARG A  93    13468  16849   9789    719   -562    445       N  
ATOM    656  N   TRP A  94     -22.050  -7.114 -76.439  1.00 81.43           N  
ANISOU  656  N   TRP A  94    10410  12264   8266    837    -56    850       N  
ATOM    657  CA  TRP A  94     -21.647  -6.174 -75.399  1.00 86.95           C  
ANISOU  657  CA  TRP A  94    11113  12746   9179    841    -21    920       C  
ATOM    658  C   TRP A  94     -21.860  -4.740 -75.862  1.00 95.04           C  
ANISOU  658  C   TRP A  94    12140  13751  10219    943     -1   1130       C  
ATOM    659  O   TRP A  94     -21.099  -4.251 -76.713  1.00100.83           O  
ANISOU  659  O   TRP A  94    12899  14501  10909    973     71   1265       O  
ATOM    660  CB  TRP A  94     -20.183  -6.399 -75.020  1.00 83.30           C  
ANISOU  660  CB  TRP A  94    10683  12143   8824    770     68    901       C  
ATOM    661  CG  TRP A  94     -19.759  -5.647 -73.801  1.00 84.82           C  
ANISOU  661  CG  TRP A  94    10884  12115   9231    738     85    928       C  
ATOM    662  CD1 TRP A  94     -18.984  -4.525 -73.755  1.00 76.37           C  
ANISOU  662  CD1 TRP A  94     9835  10910   8271    744    146   1077       C  
ATOM    663  CD2 TRP A  94     -20.093  -5.960 -72.444  1.00 90.09           C  
ANISOU  663  CD2 TRP A  94    11542  12669  10019    685     38    800       C  
ATOM    664  NE1 TRP A  94     -18.812  -4.122 -72.453  1.00 99.67           N  
ANISOU  664  NE1 TRP A  94    12800  13670  11400    692    133   1036       N  
ATOM    665  CE2 TRP A  94     -19.484  -4.987 -71.628  1.00102.12           C  
ANISOU  665  CE2 TRP A  94    13092  13996  11714    663     69    869       C  
ATOM    666  CE3 TRP A  94     -20.848  -6.970 -71.840  1.00 75.85           C  
ANISOU  666  CE3 TRP A  94     9715  10912   8192    650    -26    635       C  
ATOM    667  CZ2 TRP A  94     -19.606  -4.993 -70.241  1.00100.80           C  
ANISOU  667  CZ2 TRP A  94    12932  13688  11679    614     37    773       C  
ATOM    668  CZ3 TRP A  94     -20.968  -6.975 -70.463  1.00 92.33           C  
ANISOU  668  CZ3 TRP A  94    11801  12861  10419    607    -50    555       C  
ATOM    669  CH2 TRP A  94     -20.350  -5.993 -69.678  1.00106.38           C  
ANISOU  669  CH2 TRP A  94    13612  14456  12353    594    -19    621       C  
ATOM    670  N   PRO A  95     -22.864  -4.030 -75.346  1.00 85.94           N  
ANISOU  670  N   PRO A  95    10964  12563   9128   1008    -51   1174       N  
ATOM    671  CA  PRO A  95     -23.086  -2.627 -75.736  1.00 75.91           C  
ANISOU  671  CA  PRO A  95     9707  11249   7886   1121    -22   1383       C  
ATOM    672  C   PRO A  95     -22.601  -1.589 -74.728  1.00 79.80           C  
ANISOU  672  C   PRO A  95    10252  11471   8596   1116     31   1440       C  
ATOM    673  O   PRO A  95     -22.863  -0.400 -74.941  1.00 81.10           O  
ANISOU  673  O   PRO A  95    10443  11568   8804   1213     59   1607       O  
ATOM    674  CB  PRO A  95     -24.613  -2.577 -75.845  1.00 72.45           C  
ANISOU  674  CB  PRO A  95     9203  10963   7362   1210   -112   1393       C  
ATOM    675  CG  PRO A  95     -25.063  -3.482 -74.729  1.00 69.27           C  
ANISOU  675  CG  PRO A  95     8769  10529   7022   1130   -168   1192       C  
ATOM    676  CD  PRO A  95     -24.009  -4.569 -74.590  1.00 79.01           C  
ANISOU  676  CD  PRO A  95    10035  11728   8256    999   -139   1046       C  
ATOM    677  N   PHE A  96     -21.915  -1.993 -73.661  1.00 86.29           N  
ANISOU  677  N   PHE A  96    11097  12140   9551   1009     44   1311       N  
ATOM    678  CA  PHE A  96     -21.586  -1.089 -72.566  1.00 86.40           C  
ANISOU  678  CA  PHE A  96    11166  11903   9759    988     74   1331       C  
ATOM    679  C   PHE A  96     -20.210  -0.447 -72.698  1.00 91.87           C  
ANISOU  679  C   PHE A  96    11909  12448  10550    923    155   1433       C  
ATOM    680  O   PHE A  96     -19.790   0.269 -71.783  1.00 92.94           O  
ANISOU  680  O   PHE A  96    12100  12367  10847    876    175   1437       O  
ATOM    681  CB  PHE A  96     -21.681  -1.833 -71.231  1.00 87.21           C  
ANISOU  681  CB  PHE A  96    11261  11929   9946    906     32   1138       C  
ATOM    682  CG  PHE A  96     -23.015  -2.478 -70.994  1.00 87.07           C  
ANISOU  682  CG  PHE A  96    11185  12047   9850    953    -43   1039       C  
ATOM    683  CD1 PHE A  96     -24.120  -1.711 -70.661  1.00 90.00           C  
ANISOU  683  CD1 PHE A  96    11551  12395  10249   1063    -64   1093       C  
ATOM    684  CD2 PHE A  96     -23.165  -3.850 -71.103  1.00 83.22           C  
ANISOU  684  CD2 PHE A  96    10647  11707   9266    888    -87    897       C  
ATOM    685  CE1 PHE A  96     -25.350  -2.301 -70.443  1.00 80.44           C  
ANISOU  685  CE1 PHE A  96    10266  11326   8971   1102   -132   1016       C  
ATOM    686  CE2 PHE A  96     -24.393  -4.446 -70.886  1.00 81.04           C  
ANISOU  686  CE2 PHE A  96    10310  11558   8925    912   -159    812       C  
ATOM    687  CZ  PHE A  96     -25.486  -3.670 -70.556  1.00 76.01           C  
ANISOU  687  CZ  PHE A  96     9649  10916   8317   1017   -183    876       C  
ATOM    688  N   GLY A  97     -19.502  -0.677 -73.799  1.00 94.25           N  
ANISOU  688  N   GLY A  97    12194  12863  10755    914    202   1516       N  
ATOM    689  CA  GLY A  97     -18.222  -0.044 -74.028  1.00 96.02           C  
ANISOU  689  CA  GLY A  97    12447  12970  11066    854    285   1640       C  
ATOM    690  C   GLY A  97     -17.057  -0.817 -73.436  1.00 98.29           C  
ANISOU  690  C   GLY A  97    12712  13208  11427    719    305   1532       C  
ATOM    691  O   GLY A  97     -17.213  -1.791 -72.696  1.00 97.88           O  
ANISOU  691  O   GLY A  97    12635  13177  11377    671    257   1357       O  
ATOM    692  N   ASN A  98     -15.852  -0.352 -73.775  1.00100.06           N  
ANISOU  692  N   ASN A  98    12936  13368  11714    660    382   1655       N  
ATOM    693  CA  ASN A  98     -14.630  -1.021 -73.348  1.00 92.73           C  
ANISOU  693  CA  ASN A  98    11967  12416  10853    542    413   1592       C  
ATOM    694  C   ASN A  98     -14.252  -0.703 -71.907  1.00 93.24           C  
ANISOU  694  C   ASN A  98    12050  12275  11103    432    376   1515       C  
ATOM    695  O   ASN A  98     -13.508  -1.474 -71.292  1.00 78.14           O  
ANISOU  695  O   ASN A  98    10092  10360   9236    344    370   1419       O  
ATOM    696  CB  ASN A  98     -13.477  -0.643 -74.281  1.00 89.07           C  
ANISOU  696  CB  ASN A  98    11476  11982  10383    518    513   1769       C  
ATOM    697  CG  ASN A  98     -12.273  -1.549 -74.119  1.00 93.66           C  
ANISOU  697  CG  ASN A  98    11990  12609  10988    432    556   1717       C  
ATOM    698  OD1 ASN A  98     -12.182  -2.600 -74.754  1.00 92.57           O  
ANISOU  698  OD1 ASN A  98    11821  12639  10711    475    585   1659       O  
ATOM    699  ND2 ASN A  98     -11.339  -1.144 -73.267  1.00104.72           N  
ANISOU  699  ND2 ASN A  98    13369  13858  12561    310    562   1739       N  
ATOM    700  N   TYR A  99     -14.740   0.410 -71.357  1.00 98.39           N  
ANISOU  700  N   TYR A  99    12771  12755  11855    442    352   1556       N  
ATOM    701  CA  TYR A  99     -14.436   0.741 -69.969  1.00 95.96           C  
ANISOU  701  CA  TYR A  99    12501  12253  11707    336    312   1468       C  
ATOM    702  C   TYR A  99     -15.272  -0.085 -68.998  1.00 89.15           C  
ANISOU  702  C   TYR A  99    11636  11416  10820    353    236   1270       C  
ATOM    703  O   TYR A  99     -14.771  -0.509 -67.951  1.00 87.24           O  
ANISOU  703  O   TYR A  99    11382  11108  10656    253    202   1158       O  
ATOM    704  CB  TYR A  99     -14.656   2.234 -69.721  1.00115.95           C  
ANISOU  704  CB  TYR A  99    15132  14574  14351    343    325   1571       C  
ATOM    705  CG  TYR A  99     -13.408   3.074 -69.874  1.00139.87           C  
ANISOU  705  CG  TYR A  99    18173  17472  17500    224    381   1713       C  
ATOM    706  CD1 TYR A  99     -12.665   3.456 -68.764  1.00144.88           C  
ANISOU  706  CD1 TYR A  99    18838  17925  18284     70    352   1658       C  
ATOM    707  CD2 TYR A  99     -12.972   3.486 -71.127  1.00150.29           C  
ANISOU  707  CD2 TYR A  99    19470  18857  18776    256    460   1906       C  
ATOM    708  CE1 TYR A  99     -11.524   4.224 -68.897  1.00147.12           C  
ANISOU  708  CE1 TYR A  99    19122  18094  18682    -61    395   1790       C  
ATOM    709  CE2 TYR A  99     -11.831   4.254 -71.270  1.00152.12           C  
ANISOU  709  CE2 TYR A  99    19701  18972  19124    136    515   2047       C  
ATOM    710  CZ  TYR A  99     -11.112   4.620 -70.151  1.00149.93           C  
ANISOU  710  CZ  TYR A  99    19448  18514  19006    -28    480   1988       C  
ATOM    711  OH  TYR A  99      -9.976   5.385 -70.287  1.00152.26           O  
ANISOU  711  OH  TYR A  99    19733  18697  19420   -168    526   2131       O  
ATOM    712  N   LEU A 100     -16.541  -0.327 -69.328  1.00 94.00           N  
ANISOU  712  N   LEU A 100    12253  12135  11327    475    206   1234       N  
ATOM    713  CA  LEU A 100     -17.418  -1.068 -68.430  1.00 84.33           C  
ANISOU  713  CA  LEU A 100    11020  10939  10083    492    139   1063       C  
ATOM    714  C   LEU A 100     -17.138  -2.565 -68.424  1.00 87.58           C  
ANISOU  714  C   LEU A 100    11361  11496  10420    446    122    938       C  
ATOM    715  O   LEU A 100     -17.578  -3.256 -67.499  1.00100.04           O  
ANISOU  715  O   LEU A 100    12929  13071  12009    424     73    794       O  
ATOM    716  CB  LEU A 100     -18.884  -0.818 -68.794  1.00 85.32           C  
ANISOU  716  CB  LEU A 100    11153  11141  10122    632    112   1080       C  
ATOM    717  CG  LEU A 100     -19.484   0.469 -68.225  1.00 88.59           C  
ANISOU  717  CG  LEU A 100    11650  11377  10631    695    117   1135       C  
ATOM    718  CD1 LEU A 100     -20.933   0.630 -68.654  1.00 82.98           C  
ANISOU  718  CD1 LEU A 100    10921  10778   9828    851     94   1171       C  
ATOM    719  CD2 LEU A 100     -19.369   0.480 -66.707  1.00 90.79           C  
ANISOU  719  CD2 LEU A 100    11977  11495  11025    618     87    998       C  
ATOM    720  N  ACYS A 101     -16.432  -3.084 -69.429  0.54 86.55           N  
ANISOU  720  N  ACYS A 101    11187  11486  10210    438    170    994       N  
ATOM    721  N  BCYS A 101     -16.413  -3.079 -69.420  0.46 86.48           N  
ANISOU  721  N  BCYS A 101    11178  11476  10204    437    170    994       N  
ATOM    722  CA ACYS A 101     -16.091  -4.501 -69.416  0.54 84.70           C  
ANISOU  722  CA ACYS A 101    10903  11365   9914    402    169    875       C  
ATOM    723  CA BCYS A 101     -16.087  -4.501 -69.434  0.46 84.64           C  
ANISOU  723  CA BCYS A 101    10895  11359   9905    402    170    877       C  
ATOM    724  C  ACYS A 101     -14.877  -4.773 -68.539  0.54 84.30           C  
ANISOU  724  C  ACYS A 101    10827  11219   9983    290    183    841       C  
ATOM    725  C  BCYS A 101     -14.854  -4.800 -68.589  0.46 84.32           C  
ANISOU  725  C  BCYS A 101    10828  11228   9981    291    186    844       C  
ATOM    726  O  ACYS A 101     -14.832  -5.790 -67.836  0.54 86.43           O  
ANISOU  726  O  ACYS A 101    11073  11508  10257    254    157    711       O  
ATOM    727  O  BCYS A 101     -14.774  -5.859 -67.957  0.46 86.07           O  
ANISOU  727  O  BCYS A 101    11024  11477  10201    257    163    716       O  
ATOM    728  CB ACYS A 101     -15.834  -5.008 -70.834  0.54 84.66           C  
ANISOU  728  CB ACYS A 101    10873  11531   9763    450    223    935       C  
ATOM    729  CB BCYS A 101     -15.878  -4.984 -70.870  0.46 84.58           C  
ANISOU  729  CB BCYS A 101    10865  11524   9748    454    222    938       C  
ATOM    730  SG ACYS A 101     -15.329  -6.742 -70.867  0.54 84.12           S  
ANISOU  730  SG ACYS A 101    10769  11573   9621    415    243    790       S  
ATOM    731  SG BCYS A 101     -14.290  -4.523 -71.599  0.46 81.45           S  
ANISOU  731  SG BCYS A 101    10443  11113   9390    413    327   1106       S  
ATOM    732  N   LYS A 102     -13.884  -3.881 -68.570  1.00 83.36           N  
ANISOU  732  N   LYS A 102    10709  11003   9962    231    223    966       N  
ATOM    733  CA  LYS A 102     -12.702  -4.068 -67.735  1.00 82.46           C  
ANISOU  733  CA  LYS A 102    10555  10815   9963    115    226    949       C  
ATOM    734  C   LYS A 102     -13.053  -4.015 -66.255  1.00 86.23           C  
ANISOU  734  C   LYS A 102    11064  11170  10528     59    149    826       C  
ATOM    735  O   LYS A 102     -12.427  -4.706 -65.445  1.00 99.95           O  
ANISOU  735  O   LYS A 102    12759  12904  12312    -13    129    753       O  
ATOM    736  CB  LYS A 102     -11.646  -3.013 -68.066  1.00 74.23           C  
ANISOU  736  CB  LYS A 102     9501   9691   9012     46    276   1116       C  
ATOM    737  CG  LYS A 102     -11.051  -3.140 -69.458  1.00 70.62           C  
ANISOU  737  CG  LYS A 102     8997   9364   8472     91    368   1251       C  
ATOM    738  CD  LYS A 102      -9.956  -2.109 -69.684  1.00 71.11           C  
ANISOU  738  CD  LYS A 102     9035   9341   8643      4    419   1425       C  
ATOM    739  CE  LYS A 102      -9.256  -2.323 -71.017  1.00 55.31           C  
ANISOU  739  CE  LYS A 102     6975   7485   6557     50    524   1564       C  
ATOM    740  NZ  LYS A 102      -8.604  -3.659 -71.098  1.00 64.50           N  
ANISOU  740  NZ  LYS A 102     8058   8785   7664     60    563   1497       N  
ATOM    741  N   ILE A 103     -14.048  -3.208 -65.887  1.00 70.52           N  
ANISOU  741  N   ILE A 103     9150   9087   8556    100    111    808       N  
ATOM    742  CA  ILE A 103     -14.505  -3.173 -64.502  1.00 69.52           C  
ANISOU  742  CA  ILE A 103     9066   8857   8491     66     46    684       C  
ATOM    743  C   ILE A 103     -15.332  -4.410 -64.178  1.00 72.80           C  
ANISOU  743  C   ILE A 103     9453   9384   8824    116     13    545       C  
ATOM    744  O   ILE A 103     -15.176  -5.012 -63.110  1.00 79.68           O  
ANISOU  744  O   ILE A 103    10313  10231   9732     61    -24    439       O  
ATOM    745  CB  ILE A 103     -15.293  -1.877 -64.237  1.00 64.99           C  
ANISOU  745  CB  ILE A 103     8591   8139   7963    111     34    716       C  
ATOM    746  CG1 ILE A 103     -14.407  -0.653 -64.476  1.00 67.42           C  
ANISOU  746  CG1 ILE A 103     8941   8306   8369     38     68    851       C  
ATOM    747  CG2 ILE A 103     -15.848  -1.868 -62.820  1.00 67.81           C  
ANISOU  747  CG2 ILE A 103     9001   8400   8364     92    -22    580       C  
ATOM    748  CD1 ILE A 103     -13.212  -0.573 -63.553  1.00 80.90           C  
ANISOU  748  CD1 ILE A 103    10636   9918  10185   -123     40    825       C  
ATOM    749  N   ALA A 104     -16.213  -4.814 -65.095  1.00 58.04           N  
ANISOU  749  N   ALA A 104     7570   7643   6840    214     24    546       N  
ATOM    750  CA  ALA A 104     -17.080  -5.961 -64.840  1.00 62.26           C  
ANISOU  750  CA  ALA A 104     8079   8280   7298    247    -10    417       C  
ATOM    751  C   ALA A 104     -16.278  -7.255 -64.764  1.00 68.75           C  
ANISOU  751  C   ALA A 104     8849   9169   8103    192      7    352       C  
ATOM    752  O   ALA A 104     -16.485  -8.072 -63.860  1.00 78.95           O  
ANISOU  752  O   ALA A 104    10131  10458   9409    164    -24    239       O  
ATOM    753  CB  ALA A 104     -18.158  -6.056 -65.919  1.00 64.72           C  
ANISOU  753  CB  ALA A 104     8382   8726   7485    347    -12    442       C  
ATOM    754  N   SER A 105     -15.357  -7.461 -65.709  1.00 75.83           N  
ANISOU  754  N   SER A 105     9716  10129   8969    186     66    430       N  
ATOM    755  CA  SER A 105     -14.549  -8.675 -65.690  1.00 85.93           C  
ANISOU  755  CA  SER A 105    10950  11466  10234    154     99    380       C  
ATOM    756  C   SER A 105     -13.601  -8.702 -64.499  1.00 85.59           C  
ANISOU  756  C   SER A 105    10879  11329  10313     67     84    367       C  
ATOM    757  O   SER A 105     -13.301  -9.780 -63.972  1.00 89.23           O  
ANISOU  757  O   SER A 105    11310  11815  10778     49     86    291       O  
ATOM    758  CB  SER A 105     -13.766  -8.810 -66.995  1.00 78.39           C  
ANISOU  758  CB  SER A 105     9969  10602   9212    184    180    477       C  
ATOM    759  OG  SER A 105     -14.643  -8.958 -68.098  1.00 91.68           O  
ANISOU  759  OG  SER A 105    11681  12397  10757    261    186    473       O  
ATOM    760  N   ALA A 106     -13.120  -7.537 -64.061  1.00 78.30           N  
ANISOU  760  N   ALA A 106     9967  10297   9487      9     67    444       N  
ATOM    761  CA  ALA A 106     -12.281  -7.494 -62.870  1.00 78.01           C  
ANISOU  761  CA  ALA A 106     9905  10180   9556    -88     33    426       C  
ATOM    762  C   ALA A 106     -13.102  -7.736 -61.611  1.00 77.94           C  
ANISOU  762  C   ALA A 106     9936  10117   9560    -96    -36    296       C  
ATOM    763  O   ALA A 106     -12.628  -8.381 -60.670  1.00 65.59           O  
ANISOU  763  O   ALA A 106     8341   8549   8032   -147    -61    241       O  
ATOM    764  CB  ALA A 106     -11.552  -6.154 -62.782  1.00 69.62           C  
ANISOU  764  CB  ALA A 106     8854   9010   8589   -168     28    536       C  
ATOM    765  N   SER A 107     -14.338  -7.230 -61.579  1.00 78.95           N  
ANISOU  765  N   SER A 107    10129  10213   9655    -38    -61    257       N  
ATOM    766  CA  SER A 107     -15.184  -7.408 -60.404  1.00 67.05           C  
ANISOU  766  CA  SER A 107     8659   8662   8154    -34   -114    143       C  
ATOM    767  C   SER A 107     -15.495  -8.878 -60.152  1.00 74.03           C  
ANISOU  767  C   SER A 107     9502   9642   8985    -16   -116     47       C  
ATOM    768  O   SER A 107     -15.645  -9.290 -58.996  1.00 84.83           O  
ANISOU  768  O   SER A 107    10875  10980  10376    -45   -151    -33       O  
ATOM    769  CB  SER A 107     -16.478  -6.610 -60.564  1.00 77.62           C  
ANISOU  769  CB  SER A 107    10060   9969   9463     48   -126    138       C  
ATOM    770  OG  SER A 107     -17.300  -6.732 -59.416  1.00 97.23           O  
ANISOU  770  OG  SER A 107    12576  12415  11952     60   -165     36       O  
ATOM    771  N   VAL A 108     -15.593  -9.680 -61.212  1.00 69.41           N  
ANISOU  771  N   VAL A 108     8884   9164   8323     30    -75     54       N  
ATOM    772  CA  VAL A 108     -15.850 -11.106 -61.037  1.00 77.91           C  
ANISOU  772  CA  VAL A 108     9938  10311   9354     39    -68    -38       C  
ATOM    773  C   VAL A 108     -14.589 -11.827 -60.577  1.00 82.09           C  
ANISOU  773  C   VAL A 108    10422  10834   9935    -11    -44    -28       C  
ATOM    774  O   VAL A 108     -14.640 -12.685 -59.689  1.00 76.14           O  
ANISOU  774  O   VAL A 108     9659  10074   9196    -28    -59    -99       O  
ATOM    775  CB  VAL A 108     -16.408 -11.709 -62.339  1.00 73.06           C  
ANISOU  775  CB  VAL A 108     9322   9806   8630     96    -36    -48       C  
ATOM    776  CG1 VAL A 108     -16.783 -13.166 -62.131  1.00 56.97           C  
ANISOU  776  CG1 VAL A 108     7279   7818   6551     93    -30   -155       C  
ATOM    777  CG2 VAL A 108     -17.610 -10.912 -62.820  1.00 69.37           C  
ANISOU  777  CG2 VAL A 108     8880   9366   8112    149    -66    -32       C  
ATOM    778  N   SER A 109     -13.439 -11.491 -61.168  1.00 77.90           N  
ANISOU  778  N   SER A 109     9856  10311   9433    -29     -2     72       N  
ATOM    779  CA  SER A 109     -12.185 -12.104 -60.740  1.00 79.39           C  
ANISOU  779  CA  SER A 109     9981  10508   9675    -67     23    104       C  
ATOM    780  C   SER A 109     -11.793 -11.639 -59.344  1.00 79.08           C  
ANISOU  780  C   SER A 109     9931  10393   9722   -147    -44     98       C  
ATOM    781  O   SER A 109     -11.260 -12.422 -58.549  1.00 62.05           O  
ANISOU  781  O   SER A 109     7732   8250   7594   -169    -52     77       O  
ATOM    782  CB  SER A 109     -11.076 -11.788 -61.743  1.00 75.26           C  
ANISOU  782  CB  SER A 109     9408  10026   9162    -66     90    228       C  
ATOM    783  OG  SER A 109     -11.376 -12.321 -63.021  1.00100.32           O  
ANISOU  783  OG  SER A 109    12600  13280  12236     12    157    226       O  
ATOM    784  N   PHE A 110     -12.050 -10.367 -59.027  1.00 81.22           N  
ANISOU  784  N   PHE A 110    10247  10583  10030   -189    -92    116       N  
ATOM    785  CA  PHE A 110     -11.740  -9.852 -57.697  1.00 69.88           C  
ANISOU  785  CA  PHE A 110     8822   9069   8659   -272   -163     92       C  
ATOM    786  C   PHE A 110     -12.546 -10.582 -56.630  1.00 72.80           C  
ANISOU  786  C   PHE A 110     9221   9439   9000   -252   -200    -23       C  
ATOM    787  O   PHE A 110     -12.005 -10.985 -55.594  1.00 60.44           O  
ANISOU  787  O   PHE A 110     7627   7875   7463   -302   -236    -43       O  
ATOM    788  CB  PHE A 110     -12.012  -8.348 -57.645  1.00 64.15           C  
ANISOU  788  CB  PHE A 110     8170   8236   7969   -309   -195    118       C  
ATOM    789  CG  PHE A 110     -11.627  -7.702 -56.346  1.00 87.13           C  
ANISOU  789  CG  PHE A 110    11113  11055  10938   -409   -268     86       C  
ATOM    790  CD1 PHE A 110     -10.342  -7.227 -56.149  1.00 96.43           C  
ANISOU  790  CD1 PHE A 110    12240  12211  12186   -524   -293    164       C  
ATOM    791  CD2 PHE A 110     -12.555  -7.555 -55.327  1.00 91.29           C  
ANISOU  791  CD2 PHE A 110    11720  11524  11442   -394   -312    -21       C  
ATOM    792  CE1 PHE A 110      -9.985  -6.627 -54.958  1.00 98.70           C  
ANISOU  792  CE1 PHE A 110    12565  12421  12515   -632   -372    125       C  
ATOM    793  CE2 PHE A 110     -12.203  -6.957 -54.133  1.00 86.42           C  
ANISOU  793  CE2 PHE A 110    11150  10826  10861   -487   -380    -61       C  
ATOM    794  CZ  PHE A 110     -10.916  -6.491 -53.950  1.00 90.87           C  
ANISOU  794  CZ  PHE A 110    11671  11368  11489   -612   -415      6       C  
ATOM    795  N   ASN A 111     -13.846 -10.768 -56.872  1.00 80.28           N  
ANISOU  795  N   ASN A 111    10217  10396   9888   -180   -192    -90       N  
ATOM    796  CA  ASN A 111     -14.696 -11.434 -55.892  1.00 76.20           C  
ANISOU  796  CA  ASN A 111     9724   9885   9346   -161   -218   -190       C  
ATOM    797  C   ASN A 111     -14.311 -12.896 -55.707  1.00 80.85           C  
ANISOU  797  C   ASN A 111    10259  10538   9922   -154   -192   -211       C  
ATOM    798  O   ASN A 111     -14.478 -13.443 -54.612  1.00 91.51           O  
ANISOU  798  O   ASN A 111    11611  11883  11276   -169   -218   -263       O  
ATOM    799  CB  ASN A 111     -16.163 -11.321 -56.306  1.00 78.61           C  
ANISOU  799  CB  ASN A 111    10070  10206   9593    -88   -212   -239       C  
ATOM    800  CG  ASN A 111     -17.097 -12.012 -55.333  1.00 81.41           C  
ANISOU  800  CG  ASN A 111    10437  10575   9922    -71   -231   -330       C  
ATOM    801  OD1 ASN A 111     -17.420 -13.189 -55.494  1.00 82.05           O  
ANISOU  801  OD1 ASN A 111    10488  10717   9969    -54   -209   -368       O  
ATOM    802  ND2 ASN A 111     -17.533 -11.283 -54.313  1.00 83.41           N  
ANISOU  802  ND2 ASN A 111    10739  10764  10189    -76   -267   -365       N  
ATOM    803  N   LEU A 112     -13.799 -13.542 -56.757  1.00 86.66           N  
ANISOU  803  N   LEU A 112    10955  11331  10641   -126   -132   -169       N  
ATOM    804  CA  LEU A 112     -13.388 -14.937 -56.636  1.00 84.00           C  
ANISOU  804  CA  LEU A 112    10581  11036  10298   -107    -91   -186       C  
ATOM    805  C   LEU A 112     -12.231 -15.078 -55.653  1.00 91.62           C  
ANISOU  805  C   LEU A 112    11491  11995  11327   -154   -113   -137       C  
ATOM    806  O   LEU A 112     -12.292 -15.879 -54.715  1.00 94.22           O  
ANISOU  806  O   LEU A 112    11812  12325  11660   -154   -125   -173       O  
ATOM    807  CB  LEU A 112     -13.009 -15.494 -58.011  1.00 85.20           C  
ANISOU  807  CB  LEU A 112    10718  11242  10412    -58    -12   -152       C  
ATOM    808  CG  LEU A 112     -12.872 -17.013 -58.178  1.00 84.49           C  
ANISOU  808  CG  LEU A 112    10625  11179  10298    -15     51   -191       C  
ATOM    809  CD1 LEU A 112     -13.153 -17.409 -59.618  1.00 98.53           C  
ANISOU  809  CD1 LEU A 112    12436  13002  11998     35    115   -209       C  
ATOM    810  CD2 LEU A 112     -11.494 -17.513 -57.760  1.00 62.88           C  
ANISOU  810  CD2 LEU A 112     7819   8452   7621    -13     87   -115       C  
ATOM    811  N   TYR A 113     -11.166 -14.299 -55.853  1.00 94.23           N  
ANISOU  811  N   TYR A 113    11774  12325  11704   -199   -121    -45       N  
ATOM    812  CA  TYR A 113     -10.019 -14.382 -54.956  1.00 94.74           C  
ANISOU  812  CA  TYR A 113    11767  12406  11825   -256   -154     14       C  
ATOM    813  C   TYR A 113     -10.354 -13.842 -53.571  1.00 93.94           C  
ANISOU  813  C   TYR A 113    11704  12257  11731   -322   -247    -41       C  
ATOM    814  O   TYR A 113      -9.918 -14.403 -52.560  1.00 98.63           O  
ANISOU  814  O   TYR A 113    12261  12879  12336   -342   -279    -38       O  
ATOM    815  CB  TYR A 113      -8.830 -13.629 -55.552  1.00 99.30           C  
ANISOU  815  CB  TYR A 113    12272  13003  12453   -305   -143    132       C  
ATOM    816  CG  TYR A 113      -8.219 -14.297 -56.763  1.00106.95           C  
ANISOU  816  CG  TYR A 113    13186  14039  13411   -233    -39    203       C  
ATOM    817  CD1 TYR A 113      -7.217 -15.248 -56.623  1.00114.99           C  
ANISOU  817  CD1 TYR A 113    14113  15123  14456   -201      8    268       C  
ATOM    818  CD2 TYR A 113      -8.638 -13.972 -58.046  1.00102.11           C  
ANISOU  818  CD2 TYR A 113    12614  13429  12755   -188     17    211       C  
ATOM    819  CE1 TYR A 113      -6.653 -15.860 -57.726  1.00115.56           C  
ANISOU  819  CE1 TYR A 113    14144  15251  14512   -121    117    329       C  
ATOM    820  CE2 TYR A 113      -8.081 -14.579 -59.156  1.00101.59           C  
ANISOU  820  CE2 TYR A 113    12509  13428  12662   -118    117    268       C  
ATOM    821  CZ  TYR A 113      -7.088 -15.522 -58.989  1.00110.21           C  
ANISOU  821  CZ  TYR A 113    13519  14574  13782    -82    172    323       C  
ATOM    822  OH  TYR A 113      -6.528 -16.128 -60.089  1.00124.51           O  
ANISOU  822  OH  TYR A 113    15302  16445  15562      3    287    377       O  
ATOM    823  N   ALA A 114     -11.131 -12.758 -53.503  1.00 90.13           N  
ANISOU  823  N   ALA A 114    11301  11705  11238   -345   -286    -88       N  
ATOM    824  CA  ALA A 114     -11.419 -12.133 -52.216  1.00 75.60           C  
ANISOU  824  CA  ALA A 114     9518   9811   9398   -403   -365   -146       C  
ATOM    825  C   ALA A 114     -12.281 -13.035 -51.340  1.00 79.84           C  
ANISOU  825  C   ALA A 114    10083  10366   9887   -356   -369   -230       C  
ATOM    826  O   ALA A 114     -11.969 -13.252 -50.163  1.00 79.10           O  
ANISOU  826  O   ALA A 114     9982  10285   9788   -396   -418   -245       O  
ATOM    827  CB  ALA A 114     -12.099 -10.780 -52.427  1.00 71.38           C  
ANISOU  827  CB  ALA A 114     9076   9183   8863   -417   -385   -175       C  
ATOM    828  N   SER A 115     -13.371 -13.569 -51.896  1.00 72.67           N  
ANISOU  828  N   SER A 115     9205   9468   8940   -278   -319   -279       N  
ATOM    829  CA  SER A 115     -14.270 -14.402 -51.101  1.00 82.16           C  
ANISOU  829  CA  SER A 115    10430  10686  10103   -241   -316   -350       C  
ATOM    830  C   SER A 115     -13.578 -15.675 -50.632  1.00 81.82           C  
ANISOU  830  C   SER A 115    10326  10692  10069   -237   -298   -320       C  
ATOM    831  O   SER A 115     -13.837 -16.159 -49.524  1.00 92.39           O  
ANISOU  831  O   SER A 115    11675  12041  11389   -240   -319   -351       O  
ATOM    832  CB  SER A 115     -15.524 -14.741 -51.905  1.00 82.21           C  
ANISOU  832  CB  SER A 115    10462  10704  10070   -176   -271   -398       C  
ATOM    833  OG  SER A 115     -16.240 -13.570 -52.256  1.00 95.64           O  
ANISOU  833  OG  SER A 115    12214  12365  11760   -161   -286   -413       O  
ATOM    834  N   VAL A 116     -12.691 -16.228 -51.457  1.00 69.48           N  
ANISOU  834  N   VAL A 116     8701   9163   8534   -221   -250   -253       N  
ATOM    835  CA  VAL A 116     -12.002 -17.459 -51.086  1.00 56.10           C  
ANISOU  835  CA  VAL A 116     6951   7509   6855   -196   -217   -212       C  
ATOM    836  C   VAL A 116     -10.894 -17.179 -50.075  1.00 69.44           C  
ANISOU  836  C   VAL A 116     8581   9230   8573   -254   -281   -146       C  
ATOM    837  O   VAL A 116     -10.650 -17.981 -49.167  1.00 79.97           O  
ANISOU  837  O   VAL A 116     9887  10595   9903   -241   -288   -128       O  
ATOM    838  CB  VAL A 116     -11.473 -18.163 -52.349  1.00 60.76           C  
ANISOU  838  CB  VAL A 116     7506   8122   7459   -141   -129   -166       C  
ATOM    839  CG1 VAL A 116     -10.606 -19.344 -51.981  1.00 70.02           C  
ANISOU  839  CG1 VAL A 116     8620   9327   8659   -101    -85   -105       C  
ATOM    840  CG2 VAL A 116     -12.635 -18.624 -53.215  1.00 57.35           C  
ANISOU  840  CG2 VAL A 116     7139   7671   6981    -97    -79   -245       C  
ATOM    841  N   PHE A 117     -10.216 -16.034 -50.202  1.00 65.99           N  
ANISOU  841  N   PHE A 117     8121   8788   8163   -324   -331   -104       N  
ATOM    842  CA  PHE A 117      -9.188 -15.679 -49.226  1.00 70.33           C  
ANISOU  842  CA  PHE A 117     8612   9377   8733   -403   -410    -48       C  
ATOM    843  C   PHE A 117      -9.799 -15.378 -47.863  1.00 71.97           C  
ANISOU  843  C   PHE A 117     8890   9564   8893   -443   -487   -126       C  
ATOM    844  O   PHE A 117      -9.209 -15.708 -46.827  1.00 79.60           O  
ANISOU  844  O   PHE A 117     9812  10588   9846   -475   -540    -94       O  
ATOM    845  CB  PHE A 117      -8.377 -14.480 -49.719  1.00 67.27           C  
ANISOU  845  CB  PHE A 117     8192   8978   8390   -490   -447     10       C  
ATOM    846  CG  PHE A 117      -7.466 -14.792 -50.873  1.00 78.97           C  
ANISOU  846  CG  PHE A 117     9577  10510   9919   -458   -374    117       C  
ATOM    847  CD1 PHE A 117      -7.151 -16.102 -51.194  1.00 81.64           C  
ANISOU  847  CD1 PHE A 117     9855  10905  10260   -362   -292    162       C  
ATOM    848  CD2 PHE A 117      -6.921 -13.771 -51.634  1.00 80.48           C  
ANISOU  848  CD2 PHE A 117     9743  10684  10150   -520   -377    176       C  
ATOM    849  CE1 PHE A 117      -6.312 -16.388 -52.256  1.00 76.36           C  
ANISOU  849  CE1 PHE A 117     9105  10283   9625   -318   -211    258       C  
ATOM    850  CE2 PHE A 117      -6.082 -14.050 -52.696  1.00 76.26           C  
ANISOU  850  CE2 PHE A 117     9117  10207   9652   -483   -299    282       C  
ATOM    851  CZ  PHE A 117      -5.776 -15.359 -53.007  1.00 75.66           C  
ANISOU  851  CZ  PHE A 117     8983  10194   9570   -377   -214    320       C  
ATOM    852  N   LEU A 118     -10.976 -14.748 -47.842  1.00 73.89           N  
ANISOU  852  N   LEU A 118     9239   9736   9101   -434   -491   -222       N  
ATOM    853  CA  LEU A 118     -11.628 -14.442 -46.572  1.00 62.04           C  
ANISOU  853  CA  LEU A 118     7814   8214   7543   -456   -547   -301       C  
ATOM    854  C   LEU A 118     -12.045 -15.714 -45.844  1.00 62.25           C  
ANISOU  854  C   LEU A 118     7827   8292   7533   -395   -519   -311       C  
ATOM    855  O   LEU A 118     -11.907 -15.807 -44.619  1.00 70.39           O  
ANISOU  855  O   LEU A 118     8869   9357   8520   -423   -573   -320       O  
ATOM    856  CB  LEU A 118     -12.835 -13.533 -46.804  1.00 54.78           C  
ANISOU  856  CB  LEU A 118     7003   7211   6600   -433   -536   -389       C  
ATOM    857  CG  LEU A 118     -12.526 -12.087 -47.197  1.00 63.23           C  
ANISOU  857  CG  LEU A 118     8121   8204   7700   -500   -573   -389       C  
ATOM    858  CD1 LEU A 118     -13.801 -11.341 -47.548  1.00 78.52           C  
ANISOU  858  CD1 LEU A 118    10156  10060   9616   -442   -541   -458       C  
ATOM    859  CD2 LEU A 118     -11.782 -11.376 -46.079  1.00 50.95           C  
ANISOU  859  CD2 LEU A 118     6593   6634   6131   -610   -669   -404       C  
ATOM    860  N   LEU A 119     -12.559 -16.704 -46.579  1.00 60.46           N  
ANISOU  860  N   LEU A 119     7584   8069   7319   -317   -434   -307       N  
ATOM    861  CA  LEU A 119     -12.895 -17.981 -45.959  1.00 60.43           C  
ANISOU  861  CA  LEU A 119     7569   8097   7294   -266   -397   -303       C  
ATOM    862  C   LEU A 119     -11.653 -18.695 -45.444  1.00 62.93           C  
ANISOU  862  C   LEU A 119     7799   8479   7631   -269   -411   -204       C  
ATOM    863  O   LEU A 119     -11.726 -19.424 -44.448  1.00 66.09           O  
ANISOU  863  O   LEU A 119     8195   8914   8001   -249   -416   -188       O  
ATOM    864  CB  LEU A 119     -13.639 -18.871 -46.953  1.00 61.06           C  
ANISOU  864  CB  LEU A 119     7658   8154   7389   -200   -306   -324       C  
ATOM    865  CG  LEU A 119     -14.980 -18.355 -47.473  1.00 62.78           C  
ANISOU  865  CG  LEU A 119     7939   8332   7580   -187   -291   -409       C  
ATOM    866  CD1 LEU A 119     -15.559 -19.330 -48.481  1.00 60.00           C  
ANISOU  866  CD1 LEU A 119     7586   7974   7238   -143   -214   -426       C  
ATOM    867  CD2 LEU A 119     -15.950 -18.123 -46.326  1.00 76.82           C  
ANISOU  867  CD2 LEU A 119     9770  10110   9309   -187   -318   -467       C  
ATOM    868  N   THR A 120     -10.512 -18.500 -46.107  1.00 78.15           N  
ANISOU  868  N   THR A 120     9651  10434   9609   -289   -413   -126       N  
ATOM    869  CA  THR A 120      -9.268 -19.103 -45.642  1.00 75.88           C  
ANISOU  869  CA  THR A 120     9260  10227   9345   -286   -428    -13       C  
ATOM    870  C   THR A 120      -8.848 -18.519 -44.299  1.00 66.33           C  
ANISOU  870  C   THR A 120     8040   9073   8090   -367   -543     -5       C  
ATOM    871  O   THR A 120      -8.527 -19.259 -43.361  1.00 50.81           O  
ANISOU  871  O   THR A 120     6035   7173   6098   -344   -562     48       O  
ATOM    872  CB  THR A 120      -8.168 -18.902 -46.685  1.00 76.50           C  
ANISOU  872  CB  THR A 120     9248  10332   9487   -290   -401     75       C  
ATOM    873  OG1 THR A 120      -8.601 -19.426 -47.946  1.00 75.90           O  
ANISOU  873  OG1 THR A 120     9200  10207   9432   -214   -294     55       O  
ATOM    874  CG2 THR A 120      -6.893 -19.610 -46.258  1.00 78.32           C  
ANISOU  874  CG2 THR A 120     9351  10659   9746   -267   -404    209       C  
ATOM    875  N   CYS A 121      -8.848 -17.189 -44.188  1.00 61.24           N  
ANISOU  875  N   CYS A 121     7438   8398   7430   -462   -622    -58       N  
ATOM    876  CA  CYS A 121      -8.486 -16.551 -42.928  1.00 56.27           C  
ANISOU  876  CA  CYS A 121     6823   7814   6745   -555   -738    -74       C  
ATOM    877  C   CYS A 121      -9.543 -16.783 -41.857  1.00 64.12           C  
ANISOU  877  C   CYS A 121     7915   8795   7651   -523   -746   -159       C  
ATOM    878  O   CYS A 121      -9.207 -16.912 -40.674  1.00 64.22           O  
ANISOU  878  O   CYS A 121     7919   8883   7600   -556   -817   -143       O  
ATOM    879  CB  CYS A 121      -8.265 -15.055 -43.143  1.00 61.46           C  
ANISOU  879  CB  CYS A 121     7525   8413   7412   -670   -810   -120       C  
ATOM    880  SG  CYS A 121      -6.965 -14.666 -44.334  1.00 80.60           S  
ANISOU  880  SG  CYS A 121     9824  10863   9939   -725   -804     -3       S  
ATOM    881  N   LEU A 122     -10.819 -16.840 -42.247  1.00 70.61           N  
ANISOU  881  N   LEU A 122     8825   9539   8464   -460   -674   -243       N  
ATOM    882  CA  LEU A 122     -11.874 -17.127 -41.282  1.00 66.46           C  
ANISOU  882  CA  LEU A 122     8380   9012   7862   -421   -663   -311       C  
ATOM    883  C   LEU A 122     -11.756 -18.543 -40.734  1.00 74.58           C  
ANISOU  883  C   LEU A 122     9351  10109   8879   -356   -623   -236       C  
ATOM    884  O   LEU A 122     -12.105 -18.788 -39.573  1.00 75.63           O  
ANISOU  884  O   LEU A 122     9519  10283   8933   -348   -646   -249       O  
ATOM    885  CB  LEU A 122     -13.245 -16.908 -41.927  1.00 72.13           C  
ANISOU  885  CB  LEU A 122     9176   9646   8583   -367   -591   -397       C  
ATOM    886  CG  LEU A 122     -14.499 -16.995 -41.053  1.00 87.40           C  
ANISOU  886  CG  LEU A 122    11191  11575  10442   -324   -568   -472       C  
ATOM    887  CD1 LEU A 122     -15.529 -15.975 -41.512  1.00 91.52           C  
ANISOU  887  CD1 LEU A 122    11797  12018  10958   -309   -548   -562       C  
ATOM    888  CD2 LEU A 122     -15.096 -18.395 -41.089  1.00 87.46           C  
ANISOU  888  CD2 LEU A 122    11163  11606  10461   -252   -485   -437       C  
ATOM    889  N   SER A 123     -11.269 -19.483 -41.547  1.00 73.20           N  
ANISOU  889  N   SER A 123     9096   9940   8776   -303   -555   -153       N  
ATOM    890  CA  SER A 123     -11.074 -20.846 -41.065  1.00 76.10           C  
ANISOU  890  CA  SER A 123     9416  10353   9145   -235   -507    -70       C  
ATOM    891  C   SER A 123      -9.865 -20.935 -40.141  1.00 77.23           C  
ANISOU  891  C   SER A 123     9476  10607   9261   -263   -588     32       C  
ATOM    892  O   SER A 123      -9.885 -21.678 -39.154  1.00 81.44           O  
ANISOU  892  O   SER A 123    10000  11197   9746   -227   -590     83       O  
ATOM    893  CB  SER A 123     -10.919 -21.804 -42.246  1.00 58.95           C  
ANISOU  893  CB  SER A 123     7204   8138   7058   -163   -401    -22       C  
ATOM    894  OG  SER A 123      -9.752 -21.510 -42.992  1.00 72.84           O  
ANISOU  894  OG  SER A 123     8878   9924   8872   -178   -413     48       O  
ATOM    895  N   ILE A 124      -8.801 -20.190 -40.450  1.00 61.15           N  
ANISOU  895  N   ILE A 124     7370   8612   7253   -333   -658     73       N  
ATOM    896  CA  ILE A 124      -7.635 -20.158 -39.570  1.00 58.17           C  
ANISOU  896  CA  ILE A 124     6898   8361   6844   -380   -755    171       C  
ATOM    897  C   ILE A 124      -8.002 -19.533 -38.230  1.00 79.68           C  
ANISOU  897  C   ILE A 124     9700  11126   9450   -451   -858    100       C  
ATOM    898  O   ILE A 124      -7.524 -19.963 -37.173  1.00 74.95           O  
ANISOU  898  O   ILE A 124     9055  10638   8784   -451   -916    171       O  
ATOM    899  CB  ILE A 124      -6.472 -19.411 -40.251  1.00 56.15           C  
ANISOU  899  CB  ILE A 124     6544   8141   6650   -459   -809    229       C  
ATOM    900  CG1 ILE A 124      -6.012 -20.162 -41.502  1.00 68.06           C  
ANISOU  900  CG1 ILE A 124     7969   9630   8261   -368   -694    316       C  
ATOM    901  CG2 ILE A 124      -5.309 -19.222 -39.287  1.00 47.55           C  
ANISOU  901  CG2 ILE A 124     5349   7198   5518   -537   -934    323       C  
ATOM    902  CD1 ILE A 124      -4.842 -19.510 -42.208  1.00 60.01           C  
ANISOU  902  CD1 ILE A 124     6836   8660   7307   -434   -729    395       C  
ATOM    903  N   ASP A 125      -8.865 -18.513 -38.253  1.00 78.67           N  
ANISOU  903  N   ASP A 125     9695  10911   9285   -502   -877    -40       N  
ATOM    904  CA  ASP A 125      -9.325 -17.903 -37.011  1.00 66.99           C  
ANISOU  904  CA  ASP A 125     8316   9455   7683   -555   -955   -127       C  
ATOM    905  C   ASP A 125     -10.107 -18.892 -36.156  1.00 67.12           C  
ANISOU  905  C   ASP A 125     8368   9506   7630   -462   -899   -116       C  
ATOM    906  O   ASP A 125     -10.025 -18.847 -34.924  1.00 78.97           O  
ANISOU  906  O   ASP A 125     9897  11092   9017   -487   -968   -117       O  
ATOM    907  CB  ASP A 125     -10.181 -16.674 -37.317  1.00 63.86           C  
ANISOU  907  CB  ASP A 125     8052   8938   7273   -598   -956   -274       C  
ATOM    908  CG  ASP A 125     -10.684 -15.989 -36.063  1.00 92.48           C  
ANISOU  908  CG  ASP A 125    11801  12572  10765   -640  -1022   -377       C  
ATOM    909  OD1 ASP A 125      -9.880 -15.306 -35.395  1.00100.51           O  
ANISOU  909  OD1 ASP A 125    12825  13643  11723   -751  -1143   -389       O  
ATOM    910  OD2 ASP A 125     -11.883 -16.134 -35.741  1.00103.03           O  
ANISOU  910  OD2 ASP A 125    13228  13868  12051   -565   -953   -447       O  
ATOM    911  N   ARG A 126     -10.860 -19.795 -36.787  1.00 61.33           N  
ANISOU  911  N   ARG A 126     7636   8710   6958   -363   -775   -102       N  
ATOM    912  CA  ARG A 126     -11.623 -20.777 -36.023  1.00 56.22           C  
ANISOU  912  CA  ARG A 126     7018   8086   6259   -285   -712    -79       C  
ATOM    913  C   ARG A 126     -10.713 -21.831 -35.406  1.00 63.66           C  
ANISOU  913  C   ARG A 126     7863   9134   7192   -244   -724     71       C  
ATOM    914  O   ARG A 126     -10.980 -22.317 -34.301  1.00 79.69           O  
ANISOU  914  O   ARG A 126     9915  11230   9133   -213   -728    105       O  
ATOM    915  CB  ARG A 126     -12.679 -21.436 -36.909  1.00 60.46           C  
ANISOU  915  CB  ARG A 126     7582   8521   6869   -213   -583   -109       C  
ATOM    916  CG  ARG A 126     -13.934 -20.601 -37.113  1.00 72.49           C  
ANISOU  916  CG  ARG A 126     9207   9970   8367   -223   -561   -244       C  
ATOM    917  CD  ARG A 126     -14.591 -20.247 -35.785  1.00 92.86           C  
ANISOU  917  CD  ARG A 126    11868  12596  10820   -225   -589   -297       C  
ATOM    918  NE  ARG A 126     -14.138 -18.957 -35.271  1.00 99.21           N  
ANISOU  918  NE  ARG A 126    12727  13417  11549   -302   -697   -367       N  
ATOM    919  CZ  ARG A 126     -14.411 -18.500 -34.053  1.00 91.77           C  
ANISOU  919  CZ  ARG A 126    11866  12525  10477   -317   -743   -420       C  
ATOM    920  NH1 ARG A 126     -15.135 -19.229 -33.216  1.00 89.07           N  
ANISOU  920  NH1 ARG A 126    11547  12233  10065   -253   -686   -397       N  
ATOM    921  NH2 ARG A 126     -13.957 -17.314 -33.672  1.00 93.09           N  
ANISOU  921  NH2 ARG A 126    12099  12690  10581   -401   -842   -496       N  
ATOM    922  N   TYR A 127      -9.638 -22.203 -36.105  1.00 62.16           N  
ANISOU  922  N   TYR A 127     7560   8965   7091   -232   -720    174       N  
ATOM    923  CA  TYR A 127      -8.694 -23.159 -35.538  1.00 62.01           C  
ANISOU  923  CA  TYR A 127     7436   9055   7069   -179   -730    335       C  
ATOM    924  C   TYR A 127      -8.013 -22.591 -34.300  1.00 76.04           C  
ANISOU  924  C   TYR A 127     9186  10980   8727   -256   -876    364       C  
ATOM    925  O   TYR A 127      -7.733 -23.323 -33.343  1.00 82.81           O  
ANISOU  925  O   TYR A 127    10003  11940   9519   -208   -892    469       O  
ATOM    926  CB  TYR A 127      -7.654 -23.560 -36.584  1.00 52.01           C  
ANISOU  926  CB  TYR A 127     6050   7788   5921   -143   -691    439       C  
ATOM    927  CG  TYR A 127      -6.429 -24.218 -35.993  1.00 57.42           C  
ANISOU  927  CG  TYR A 127     6600   8614   6602   -102   -731    617       C  
ATOM    928  CD1 TYR A 127      -6.501 -25.487 -35.434  1.00 46.20           C  
ANISOU  928  CD1 TYR A 127     5165   7215   5175     12   -659    729       C  
ATOM    929  CD2 TYR A 127      -5.201 -23.570 -35.993  1.00 66.38           C  
ANISOU  929  CD2 TYR A 127     7616   9865   7741   -177   -840    685       C  
ATOM    930  CE1 TYR A 127      -5.384 -26.091 -34.889  1.00 60.82           C  
ANISOU  930  CE1 TYR A 127     6885   9202   7021     67   -692    909       C  
ATOM    931  CE2 TYR A 127      -4.077 -24.167 -35.452  1.00 68.25           C  
ANISOU  931  CE2 TYR A 127     7709  10252   7972   -134   -880    863       C  
ATOM    932  CZ  TYR A 127      -4.175 -25.428 -34.902  1.00 73.05           C  
ANISOU  932  CZ  TYR A 127     8303  10882   8570     -3   -805    977       C  
ATOM    933  OH  TYR A 127      -3.060 -26.028 -34.362  1.00 81.01           O  
ANISOU  933  OH  TYR A 127     9162  12048   9572     56   -843   1170       O  
ATOM    934  N   LEU A 128      -7.743 -21.285 -34.296  1.00 71.56           N  
ANISOU  934  N   LEU A 128     8644  10421   8123   -379   -984    272       N  
ATOM    935  CA  LEU A 128      -7.084 -20.670 -33.150  1.00 71.94           C  
ANISOU  935  CA  LEU A 128     8678  10607   8048   -476  -1137    280       C  
ATOM    936  C   LEU A 128      -8.067 -20.384 -32.020  1.00 74.00           C  
ANISOU  936  C   LEU A 128     9083  10873   8160   -483  -1158    173       C  
ATOM    937  O   LEU A 128      -7.712 -20.503 -30.844  1.00 63.78           O  
ANISOU  937  O   LEU A 128     7780   9716   6740   -504  -1243    218       O  
ATOM    938  CB  LEU A 128      -6.379 -19.384 -33.582  1.00 68.54           C  
ANISOU  938  CB  LEU A 128     8231  10171   7642   -621  -1245    220       C  
ATOM    939  CG  LEU A 128      -5.300 -19.529 -34.657  1.00 61.73           C  
ANISOU  939  CG  LEU A 128     7213   9325   6916   -627  -1232    335       C  
ATOM    940  CD1 LEU A 128      -4.745 -18.168 -35.049  1.00 50.34           C  
ANISOU  940  CD1 LEU A 128     5769   7861   5495   -786  -1333    269       C  
ATOM    941  CD2 LEU A 128      -4.187 -20.451 -34.180  1.00 54.70           C  
ANISOU  941  CD2 LEU A 128     6153   8606   6023   -579  -1266    529       C  
ATOM    942  N   ALA A 129      -9.305 -20.013 -32.354  1.00 75.40           N  
ANISOU  942  N   ALA A 129     9389  10916   8344   -461  -1078     38       N  
ATOM    943  CA  ALA A 129     -10.275 -19.655 -31.326  1.00 67.63           C  
ANISOU  943  CA  ALA A 129     8542   9935   7218   -458  -1083    -67       C  
ATOM    944  C   ALA A 129     -10.816 -20.868 -30.580  1.00 73.26           C  
ANISOU  944  C   ALA A 129     9251  10706   7878   -348  -1003     20       C  
ATOM    945  O   ALA A 129     -11.261 -20.727 -29.436  1.00 84.09           O  
ANISOU  945  O   ALA A 129    10704  12145   9102   -346  -1030    -18       O  
ATOM    946  CB  ALA A 129     -11.433 -18.871 -31.946  1.00 72.87           C  
ANISOU  946  CB  ALA A 129     9328  10447   7913   -454  -1014   -221       C  
ATOM    947  N   ILE A 130     -10.785 -22.047 -31.192  1.00 71.59           N  
ANISOU  947  N   ILE A 130     8957  10465   7781   -257   -901    135       N  
ATOM    948  CA  ILE A 130     -11.354 -23.247 -30.596  1.00 68.46           C  
ANISOU  948  CA  ILE A 130     8563  10093   7358   -156   -808    224       C  
ATOM    949  C   ILE A 130     -10.286 -24.106 -29.929  1.00 75.29           C  
ANISOU  949  C   ILE A 130     9319  11095   8193   -117   -851    405       C  
ATOM    950  O   ILE A 130     -10.520 -24.671 -28.860  1.00 69.05           O  
ANISOU  950  O   ILE A 130     8547  10390   7298    -69   -843    473       O  
ATOM    951  CB  ILE A 130     -12.129 -24.050 -31.664  1.00 67.55           C  
ANISOU  951  CB  ILE A 130     8447   9835   7384    -83   -657    228       C  
ATOM    952  CG1 ILE A 130     -13.260 -23.202 -32.247  1.00 75.61           C  
ANISOU  952  CG1 ILE A 130     9563  10744   8419   -114   -620     63       C  
ATOM    953  CG2 ILE A 130     -12.678 -25.343 -31.077  1.00 54.88           C  
ANISOU  953  CG2 ILE A 130     6844   8238   5768      8   -556    330       C  
ATOM    954  CD1 ILE A 130     -13.990 -23.861 -33.397  1.00 68.96           C  
ANISOU  954  CD1 ILE A 130     8716   9777   7709    -67   -496     53       C  
ATOM    955  N   VAL A 131      -9.107 -24.205 -30.537  1.00 81.87           N  
ANISOU  955  N   VAL A 131    10031  11962   9114   -130   -894    495       N  
ATOM    956  CA  VAL A 131      -8.071 -25.102 -30.031  1.00 78.48           C  
ANISOU  956  CA  VAL A 131     9477  11664   8676    -70   -920    690       C  
ATOM    957  C   VAL A 131      -7.099 -24.376 -29.107  1.00 75.08           C  
ANISOU  957  C   VAL A 131     8993  11420   8116   -165  -1099    718       C  
ATOM    958  O   VAL A 131      -6.666 -24.934 -28.096  1.00 77.83           O  
ANISOU  958  O   VAL A 131     9290  11917   8366   -125  -1146    846       O  
ATOM    959  CB  VAL A 131      -7.341 -25.770 -31.212  1.00 67.06           C  
ANISOU  959  CB  VAL A 131     7919  10159   7403     -5   -844    794       C  
ATOM    960  CG1 VAL A 131      -6.355 -26.813 -30.707  1.00 76.00           C  
ANISOU  960  CG1 VAL A 131     8923  11416   8539     90   -843   1013       C  
ATOM    961  CG2 VAL A 131      -8.347 -26.398 -32.164  1.00 53.86           C  
ANISOU  961  CG2 VAL A 131     6321   8298   5846     64   -680    737       C  
ATOM    962  N   HIS A 132      -6.748 -23.128 -29.422  1.00 71.46           N  
ANISOU  962  N   HIS A 132     8546  10958   7649   -297  -1206    602       N  
ATOM    963  CA  HIS A 132      -5.798 -22.341 -28.636  1.00 59.66           C  
ANISOU  963  CA  HIS A 132     7003   9628   6035   -421  -1390    610       C  
ATOM    964  C   HIS A 132      -6.465 -21.045 -28.182  1.00 70.23           C  
ANISOU  964  C   HIS A 132     8509  10921   7255   -541  -1465    399       C  
ATOM    965  O   HIS A 132      -6.108 -19.955 -28.650  1.00 71.07           O  
ANISOU  965  O   HIS A 132     8630  10983   7390   -668  -1545    300       O  
ATOM    966  CB  HIS A 132      -4.535 -22.040 -29.441  1.00 75.94           C  
ANISOU  966  CB  HIS A 132     8908  11735   8209   -487  -1457    688       C  
ATOM    967  CG  HIS A 132      -3.860 -23.259 -29.990  1.00 98.02           C  
ANISOU  967  CG  HIS A 132    11547  14564  11131   -353  -1365    890       C  
ATOM    968  ND1 HIS A 132      -3.922 -24.489 -29.371  1.00101.96           N  
ANISOU  968  ND1 HIS A 132    12012  15126  11601   -214  -1298   1037       N  
ATOM    969  CD2 HIS A 132      -3.109 -23.435 -31.103  1.00100.00           C  
ANISOU  969  CD2 HIS A 132    11673  14786  11535   -328  -1319    972       C  
ATOM    970  CE1 HIS A 132      -3.237 -25.370 -30.078  1.00104.53           C  
ANISOU  970  CE1 HIS A 132    12206  15449  12061   -105  -1213   1196       C  
ATOM    971  NE2 HIS A 132      -2.734 -24.756 -31.134  1.00100.31           N  
ANISOU  971  NE2 HIS A 132    11613  14865  11635   -168  -1223   1158       N  
ATOM    972  N   PRO A 133      -7.431 -21.126 -27.261  1.00 85.61           N  
ANISOU  972  N   PRO A 133    10588  12874   9068   -501  -1434    331       N  
ATOM    973  CA  PRO A 133      -8.163 -19.904 -26.886  1.00 92.34           C  
ANISOU  973  CA  PRO A 133    11616  13658   9810   -589  -1477    122       C  
ATOM    974  C   PRO A 133      -7.314 -18.905 -26.123  1.00 90.31           C  
ANISOU  974  C   PRO A 133    11378  13522   9415   -748  -1670     63       C  
ATOM    975  O   PRO A 133      -7.431 -17.695 -26.358  1.00 84.57           O  
ANISOU  975  O   PRO A 133    10754  12699   8679   -862  -1724    -98       O  
ATOM    976  CB  PRO A 133      -9.322 -20.437 -26.027  1.00103.14           C  
ANISOU  976  CB  PRO A 133    13094  15033  11063   -483  -1382    102       C  
ATOM    977  CG  PRO A 133      -9.352 -21.925 -26.263  1.00106.48           C  
ANISOU  977  CG  PRO A 133    13406  15468  11582   -346  -1264    285       C  
ATOM    978  CD  PRO A 133      -7.937 -22.306 -26.544  1.00 99.94           C  
ANISOU  978  CD  PRO A 133    12404  14744  10825   -368  -1345    441       C  
ATOM    979  N   MET A 134      -6.459 -19.373 -25.215  1.00 84.26           N  
ANISOU  979  N   MET A 134    10516  12962   8539   -764  -1778    193       N  
ATOM    980  CA  MET A 134      -5.687 -18.479 -24.360  1.00 74.35           C  
ANISOU  980  CA  MET A 134     9281  11844   7124   -930  -1976    134       C  
ATOM    981  C   MET A 134      -4.386 -18.017 -25.008  1.00 79.20           C  
ANISOU  981  C   MET A 134     9743  12507   7843  -1065  -2098    193       C  
ATOM    982  O   MET A 134      -3.976 -16.867 -24.814  1.00 80.09           O  
ANISOU  982  O   MET A 134     9916  12623   7892  -1244  -2237     70       O  
ATOM    983  CB  MET A 134      -5.383 -19.164 -23.025  1.00 76.47           C  
ANISOU  983  CB  MET A 134     9514  12340   7203   -891  -2049    251       C  
ATOM    984  CG  MET A 134      -6.613 -19.446 -22.178  1.00 86.56           C  
ANISOU  984  CG  MET A 134    10955  13598   8334   -784  -1950    184       C  
ATOM    985  SD  MET A 134      -7.436 -17.941 -21.623  1.00 89.20           S  
ANISOU  985  SD  MET A 134    11558  13834   8501   -896  -1997   -109       S  
ATOM    986  CE  MET A 134      -8.835 -18.625 -20.739  1.00 87.57           C  
ANISOU  986  CE  MET A 134    11484  13634   8156   -722  -1839   -117       C  
ATOM    987  N   LYS A 135      -3.728 -18.886 -25.776  1.00 76.40           N  
ANISOU  987  N   LYS A 135     9193  12185   7649   -985  -2042    380       N  
ATOM    988  CA  LYS A 135      -2.427 -18.548 -26.340  1.00 74.18           C  
ANISOU  988  CA  LYS A 135     8737  11983   7466  -1100  -2150    469       C  
ATOM    989  C   LYS A 135      -2.521 -17.676 -27.586  1.00 74.99           C  
ANISOU  989  C   LYS A 135     8876  11892   7727  -1177  -2108    358       C  
ATOM    990  O   LYS A 135      -1.558 -16.970 -27.901  1.00 77.09           O  
ANISOU  990  O   LYS A 135     9048  12205   8037  -1330  -2225    373       O  
ATOM    991  CB  LYS A 135      -1.647 -19.824 -26.666  1.00 71.04           C  
ANISOU  991  CB  LYS A 135     8115  11704   7174   -964  -2094    724       C  
ATOM    992  CG  LYS A 135      -1.286 -20.659 -25.447  1.00 80.03           C  
ANISOU  992  CG  LYS A 135     9180  13066   8162   -896  -2159    877       C  
ATOM    993  CD  LYS A 135      -0.420 -21.849 -25.827  1.00 90.48           C  
ANISOU  993  CD  LYS A 135    10276  14496   9605   -756  -2100   1139       C  
ATOM    994  CE  LYS A 135      -1.158 -22.798 -26.757  1.00 98.10           C  
ANISOU  994  CE  LYS A 135    11273  15266  10734   -566  -1869   1174       C  
ATOM    995  NZ  LYS A 135      -2.375 -23.366 -26.114  1.00 94.73           N  
ANISOU  995  NZ  LYS A 135    11009  14767  10219   -457  -1766   1122       N  
ATOM    996  N   SER A 136      -3.649 -17.704 -28.296  1.00 74.64           N  
ANISOU  996  N   SER A 136     8956  11640   7764  -1079  -1947    258       N  
ATOM    997  CA  SER A 136      -3.802 -16.963 -29.541  1.00 73.54           C  
ANISOU  997  CA  SER A 136     8848  11319   7775  -1128  -1892    171       C  
ATOM    998  C   SER A 136      -4.758 -15.783 -29.416  1.00 82.39           C  
ANISOU  998  C   SER A 136    10196  12278   8831  -1203  -1895    -58       C  
ATOM    999  O   SER A 136      -5.175 -15.227 -30.436  1.00103.04           O  
ANISOU  999  O   SER A 136    12866  14720  11563  -1207  -1820   -136       O  
ATOM   1000  CB  SER A 136      -4.274 -17.899 -30.656  1.00 69.61           C  
ANISOU 1000  CB  SER A 136     8299  10711   7438   -957  -1704    245       C  
ATOM   1001  OG  SER A 136      -5.551 -18.437 -30.361  1.00 59.63           O  
ANISOU 1001  OG  SER A 136     7163   9366   6127   -829  -1584    183       O  
ATOM   1002  N   ARG A 137      -5.113 -15.384 -28.194  1.00 84.17           N  
ANISOU 1002  N   ARG A 137    10557  12556   8868  -1252  -1975   -162       N  
ATOM   1003  CA  ARG A 137      -6.043 -14.273 -28.021  1.00 82.32           C  
ANISOU 1003  CA  ARG A 137    10551  12162   8566  -1301  -1963   -379       C  
ATOM   1004  C   ARG A 137      -5.357 -12.927 -28.229  1.00 87.05           C  
ANISOU 1004  C   ARG A 137    11195  12701   9179  -1509  -2094   -479       C  
ATOM   1005  O   ARG A 137      -5.930 -12.025 -28.850  1.00 79.44           O  
ANISOU 1005  O   ARG A 137    10363  11541   8279  -1536  -2041   -610       O  
ATOM   1006  CB  ARG A 137      -6.689 -14.346 -26.635  1.00 69.31           C  
ANISOU 1006  CB  ARG A 137     9045  10589   6700  -1267  -1985   -459       C  
ATOM   1007  CG  ARG A 137      -7.564 -13.152 -26.264  1.00 82.32           C  
ANISOU 1007  CG  ARG A 137    10941  12090   8247  -1315  -1981   -688       C  
ATOM   1008  CD  ARG A 137      -8.596 -12.831 -27.339  1.00 95.18           C  
ANISOU 1008  CD  ARG A 137    12650  13497  10017  -1223  -1822   -765       C  
ATOM   1009  NE  ARG A 137      -9.406 -13.987 -27.708  1.00102.55           N  
ANISOU 1009  NE  ARG A 137    13518  14426  11021  -1034  -1660   -670       N  
ATOM   1010  CZ  ARG A 137     -10.292 -13.987 -28.699  1.00102.74           C  
ANISOU 1010  CZ  ARG A 137    13567  14295  11173   -939  -1520   -700       C  
ATOM   1011  NH1 ARG A 137     -10.988 -15.082 -28.972  1.00108.18           N  
ANISOU 1011  NH1 ARG A 137    14196  14992  11918   -790  -1387   -616       N  
ATOM   1012  NH2 ARG A 137     -10.479 -12.890 -29.422  1.00 86.98           N  
ANISOU 1012  NH2 ARG A 137    11660  12139   9251   -998  -1514   -811       N  
ATOM   1013  N   LEU A 138      -4.130 -12.774 -27.729  1.00101.97           N  
ANISOU 1013  N   LEU A 138    12972  14756  11015  -1662  -2266   -409       N  
ATOM   1014  CA  LEU A 138      -3.438 -11.496 -27.849  1.00113.65           C  
ANISOU 1014  CA  LEU A 138    14495  16183  12505  -1887  -2403   -502       C  
ATOM   1015  C   LEU A 138      -2.941 -11.232 -29.264  1.00114.64           C  
ANISOU 1015  C   LEU A 138    14501  16208  12851  -1924  -2356   -430       C  
ATOM   1016  O   LEU A 138      -2.592 -10.090 -29.581  1.00122.97           O  
ANISOU 1016  O   LEU A 138    15619  17158  13948  -2097  -2429   -518       O  
ATOM   1017  CB  LEU A 138      -2.273 -11.440 -26.862  1.00113.06           C  
ANISOU 1017  CB  LEU A 138    14321  16339  12298  -2055  -2613   -443       C  
ATOM   1018  CG  LEU A 138      -2.678 -11.616 -25.397  1.00105.77           C  
ANISOU 1018  CG  LEU A 138    13524  15535  11128  -2036  -2678   -518       C  
ATOM   1019  CD1 LEU A 138      -1.458 -11.585 -24.496  1.00116.31           C  
ANISOU 1019  CD1 LEU A 138    14738  17122  12331  -2209  -2899   -444       C  
ATOM   1020  CD2 LEU A 138      -3.683 -10.551 -24.985  1.00 79.30           C  
ANISOU 1020  CD2 LEU A 138    10473  11991   7665  -2073  -2653   -773       C  
ATOM   1021  N   ARG A 139      -2.898 -12.255 -30.118  1.00100.71           N  
ANISOU 1021  N   ARG A 139    12574  14468  11223  -1768  -2232   -272       N  
ATOM   1022  CA  ARG A 139      -2.501 -12.088 -31.508  1.00 92.37           C  
ANISOU 1022  CA  ARG A 139    11410  13321  10364  -1776  -2165   -199       C  
ATOM   1023  C   ARG A 139      -3.686 -11.917 -32.449  1.00 92.32           C  
ANISOU 1023  C   ARG A 139    11536  13093  10449  -1651  -1994   -292       C  
ATOM   1024  O   ARG A 139      -3.484 -11.570 -33.618  1.00113.47           O  
ANISOU 1024  O   ARG A 139    14166  15674  13274  -1668  -1938   -261       O  
ATOM   1025  CB  ARG A 139      -1.655 -13.283 -31.965  1.00 86.76           C  
ANISOU 1025  CB  ARG A 139    10443  12771   9749  -1680  -2128     31       C  
ATOM   1026  N   ARG A 140      -4.905 -12.150 -31.973  1.00 64.73           N  
ANISOU 1026  N   ARG A 140     8196   9531   6866  -1527  -1909   -394       N  
ATOM   1027  CA  ARG A 140      -6.123 -12.024 -32.772  1.00 59.06           C  
ANISOU 1027  CA  ARG A 140     7595   8626   6219  -1403  -1753   -478       C  
ATOM   1028  C   ARG A 140      -6.913 -10.832 -32.236  1.00 72.61           C  
ANISOU 1028  C   ARG A 140     9549  10202   7838  -1462  -1776   -678       C  
ATOM   1029  O   ARG A 140      -7.773 -10.978 -31.366  1.00 89.11           O  
ANISOU 1029  O   ARG A 140    11764  12296   9799  -1385  -1746   -763       O  
ATOM   1030  CB  ARG A 140      -6.942 -13.311 -32.720  1.00 61.73           C  
ANISOU 1030  CB  ARG A 140     7906   9001   6549  -1204  -1622   -419       C  
ATOM   1031  CG  ARG A 140      -6.330 -14.473 -33.488  1.00 81.18           C  
ANISOU 1031  CG  ARG A 140    10167  11544   9132  -1117  -1559   -237       C  
ATOM   1032  CD  ARG A 140      -6.965 -15.804 -33.104  1.00 87.54           C  
ANISOU 1032  CD  ARG A 140    10952  12406   9904   -951  -1459   -172       C  
ATOM   1033  NE  ARG A 140      -8.423 -15.740 -33.054  1.00 99.74           N  
ANISOU 1033  NE  ARG A 140    12653  13832  11413   -860  -1355   -293       N  
ATOM   1034  CZ  ARG A 140      -9.133 -15.740 -31.929  1.00 98.68           C  
ANISOU 1034  CZ  ARG A 140    12632  13728  11136   -833  -1363   -366       C  
ATOM   1035  NH1 ARG A 140      -8.518 -15.805 -30.756  1.00 81.67           N  
ANISOU 1035  NH1 ARG A 140    10463  11718   8848   -892  -1477   -337       N  
ATOM   1036  NH2 ARG A 140     -10.456 -15.675 -31.976  1.00102.86           N  
ANISOU 1036  NH2 ARG A 140    13280  14155  11646   -744  -1257   -462       N  
ATOM   1037  N   THR A 141      -6.617  -9.651 -32.764  1.00 79.05           N  
ANISOU 1037  N   THR A 141    10430  10888   8718  -1593  -1819   -748       N  
ATOM   1038  CA  THR A 141      -7.261  -8.411 -32.354  1.00 76.68           C  
ANISOU 1038  CA  THR A 141    10366  10425   8343  -1655  -1836   -937       C  
ATOM   1039  C   THR A 141      -8.011  -7.802 -33.535  1.00 71.73           C  
ANISOU 1039  C   THR A 141     9817   9593   7846  -1585  -1712   -980       C  
ATOM   1040  O   THR A 141      -7.972  -8.310 -34.658  1.00 77.80           O  
ANISOU 1040  O   THR A 141    10454  10356   8750  -1508  -1627   -869       O  
ATOM   1041  CB  THR A 141      -6.236  -7.420 -31.793  1.00 82.89           C  
ANISOU 1041  CB  THR A 141    11196  11222   9077  -1895  -2012   -995       C  
ATOM   1042  OG1 THR A 141      -5.312  -7.050 -32.824  1.00 81.51           O  
ANISOU 1042  OG1 THR A 141    10891  11017   9061  -2010  -2044   -899       O  
ATOM   1043  CG2 THR A 141      -5.471  -8.043 -30.635  1.00106.03           C  
ANISOU 1043  CG2 THR A 141    14034  14385  11868  -1965  -2148   -939       C  
ATOM   1044  N   MET A 142      -8.702  -6.691 -33.265  1.00 71.89           N  
ANISOU 1044  N   MET A 142    10058   9443   7815  -1607  -1698  -1142       N  
ATOM   1045  CA  MET A 142      -9.450  -6.007 -34.314  1.00 65.54           C  
ANISOU 1045  CA  MET A 142     9339   8442   7121  -1535  -1584  -1181       C  
ATOM   1046  C   MET A 142      -8.524  -5.356 -35.333  1.00 69.74           C  
ANISOU 1046  C   MET A 142     9797   8901   7800  -1672  -1626  -1112       C  
ATOM   1047  O   MET A 142      -8.865  -5.283 -36.520  1.00 69.01           O  
ANISOU 1047  O   MET A 142     9668   8721   7832  -1592  -1525  -1057       O  
ATOM   1048  CB  MET A 142     -10.379  -4.962 -33.698  1.00 71.26           C  
ANISOU 1048  CB  MET A 142    10325   9000   7751  -1513  -1554  -1364       C  
ATOM   1049  CG  MET A 142     -11.433  -5.541 -32.769  1.00 78.30           C  
ANISOU 1049  CG  MET A 142    11295   9956   8502  -1356  -1486  -1428       C  
ATOM   1050  SD  MET A 142     -12.659  -6.528 -33.646  1.00 90.30           S  
ANISOU 1050  SD  MET A 142    12713  11491  10104  -1113  -1303  -1341       S  
ATOM   1051  CE  MET A 142     -13.405  -5.278 -34.690  1.00 93.26           C  
ANISOU 1051  CE  MET A 142    13224  11625  10587  -1063  -1209  -1407       C  
ATOM   1052  N   LEU A 143      -7.359  -4.875 -34.894  1.00 69.54           N  
ANISOU 1052  N   LEU A 143     9745   8920   7757  -1884  -1775  -1109       N  
ATOM   1053  CA  LEU A 143      -6.415  -4.261 -35.823  1.00 66.88           C  
ANISOU 1053  CA  LEU A 143     9323   8526   7562  -2030  -1816  -1028       C  
ATOM   1054  C   LEU A 143      -5.835  -5.293 -36.783  1.00 78.98           C  
ANISOU 1054  C   LEU A 143    10598  10199   9210  -1964  -1769   -833       C  
ATOM   1055  O   LEU A 143      -5.599  -4.990 -37.959  1.00 84.45           O  
ANISOU 1055  O   LEU A 143    11229  10819  10040  -1971  -1712   -755       O  
ATOM   1056  CB  LEU A 143      -5.300  -3.559 -35.048  1.00 64.68           C  
ANISOU 1056  CB  LEU A 143     9061   8281   7231  -2288  -1997  -1067       C  
ATOM   1057  CG  LEU A 143      -4.185  -2.913 -35.874  1.00 73.19           C  
ANISOU 1057  CG  LEU A 143    10033   9324   8453  -2478  -2059   -972       C  
ATOM   1058  CD1 LEU A 143      -4.749  -1.853 -36.807  1.00 75.53           C  
ANISOU 1058  CD1 LEU A 143    10479   9361   8857  -2464  -1961  -1023       C  
ATOM   1059  CD2 LEU A 143      -3.117  -2.322 -34.966  1.00 65.20           C  
ANISOU 1059  CD2 LEU A 143     9027   8374   7372  -2748  -2255  -1014       C  
ATOM   1060  N   VAL A 144      -5.603  -6.516 -36.304  1.00 79.48           N  
ANISOU 1060  N   VAL A 144    10519  10462   9218  -1890  -1783   -750       N  
ATOM   1061  CA  VAL A 144      -5.047  -7.559 -37.161  1.00 78.21           C  
ANISOU 1061  CA  VAL A 144    10128  10429   9161  -1811  -1726   -570       C  
ATOM   1062  C   VAL A 144      -6.057  -7.973 -38.225  1.00 78.06           C  
ANISOU 1062  C   VAL A 144    10125  10318   9216  -1617  -1556   -556       C  
ATOM   1063  O   VAL A 144      -5.694  -8.225 -39.381  1.00 85.82           O  
ANISOU 1063  O   VAL A 144    10986  11306  10316  -1583  -1491   -445       O  
ATOM   1064  CB  VAL A 144      -4.591  -8.759 -36.311  1.00 77.61           C  
ANISOU 1064  CB  VAL A 144     9915  10572   9003  -1769  -1777   -484       C  
ATOM   1065  CG1 VAL A 144      -4.048  -9.869 -37.199  1.00 72.67           C  
ANISOU 1065  CG1 VAL A 144     9069  10059   8484  -1666  -1700   -301       C  
ATOM   1066  CG2 VAL A 144      -3.545  -8.322 -35.297  1.00 73.72           C  
ANISOU 1066  CG2 VAL A 144     9390  10194   8428  -1973  -1961   -487       C  
ATOM   1067  N   ALA A 145      -7.339  -8.046 -37.858  1.00 71.44           N  
ANISOU 1067  N   ALA A 145     9435   9406   8304  -1489  -1483   -668       N  
ATOM   1068  CA  ALA A 145      -8.360  -8.457 -38.816  1.00 74.20           C  
ANISOU 1068  CA  ALA A 145     9794   9686   8713  -1314  -1334   -658       C  
ATOM   1069  C   ALA A 145      -8.529  -7.427 -39.925  1.00 81.15           C  
ANISOU 1069  C   ALA A 145    10736  10404   9692  -1338  -1287   -671       C  
ATOM   1070  O   ALA A 145      -8.773  -7.788 -41.082  1.00101.33           O  
ANISOU 1070  O   ALA A 145    13221  12947  12334  -1244  -1190   -600       O  
ATOM   1071  CB  ALA A 145      -9.687  -8.697 -38.099  1.00 82.07           C  
ANISOU 1071  CB  ALA A 145    10922  10653   9606  -1186  -1273   -766       C  
ATOM   1072  N   LYS A 146      -8.403  -6.140 -39.595  1.00 76.63           N  
ANISOU 1072  N   LYS A 146    10304   9704   9107  -1465  -1352   -762       N  
ATOM   1073  CA  LYS A 146      -8.560  -5.103 -40.609  1.00 84.45           C  
ANISOU 1073  CA  LYS A 146    11366  10526  10195  -1487  -1303   -765       C  
ATOM   1074  C   LYS A 146      -7.358  -5.055 -41.545  1.00 76.41           C  
ANISOU 1074  C   LYS A 146    10186   9552   9294  -1593  -1328   -623       C  
ATOM   1075  O   LYS A 146      -7.514  -4.846 -42.753  1.00 71.72           O  
ANISOU 1075  O   LYS A 146     9565   8893   8793  -1539  -1243   -558       O  
ATOM   1076  CB  LYS A 146      -8.783  -3.745 -39.943  1.00 94.47           C  
ANISOU 1076  CB  LYS A 146    12853  11622  11419  -1590  -1357   -907       C  
ATOM   1077  CG  LYS A 146     -10.072  -3.658 -39.142  1.00 89.65           C  
ANISOU 1077  CG  LYS A 146    12417  10948  10696  -1461  -1304  -1047       C  
ATOM   1078  CD  LYS A 146     -10.269  -2.271 -38.552  1.00 85.55           C  
ANISOU 1078  CD  LYS A 146    12134  10237  10136  -1551  -1341  -1192       C  
ATOM   1079  CE  LYS A 146     -11.570  -2.187 -37.769  1.00 94.53           C  
ANISOU 1079  CE  LYS A 146    13441  11318  11156  -1400  -1270  -1324       C  
ATOM   1080  NZ  LYS A 146     -11.783  -0.833 -37.187  1.00101.09           N  
ANISOU 1080  NZ  LYS A 146    14524  11944  11940  -1470  -1290  -1476       N  
ATOM   1081  N   VAL A 147      -6.151  -5.246 -41.006  1.00 69.20           N  
ANISOU 1081  N   VAL A 147     9155   8763   8373  -1742  -1443   -563       N  
ATOM   1082  CA  VAL A 147      -4.964  -5.285 -41.855  1.00 72.05           C  
ANISOU 1082  CA  VAL A 147     9335   9195   8846  -1835  -1460   -409       C  
ATOM   1083  C   VAL A 147      -4.958  -6.547 -42.709  1.00 72.80           C  
ANISOU 1083  C   VAL A 147     9261   9414   8986  -1671  -1355   -283       C  
ATOM   1084  O   VAL A 147      -4.470  -6.534 -43.846  1.00 74.02           O  
ANISOU 1084  O   VAL A 147     9310   9575   9239  -1666  -1297   -169       O  
ATOM   1085  CB  VAL A 147      -3.691  -5.168 -40.996  1.00 75.22           C  
ANISOU 1085  CB  VAL A 147     9640   9718   9223  -2037  -1617   -371       C  
ATOM   1086  CG1 VAL A 147      -2.443  -5.304 -41.855  1.00 79.05           C  
ANISOU 1086  CG1 VAL A 147     9906  10305   9825  -2121  -1626   -190       C  
ATOM   1087  CG2 VAL A 147      -3.677  -3.840 -40.255  1.00 75.98           C  
ANISOU 1087  CG2 VAL A 147     9925   9667   9277  -2221  -1722   -509       C  
ATOM   1088  N   THR A 148      -5.503  -7.649 -42.190  1.00 72.72           N  
ANISOU 1088  N   THR A 148     9232   9497   8902  -1535  -1322   -302       N  
ATOM   1089  CA  THR A 148      -5.623  -8.859 -42.996  1.00 85.41           C  
ANISOU 1089  CA  THR A 148    10713  11191  10547  -1375  -1212   -205       C  
ATOM   1090  C   THR A 148      -6.534  -8.629 -44.196  1.00 78.56           C  
ANISOU 1090  C   THR A 148     9915  10205   9729  -1263  -1090   -225       C  
ATOM   1091  O   THR A 148      -6.245  -9.096 -45.304  1.00 83.19           O  
ANISOU 1091  O   THR A 148    10396  10829  10383  -1199  -1010   -124       O  
ATOM   1092  CB  THR A 148      -6.145 -10.013 -42.138  1.00 93.03           C  
ANISOU 1092  CB  THR A 148    11673  12249  11424  -1261  -1198   -232       C  
ATOM   1093  OG1 THR A 148      -5.180 -10.334 -41.127  1.00 94.83           O  
ANISOU 1093  OG1 THR A 148    11807  12618  11606  -1353  -1310   -181       O  
ATOM   1094  CG2 THR A 148      -6.405 -11.248 -42.991  1.00 95.93           C  
ANISOU 1094  CG2 THR A 148    11946  12671  11832  -1097  -1075   -153       C  
ATOM   1095  N   CYS A 149      -7.628  -7.889 -43.999  1.00 77.59           N  
ANISOU 1095  N   CYS A 149     9969   9944   9567  -1232  -1072   -349       N  
ATOM   1096  CA  CYS A 149      -8.581  -7.676 -45.083  1.00 79.81           C  
ANISOU 1096  CA  CYS A 149    10311  10130   9884  -1116   -963   -362       C  
ATOM   1097  C   CYS A 149      -8.006  -6.771 -46.167  1.00 75.72           C  
ANISOU 1097  C   CYS A 149     9774   9536   9459  -1189   -948   -288       C  
ATOM   1098  O   CYS A 149      -8.194  -7.033 -47.361  1.00 91.10           O  
ANISOU 1098  O   CYS A 149    11671  11491  11451  -1100   -858   -220       O  
ATOM   1099  CB  CYS A 149      -9.883  -7.097 -44.531  1.00 86.52           C  
ANISOU 1099  CB  CYS A 149    11343  10864  10668  -1054   -945   -500       C  
ATOM   1100  SG  CYS A 149     -10.826  -8.247 -43.504  1.00 91.25           S  
ANISOU 1100  SG  CYS A 149    11958  11553  11160   -932   -924   -571       S  
ATOM   1101  N   ILE A 150      -7.304  -5.703 -45.777  1.00 69.45           N  
ANISOU 1101  N   ILE A 150     9026   8670   8692  -1356  -1034   -297       N  
ATOM   1102  CA  ILE A 150      -6.760  -4.791 -46.780  1.00 85.44           C  
ANISOU 1102  CA  ILE A 150    11038  10612  10812  -1437  -1015   -217       C  
ATOM   1103  C   ILE A 150      -5.659  -5.468 -47.587  1.00 95.05           C  
ANISOU 1103  C   ILE A 150    12048  11972  12096  -1453   -991    -56       C  
ATOM   1104  O   ILE A 150      -5.445  -5.133 -48.758  1.00111.21           O  
ANISOU 1104  O   ILE A 150    14055  13988  14211  -1441   -923     36       O  
ATOM   1105  CB  ILE A 150      -6.265  -3.486 -46.125  1.00 83.46           C  
ANISOU 1105  CB  ILE A 150    10896  10236  10580  -1632  -1116   -271       C  
ATOM   1106  CG1 ILE A 150      -5.101  -3.758 -45.173  1.00101.78           C  
ANISOU 1106  CG1 ILE A 150    13109  12682  12880  -1794  -1244   -246       C  
ATOM   1107  CG2 ILE A 150      -7.406  -2.790 -45.397  1.00 74.25           C  
ANISOU 1107  CG2 ILE A 150     9954   8912   9344  -1589  -1117   -434       C  
ATOM   1108  CD1 ILE A 150      -4.546  -2.513 -44.515  1.00118.44           C  
ANISOU 1108  CD1 ILE A 150    15323  14676  15002  -2015  -1358   -307       C  
ATOM   1109  N   ILE A 151      -4.947  -6.426 -46.989  1.00 84.05           N  
ANISOU 1109  N   ILE A 151    10518  10738  10678  -1469  -1037    -10       N  
ATOM   1110  CA  ILE A 151      -4.006  -7.229 -47.762  1.00 82.92           C  
ANISOU 1110  CA  ILE A 151    10177  10739  10591  -1439   -989    145       C  
ATOM   1111  C   ILE A 151      -4.759  -8.148 -48.715  1.00 84.06           C  
ANISOU 1111  C   ILE A 151    10311  10906  10722  -1240   -855    158       C  
ATOM   1112  O   ILE A 151      -4.349  -8.347 -49.865  1.00 86.94           O  
ANISOU 1112  O   ILE A 151    10585  11309  11138  -1194   -773    264       O  
ATOM   1113  CB  ILE A 151      -3.076  -8.019 -46.822  1.00 73.68           C  
ANISOU 1113  CB  ILE A 151     8864   9734   9396  -1491  -1071    199       C  
ATOM   1114  CG1 ILE A 151      -2.146  -7.068 -46.067  1.00 79.48           C  
ANISOU 1114  CG1 ILE A 151     9581  10469  10149  -1718  -1213    208       C  
ATOM   1115  CG2 ILE A 151      -2.267  -9.046 -47.600  1.00 69.96           C  
ANISOU 1115  CG2 ILE A 151     8197   9412   8974  -1406   -992    355       C  
ATOM   1116  CD1 ILE A 151      -1.159  -7.772 -45.161  1.00 84.65           C  
ANISOU 1116  CD1 ILE A 151    10076  11311  10775  -1780  -1308    280       C  
ATOM   1117  N   ILE A 152      -5.880  -8.711 -48.257  1.00 82.65           N  
ANISOU 1117  N   ILE A 152    10226  10706  10470  -1125   -832     50       N  
ATOM   1118  CA  ILE A 152      -6.696  -9.562 -49.118  1.00 79.50           C  
ANISOU 1118  CA  ILE A 152     9831  10323  10054   -956   -717     45       C  
ATOM   1119  C   ILE A 152      -7.253  -8.759 -50.287  1.00 72.73           C  
ANISOU 1119  C   ILE A 152     9045   9365   9223   -923   -652     48       C  
ATOM   1120  O   ILE A 152      -7.342  -9.260 -51.415  1.00 71.26           O  
ANISOU 1120  O   ILE A 152     8811   9218   9046   -829   -560    104       O  
ATOM   1121  CB  ILE A 152      -7.812 -10.235 -48.296  1.00 71.35           C  
ANISOU 1121  CB  ILE A 152     8882   9286   8942   -865   -714    -69       C  
ATOM   1122  CG1 ILE A 152      -7.216 -11.297 -47.369  1.00 71.49           C  
ANISOU 1122  CG1 ILE A 152     8806   9425   8933   -864   -752    -37       C  
ATOM   1123  CG2 ILE A 152      -8.867 -10.848 -49.204  1.00 72.44           C  
ANISOU 1123  CG2 ILE A 152     9053   9411   9060   -719   -610    -96       C  
ATOM   1124  CD1 ILE A 152      -8.233 -11.990 -46.495  1.00 66.21           C  
ANISOU 1124  CD1 ILE A 152     8211   8759   8187   -784   -747   -132       C  
ATOM   1125  N   TRP A 153      -7.624  -7.498 -50.044  1.00 75.87           N  
ANISOU 1125  N   TRP A 153     9566   9631   9629   -995   -695     -9       N  
ATOM   1126  CA  TRP A 153      -8.077  -6.648 -51.141  1.00 81.34           C  
ANISOU 1126  CA  TRP A 153    10324  10227  10353   -963   -634     16       C  
ATOM   1127  C   TRP A 153      -6.963  -6.419 -52.155  1.00 80.77           C  
ANISOU 1127  C   TRP A 153    10138  10196  10354  -1022   -602    162       C  
ATOM   1128  O   TRP A 153      -7.213  -6.378 -53.365  1.00 79.35           O  
ANISOU 1128  O   TRP A 153     9951  10016  10183   -942   -517    221       O  
ATOM   1129  CB  TRP A 153      -8.589  -5.306 -50.611  1.00 81.15           C  
ANISOU 1129  CB  TRP A 153    10463  10037  10335  -1030   -682    -65       C  
ATOM   1130  CG  TRP A 153      -9.724  -5.381 -49.622  1.00 88.91           C  
ANISOU 1130  CG  TRP A 153    11566  10973  11241   -963   -701   -205       C  
ATOM   1131  CD1 TRP A 153      -9.812  -4.713 -48.435  1.00109.81           C  
ANISOU 1131  CD1 TRP A 153    14327  13534  13861  -1045   -776   -303       C  
ATOM   1132  CD2 TRP A 153     -10.931  -6.149 -49.738  1.00 88.04           C  
ANISOU 1132  CD2 TRP A 153    11477  10904  11070   -804   -640   -261       C  
ATOM   1133  NE1 TRP A 153     -10.991  -5.020 -47.803  1.00115.96           N  
ANISOU 1133  NE1 TRP A 153    15192  14303  14563   -934   -756   -410       N  
ATOM   1134  CE2 TRP A 153     -11.696  -5.899 -48.581  1.00102.65           C  
ANISOU 1134  CE2 TRP A 153    13443  12696  12862   -791   -675   -381       C  
ATOM   1135  CE3 TRP A 153     -11.438  -7.026 -50.703  1.00 98.30           C  
ANISOU 1135  CE3 TRP A 153    12710  12286  12354   -681   -560   -224       C  
ATOM   1136  CZ2 TRP A 153     -12.937  -6.492 -48.365  1.00106.28           C  
ANISOU 1136  CZ2 TRP A 153    13937  13186  13259   -658   -629   -449       C  
ATOM   1137  CZ3 TRP A 153     -12.670  -7.613 -50.485  1.00105.92           C  
ANISOU 1137  CZ3 TRP A 153    13713  13274  13256   -565   -527   -301       C  
ATOM   1138  CH2 TRP A 153     -13.406  -7.344 -49.326  1.00102.31           C  
ANISOU 1138  CH2 TRP A 153    13354  12765  12752   -554   -559   -405       C  
ATOM   1139  N   LEU A 154      -5.725  -6.267 -51.679  1.00 76.43           N  
ANISOU 1139  N   LEU A 154     9493   9695   9853  -1164   -669    229       N  
ATOM   1140  CA  LEU A 154      -4.610  -6.032 -52.592  1.00 71.61           C  
ANISOU 1140  CA  LEU A 154     8756   9136   9317  -1227   -635    383       C  
ATOM   1141  C   LEU A 154      -4.225  -7.304 -53.337  1.00 79.65           C  
ANISOU 1141  C   LEU A 154     9634  10308  10323  -1105   -544    469       C  
ATOM   1142  O   LEU A 154      -3.955  -7.263 -54.543  1.00 91.38           O  
ANISOU 1142  O   LEU A 154    11067  11821  11833  -1058   -455    568       O  
ATOM   1143  CB  LEU A 154      -3.411  -5.473 -51.826  1.00 67.14           C  
ANISOU 1143  CB  LEU A 154     8116   8587   8808  -1428   -742    434       C  
ATOM   1144  CG  LEU A 154      -3.579  -4.069 -51.242  1.00 80.20           C  
ANISOU 1144  CG  LEU A 154     9917  10067  10486  -1580   -826    360       C  
ATOM   1145  CD1 LEU A 154      -2.285  -3.598 -50.594  1.00 86.08           C  
ANISOU 1145  CD1 LEU A 154    10567  10852  11287  -1801   -938    421       C  
ATOM   1146  CD2 LEU A 154      -4.035  -3.090 -52.313  1.00 77.85           C  
ANISOU 1146  CD2 LEU A 154     9717   9629  10234  -1557   -750    396       C  
ATOM   1147  N   LEU A 155      -4.191  -8.442 -52.640  1.00 81.34           N  
ANISOU 1147  N   LEU A 155     9793  10619  10496  -1046   -559    435       N  
ATOM   1148  CA  LEU A 155      -3.852  -9.697 -53.302  1.00 79.70           C  
ANISOU 1148  CA  LEU A 155     9472  10535  10276   -919   -463    506       C  
ATOM   1149  C   LEU A 155      -4.925 -10.113 -54.301  1.00 79.76           C  
ANISOU 1149  C   LEU A 155     9564  10510  10230   -768   -361    453       C  
ATOM   1150  O   LEU A 155      -4.607 -10.716 -55.332  1.00 89.67           O  
ANISOU 1150  O   LEU A 155    10755  11835  11482   -680   -261    526       O  
ATOM   1151  CB  LEU A 155      -3.632 -10.800 -52.267  1.00 80.67           C  
ANISOU 1151  CB  LEU A 155     9533  10748  10369   -887   -500    483       C  
ATOM   1152  CG  LEU A 155      -2.449 -10.608 -51.315  1.00 78.43           C  
ANISOU 1152  CG  LEU A 155     9131  10544  10126  -1025   -603    557       C  
ATOM   1153  CD1 LEU A 155      -2.271 -11.827 -50.423  1.00 74.85           C  
ANISOU 1153  CD1 LEU A 155     8611  10194   9635   -958   -621    556       C  
ATOM   1154  CD2 LEU A 155      -1.173 -10.313 -52.090  1.00 70.16           C  
ANISOU 1154  CD2 LEU A 155     7924   9577   9155  -1086   -571    725       C  
ATOM   1155  N   ALA A 156      -6.192  -9.805 -54.017  1.00 77.38           N  
ANISOU 1155  N   ALA A 156     9406  10113   9881   -736   -384    328       N  
ATOM   1156  CA  ALA A 156      -7.252 -10.102 -54.974  1.00 85.00           C  
ANISOU 1156  CA  ALA A 156    10444  11061  10793   -609   -303    283       C  
ATOM   1157  C   ALA A 156      -7.202  -9.148 -56.161  1.00 86.31           C  
ANISOU 1157  C   ALA A 156    10629  11185  10979   -616   -256    357       C  
ATOM   1158  O   ALA A 156      -7.391  -9.566 -57.309  1.00 92.07           O  
ANISOU 1158  O   ALA A 156    11346  11964  11672   -521   -169    392       O  
ATOM   1159  CB  ALA A 156      -8.616 -10.039 -54.289  1.00 89.52           C  
ANISOU 1159  CB  ALA A 156    11140  11561  11312   -571   -341    145       C  
ATOM   1160  N   GLY A 157      -6.950  -7.863 -55.903  1.00 77.44           N  
ANISOU 1160  N   GLY A 157     9546   9969   9910   -729   -312    383       N  
ATOM   1161  CA  GLY A 157      -6.796  -6.918 -56.997  1.00 74.28           C  
ANISOU 1161  CA  GLY A 157     9160   9523   9541   -743   -264    477       C  
ATOM   1162  C   GLY A 157      -5.568  -7.206 -57.839  1.00 84.33           C  
ANISOU 1162  C   GLY A 157    10291  10901  10849   -758   -199    626       C  
ATOM   1163  O   GLY A 157      -5.585  -7.028 -59.060  1.00 97.98           O  
ANISOU 1163  O   GLY A 157    12014  12652  12561   -698   -115    704       O  
ATOM   1164  N   LEU A 158      -4.484  -7.652 -57.199  1.00 74.06           N  
ANISOU 1164  N   LEU A 158     8869   9678   9593   -831   -233    675       N  
ATOM   1165  CA  LEU A 158      -3.301  -8.066 -57.945  1.00 75.00           C  
ANISOU 1165  CA  LEU A 158     8833   9918   9744   -824   -158    824       C  
ATOM   1166  C   LEU A 158      -3.579  -9.309 -58.781  1.00 77.74           C  
ANISOU 1166  C   LEU A 158     9162  10360  10017   -651    -47    815       C  
ATOM   1167  O   LEU A 158      -3.016  -9.461 -59.872  1.00 88.74           O  
ANISOU 1167  O   LEU A 158    10486  11828  11405   -597     53    924       O  
ATOM   1168  CB  LEU A 158      -2.138  -8.319 -56.986  1.00 73.18           C  
ANISOU 1168  CB  LEU A 158     8465   9765   9574   -931   -227    882       C  
ATOM   1169  CG  LEU A 158      -0.800  -8.741 -57.597  1.00 86.87           C  
ANISOU 1169  CG  LEU A 158    10011  11642  11354   -926   -153   1053       C  
ATOM   1170  CD1 LEU A 158      -0.222  -7.623 -58.451  1.00 99.76           C  
ANISOU 1170  CD1 LEU A 158    11606  13250  13049  -1019   -120   1186       C  
ATOM   1171  CD2 LEU A 158       0.180  -9.156 -56.511  1.00 84.65           C  
ANISOU 1171  CD2 LEU A 158     9589  11458  11118  -1010   -233   1100       C  
ATOM   1172  N   ALA A 159      -4.444 -10.200 -58.293  1.00 63.96           N  
ANISOU 1172  N   ALA A 159     7483   8611   8209   -565    -58    686       N  
ATOM   1173  CA  ALA A 159      -4.791 -11.395 -59.053  1.00 65.97           C  
ANISOU 1173  CA  ALA A 159     7744   8932   8390   -415     42    656       C  
ATOM   1174  C   ALA A 159      -5.736 -11.072 -60.204  1.00 80.98           C  
ANISOU 1174  C   ALA A 159     9745  10804  10220   -342     96    626       C  
ATOM   1175  O   ALA A 159      -5.637 -11.672 -61.279  1.00 76.36           O  
ANISOU 1175  O   ALA A 159     9147  10289   9578   -245    197    657       O  
ATOM   1176  CB  ALA A 159      -5.411 -12.442 -58.128  1.00 51.90           C  
ANISOU 1176  CB  ALA A 159     6001   7147   6573   -366      9    535       C  
ATOM   1177  N   SER A 160      -6.657 -10.132 -59.997  1.00 89.93           N  
ANISOU 1177  N   SER A 160    10982  11840  11349   -380     33    566       N  
ATOM   1178  CA  SER A 160      -7.559  -9.683 -61.050  1.00 98.46           C  
ANISOU 1178  CA  SER A 160    12146  12901  12364   -313     72    557       C  
ATOM   1179  C   SER A 160      -6.934  -8.621 -61.945  1.00 98.89           C  
ANISOU 1179  C   SER A 160    12174  12946  12453   -353    113    699       C  
ATOM   1180  O   SER A 160      -7.638  -8.039 -62.776  1.00 86.32           O  
ANISOU 1180  O   SER A 160    10653  11332  10813   -305    137    714       O  
ATOM   1181  CB  SER A 160      -8.857  -9.147 -60.440  1.00104.58           C  
ANISOU 1181  CB  SER A 160    13036  13580  13120   -315     -2    446       C  
ATOM   1182  OG  SER A 160      -8.617  -7.976 -59.678  1.00115.73           O  
ANISOU 1182  OG  SER A 160    14474  14885  14611   -424    -72    466       O  
ATOM   1183  N   LEU A 161      -5.637  -8.359 -61.787  1.00102.72           N  
ANISOU 1183  N   LEU A 161    12552  13456  13020   -441    119    813       N  
ATOM   1184  CA  LEU A 161      -4.978  -7.356 -62.618  1.00101.53           C  
ANISOU 1184  CA  LEU A 161    12366  13297  12913   -493    164    964       C  
ATOM   1185  C   LEU A 161      -4.967  -7.708 -64.103  1.00102.45           C  
ANISOU 1185  C   LEU A 161    12471  13512  12944   -374    285   1037       C  
ATOM   1186  O   LEU A 161      -5.206  -6.800 -64.920  1.00117.58           O  
ANISOU 1186  O   LEU A 161    14433  15396  14848   -371    315   1114       O  
ATOM   1187  CB  LEU A 161      -3.553  -7.118 -62.100  1.00 96.40           C  
ANISOU 1187  CB  LEU A 161    11580  12676  12370   -622    143   1077       C  
ATOM   1188  CG  LEU A 161      -2.852  -5.846 -62.580  1.00 91.02           C  
ANISOU 1188  CG  LEU A 161    10865  11948  11770   -736    155   1229       C  
ATOM   1189  CD1 LEU A 161      -3.616  -4.614 -62.122  1.00 75.33           C  
ANISOU 1189  CD1 LEU A 161     9019   9784   9820   -817     74   1172       C  
ATOM   1190  CD2 LEU A 161      -1.416  -5.807 -62.082  1.00 95.60           C  
ANISOU 1190  CD2 LEU A 161    11283  12592  12451   -866    133   1343       C  
ATOM   1191  N   PRO A 162      -4.699  -8.950 -64.529  1.00 92.70           N  
ANISOU 1191  N   PRO A 162    11186  12392  11643   -273    363   1021       N  
ATOM   1192  CA  PRO A 162      -4.797  -9.255 -65.966  1.00 84.85           C  
ANISOU 1192  CA  PRO A 162    10208  11488  10543   -157    477   1070       C  
ATOM   1193  C   PRO A 162      -6.200  -9.106 -66.525  1.00 81.74           C  
ANISOU 1193  C   PRO A 162     9947  11069  10043    -85    459    978       C  
ATOM   1194  O   PRO A 162      -6.346  -8.884 -67.733  1.00 92.61           O  
ANISOU 1194  O   PRO A 162    11349  12504  11334    -18    531   1043       O  
ATOM   1195  CB  PRO A 162      -4.310 -10.709 -66.054  1.00 87.59           C  
ANISOU 1195  CB  PRO A 162    10501  11934  10845    -66    553   1035       C  
ATOM   1196  CG  PRO A 162      -4.491 -11.254 -64.680  1.00 83.14           C  
ANISOU 1196  CG  PRO A 162     9935  11319  10337   -108    463    926       C  
ATOM   1197  CD  PRO A 162      -4.192 -10.109 -63.772  1.00 82.16           C  
ANISOU 1197  CD  PRO A 162     9780  11112  10327   -255    361    974       C  
ATOM   1198  N   ALA A 163      -7.237  -9.222 -65.692  1.00 89.27           N  
ANISOU 1198  N   ALA A 163    10977  11950  10992    -93    368    837       N  
ATOM   1199  CA  ALA A 163      -8.604  -8.995 -66.146  1.00102.60           C  
ANISOU 1199  CA  ALA A 163    12771  13624  12589    -31    340    764       C  
ATOM   1200  C   ALA A 163      -8.892  -7.521 -66.400  1.00108.56           C  
ANISOU 1200  C   ALA A 163    13569  14298  13380    -67    315    854       C  
ATOM   1201  O   ALA A 163      -9.948  -7.193 -66.948  1.00117.26           O  
ANISOU 1201  O   ALA A 163    14744  15404  14405     -2    303    832       O  
ATOM   1202  CB  ALA A 163      -9.594  -9.556 -65.123  1.00105.50           C  
ANISOU 1202  CB  ALA A 163    13191  13945  12950    -30    258    601       C  
ATOM   1203  N   ILE A 164      -7.980  -6.629 -66.015  1.00107.43           N  
ANISOU 1203  N   ILE A 164    13382  14081  13355   -171    305    959       N  
ATOM   1204  CA  ILE A 164      -8.103  -5.212 -66.317  1.00 98.93           C  
ANISOU 1204  CA  ILE A 164    12354  12909  12327   -211    298   1062       C  
ATOM   1205  C   ILE A 164      -7.248  -4.807 -67.514  1.00 99.59           C  
ANISOU 1205  C   ILE A 164    12381  13059  12401   -205    396   1241       C  
ATOM   1206  O   ILE A 164      -7.596  -3.849 -68.216  1.00101.12           O  
ANISOU 1206  O   ILE A 164    12627  13212  12581   -184    419   1336       O  
ATOM   1207  CB  ILE A 164      -7.749  -4.356 -65.080  1.00 90.60           C  
ANISOU 1207  CB  ILE A 164    11312  11701  11410   -351    215   1054       C  
ATOM   1208  CG1 ILE A 164      -8.317  -5.008 -63.816  1.00107.74           C  
ANISOU 1208  CG1 ILE A 164    13512  13841  13582   -359    132    883       C  
ATOM   1209  CG2 ILE A 164      -8.278  -2.940 -65.235  1.00 81.86           C  
ANISOU 1209  CG2 ILE A 164    10304  10454  10345   -371    199   1113       C  
ATOM   1210  CD1 ILE A 164      -7.923  -4.313 -62.537  1.00121.09           C  
ANISOU 1210  CD1 ILE A 164    15221  15402  15385   -497     47    855       C  
ATOM   1211  N   ILE A 165      -6.160  -5.522 -67.780  1.00 96.03           N  
ANISOU 1211  N   ILE A 165    11822  12714  11953   -210    464   1299       N  
ATOM   1212  CA  ILE A 165      -5.215  -5.137 -68.822  1.00 93.32           C  
ANISOU 1212  CA  ILE A 165    11406  12442  11610   -212    568   1483       C  
ATOM   1213  C   ILE A 165      -5.579  -5.761 -70.161  1.00 99.85           C  
ANISOU 1213  C   ILE A 165    12259  13410  12272    -63    663   1495       C  
ATOM   1214  O   ILE A 165      -5.587  -5.081 -71.190  1.00 99.92           O  
ANISOU 1214  O   ILE A 165    12286  13447  12232    -28    726   1623       O  
ATOM   1215  CB  ILE A 165      -3.779  -5.520 -68.396  1.00 89.78           C  
ANISOU 1215  CB  ILE A 165    10811  12047  11256   -292    598   1560       C  
ATOM   1216  CG1 ILE A 165      -3.410  -4.845 -67.076  1.00 94.02           C  
ANISOU 1216  CG1 ILE A 165    11325  12454  11943   -459    488   1546       C  
ATOM   1217  CG2 ILE A 165      -2.761  -5.173 -69.492  1.00 92.47           C  
ANISOU 1217  CG2 ILE A 165    11058  12479  11598   -289    720   1763       C  
ATOM   1218  CD1 ILE A 165      -3.388  -3.334 -67.146  1.00104.32           C  
ANISOU 1218  CD1 ILE A 165    12679  13623  13336   -568    462   1650       C  
ATOM   1219  N   HIS A 166      -5.891  -7.059 -70.164  1.00 97.44           N  
ANISOU 1219  N   HIS A 166    11963  13188  11871     23    676   1362       N  
ATOM   1220  CA  HIS A 166      -6.086  -7.809 -71.397  1.00 90.88           C  
ANISOU 1220  CA  HIS A 166    11160  12497  10874    152    771   1354       C  
ATOM   1221  C   HIS A 166      -7.549  -7.965 -71.795  1.00 86.82           C  
ANISOU 1221  C   HIS A 166    10763  11999  10227    228    719   1236       C  
ATOM   1222  O   HIS A 166      -7.824  -8.469 -72.890  1.00 89.10           O  
ANISOU 1222  O   HIS A 166    11090  12405  10357    325    783   1226       O  
ATOM   1223  CB  HIS A 166      -5.436  -9.192 -71.272  1.00 89.10           C  
ANISOU 1223  CB  HIS A 166    10881  12352  10621    202    835   1287       C  
ATOM   1224  CG  HIS A 166      -3.966  -9.144 -70.995  1.00 96.35           C  
ANISOU 1224  CG  HIS A 166    11660  13293  11656    147    896   1422       C  
ATOM   1225  ND1 HIS A 166      -3.446  -8.782 -69.770  1.00102.27           N  
ANISOU 1225  ND1 HIS A 166    12335  13957  12565     24    816   1439       N  
ATOM   1226  CD2 HIS A 166      -2.902  -9.405 -71.791  1.00104.60           C  
ANISOU 1226  CD2 HIS A 166    12618  14450  12675    200   1031   1552       C  
ATOM   1227  CE1 HIS A 166      -2.127  -8.827 -69.823  1.00105.07           C  
ANISOU 1227  CE1 HIS A 166    12551  14377  12992     -5    889   1578       C  
ATOM   1228  NE2 HIS A 166      -1.772  -9.202 -71.038  1.00105.01           N  
ANISOU 1228  NE2 HIS A 166    12530  14489  12879    106   1026   1654       N  
ATOM   1229  N   ARG A 167      -8.488  -7.560 -70.944  1.00 78.80           N  
ANISOU 1229  N   ARG A 167     9801  10877   9262    188    607   1147       N  
ATOM   1230  CA  ARG A 167      -9.910  -7.635 -71.275  1.00 74.54           C  
ANISOU 1230  CA  ARG A 167     9351  10364   8607    256    551   1051       C  
ATOM   1231  C   ARG A 167     -10.270  -6.445 -72.155  1.00 84.97           C  
ANISOU 1231  C   ARG A 167    10706  11690   9888    290    566   1191       C  
ATOM   1232  O   ARG A 167     -10.432  -5.324 -71.670  1.00 86.55           O  
ANISOU 1232  O   ARG A 167    10925  11766  10194    240    521   1256       O  
ATOM   1233  CB  ARG A 167     -10.759  -7.658 -70.010  1.00 89.62           C  
ANISOU 1233  CB  ARG A 167    11294  12169  10588    213    440    917       C  
ATOM   1234  CG  ARG A 167     -11.218  -9.041 -69.587  1.00 89.60           C  
ANISOU 1234  CG  ARG A 167    11303  12211  10529    235    415    744       C  
ATOM   1235  CD  ARG A 167     -12.410  -9.512 -70.405  1.00 64.22           C  
ANISOU 1235  CD  ARG A 167     8149   9098   7153    313    397    664       C  
ATOM   1236  NE  ARG A 167     -12.917 -10.797 -69.929  1.00 74.02           N  
ANISOU 1236  NE  ARG A 167     9410  10360   8355    314    368    495       N  
ATOM   1237  CZ  ARG A 167     -14.091 -11.313 -70.276  1.00 77.20           C  
ANISOU 1237  CZ  ARG A 167     9859  10831   8642    347    322    391       C  
ATOM   1238  NH1 ARG A 167     -14.892 -10.652 -71.100  1.00 74.54           N  
ANISOU 1238  NH1 ARG A 167     9546  10565   8210    392    296    442       N  
ATOM   1239  NH2 ARG A 167     -14.468 -12.488 -69.793  1.00 81.48           N  
ANISOU 1239  NH2 ARG A 167    10418  11375   9165    331    301    244       N  
ATOM   1240  N   ASN A 168     -10.401  -6.686 -73.455  1.00 92.81           N  
ANISOU 1240  N   ASN A 168    11718  12824  10723    377    631   1239       N  
ATOM   1241  CA  ASN A 168     -10.765  -5.652 -74.410  1.00 85.25           C  
ANISOU 1241  CA  ASN A 168    10792  11897   9701    428    651   1385       C  
ATOM   1242  C   ASN A 168     -12.002  -6.077 -75.189  1.00 76.41           C  
ANISOU 1242  C   ASN A 168     9733  10908   8393    524    614   1308       C  
ATOM   1243  O   ASN A 168     -12.401  -7.245 -75.187  1.00 66.12           O  
ANISOU 1243  O   ASN A 168     8446   9682   6993    544    593   1150       O  
ATOM   1244  CB  ASN A 168      -9.607  -5.349 -75.371  1.00 90.62           C  
ANISOU 1244  CB  ASN A 168    11426  12646  10359    440    776   1564       C  
ATOM   1245  CG  ASN A 168      -8.476  -4.595 -74.700  1.00105.90           C  
ANISOU 1245  CG  ASN A 168    13293  14454  12492    328    801   1683       C  
ATOM   1246  OD1 ASN A 168      -8.489  -3.366 -74.633  1.00109.28           O  
ANISOU 1246  OD1 ASN A 168    13736  14774  13011    285    788   1809       O  
ATOM   1247  ND2 ASN A 168      -7.489  -5.330 -74.201  1.00112.75           N  
ANISOU 1247  ND2 ASN A 168    14083  15331  13425    279    836   1649       N  
ATOM   1248  N   VAL A 169     -12.610  -5.104 -75.859  1.00 81.88           N  
ANISOU 1248  N   VAL A 169    10457  11623   9031    578    603   1428       N  
ATOM   1249  CA  VAL A 169     -13.786  -5.340 -76.687  1.00 85.55           C  
ANISOU 1249  CA  VAL A 169    10963  12233   9308    668    559   1390       C  
ATOM   1250  C   VAL A 169     -13.321  -5.629 -78.108  1.00 93.97           C  
ANISOU 1250  C   VAL A 169    12038  13474  10194    734    652   1473       C  
ATOM   1251  O   VAL A 169     -12.602  -4.825 -78.712  1.00 91.80           O  
ANISOU 1251  O   VAL A 169    11748  13198   9935    749    735   1661       O  
ATOM   1252  CB  VAL A 169     -14.742  -4.139 -76.649  1.00 78.93           C  
ANISOU 1252  CB  VAL A 169    10150  11339   8500    711    499   1487       C  
ATOM   1253  CG1 VAL A 169     -15.795  -4.267 -77.732  1.00 87.63           C  
ANISOU 1253  CG1 VAL A 169    11274  12631   9390    811    463   1500       C  
ATOM   1254  CG2 VAL A 169     -15.398  -4.034 -75.282  1.00 71.15           C  
ANISOU 1254  CG2 VAL A 169     9171  10210   7654    666    407   1371       C  
ATOM   1255  N   PHE A 170     -13.726  -6.779 -78.640  1.00 93.73           N  
ANISOU 1255  N   PHE A 170    12037  13589   9987    768    642   1333       N  
ATOM   1256  CA  PHE A 170     -13.323  -7.215 -79.967  1.00 78.44           C  
ANISOU 1256  CA  PHE A 170    10126  11826   7850    835    731   1375       C  
ATOM   1257  C   PHE A 170     -14.530  -7.280 -80.893  1.00 80.86           C  
ANISOU 1257  C   PHE A 170    10481  12304   7938    902    661   1350       C  
ATOM   1258  O   PHE A 170     -15.661  -7.513 -80.456  1.00 74.85           O  
ANISOU 1258  O   PHE A 170     9727  11550   7162    888    543   1233       O  
ATOM   1259  CB  PHE A 170     -12.637  -8.586 -79.918  1.00 60.19           C  
ANISOU 1259  CB  PHE A 170     7827   9544   5497    820    796   1226       C  
ATOM   1260  CG  PHE A 170     -11.374  -8.603 -79.106  1.00 74.81           C  
ANISOU 1260  CG  PHE A 170     9614  11265   7544    764    870   1267       C  
ATOM   1261  CD1 PHE A 170     -10.166  -8.229 -79.671  1.00 72.05           C  
ANISOU 1261  CD1 PHE A 170     9221  10944   7211    785   1001   1435       C  
ATOM   1262  CD2 PHE A 170     -11.393  -8.996 -77.778  1.00 71.75           C  
ANISOU 1262  CD2 PHE A 170     9201  10741   7320    689    808   1147       C  
ATOM   1263  CE1 PHE A 170      -9.001  -8.245 -78.927  1.00 68.90           C  
ANISOU 1263  CE1 PHE A 170     8742  10445   6991    727   1060   1483       C  
ATOM   1264  CE2 PHE A 170     -10.231  -9.015 -77.029  1.00 71.19           C  
ANISOU 1264  CE2 PHE A 170     9060  10569   7418    635    864   1191       C  
ATOM   1265  CZ  PHE A 170      -9.034  -8.639 -77.605  1.00 72.00           C  
ANISOU 1265  CZ  PHE A 170     9109  10709   7540    651    986   1360       C  
ATOM   1266  N   PHE A 171     -14.274  -7.069 -82.181  1.00 88.67           N  
ANISOU 1266  N   PHE A 171    11494  13445   8750    976    734   1470       N  
ATOM   1267  CA  PHE A 171     -15.290  -7.150 -83.225  1.00 84.84           C  
ANISOU 1267  CA  PHE A 171    11052  13160   8023   1042    673   1463       C  
ATOM   1268  C   PHE A 171     -15.052  -8.434 -84.011  1.00 80.76           C  
ANISOU 1268  C   PHE A 171    10601  12792   7293   1057    722   1315       C  
ATOM   1269  O   PHE A 171     -14.122  -8.510 -84.821  1.00 90.86           O  
ANISOU 1269  O   PHE A 171    11902  14143   8479   1105    852   1398       O  
ATOM   1270  CB  PHE A 171     -15.237  -5.923 -84.133  1.00 84.40           C  
ANISOU 1270  CB  PHE A 171    10988  13176   7904   1122    717   1716       C  
ATOM   1271  CG  PHE A 171     -16.265  -5.931 -85.229  1.00 93.24           C  
ANISOU 1271  CG  PHE A 171    12141  14522   8763   1198    648   1734       C  
ATOM   1272  CD1 PHE A 171     -17.552  -5.478 -84.992  1.00 97.21           C  
ANISOU 1272  CD1 PHE A 171    12621  15052   9264   1216    514   1739       C  
ATOM   1273  CD2 PHE A 171     -15.942  -6.381 -86.500  1.00 96.80           C  
ANISOU 1273  CD2 PHE A 171    12644  15171   8964   1254    719   1751       C  
ATOM   1274  CE1 PHE A 171     -18.500  -5.482 -85.997  1.00101.07           C  
ANISOU 1274  CE1 PHE A 171    13123  15770   9510   1282    439   1767       C  
ATOM   1275  CE2 PHE A 171     -16.886  -6.387 -87.510  1.00101.08           C  
ANISOU 1275  CE2 PHE A 171    13216  15938   9250   1315    644   1767       C  
ATOM   1276  CZ  PHE A 171     -18.166  -5.936 -87.257  1.00104.12           C  
ANISOU 1276  CZ  PHE A 171    13563  16357   9639   1326    498   1778       C  
ATOM   1277  N   ILE A 172     -15.884  -9.440 -83.765  1.00 76.43           N  
ANISOU 1277  N   ILE A 172    10089  12283   6667   1014    625   1097       N  
ATOM   1278  CA  ILE A 172     -15.745 -10.733 -84.427  1.00 80.60           C  
ANISOU 1278  CA  ILE A 172    10703  12923   6998   1015    664    924       C  
ATOM   1279  C   ILE A 172     -16.203 -10.601 -85.874  1.00 82.52           C  
ANISOU 1279  C   ILE A 172    11000  13402   6950   1084    655    980       C  
ATOM   1280  O   ILE A 172     -17.371 -10.304 -86.142  1.00 85.09           O  
ANISOU 1280  O   ILE A 172    11315  13843   7174   1084    524    983       O  
ATOM   1281  CB  ILE A 172     -16.542 -11.820 -83.691  1.00 80.50           C  
ANISOU 1281  CB  ILE A 172    10718  12866   7004    930    557    678       C  
ATOM   1282  CG1 ILE A 172     -16.043 -11.963 -82.251  1.00 76.59           C  
ANISOU 1282  CG1 ILE A 172    10170  12146   6784    869    571    633       C  
ATOM   1283  CG2 ILE A 172     -16.445 -13.146 -84.432  1.00 80.55           C  
ANISOU 1283  CG2 ILE A 172    10837  12972   6797    925    598    491       C  
ATOM   1284  CD1 ILE A 172     -16.789 -13.010 -81.450  1.00 83.28           C  
ANISOU 1284  CD1 ILE A 172    11040  12936   7667    785    478    409       C  
ATOM   1285  N   GLU A 173     -15.281 -10.827 -86.812  1.00 88.29           N  
ANISOU 1285  N   GLU A 173    11786  14221   7540   1148    796   1030       N  
ATOM   1286  CA  GLU A 173     -15.600 -10.723 -88.230  1.00 80.75           C  
ANISOU 1286  CA  GLU A 173    10892  13502   6285   1220    802   1087       C  
ATOM   1287  C   GLU A 173     -16.417 -11.902 -88.742  1.00 78.72           C  
ANISOU 1287  C   GLU A 173    10739  13384   5787   1181    715    844       C  
ATOM   1288  O   GLU A 173     -17.101 -11.765 -89.761  1.00 80.14           O  
ANISOU 1288  O   GLU A 173    10957  13777   5715   1213    650    868       O  
ATOM   1289  CB  GLU A 173     -14.314 -10.600 -89.051  1.00 72.27           C  
ANISOU 1289  CB  GLU A 173     9846  12479   5134   1305    996   1220       C  
ATOM   1290  N   ASN A 174     -16.363 -13.050 -88.062  1.00 96.50           N  
ANISOU 1290  N   ASN A 174    13038  15521   8107   1106    709    616       N  
ATOM   1291  CA  ASN A 174     -17.110 -14.217 -88.523  1.00103.32           C  
ANISOU 1291  CA  ASN A 174    14014  16492   8752   1049    630    372       C  
ATOM   1292  C   ASN A 174     -18.613 -14.006 -88.391  1.00111.36           C  
ANISOU 1292  C   ASN A 174    14983  17607   9722    978    421    331       C  
ATOM   1293  O   ASN A 174     -19.381 -14.419 -89.267  1.00127.03           O  
ANISOU 1293  O   ASN A 174    17034  19788  11445    954    332    237       O  
ATOM   1294  CB  ASN A 174     -16.677 -15.461 -87.746  1.00108.61           C  
ANISOU 1294  CB  ASN A 174    14745  16985   9535    987    682    154       C  
ATOM   1295  CG  ASN A 174     -15.398 -16.071 -88.286  1.00111.87           C  
ANISOU 1295  CG  ASN A 174    15252  17379   9874   1067    883    131       C  
ATOM   1296  OD1 ASN A 174     -14.370 -16.088 -87.609  1.00106.50           O  
ANISOU 1296  OD1 ASN A 174    14525  16541   9399   1096   1004    188       O  
ATOM   1297  ND2 ASN A 174     -15.459 -16.585 -89.509  1.00127.14           N  
ANISOU 1297  ND2 ASN A 174    17319  19484  11507   1106    920     49       N  
ATOM   1298  N   THR A 175     -19.052 -13.367 -87.307  1.00111.15           N  
ANISOU 1298  N   THR A 175    14838  17456   9939    945    341    401       N  
ATOM   1299  CA  THR A 175     -20.472 -13.197 -87.036  1.00104.88           C  
ANISOU 1299  CA  THR A 175    13978  16742   9130    885    153    367       C  
ATOM   1300  C   THR A 175     -20.901 -11.743 -86.900  1.00107.34           C  
ANISOU 1300  C   THR A 175    14171  17076   9537    955    104    612       C  
ATOM   1301  O   THR A 175     -22.084 -11.490 -86.642  1.00114.73           O  
ANISOU 1301  O   THR A 175    15033  18083  10475    927    -43    613       O  
ATOM   1302  CB  THR A 175     -20.865 -13.960 -85.763  1.00100.19           C  
ANISOU 1302  CB  THR A 175    13362  15978   8728    774     89    185       C  
ATOM   1303  OG1 THR A 175     -20.052 -13.518 -84.669  1.00105.36           O  
ANISOU 1303  OG1 THR A 175    13959  16404   9669    791    175    266       O  
ATOM   1304  CG2 THR A 175     -20.677 -15.457 -85.957  1.00107.21           C  
ANISOU 1304  CG2 THR A 175    14381  16852   9503    697    118    -69       C  
ATOM   1305  N   ASN A 176     -19.985 -10.787 -87.070  1.00104.27           N  
ANISOU 1305  N   ASN A 176    13761  16628   9230   1046    226    824       N  
ATOM   1306  CA  ASN A 176     -20.293  -9.361 -86.933  1.00 98.49           C  
ANISOU 1306  CA  ASN A 176    12936  15880   8605   1117    199   1066       C  
ATOM   1307  C   ASN A 176     -20.908  -9.063 -85.568  1.00 97.14           C  
ANISOU 1307  C   ASN A 176    12682  15540   8688   1068    114   1038       C  
ATOM   1308  O   ASN A 176     -21.856  -8.284 -85.443  1.00 91.76           O  
ANISOU 1308  O   ASN A 176    11928  14905   8029   1106     18   1143       O  
ATOM   1309  CB  ASN A 176     -21.208  -8.883 -88.063  1.00 88.02           C  
ANISOU 1309  CB  ASN A 176    11597  14817   7030   1184    109   1178       C  
ATOM   1310  N   ILE A 177     -20.360  -9.694 -84.534  1.00101.75           N  
ANISOU 1310  N   ILE A 177    13275  15928   9456    993    154    900       N  
ATOM   1311  CA  ILE A 177     -20.869  -9.583 -83.172  1.00 94.56           C  
ANISOU 1311  CA  ILE A 177    12301  14854   8774    938     83    843       C  
ATOM   1312  C   ILE A 177     -19.786  -8.951 -82.309  1.00 90.44           C  
ANISOU 1312  C   ILE A 177    11759  14100   8504    943    188    940       C  
ATOM   1313  O   ILE A 177     -18.665  -9.471 -82.229  1.00 89.83           O  
ANISOU 1313  O   ILE A 177    11719  13942   8470    919    296    895       O  
ATOM   1314  CB  ILE A 177     -21.295 -10.947 -82.611  1.00 93.19           C  
ANISOU 1314  CB  ILE A 177    12154  14661   8594    830     20    586       C  
ATOM   1315  CG1 ILE A 177     -22.449 -11.526 -83.432  1.00102.35           C  
ANISOU 1315  CG1 ILE A 177    13326  16053   9509    801   -104    489       C  
ATOM   1316  CG2 ILE A 177     -21.704 -10.815 -81.163  1.00 89.85           C  
ANISOU 1316  CG2 ILE A 177    11665  14064   8409    781    -34    542       C  
ATOM   1317  CD1 ILE A 177     -22.964 -12.852 -82.915  1.00103.89           C  
ANISOU 1317  CD1 ILE A 177    13549  16226   9697    678   -174    240       C  
ATOM   1318  N   THR A 178     -20.122  -7.837 -81.663  1.00 95.56           N  
ANISOU 1318  N   THR A 178    12349  14644   9316    973    158   1072       N  
ATOM   1319  CA  THR A 178     -19.188  -7.105 -80.814  1.00 88.69           C  
ANISOU 1319  CA  THR A 178    11463  13550   8685    962    239   1168       C  
ATOM   1320  C   THR A 178     -19.230  -7.697 -79.409  1.00 93.54           C  
ANISOU 1320  C   THR A 178    12061  14002   9479    874    201   1002       C  
ATOM   1321  O   THR A 178     -20.254  -7.614 -78.724  1.00 89.97           O  
ANISOU 1321  O   THR A 178    11575  13528   9080    863    104    946       O  
ATOM   1322  CB  THR A 178     -19.536  -5.618 -80.796  1.00 76.76           C  
ANISOU 1322  CB  THR A 178     9922  11985   7258   1035    229   1379       C  
ATOM   1323  OG1 THR A 178     -19.390  -5.075 -82.114  1.00 95.33           O  
ANISOU 1323  OG1 THR A 178    12291  14488   9444   1120    277   1552       O  
ATOM   1324  CG2 THR A 178     -18.626  -4.869 -79.842  1.00 66.96           C  
ANISOU 1324  CG2 THR A 178     8676  10500   6268    998    298   1456       C  
ATOM   1325  N   VAL A 179     -18.118  -8.296 -78.981  1.00 95.39           N  
ANISOU 1325  N   VAL A 179    12312  14131   9801    819    283    935       N  
ATOM   1326  CA  VAL A 179     -18.020  -8.948 -77.683  1.00 80.12           C  
ANISOU 1326  CA  VAL A 179    10366  12052   8025    739    258    785       C  
ATOM   1327  C   VAL A 179     -16.782  -8.434 -76.959  1.00 86.69           C  
ANISOU 1327  C   VAL A 179    11176  12707   9055    708    340    869       C  
ATOM   1328  O   VAL A 179     -15.914  -7.781 -77.540  1.00 91.96           O  
ANISOU 1328  O   VAL A 179    11840  13372   9728    737    426   1024       O  
ATOM   1329  CB  VAL A 179     -17.959 -10.487 -77.798  1.00 65.33           C  
ANISOU 1329  CB  VAL A 179     8534  10238   6051    693    263    587       C  
ATOM   1330  CG1 VAL A 179     -19.079 -11.010 -78.675  1.00 68.60           C  
ANISOU 1330  CG1 VAL A 179     8975  10843   6246    704    182    504       C  
ATOM   1331  CG2 VAL A 179     -16.603 -10.925 -78.334  1.00 52.87           C  
ANISOU 1331  CG2 VAL A 179     6987   8660   4441    709    397    610       C  
ATOM   1332  N  ACYS A 180     -16.710  -8.752 -75.669  0.37 81.22           N  
ANISOU 1332  N  ACYS A 180    10465  11873   8520    641    308    768       N  
ATOM   1333  N  BCYS A 180     -16.719  -8.731 -75.663  0.63 80.82           N  
ANISOU 1333  N  BCYS A 180    10414  11821   8471    642    307    770       N  
ATOM   1334  CA ACYS A 180     -15.550  -8.462 -74.838  0.37 78.11           C  
ANISOU 1334  CA ACYS A 180    10044  11323   8310    590    366    815       C  
ATOM   1335  CA BCYS A 180     -15.548  -8.463 -74.839  0.63 79.41           C  
ANISOU 1335  CA BCYS A 180    10209  11487   8475    590    366    815       C  
ATOM   1336  C  ACYS A 180     -15.060  -9.766 -74.226  0.37 66.77           C  
ANISOU 1336  C  ACYS A 180     8607   9857   6905    539    385    660       C  
ATOM   1337  C  BCYS A 180     -15.065  -9.781 -74.254  0.63 66.68           C  
ANISOU 1337  C  BCYS A 180     8596   9849   6889    540    386    660       C  
ATOM   1338  O  ACYS A 180     -15.841 -10.493 -73.603  0.37 59.17           O  
ANISOU 1338  O  ACYS A 180     7656   8886   5941    510    315    512       O  
ATOM   1339  O  BCYS A 180     -15.859 -10.539 -73.687  0.63 57.33           O  
ANISOU 1339  O  BCYS A 180     7425   8663   5694    514    317    509       O  
ATOM   1340  CB ACYS A 180     -15.893  -7.454 -73.740  0.37 82.05           C  
ANISOU 1340  CB ACYS A 180    10528  11666   8980    560    307    855       C  
ATOM   1341  CB BCYS A 180     -15.859  -7.456 -73.725  0.63 83.98           C  
ANISOU 1341  CB BCYS A 180    10773  11908   9229    558    308    856       C  
ATOM   1342  SG ACYS A 180     -14.497  -7.004 -72.697  0.37 79.86           S  
ANISOU 1342  SG ACYS A 180    10218  11204   8919    472    355    912       S  
ATOM   1343  SG BCYS A 180     -17.093  -7.991 -72.510  0.63 68.26           S  
ANISOU 1343  SG BCYS A 180     8782   9871   7285    528    195    678       S  
ATOM   1344  N   ALA A 181     -13.774 -10.056 -74.401  1.00 57.88           N  
ANISOU 1344  N   ALA A 181     7462   8719   5810    533    486    708       N  
ATOM   1345  CA  ALA A 181     -13.216 -11.336 -73.983  1.00 65.63           C  
ANISOU 1345  CA  ALA A 181     8446   9685   6807    511    526    583       C  
ATOM   1346  C   ALA A 181     -11.697 -11.237 -73.952  1.00 76.37           C  
ANISOU 1346  C   ALA A 181     9751  11010   8258    505    634    693       C  
ATOM   1347  O   ALA A 181     -11.112 -10.194 -74.258  1.00 75.74           O  
ANISOU 1347  O   ALA A 181     9632  10919   8228    504    673    860       O  
ATOM   1348  CB  ALA A 181     -13.662 -12.454 -74.926  1.00 68.54           C  
ANISOU 1348  CB  ALA A 181     8883  10182   6978    554    548    462       C  
ATOM   1349  N   PHE A 182     -11.066 -12.342 -73.565  1.00 78.55           N  
ANISOU 1349  N   PHE A 182    10018  11269   8559    502    685    607       N  
ATOM   1350  CA  PHE A 182      -9.644 -12.546 -73.785  1.00 87.50           C  
ANISOU 1350  CA  PHE A 182    11094  12418   9734    525    807    704       C  
ATOM   1351  C   PHE A 182      -9.451 -13.203 -75.145  1.00 86.64           C  
ANISOU 1351  C   PHE A 182    11043  12442   9436    618    915    694       C  
ATOM   1352  O   PHE A 182     -10.212 -14.096 -75.528  1.00 91.62           O  
ANISOU 1352  O   PHE A 182    11762  13119   9929    647    897    542       O  
ATOM   1353  CB  PHE A 182      -9.035 -13.427 -72.692  1.00 89.00           C  
ANISOU 1353  CB  PHE A 182    11242  12529  10043    495    817    631       C  
ATOM   1354  CG  PHE A 182      -9.145 -12.852 -71.307  1.00 91.91           C  
ANISOU 1354  CG  PHE A 182    11561  12778  10584    402    714    633       C  
ATOM   1355  CD1 PHE A 182      -8.186 -11.973 -70.830  1.00 98.79           C  
ANISOU 1355  CD1 PHE A 182    12341  13599  11596    344    722    776       C  
ATOM   1356  CD2 PHE A 182     -10.196 -13.204 -70.477  1.00 81.79           C  
ANISOU 1356  CD2 PHE A 182    10324  11435   9317    368    611    490       C  
ATOM   1357  CE1 PHE A 182      -8.279 -11.449 -69.554  1.00 92.98           C  
ANISOU 1357  CE1 PHE A 182    11574  12752  11002    252    624    764       C  
ATOM   1358  CE2 PHE A 182     -10.295 -12.683 -69.199  1.00 69.14           C  
ANISOU 1358  CE2 PHE A 182     8687   9727   7857    291    524    487       C  
ATOM   1359  CZ  PHE A 182      -9.334 -11.806 -68.737  1.00 75.56           C  
ANISOU 1359  CZ  PHE A 182     9423  10488   8798    233    528    617       C  
ATOM   1360  N   HIS A 183      -8.436 -12.754 -75.876  1.00 68.50           N  
ANISOU 1360  N   HIS A 183     8697  10205   7124    660   1028    854       N  
ATOM   1361  CA  HIS A 183      -8.147 -13.274 -77.211  1.00 56.18           C  
ANISOU 1361  CA  HIS A 183     7194   8780   5374    759   1148    863       C  
ATOM   1362  C   HIS A 183      -6.945 -14.206 -77.112  1.00 61.03           C  
ANISOU 1362  C   HIS A 183     7770   9396   6024    811   1283    863       C  
ATOM   1363  O   HIS A 183      -5.801 -13.755 -77.018  1.00 70.14           O  
ANISOU 1363  O   HIS A 183     8813  10553   7283    812   1365   1026       O  
ATOM   1364  CB  HIS A 183      -7.894 -12.138 -78.196  1.00 73.57           C  
ANISOU 1364  CB  HIS A 183     9371  11068   7515    788   1198   1056       C  
ATOM   1365  CG  HIS A 183      -7.760 -12.593 -79.616  1.00 81.62           C  
ANISOU 1365  CG  HIS A 183    10462  12242   8307    893   1311   1061       C  
ATOM   1366  ND1 HIS A 183      -7.106 -11.852 -80.577  1.00 78.74           N  
ANISOU 1366  ND1 HIS A 183    10064  11974   7881    944   1416   1254       N  
ATOM   1367  CD2 HIS A 183      -8.199 -13.713 -80.238  1.00 78.98           C  
ANISOU 1367  CD2 HIS A 183    10243  11982   7784    954   1338    893       C  
ATOM   1368  CE1 HIS A 183      -7.146 -12.498 -81.729  1.00 82.68           C  
ANISOU 1368  CE1 HIS A 183    10653  12610   8153   1041   1504   1205       C  
ATOM   1369  NE2 HIS A 183      -7.804 -13.629 -81.551  1.00 82.76           N  
ANISOU 1369  NE2 HIS A 183    10759  12604   8081   1045   1457    980       N  
ATOM   1370  N   TYR A 184      -7.209 -15.514 -77.137  1.00 64.37           N  
ANISOU 1370  N   TYR A 184     8281   9814   6361    855   1309    685       N  
ATOM   1371  CA  TYR A 184      -6.152 -16.524 -77.071  1.00 83.49           C  
ANISOU 1371  CA  TYR A 184    10685  12230   8806    930   1448    673       C  
ATOM   1372  C   TYR A 184      -5.532 -16.663 -78.458  1.00 73.37           C  
ANISOU 1372  C   TYR A 184     9443  11082   7354   1046   1610    745       C  
ATOM   1373  O   TYR A 184      -5.798 -17.607 -79.207  1.00 89.51           O  
ANISOU 1373  O   TYR A 184    11617  13170   9221   1122   1677    610       O  
ATOM   1374  CB  TYR A 184      -6.701 -17.854 -76.569  1.00 94.84           C  
ANISOU 1374  CB  TYR A 184    12222  13590  10222    934   1422    458       C  
ATOM   1375  CG  TYR A 184      -7.206 -17.834 -75.142  1.00 89.57           C  
ANISOU 1375  CG  TYR A 184    11512  12798   9723    831   1283    396       C  
ATOM   1376  CD1 TYR A 184      -6.903 -16.781 -74.288  1.00 79.11           C  
ANISOU 1376  CD1 TYR A 184    10061  11427   8569    753   1209    526       C  
ATOM   1377  CD2 TYR A 184      -7.981 -18.875 -74.648  1.00 97.09           C  
ANISOU 1377  CD2 TYR A 184    12557  13676  10657    809   1229    205       C  
ATOM   1378  CE1 TYR A 184      -7.363 -16.764 -72.984  1.00 83.13           C  
ANISOU 1378  CE1 TYR A 184    10542  11829   9214    666   1088    464       C  
ATOM   1379  CE2 TYR A 184      -8.444 -18.867 -73.346  1.00 92.84           C  
ANISOU 1379  CE2 TYR A 184    11979  13034  10263    723   1112    156       C  
ATOM   1380  CZ  TYR A 184      -8.133 -17.810 -72.519  1.00 95.88           C  
ANISOU 1380  CZ  TYR A 184    12243  13385  10804    657   1043    284       C  
ATOM   1381  OH  TYR A 184      -8.593 -17.799 -71.222  1.00104.39           O  
ANISOU 1381  OH  TYR A 184    13290  14365  12007    577    931    230       O  
ATOM   1382  N   GLU A 185      -4.683 -15.696 -78.801  1.00 65.49           N  
ANISOU 1382  N   GLU A 185     8333  10145   6406   1055   1678    961       N  
ATOM   1383  CA  GLU A 185      -4.061 -15.678 -80.118  1.00 78.53           C  
ANISOU 1383  CA  GLU A 185    10006  11936   7898   1166   1840   1060       C  
ATOM   1384  C   GLU A 185      -3.163 -16.895 -80.307  1.00 92.33           C  
ANISOU 1384  C   GLU A 185    11772  13702   9607   1288   2010   1013       C  
ATOM   1385  O   GLU A 185      -2.493 -17.347 -79.374  1.00 96.79           O  
ANISOU 1385  O   GLU A 185    12248  14189  10337   1284   2033   1025       O  
ATOM   1386  CB  GLU A 185      -3.254 -14.393 -80.306  1.00 73.61           C  
ANISOU 1386  CB  GLU A 185     9238  11361   7371   1137   1882   1320       C  
ATOM   1387  N   SER A 186      -3.156 -17.428 -81.531  1.00102.37           N  
ANISOU 1387  N   SER A 186    13165  15080  10653   1404   2134    962       N  
ATOM   1388  CA  SER A 186      -2.362 -18.618 -81.818  1.00111.72           C  
ANISOU 1388  CA  SER A 186    14397  16274  11777   1541   2315    905       C  
ATOM   1389  C   SER A 186      -0.869 -18.331 -81.710  1.00104.01           C  
ANISOU 1389  C   SER A 186    13237  15348  10933   1607   2468   1135       C  
ATOM   1390  O   SER A 186      -0.110 -19.156 -81.189  1.00102.28           O  
ANISOU 1390  O   SER A 186    12971  15081  10808   1679   2564   1127       O  
ATOM   1391  CB  SER A 186      -2.711 -19.157 -83.205  1.00122.21           C  
ANISOU 1391  CB  SER A 186    15911  17711  12814   1647   2412    796       C  
ATOM   1392  OG  SER A 186      -2.639 -18.134 -84.183  1.00129.13           O  
ANISOU 1392  OG  SER A 186    16757  18732  13575   1662   2443    958       O  
ATOM   1393  N   GLN A 187      -0.429 -17.172 -82.196  1.00 91.89           N  
ANISOU 1393  N   GLN A 187    11591  13912   9411   1585   2496   1352       N  
ATOM   1394  CA  GLN A 187       0.964 -16.767 -82.091  1.00 75.35           C  
ANISOU 1394  CA  GLN A 187     9297  11878   7454   1619   2627   1593       C  
ATOM   1395  C   GLN A 187       1.040 -15.274 -81.809  1.00 90.21           C  
ANISOU 1395  C   GLN A 187    11037  13763   9477   1475   2524   1790       C  
ATOM   1396  O   GLN A 187       0.138 -14.512 -82.169  1.00 99.37           O  
ANISOU 1396  O   GLN A 187    12270  14923  10561   1407   2416   1777       O  
ATOM   1397  CB  GLN A 187       1.758 -17.097 -83.362  1.00 72.91           C  
ANISOU 1397  CB  GLN A 187     9011  11722   6967   1793   2864   1683       C  
ATOM   1398  CG  GLN A 187       2.071 -18.572 -83.532  1.00 78.83           C  
ANISOU 1398  CG  GLN A 187     9871  12457   7624   1956   3014   1531       C  
ATOM   1399  CD  GLN A 187       3.358 -18.807 -84.294  1.00 79.70           C  
ANISOU 1399  CD  GLN A 187     9900  12703   7679   2128   3272   1699       C  
ATOM   1400  OE1 GLN A 187       3.512 -18.364 -85.432  1.00 93.48           O  
ANISOU 1400  OE1 GLN A 187    11676  14588   9256   2194   3379   1796       O  
ATOM   1401  NE2 GLN A 187       4.297 -19.500 -83.663  1.00 87.13           N  
ANISOU 1401  NE2 GLN A 187    10731  13614   8760   2211   3377   1747       N  
ATOM   1402  N   ASN A 188       2.134 -14.869 -81.160  1.00 98.20           N  
ANISOU 1402  N   ASN A 188    11844  14774  10694   1429   2560   1976       N  
ATOM   1403  CA  ASN A 188       2.391 -13.472 -80.812  1.00110.66           C  
ANISOU 1403  CA  ASN A 188    13278  16336  12432   1277   2475   2174       C  
ATOM   1404  C   ASN A 188       1.246 -12.896 -79.976  1.00111.33           C  
ANISOU 1404  C   ASN A 188    13428  16277  12596   1125   2244   2056       C  
ATOM   1405  O   ASN A 188       0.597 -11.914 -80.343  1.00116.31           O  
ANISOU 1405  O   ASN A 188    14105  16897  13190   1060   2168   2104       O  
ATOM   1406  CB  ASN A 188       2.641 -12.632 -82.069  1.00115.45           C  
ANISOU 1406  CB  ASN A 188    13875  17072  12918   1316   2585   2360       C  
ATOM   1407  CG  ASN A 188       3.871 -13.080 -82.833  1.00124.94           C  
ANISOU 1407  CG  ASN A 188    14985  18426  14060   1463   2824   2508       C  
ATOM   1408  OD1 ASN A 188       4.863 -13.502 -82.240  1.00132.22           O  
ANISOU 1408  OD1 ASN A 188    15756  19358  15122   1482   2894   2582       O  
ATOM   1409  ND2 ASN A 188       3.810 -12.994 -84.157  1.00128.38           N  
ANISOU 1409  ND2 ASN A 188    15508  18991  14279   1575   2954   2559       N  
ATOM   1410  N   SER A 189       1.007 -13.533 -78.834  1.00104.29           N  
ANISOU 1410  N   SER A 189    12539  15275  11813   1081   2144   1910       N  
ATOM   1411  CA  SER A 189      -0.043 -13.134 -77.908  1.00106.98           C  
ANISOU 1411  CA  SER A 189    12936  15478  12233    950   1937   1786       C  
ATOM   1412  C   SER A 189       0.583 -12.476 -76.686  1.00122.05           C  
ANISOU 1412  C   SER A 189    14683  17306  14384    807   1847   1893       C  
ATOM   1413  O   SER A 189       1.532 -13.013 -76.105  1.00121.88           O  
ANISOU 1413  O   SER A 189    14539  17302  14468    821   1900   1942       O  
ATOM   1414  CB  SER A 189      -0.890 -14.337 -77.487  1.00116.38           C  
ANISOU 1414  CB  SER A 189    14262  16600  13355    995   1880   1533       C  
ATOM   1415  OG  SER A 189      -0.091 -15.330 -76.868  1.00133.37           O  
ANISOU 1415  OG  SER A 189    16347  18739  15590   1051   1952   1510       O  
ATOM   1416  N   THR A 190       0.051 -11.317 -76.303  1.00135.32           N  
ANISOU 1416  N   THR A 190    16368  18902  16146    672   1712   1930       N  
ATOM   1417  CA  THR A 190       0.539 -10.594 -75.135  1.00144.76           C  
ANISOU 1417  CA  THR A 190    17438  20008  17558    514   1609   2011       C  
ATOM   1418  C   THR A 190      -0.082 -11.083 -73.833  1.00134.78           C  
ANISOU 1418  C   THR A 190    16214  18625  16370    455   1463   1828       C  
ATOM   1419  O   THR A 190       0.295 -10.589 -72.764  1.00132.34           O  
ANISOU 1419  O   THR A 190    15813  18243  16226    325   1367   1869       O  
ATOM   1420  CB  THR A 190       0.278  -9.094 -75.296  1.00154.31           C  
ANISOU 1420  CB  THR A 190    18650  21156  18824    397   1541   2133       C  
ATOM   1421  OG1 THR A 190      -1.125  -8.868 -75.483  1.00156.48           O  
ANISOU 1421  OG1 THR A 190    19090  21367  18997    412   1447   1998       O  
ATOM   1422  CG2 THR A 190       1.039  -8.546 -76.494  1.00155.78           C  
ANISOU 1422  CG2 THR A 190    18771  21460  18959    439   1691   2350       C  
ATOM   1423  N   LEU A 191      -1.015 -12.030 -73.892  1.00123.35           N  
ANISOU 1423  N   LEU A 191    14904  17161  14803    540   1442   1629       N  
ATOM   1424  CA  LEU A 191      -1.632 -12.553 -72.687  1.00107.90           C  
ANISOU 1424  CA  LEU A 191    12987  15099  12911    492   1316   1461       C  
ATOM   1425  C   LEU A 191      -0.768 -13.657 -72.080  1.00108.98           C  
ANISOU 1425  C   LEU A 191    13038  15260  13109    544   1378   1449       C  
ATOM   1426  O   LEU A 191      -0.094 -14.395 -72.804  1.00116.03           O  
ANISOU 1426  O   LEU A 191    13908  16246  13931    669   1531   1493       O  
ATOM   1427  CB  LEU A 191      -3.024 -13.097 -72.992  1.00 95.76           C  
ANISOU 1427  CB  LEU A 191    11623  13533  11227    546   1265   1264       C  
ATOM   1428  N   PRO A 192      -0.760 -13.778 -70.752  1.00100.78           N  
ANISOU 1428  N   PRO A 192    11953  14141  12198    459   1267   1398       N  
ATOM   1429  CA  PRO A 192       0.010 -14.853 -70.117  1.00100.04           C  
ANISOU 1429  CA  PRO A 192    11777  14071  12162    518   1319   1395       C  
ATOM   1430  C   PRO A 192      -0.481 -16.226 -70.554  1.00103.98           C  
ANISOU 1430  C   PRO A 192    12405  14569  12532    665   1404   1239       C  
ATOM   1431  O   PRO A 192      -1.644 -16.408 -70.922  1.00 98.67           O  
ANISOU 1431  O   PRO A 192    11890  13853  11747    678   1362   1087       O  
ATOM   1432  CB  PRO A 192      -0.228 -14.624 -68.620  1.00104.50           C  
ANISOU 1432  CB  PRO A 192    12308  14541  12856    390   1155   1340       C  
ATOM   1433  CG  PRO A 192      -0.580 -13.174 -68.514  1.00 98.94           C  
ANISOU 1433  CG  PRO A 192    11608  13781  12202    248   1047   1390       C  
ATOM   1434  CD  PRO A 192      -1.348 -12.859 -69.764  1.00 97.28           C  
ANISOU 1434  CD  PRO A 192    11520  13588  11854    309   1097   1364       C  
ATOM   1435  N   ILE A 193       0.429 -17.199 -70.505  1.00109.95           N  
ANISOU 1435  N   ILE A 193    13093  15376  13308    774   1525   1283       N  
ATOM   1436  CA  ILE A 193       0.121 -18.539 -70.999  1.00114.20           C  
ANISOU 1436  CA  ILE A 193    13763  15901  13727    923   1633   1146       C  
ATOM   1437  C   ILE A 193      -0.903 -19.220 -70.099  1.00118.48           C  
ANISOU 1437  C   ILE A 193    14418  16321  14277    885   1520    953       C  
ATOM   1438  O   ILE A 193      -1.979 -19.629 -70.550  1.00126.70           O  
ANISOU 1438  O   ILE A 193    15626  17315  15198    902   1501    787       O  
ATOM   1439  CB  ILE A 193       1.406 -19.377 -71.121  1.00107.45           C  
ANISOU 1439  CB  ILE A 193    12802  15119  12904   1064   1804   1257       C  
ATOM   1440  N   GLY A 194      -0.584 -19.353 -68.814  1.00115.80           N  
ANISOU 1440  N   GLY A 194    13984  15939  14076    829   1441    979       N  
ATOM   1441  CA  GLY A 194      -1.468 -20.037 -67.892  1.00119.37           C  
ANISOU 1441  CA  GLY A 194    14529  16281  14543    799   1346    817       C  
ATOM   1442  C   GLY A 194      -2.192 -19.110 -66.940  1.00125.47           C  
ANISOU 1442  C   GLY A 194    15291  16995  15386    639   1159    783       C  
ATOM   1443  O   GLY A 194      -1.932 -19.123 -65.733  1.00131.48           O  
ANISOU 1443  O   GLY A 194    15973  17727  16257    579   1077    807       O  
ATOM   1444  N   LEU A 195      -3.109 -18.298 -67.471  1.00127.31           N  
ANISOU 1444  N   LEU A 195    15607  17213  15550    578   1092    729       N  
ATOM   1445  CA  LEU A 195      -3.865 -17.391 -66.614  1.00124.52           C  
ANISOU 1445  CA  LEU A 195    15261  16795  15256    444    928    691       C  
ATOM   1446  C   LEU A 195      -4.902 -18.147 -65.794  1.00115.53           C  
ANISOU 1446  C   LEU A 195    14218  15569  14107    430    851    523       C  
ATOM   1447  O   LEU A 195      -5.127 -17.829 -64.620  1.00122.90           O  
ANISOU 1447  O   LEU A 195    15122  16450  15126    344    739    506       O  
ATOM   1448  CB  LEU A 195      -4.532 -16.303 -67.456  1.00136.65           C  
ANISOU 1448  CB  LEU A 195    16854  18343  16723    403    894    701       C  
ATOM   1449  CG  LEU A 195      -4.833 -15.001 -66.714  1.00136.62           C  
ANISOU 1449  CG  LEU A 195    16819  18281  16809    271    759    739       C  
ATOM   1450  CD1 LEU A 195      -3.538 -14.380 -66.213  1.00136.72           C  
ANISOU 1450  CD1 LEU A 195    16680  18318  16951    202    759    902       C  
ATOM   1451  CD2 LEU A 195      -5.591 -14.030 -67.605  1.00132.78           C  
ANISOU 1451  CD2 LEU A 195    16404  17799  16248    258    738    750       C  
ATOM   1452  N   GLY A 196      -5.544 -19.151 -66.394  1.00104.73           N  
ANISOU 1452  N   GLY A 196    12972  14188  12633    507    911    397       N  
ATOM   1453  CA  GLY A 196      -6.489 -19.973 -65.661  1.00 89.74           C  
ANISOU 1453  CA  GLY A 196    11160  12208  10730    490    851    247       C  
ATOM   1454  C   GLY A 196      -5.847 -20.866 -64.621  1.00 75.92           C  
ANISOU 1454  C   GLY A 196     9355  10419   9073    520    875    264       C  
ATOM   1455  O   GLY A 196      -6.539 -21.336 -63.711  1.00 70.27           O  
ANISOU 1455  O   GLY A 196     8682   9633   8384    482    805    172       O  
ATOM   1456  N   LEU A 197      -4.540 -21.115 -64.737  1.00 71.94           N  
ANISOU 1456  N   LEU A 197     8751   9968   8616    593    976    393       N  
ATOM   1457  CA  LEU A 197      -3.844 -21.889 -63.715  1.00 75.15           C  
ANISOU 1457  CA  LEU A 197     9083  10354   9115    629    994    440       C  
ATOM   1458  C   LEU A 197      -3.782 -21.137 -62.393  1.00 89.44           C  
ANISOU 1458  C   LEU A 197    10796  12159  11028    511    849    490       C  
ATOM   1459  O   LEU A 197      -3.821 -21.761 -61.327  1.00 91.02           O  
ANISOU 1459  O   LEU A 197    10984  12319  11280    509    811    468       O  
ATOM   1460  CB  LEU A 197      -2.434 -22.246 -64.187  1.00 66.41           C  
ANISOU 1460  CB  LEU A 197     7870   9327   8037    744   1138    588       C  
ATOM   1461  CG  LEU A 197      -2.323 -23.251 -65.334  1.00 66.20           C  
ANISOU 1461  CG  LEU A 197     7949   9294   7911    892   1310    536       C  
ATOM   1462  CD1 LEU A 197      -0.864 -23.530 -65.660  1.00 56.42           C  
ANISOU 1462  CD1 LEU A 197     6580   8143   6713   1016   1457    705       C  
ATOM   1463  CD2 LEU A 197      -3.055 -24.540 -64.990  1.00 69.86           C  
ANISOU 1463  CD2 LEU A 197     8556   9640   8346    938   1332    382       C  
ATOM   1464  N   THR A 198      -3.688 -19.806 -62.440  1.00 89.00           N  
ANISOU 1464  N   THR A 198    10679  12138  10997    411    770    556       N  
ATOM   1465  CA  THR A 198      -3.671 -19.022 -61.209  1.00 93.79           C  
ANISOU 1465  CA  THR A 198    11219  12729  11689    288    628    585       C  
ATOM   1466  C   THR A 198      -4.989 -19.155 -60.456  1.00 76.96           C  
ANISOU 1466  C   THR A 198     9199  10509   9531    238    529    433       C  
ATOM   1467  O   THR A 198      -5.000 -19.277 -59.226  1.00 68.96           O  
ANISOU 1467  O   THR A 198     8156   9473   8571    192    450    423       O  
ATOM   1468  CB  THR A 198      -3.373 -17.555 -61.523  1.00109.32           C  
ANISOU 1468  CB  THR A 198    13128  14725  13684    188    575    674       C  
ATOM   1469  OG1 THR A 198      -2.124 -17.458 -62.219  1.00115.38           O  
ANISOU 1469  OG1 THR A 198    13775  15585  14478    230    674    830       O  
ATOM   1470  CG2 THR A 198      -3.293 -16.739 -60.241  1.00112.14           C  
ANISOU 1470  CG2 THR A 198    13431  15055  14123     53    431    692       C  
ATOM   1471  N   LYS A 199      -6.112 -19.144 -61.179  1.00 68.08           N  
ANISOU 1471  N   LYS A 199     8198   9348   8321    249    533    320       N  
ATOM   1472  CA  LYS A 199      -7.404 -19.366 -60.540  1.00 72.30           C  
ANISOU 1472  CA  LYS A 199     8828   9813   8829    212    453    183       C  
ATOM   1473  C   LYS A 199      -7.541 -20.781 -59.995  1.00 82.72           C  
ANISOU 1473  C   LYS A 199    10184  11093  10152    269    496    119       C  
ATOM   1474  O   LYS A 199      -8.407 -21.024 -59.148  1.00 93.00           O  
ANISOU 1474  O   LYS A 199    11535  12343  11458    229    427     34       O  
ATOM   1475  CB  LYS A 199      -8.543 -19.078 -61.521  1.00 72.03           C  
ANISOU 1475  CB  LYS A 199     8898   9772   8699    213    449     91       C  
ATOM   1476  CG  LYS A 199      -8.672 -17.617 -61.921  1.00 87.72           C  
ANISOU 1476  CG  LYS A 199    10869  11777  10684    156    394    147       C  
ATOM   1477  CD  LYS A 199      -9.982 -17.355 -62.649  1.00102.95           C  
ANISOU 1477  CD  LYS A 199    12894  13705  12519    159    367     57       C  
ATOM   1478  CE  LYS A 199     -10.086 -18.181 -63.920  1.00125.41           C  
ANISOU 1478  CE  LYS A 199    15798  16596  15256    237    463     14       C  
ATOM   1479  NZ  LYS A 199     -11.383 -17.966 -64.619  1.00136.74           N  
ANISOU 1479  NZ  LYS A 199    17315  18052  16589    231    421    -71       N  
ATOM   1480  N   ASN A 200      -6.709 -21.716 -60.457  1.00 81.35           N  
ANISOU 1480  N   ASN A 200     9993  10938   9979    368    616    165       N  
ATOM   1481  CA  ASN A 200      -6.778 -23.090 -59.972  1.00 81.17           C  
ANISOU 1481  CA  ASN A 200    10015  10857   9966    433    672    116       C  
ATOM   1482  C   ASN A 200      -6.032 -23.251 -58.652  1.00 78.99           C  
ANISOU 1482  C   ASN A 200     9634  10595   9784    426    632    210       C  
ATOM   1483  O   ASN A 200      -6.616 -23.659 -57.642  1.00 85.49           O  
ANISOU 1483  O   ASN A 200    10488  11368  10626    394    574    156       O  
ATOM   1484  CB  ASN A 200      -6.218 -24.050 -61.027  1.00 82.28           C  
ANISOU 1484  CB  ASN A 200    10201  10999  10065    558    830    121       C  
ATOM   1485  CG  ASN A 200      -7.103 -24.151 -62.253  1.00 84.05           C  
ANISOU 1485  CG  ASN A 200    10557  11206  10173    563    865     -2       C  
ATOM   1486  OD1 ASN A 200      -8.323 -24.013 -62.165  1.00 90.92           O  
ANISOU 1486  OD1 ASN A 200    11505  12040  10999    488    781   -116       O  
ATOM   1487  ND2 ASN A 200      -6.491 -24.397 -63.405  1.00 83.67           N  
ANISOU 1487  ND2 ASN A 200    10530  11196  10066    654    988     27       N  
ATOM   1488  N   ILE A 201      -4.737 -22.933 -58.640  1.00 74.28           N  
ANISOU 1488  N   ILE A 201     8903  10078   9243    452    661    359       N  
ATOM   1489  CA  ILE A 201      -3.933 -23.161 -57.444  1.00 80.60           C  
ANISOU 1489  CA  ILE A 201     9587  10915  10122    452    623    462       C  
ATOM   1490  C   ILE A 201      -4.134 -22.041 -56.429  1.00 87.37           C  
ANISOU 1490  C   ILE A 201    10393  11793  11009    310    462    469       C  
ATOM   1491  O   ILE A 201      -4.422 -22.295 -55.254  1.00 90.80           O  
ANISOU 1491  O   ILE A 201    10831  12208  11461    277    388    447       O  
ATOM   1492  CB  ILE A 201      -2.447 -23.339 -57.818  1.00 85.20           C  
ANISOU 1492  CB  ILE A 201    10029  11593  10752    539    720    630       C  
ATOM   1493  CG1 ILE A 201      -1.575 -23.349 -56.561  1.00 97.40           C  
ANISOU 1493  CG1 ILE A 201    11423  13208  12375    516    651    756       C  
ATOM   1494  CG2 ILE A 201      -1.987 -22.266 -58.797  1.00 87.34           C  
ANISOU 1494  CG2 ILE A 201    10240  11932  11012    499    733    695       C  
ATOM   1495  N   LEU A 202      -3.993 -20.785 -56.862  1.00 85.44           N  
ANISOU 1495  N   LEU A 202    10113  11582  10766    226    410    500       N  
ATOM   1496  CA  LEU A 202      -4.139 -19.669 -55.933  1.00 80.29           C  
ANISOU 1496  CA  LEU A 202     9432  10932  10141     89    263    500       C  
ATOM   1497  C   LEU A 202      -5.599 -19.420 -55.576  1.00 66.83           C  
ANISOU 1497  C   LEU A 202     7864   9141   8388     40    192    348       C  
ATOM   1498  O   LEU A 202      -5.897 -18.985 -54.457  1.00 81.72           O  
ANISOU 1498  O   LEU A 202     9755  11011  10286    -38     85    318       O  
ATOM   1499  CB  LEU A 202      -3.511 -18.406 -56.525  1.00 88.89           C  
ANISOU 1499  CB  LEU A 202    10450  12065  11258     11    240    587       C  
ATOM   1500  CG  LEU A 202      -3.632 -17.116 -55.710  1.00 89.65           C  
ANISOU 1500  CG  LEU A 202    10539  12140  11384   -141     97    578       C  
ATOM   1501  CD1 LEU A 202      -2.963 -17.272 -54.353  1.00 93.59           C  
ANISOU 1501  CD1 LEU A 202    10945  12690  11925   -197     10    632       C  
ATOM   1502  CD2 LEU A 202      -3.046 -15.937 -56.472  1.00 79.06           C  
ANISOU 1502  CD2 LEU A 202     9144  10821  10074   -215     95    668       C  
ATOM   1503  N   GLY A 203      -6.516 -19.697 -56.498  1.00 69.87           N  
ANISOU 1503  N   GLY A 203     8355   9480   8712     88    249    254       N  
ATOM   1504  CA  GLY A 203      -7.925 -19.452 -56.295  1.00 67.93           C  
ANISOU 1504  CA  GLY A 203     8219   9170   8419     49    189    125       C  
ATOM   1505  C   GLY A 203      -8.732 -20.613 -55.764  1.00 63.43           C  
ANISOU 1505  C   GLY A 203     7719   8554   7826     88    206     33       C  
ATOM   1506  O   GLY A 203      -9.916 -20.434 -55.466  1.00 65.02           O  
ANISOU 1506  O   GLY A 203     7994   8715   7994     52    154    -64       O  
ATOM   1507  N   PHE A 204      -8.138 -21.799 -55.632  1.00 59.43           N  
ANISOU 1507  N   PHE A 204     7191   8050   7342    163    284     70       N  
ATOM   1508  CA  PHE A 204      -8.885 -22.949 -55.138  1.00 66.62           C  
ANISOU 1508  CA  PHE A 204     8175   8899   8238    195    309     -9       C  
ATOM   1509  C   PHE A 204      -7.993 -23.948 -54.412  1.00 66.94           C  
ANISOU 1509  C   PHE A 204     8159   8945   8329    262    359     77       C  
ATOM   1510  O   PHE A 204      -8.230 -24.251 -53.240  1.00 71.09           O  
ANISOU 1510  O   PHE A 204     8680   9458   8872    241    308     77       O  
ATOM   1511  CB  PHE A 204      -9.617 -23.646 -56.288  1.00 65.82           C  
ANISOU 1511  CB  PHE A 204     8180   8752   8078    238    391   -107       C  
ATOM   1512  CG  PHE A 204     -10.369 -24.876 -55.868  1.00 75.48           C  
ANISOU 1512  CG  PHE A 204     9486   9899   9295    255    425   -187       C  
ATOM   1513  CD1 PHE A 204     -11.608 -24.771 -55.257  1.00 75.99           C  
ANISOU 1513  CD1 PHE A 204     9598   9936   9340    186    351   -273       C  
ATOM   1514  CD2 PHE A 204      -9.839 -26.138 -56.083  1.00 76.81           C  
ANISOU 1514  CD2 PHE A 204     9685  10020   9481    344    538   -170       C  
ATOM   1515  CE1 PHE A 204     -12.303 -25.900 -54.867  1.00 76.44           C  
ANISOU 1515  CE1 PHE A 204     9724   9923   9398    188    384   -337       C  
ATOM   1516  CE2 PHE A 204     -10.529 -27.271 -55.695  1.00 77.70           C  
ANISOU 1516  CE2 PHE A 204     9883  10043   9595    350    573   -240       C  
ATOM   1517  CZ  PHE A 204     -11.763 -27.152 -55.087  1.00 73.62           C  
ANISOU 1517  CZ  PHE A 204     9405   9503   9062    264    493   -322       C  
ATOM   1518  N   LEU A 205      -6.970 -24.463 -55.099  1.00 59.45           N  
ANISOU 1518  N   LEU A 205     7166   8022   7402    353    463    158       N  
ATOM   1519  CA  LEU A 205      -6.167 -25.554 -54.551  1.00 80.86           C  
ANISOU 1519  CA  LEU A 205     9831  10732  10161    447    534    246       C  
ATOM   1520  C   LEU A 205      -5.528 -25.165 -53.222  1.00 86.36           C  
ANISOU 1520  C   LEU A 205    10408  11502  10904    404    436    351       C  
ATOM   1521  O   LEU A 205      -5.756 -25.814 -52.195  1.00 85.61           O  
ANISOU 1521  O   LEU A 205    10325  11382  10821    416    415    355       O  
ATOM   1522  CB  LEU A 205      -5.099 -25.976 -55.561  1.00 98.82           C  
ANISOU 1522  CB  LEU A 205    12062  13037  12448    562    668    331       C  
ATOM   1523  CG  LEU A 205      -4.103 -27.038 -55.088  1.00111.35           C  
ANISOU 1523  CG  LEU A 205    13582  14634  14092    687    758    451       C  
ATOM   1524  CD1 LEU A 205      -4.820 -28.335 -54.744  1.00112.80           C  
ANISOU 1524  CD1 LEU A 205    13894  14692  14272    742    820    371       C  
ATOM   1525  CD2 LEU A 205      -3.028 -27.274 -56.137  1.00112.58           C  
ANISOU 1525  CD2 LEU A 205    13682  14837  14257    806    895    544       C  
ATOM   1526  N   PHE A 206      -4.721 -24.104 -53.222  1.00 84.48           N  
ANISOU 1526  N   PHE A 206    10054  11356  10688    346    373    439       N  
ATOM   1527  CA  PHE A 206      -4.053 -23.687 -51.990  1.00 75.18           C  
ANISOU 1527  CA  PHE A 206     8760  10262   9544    287    266    534       C  
ATOM   1528  C   PHE A 206      -5.027 -23.272 -50.893  1.00 87.14           C  
ANISOU 1528  C   PHE A 206    10341  11743  11024    189    145    441       C  
ATOM   1529  O   PHE A 206      -4.852 -23.719 -49.746  1.00113.62           O  
ANISOU 1529  O   PHE A 206    13661  15128  14383    195    102    486       O  
ATOM   1530  CB  PHE A 206      -3.047 -22.571 -52.294  1.00 62.94           C  
ANISOU 1530  CB  PHE A 206     7080   8809   8024    218    218    636       C  
ATOM   1531  CG  PHE A 206      -1.740 -23.064 -52.846  1.00 77.51           C  
ANISOU 1531  CG  PHE A 206     8795  10738   9917    320    321    789       C  
ATOM   1532  CD1 PHE A 206      -1.486 -24.421 -52.961  1.00 86.15           C  
ANISOU 1532  CD1 PHE A 206     9900  11810  11024    474    448    828       C  
ATOM   1533  CD2 PHE A 206      -0.758 -22.169 -53.237  1.00 79.84           C  
ANISOU 1533  CD2 PHE A 206     8956  11131  10248    263    299    901       C  
ATOM   1534  CE1 PHE A 206      -0.281 -24.876 -53.465  1.00 87.35           C  
ANISOU 1534  CE1 PHE A 206     9930  12041  11219    589    557    976       C  
ATOM   1535  CE2 PHE A 206       0.449 -22.617 -53.741  1.00 83.53           C  
ANISOU 1535  CE2 PHE A 206     9287  11691  10760    365    402   1056       C  
ATOM   1536  CZ  PHE A 206       0.688 -23.972 -53.855  1.00 85.55           C  
ANISOU 1536  CZ  PHE A 206     9553  11929  11024    537    535   1094       C  
ATOM   1537  N   PRO A 207      -6.047 -22.441 -51.145  1.00 72.73           N  
ANISOU 1537  N   PRO A 207     8609   9866   9160    109     91    322       N  
ATOM   1538  CA  PRO A 207      -6.945 -22.073 -50.036  1.00 70.43           C  
ANISOU 1538  CA  PRO A 207     8378   9549   8834     34    -10    241       C  
ATOM   1539  C   PRO A 207      -7.773 -23.234 -49.515  1.00 71.17           C  
ANISOU 1539  C   PRO A 207     8549   9585   8908     91     34    186       C  
ATOM   1540  O   PRO A 207      -8.014 -23.314 -48.304  1.00 87.12           O  
ANISOU 1540  O   PRO A 207    10571  11621  10909     62    -30    186       O  
ATOM   1541  CB  PRO A 207      -7.826 -20.975 -50.647  1.00 63.20           C  
ANISOU 1541  CB  PRO A 207     7540   8586   7887    -35    -49    140       C  
ATOM   1542  CG  PRO A 207      -7.055 -20.462 -51.808  1.00 52.16           C  
ANISOU 1542  CG  PRO A 207     6087   7216   6514    -30     -7    203       C  
ATOM   1543  CD  PRO A 207      -6.348 -21.656 -52.356  1.00 68.05           C  
ANISOU 1543  CD  PRO A 207     8056   9249   8550     83    112    274       C  
ATOM   1544  N   PHE A 208      -8.224 -24.136 -50.392  1.00 73.57           N  
ANISOU 1544  N   PHE A 208     8922   9820   9210    163    143    139       N  
ATOM   1545  CA  PHE A 208      -9.031 -25.264 -49.935  1.00 66.36           C  
ANISOU 1545  CA  PHE A 208     8088   8837   8287    201    189     87       C  
ATOM   1546  C   PHE A 208      -8.232 -26.176 -49.014  1.00 65.83           C  
ANISOU 1546  C   PHE A 208     7961   8797   8256    269    215    202       C  
ATOM   1547  O   PHE A 208      -8.775 -26.721 -48.046  1.00 84.90           O  
ANISOU 1547  O   PHE A 208    10411  11187  10660    267    200    192       O  
ATOM   1548  CB  PHE A 208      -9.570 -26.050 -51.131  1.00 57.84           C  
ANISOU 1548  CB  PHE A 208     7101   7676   7200    251    297     10       C  
ATOM   1549  CG  PHE A 208     -10.217 -27.354 -50.760  1.00 60.44           C  
ANISOU 1549  CG  PHE A 208     7511   7918   7536    287    362    -28       C  
ATOM   1550  CD1 PHE A 208     -11.493 -27.382 -50.221  1.00 57.40           C  
ANISOU 1550  CD1 PHE A 208     7190   7497   7122    220    317   -117       C  
ATOM   1551  CD2 PHE A 208      -9.553 -28.554 -50.958  1.00 66.09           C  
ANISOU 1551  CD2 PHE A 208     8239   8583   8291    390    476     31       C  
ATOM   1552  CE1 PHE A 208     -12.091 -28.581 -49.880  1.00 63.73           C  
ANISOU 1552  CE1 PHE A 208     8063   8215   7938    239    378   -144       C  
ATOM   1553  CE2 PHE A 208     -10.145 -29.756 -50.619  1.00 69.29           C  
ANISOU 1553  CE2 PHE A 208     8731   8887   8710    415    542     -1       C  
ATOM   1554  CZ  PHE A 208     -11.416 -29.769 -50.079  1.00 64.93           C  
ANISOU 1554  CZ  PHE A 208     8238   8300   8133    331    490    -87       C  
ATOM   1555  N   LEU A 209      -6.940 -26.354 -49.296  1.00 56.18           N  
ANISOU 1555  N   LEU A 209     6640   7631   7074    335    259    324       N  
ATOM   1556  CA  LEU A 209      -6.109 -27.185 -48.434  1.00 73.00           C  
ANISOU 1556  CA  LEU A 209     8695   9804   9239    414    283    456       C  
ATOM   1557  C   LEU A 209      -5.897 -26.541 -47.070  1.00 80.80           C  
ANISOU 1557  C   LEU A 209     9608  10889  10202    336    145    507       C  
ATOM   1558  O   LEU A 209      -5.666 -27.248 -46.083  1.00 88.61           O  
ANISOU 1558  O   LEU A 209    10568  11906  11193    383    142    587       O  
ATOM   1559  CB  LEU A 209      -4.769 -27.467 -49.111  1.00 77.10           C  
ANISOU 1559  CB  LEU A 209     9110  10379   9807    513    366    585       C  
ATOM   1560  CG  LEU A 209      -4.862 -28.304 -50.388  1.00 90.72           C  
ANISOU 1560  CG  LEU A 209    10921  12004  11545    616    524    541       C  
ATOM   1561  CD1 LEU A 209      -3.514 -28.387 -51.079  1.00102.20           C  
ANISOU 1561  CD1 LEU A 209    12261  13531  13040    715    609    673       C  
ATOM   1562  CD2 LEU A 209      -5.400 -29.695 -50.082  1.00 90.84           C  
ANISOU 1562  CD2 LEU A 209    11044  11897  11572    697    617    514       C  
ATOM   1563  N   ILE A 210      -5.970 -25.212 -46.993  1.00 70.75           N  
ANISOU 1563  N   ILE A 210     8314   9667   8902    220     32    462       N  
ATOM   1564  CA  ILE A 210      -5.915 -24.544 -45.697  1.00 65.11           C  
ANISOU 1564  CA  ILE A 210     7563   9030   8145    131   -104    477       C  
ATOM   1565  C   ILE A 210      -7.269 -24.614 -45.004  1.00 61.00           C  
ANISOU 1565  C   ILE A 210     7165   8445   7570     97   -130    361       C  
ATOM   1566  O   ILE A 210      -7.348 -24.832 -43.790  1.00 63.82           O  
ANISOU 1566  O   ILE A 210     7516   8846   7887     89   -184    391       O  
ATOM   1567  CB  ILE A 210      -5.438 -23.091 -45.864  1.00 69.00           C  
ANISOU 1567  CB  ILE A 210     8001   9583   8634     14   -208    471       C  
ATOM   1568  CG1 ILE A 210      -4.088 -23.050 -46.582  1.00 68.42           C  
ANISOU 1568  CG1 ILE A 210     7790   9586   8621     45   -172    603       C  
ATOM   1569  CG2 ILE A 210      -5.338 -22.406 -44.511  1.00 79.53           C  
ANISOU 1569  CG2 ILE A 210     9313  10991   9913    -85   -351    473       C  
ATOM   1570  CD1 ILE A 210      -3.553 -21.650 -46.789  1.00 72.73           C  
ANISOU 1570  CD1 ILE A 210     8275  10184   9175    -83   -269    612       C  
ATOM   1571  N   ILE A 211      -8.354 -24.433 -45.761  1.00 67.25           N  
ANISOU 1571  N   ILE A 211     8059   9142   8350     80    -92    235       N  
ATOM   1572  CA  ILE A 211      -9.692 -24.548 -45.189  1.00 64.88           C  
ANISOU 1572  CA  ILE A 211     7860   8788   8004     55   -103    134       C  
ATOM   1573  C   ILE A 211      -9.943 -25.972 -44.707  1.00 68.93           C  
ANISOU 1573  C   ILE A 211     8400   9262   8530    132    -23    174       C  
ATOM   1574  O   ILE A 211     -10.508 -26.188 -43.628  1.00 73.49           O  
ANISOU 1574  O   ILE A 211     9006   9850   9067    119    -53    168       O  
ATOM   1575  CB  ILE A 211     -10.751 -24.099 -46.214  1.00 60.72           C  
ANISOU 1575  CB  ILE A 211     7415   8186   7468     26    -77      9       C  
ATOM   1576  CG1 ILE A 211     -10.597 -22.608 -46.524  1.00 61.92           C  
ANISOU 1576  CG1 ILE A 211     7554   8366   7607    -49   -159    -24       C  
ATOM   1577  CG2 ILE A 211     -12.154 -24.397 -45.707  1.00 64.31           C  
ANISOU 1577  CG2 ILE A 211     7955   8594   7885     11    -71    -80       C  
ATOM   1578  CD1 ILE A 211     -11.592 -22.088 -47.537  1.00 59.01           C  
ANISOU 1578  CD1 ILE A 211     7256   7939   7225    -66   -138   -126       C  
ATOM   1579  N   LEU A 212      -9.517 -26.964 -45.492  1.00 74.19           N  
ANISOU 1579  N   LEU A 212     9063   9876   9250    217     87    219       N  
ATOM   1580  CA  LEU A 212      -9.697 -28.355 -45.087  1.00 73.23           C  
ANISOU 1580  CA  LEU A 212     8980   9692   9153    294    176    264       C  
ATOM   1581  C   LEU A 212      -8.846 -28.691 -43.868  1.00 76.70           C  
ANISOU 1581  C   LEU A 212     9336  10219   9589    338    141    408       C  
ATOM   1582  O   LEU A 212      -9.293 -29.422 -42.976  1.00 64.65           O  
ANISOU 1582  O   LEU A 212     7845   8672   8049    361    160    437       O  
ATOM   1583  CB  LEU A 212      -9.360 -29.289 -46.250  1.00 60.82           C  
ANISOU 1583  CB  LEU A 212     7441   8031   7637    381    309    273       C  
ATOM   1584  CG  LEU A 212      -9.462 -30.792 -45.978  1.00 65.23           C  
ANISOU 1584  CG  LEU A 212     8058   8491   8235    469    422    321       C  
ATOM   1585  CD1 LEU A 212     -10.895 -31.187 -45.657  1.00 69.56           C  
ANISOU 1585  CD1 LEU A 212     8713   8954   8763    404    429    219       C  
ATOM   1586  CD2 LEU A 212      -8.932 -31.591 -47.158  1.00 54.43           C  
ANISOU 1586  CD2 LEU A 212     6727   7036   6917    565    556    329       C  
ATOM   1587  N   THR A 213      -7.621 -28.165 -43.809  1.00 73.38           N  
ANISOU 1587  N   THR A 213     8796   9907   9177    346     87    507       N  
ATOM   1588  CA  THR A 213      -6.739 -28.468 -42.685  1.00 68.28           C  
ANISOU 1588  CA  THR A 213     8052   9370   8520    386     42    656       C  
ATOM   1589  C   THR A 213      -7.230 -27.809 -41.401  1.00 64.97           C  
ANISOU 1589  C   THR A 213     7646   9026   8015    295    -84    623       C  
ATOM   1590  O   THR A 213      -7.136 -28.401 -40.319  1.00 75.40           O  
ANISOU 1590  O   THR A 213     8949  10396   9302    333    -97    710       O  
ATOM   1591  CB  THR A 213      -5.310 -28.023 -43.002  1.00 67.86           C  
ANISOU 1591  CB  THR A 213     7852   9433   8500    402      9    773       C  
ATOM   1592  OG1 THR A 213      -4.867 -28.660 -44.207  1.00 72.68           O  
ANISOU 1592  OG1 THR A 213     8457   9976   9181    503    143    803       O  
ATOM   1593  CG2 THR A 213      -4.366 -28.392 -41.866  1.00 75.11           C  
ANISOU 1593  CG2 THR A 213     8649  10486   9402    448    -44    942       C  
ATOM   1594  N   SER A 214      -7.759 -26.587 -41.500  1.00 54.00           N  
ANISOU 1594  N   SER A 214     6294   7642   6580    183   -171    502       N  
ATOM   1595  CA  SER A 214      -8.212 -25.876 -40.309  1.00 54.80           C  
ANISOU 1595  CA  SER A 214     6424   7807   6589    101   -284    457       C  
ATOM   1596  C   SER A 214      -9.373 -26.601 -39.640  1.00 77.52           C  
ANISOU 1596  C   SER A 214     9396  10627   9429    130   -233    417       C  
ATOM   1597  O   SER A 214      -9.358 -26.834 -38.426  1.00 93.36           O  
ANISOU 1597  O   SER A 214    11395  12706  11370    136   -276    474       O  
ATOM   1598  CB  SER A 214      -8.606 -24.443 -40.671  1.00 50.22           C  
ANISOU 1598  CB  SER A 214     5886   7214   5981     -9   -363    329       C  
ATOM   1599  OG  SER A 214      -7.477 -23.693 -41.084  1.00 57.10           O  
ANISOU 1599  OG  SER A 214     6663   8152   6881    -57   -426    380       O  
ATOM   1600  N   TYR A 215     -10.390 -26.974 -40.419  1.00 70.08           N  
ANISOU 1600  N   TYR A 215     8540   9563   8524    142   -143    325       N  
ATOM   1601  CA  TYR A 215     -11.554 -27.645 -39.854  1.00 69.76           C  
ANISOU 1601  CA  TYR A 215     8581   9468   8458    154    -91    289       C  
ATOM   1602  C   TYR A 215     -11.287 -29.103 -39.505  1.00 63.43           C  
ANISOU 1602  C   TYR A 215     7772   8632   7698    247      3    409       C  
ATOM   1603  O   TYR A 215     -12.005 -29.666 -38.673  1.00 69.19           O  
ANISOU 1603  O   TYR A 215     8546   9348   8394    255     30    425       O  
ATOM   1604  CB  TYR A 215     -12.739 -27.544 -40.817  1.00 62.89           C  
ANISOU 1604  CB  TYR A 215     7791   8492   7613    120    -37    155       C  
ATOM   1605  CG  TYR A 215     -13.299 -26.144 -40.934  1.00 61.39           C  
ANISOU 1605  CG  TYR A 215     7625   8328   7372     42   -119     42       C  
ATOM   1606  CD1 TYR A 215     -14.059 -25.593 -39.910  1.00 55.33           C  
ANISOU 1606  CD1 TYR A 215     6896   7603   6524      6   -171     -5       C  
ATOM   1607  CD2 TYR A 215     -13.067 -25.373 -42.064  1.00 69.14           C  
ANISOU 1607  CD2 TYR A 215     8598   9288   8384     14   -134    -13       C  
ATOM   1608  CE1 TYR A 215     -14.571 -24.313 -40.008  1.00 52.36           C  
ANISOU 1608  CE1 TYR A 215     6555   7235   6104    -50   -233   -107       C  
ATOM   1609  CE2 TYR A 215     -13.576 -24.092 -42.172  1.00 71.45           C  
ANISOU 1609  CE2 TYR A 215     8921   9590   8638    -47   -201   -106       C  
ATOM   1610  CZ  TYR A 215     -14.326 -23.567 -41.141  1.00 69.05           C  
ANISOU 1610  CZ  TYR A 215     8661   9316   8259    -76   -248   -154       C  
ATOM   1611  OH  TYR A 215     -14.835 -22.293 -41.244  1.00 81.79           O  
ANISOU 1611  OH  TYR A 215    10316  10923   9836   -121   -302   -245       O  
ATOM   1612  N   THR A 216     -10.278 -29.728 -40.118  1.00 66.47           N  
ANISOU 1612  N   THR A 216     8104   8998   8154    324     62    502       N  
ATOM   1613  CA  THR A 216      -9.903 -31.079 -39.713  1.00 63.74           C  
ANISOU 1613  CA  THR A 216     7752   8617   7850    430    154    635       C  
ATOM   1614  C   THR A 216      -9.283 -31.077 -38.321  1.00 64.97           C  
ANISOU 1614  C   THR A 216     7833   8913   7940    454     77    768       C  
ATOM   1615  O   THR A 216      -9.546 -31.977 -37.515  1.00 59.46           O  
ANISOU 1615  O   THR A 216     7162   8199   7232    508    126    852       O  
ATOM   1616  CB  THR A 216      -8.938 -31.690 -40.732  1.00 63.38           C  
ANISOU 1616  CB  THR A 216     7669   8519   7893    525    246    703       C  
ATOM   1617  OG1 THR A 216      -9.571 -31.752 -42.016  1.00 62.03           O  
ANISOU 1617  OG1 THR A 216     7583   8220   7765    500    318    571       O  
ATOM   1618  CG2 THR A 216      -8.526 -33.094 -40.311  1.00 53.27           C  
ANISOU 1618  CG2 THR A 216     6392   7185   6663    652    353    849       C  
ATOM   1619  N   LEU A 217      -8.463 -30.067 -38.021  1.00 72.76           N  
ANISOU 1619  N   LEU A 217     8726  10041   8876    407    -48    793       N  
ATOM   1620  CA  LEU A 217      -7.899 -29.945 -36.682  1.00 80.09           C  
ANISOU 1620  CA  LEU A 217     9585  11126   9720    408   -145    904       C  
ATOM   1621  C   LEU A 217      -8.971 -29.608 -35.653  1.00 80.77           C  
ANISOU 1621  C   LEU A 217     9756  11234   9700    344   -195    827       C  
ATOM   1622  O   LEU A 217      -8.886 -30.055 -34.504  1.00 86.98           O  
ANISOU 1622  O   LEU A 217    10528  12104  10417    379   -216    928       O  
ATOM   1623  CB  LEU A 217      -6.793 -28.891 -36.677  1.00 72.98           C  
ANISOU 1623  CB  LEU A 217     8569  10368   8791    346   -276    933       C  
ATOM   1624  CG  LEU A 217      -5.541 -29.286 -37.463  1.00 66.37           C  
ANISOU 1624  CG  LEU A 217     7612   9557   8049    427   -228   1059       C  
ATOM   1625  CD1 LEU A 217      -4.615 -28.097 -37.661  1.00 63.24           C  
ANISOU 1625  CD1 LEU A 217     7105   9284   7638    332   -354   1061       C  
ATOM   1626  CD2 LEU A 217      -4.818 -30.418 -36.752  1.00 62.42           C  
ANISOU 1626  CD2 LEU A 217     7034   9125   7559    558   -185   1261       C  
ATOM   1627  N   ILE A 218      -9.978 -28.824 -36.043  1.00 72.15           N  
ANISOU 1627  N   ILE A 218     8748  10077   8589    259   -209    658       N  
ATOM   1628  CA  ILE A 218     -11.124 -28.602 -35.167  1.00 65.73           C  
ANISOU 1628  CA  ILE A 218     8019   9270   7684    218   -224    584       C  
ATOM   1629  C   ILE A 218     -11.897 -29.900 -34.975  1.00 74.53           C  
ANISOU 1629  C   ILE A 218     9189  10294   8837    284    -97    635       C  
ATOM   1630  O   ILE A 218     -12.392 -30.191 -33.879  1.00 87.44           O  
ANISOU 1630  O   ILE A 218    10852  11977  10393    294    -96    677       O  
ATOM   1631  CB  ILE A 218     -12.020 -27.485 -35.734  1.00 50.84           C  
ANISOU 1631  CB  ILE A 218     6201   7332   5782    131   -254    404       C  
ATOM   1632  CG1 ILE A 218     -11.220 -26.192 -35.898  1.00 53.45           C  
ANISOU 1632  CG1 ILE A 218     6489   7735   6083     57   -376    361       C  
ATOM   1633  CG2 ILE A 218     -13.226 -27.255 -34.836  1.00 47.44           C  
ANISOU 1633  CG2 ILE A 218     5852   6915   5258    105   -255    335       C  
ATOM   1634  CD1 ILE A 218     -11.984 -25.088 -36.598  1.00 47.41           C  
ANISOU 1634  CD1 ILE A 218     5790   6903   5320    -13   -395    201       C  
ATOM   1635  N   TRP A 219     -12.007 -30.702 -36.037  1.00 62.50           N  
ANISOU 1635  N   TRP A 219     7685   8633   7428    324     14    632       N  
ATOM   1636  CA  TRP A 219     -12.652 -32.007 -35.933  1.00 63.55           C  
ANISOU 1636  CA  TRP A 219     7876   8655   7613    376    140    684       C  
ATOM   1637  C   TRP A 219     -11.907 -32.908 -34.955  1.00 67.92           C  
ANISOU 1637  C   TRP A 219     8386   9267   8154    471    163    875       C  
ATOM   1638  O   TRP A 219     -12.516 -33.542 -34.086  1.00 51.67           O  
ANISOU 1638  O   TRP A 219     6368   7202   6062    489    208    935       O  
ATOM   1639  CB  TRP A 219     -12.725 -32.654 -37.319  1.00 54.98           C  
ANISOU 1639  CB  TRP A 219     6830   7412   6650    396    246    638       C  
ATOM   1640  CG  TRP A 219     -13.498 -33.942 -37.386  1.00 57.17           C  
ANISOU 1640  CG  TRP A 219     7188   7542   6991    419    376    659       C  
ATOM   1641  CD1 TRP A 219     -13.179 -35.126 -36.785  1.00 67.29           C  
ANISOU 1641  CD1 TRP A 219     8481   8779   8308    506    459    808       C  
ATOM   1642  CD2 TRP A 219     -14.702 -34.181 -38.125  1.00 67.40           C  
ANISOU 1642  CD2 TRP A 219     8567   8714   8329    347    437    531       C  
ATOM   1643  NE1 TRP A 219     -14.118 -36.081 -37.089  1.00 73.91           N  
ANISOU 1643  NE1 TRP A 219     9414   9457   9213    483    571    775       N  
ATOM   1644  CE2 TRP A 219     -15.063 -35.526 -37.912  1.00 72.64           C  
ANISOU 1644  CE2 TRP A 219     9293   9252   9055    379    554    603       C  
ATOM   1645  CE3 TRP A 219     -15.513 -33.386 -38.940  1.00 71.73           C  
ANISOU 1645  CE3 TRP A 219     9138   9249   8867    257    401    371       C  
ATOM   1646  CZ2 TRP A 219     -16.200 -36.093 -38.484  1.00 78.16           C  
ANISOU 1646  CZ2 TRP A 219    10075   9818   9807    305    628    511       C  
ATOM   1647  CZ3 TRP A 219     -16.640 -33.951 -39.507  1.00 80.56           C  
ANISOU 1647  CZ3 TRP A 219    10327  10252  10030    195    472    287       C  
ATOM   1648  CH2 TRP A 219     -16.974 -35.291 -39.276  1.00 84.30           C  
ANISOU 1648  CH2 TRP A 219    10859  10604  10565    210    580    353       C  
ATOM   1649  N   LYS A 220     -10.579 -32.972 -35.081  1.00 71.57           N  
ANISOU 1649  N   LYS A 220     8757   9796   8641    537    135    985       N  
ATOM   1650  CA  LYS A 220      -9.794 -33.862 -34.233  1.00 72.21           C  
ANISOU 1650  CA  LYS A 220     8782   9939   8715    647    160   1187       C  
ATOM   1651  C   LYS A 220      -9.760 -33.388 -32.786  1.00 75.87           C  
ANISOU 1651  C   LYS A 220     9212  10582   9033    620     47   1245       C  
ATOM   1652  O   LYS A 220      -9.714 -34.214 -31.867  1.00 77.15           O  
ANISOU 1652  O   LYS A 220     9372  10778   9164    694     85   1391       O  
ATOM   1653  CB  LYS A 220      -8.373 -33.990 -34.783  1.00 57.59           C  
ANISOU 1653  CB  LYS A 220     6821   8132   6927    730    158   1297       C  
ATOM   1654  N   ALA A 221      -9.782 -32.073 -32.561  1.00 68.75           N  
ANISOU 1654  N   ALA A 221     8294   9792   8036    516    -89   1135       N  
ATOM   1655  CA  ALA A 221      -9.740 -31.557 -31.196  1.00 55.69           C  
ANISOU 1655  CA  ALA A 221     6624   8309   6225    482   -203   1168       C  
ATOM   1656  C   ALA A 221     -11.059 -31.803 -30.475  1.00 66.71           C  
ANISOU 1656  C   ALA A 221     8126   9668   7554    467   -148   1122       C  
ATOM   1657  O   ALA A 221     -11.075 -32.257 -29.324  1.00 77.71           O  
ANISOU 1657  O   ALA A 221     9518  11155   8855    511   -152   1238       O  
ATOM   1658  CB  ALA A 221      -9.398 -30.067 -31.207  1.00 48.30           C  
ANISOU 1658  CB  ALA A 221     5663   7477   5210    368   -356   1048       C  
ATOM   1659  N   LEU A 222     -12.181 -31.507 -31.137  1.00 65.34           N  
ANISOU 1659  N   LEU A 222     8035   9370   7423    407    -94    964       N  
ATOM   1660  CA  LEU A 222     -13.483 -31.744 -30.524  1.00 60.10           C  
ANISOU 1660  CA  LEU A 222     7454   8676   6707    391    -31    926       C  
ATOM   1661  C   LEU A 222     -13.750 -33.230 -30.325  1.00 67.65           C  
ANISOU 1661  C   LEU A 222     8430   9540   7735    470    105   1067       C  
ATOM   1662  O   LEU A 222     -14.503 -33.606 -29.420  1.00 74.58           O  
ANISOU 1662  O   LEU A 222     9349  10444   8546    478    149   1114       O  
ATOM   1663  CB  LEU A 222     -14.588 -31.115 -31.374  1.00 59.81           C  
ANISOU 1663  CB  LEU A 222     7480   8537   6711    313     -5    740       C  
ATOM   1664  CG  LEU A 222     -14.582 -29.588 -31.480  1.00 65.25           C  
ANISOU 1664  CG  LEU A 222     8175   9293   7322    236   -123    593       C  
ATOM   1665  CD1 LEU A 222     -15.666 -29.111 -32.433  1.00 62.84           C  
ANISOU 1665  CD1 LEU A 222     7922   8880   7075    182    -80    437       C  
ATOM   1666  CD2 LEU A 222     -14.756 -28.957 -30.107  1.00 59.56           C  
ANISOU 1666  CD2 LEU A 222     7484   8717   6429    220   -200    588       C  
ATOM   1667  N   LYS A 223     -13.149 -34.085 -31.155  1.00 75.06           N  
ANISOU 1667  N   LYS A 223     9346  10365   8808    531    182   1138       N  
ATOM   1668  CA  LYS A 223     -13.316 -35.524 -30.983  1.00 78.00           C  
ANISOU 1668  CA  LYS A 223     9752  10625   9259    610    319   1277       C  
ATOM   1669  C   LYS A 223     -12.609 -36.011 -29.725  1.00 80.73           C  
ANISOU 1669  C   LYS A 223    10047  11104   9521    702    296   1482       C  
ATOM   1670  O   LYS A 223     -13.175 -36.782 -28.941  1.00 89.94           O  
ANISOU 1670  O   LYS A 223    11257  12252  10665    735    373   1582       O  
ATOM   1671  CB  LYS A 223     -12.798 -36.266 -32.214  1.00 84.59           C  
ANISOU 1671  CB  LYS A 223    10592  11295  10251    663    411   1290       C  
ATOM   1672  CG  LYS A 223     -13.892 -36.787 -33.129  1.00 83.36           C  
ANISOU 1672  CG  LYS A 223    10534  10939  10200    604    523   1174       C  
ATOM   1673  CD  LYS A 223     -14.766 -37.803 -32.412  1.00 85.31           C  
ANISOU 1673  CD  LYS A 223    10847  11107  10461    609    627   1258       C  
ATOM   1674  CE  LYS A 223     -15.861 -38.331 -33.322  1.00 93.90           C  
ANISOU 1674  CE  LYS A 223    12024  12002  11652    526    727   1141       C  
ATOM   1675  NZ  LYS A 223     -16.707 -39.350 -32.641  1.00 98.12           N  
ANISOU 1675  NZ  LYS A 223    12618  12451  12213    514    833   1233       N  
ATOM   1676  N   LYS A 224     -11.365 -35.570 -29.514  1.00 77.27           N  
ANISOU 1676  N   LYS A 224     9512  10813   9034    742    191   1555       N  
ATOM   1677  CA  LYS A 224     -10.635 -35.968 -28.316  1.00 76.15           C  
ANISOU 1677  CA  LYS A 224     9306  10829   8797    828    150   1757       C  
ATOM   1678  C   LYS A 224     -11.295 -35.429 -27.054  1.00 81.94           C  
ANISOU 1678  C   LYS A 224    10074  11709   9350    774     77   1735       C  
ATOM   1679  O   LYS A 224     -11.204 -36.054 -25.991  1.00 94.90           O  
ANISOU 1679  O   LYS A 224    11708  13438  10913    845     95   1902       O  
ATOM   1680  CB  LYS A 224      -9.184 -35.493 -28.403  1.00 70.06           C  
ANISOU 1680  CB  LYS A 224     8405  10208   8006    860     33   1830       C  
ATOM   1681  N   ALA A 225     -11.964 -34.279 -27.150  1.00 69.37           N  
ANISOU 1681  N   ALA A 225     8525  10144   7686    659      4   1538       N  
ATOM   1682  CA  ALA A 225     -12.658 -33.725 -25.993  1.00 64.85           C  
ANISOU 1682  CA  ALA A 225     8003   9700   6937    616    -49   1498       C  
ATOM   1683  C   ALA A 225     -13.988 -34.428 -25.749  1.00 60.45           C  
ANISOU 1683  C   ALA A 225     7529   9035   6402    622     92   1503       C  
ATOM   1684  O   ALA A 225     -14.363 -34.668 -24.596  1.00 86.58           O  
ANISOU 1684  O   ALA A 225    10864  12446   9587    650    106   1592       O  
ATOM   1685  CB  ALA A 225     -12.873 -32.223 -26.178  1.00 60.59           C  
ANISOU 1685  CB  ALA A 225     7488   9217   6316    504   -167   1288       C  
ATOM   1686  N   TYR A 226     -14.714 -34.766 -26.818  1.00 86.32           N  
ANISOU 1686  N   TYR A 226    11470  12136   9193   -437   1060   1606       N  
ATOM   1687  CA  TYR A 226     -15.996 -35.443 -26.649  1.00 85.53           C  
ANISOU 1687  CA  TYR A 226    11558  12141   8798   -513    811   1421       C  
ATOM   1688  C   TYR A 226     -15.805 -36.906 -26.268  1.00 84.85           C  
ANISOU 1688  C   TYR A 226    11563  11985   8690   -449   1079   1261       C  
ATOM   1689  O   TYR A 226     -16.563 -37.441 -25.450  1.00 83.02           O  
ANISOU 1689  O   TYR A 226    11227  11836   8480   -436    855   1161       O  
ATOM   1690  CB  TYR A 226     -16.832 -35.324 -27.924  1.00 88.75           C  
ANISOU 1690  CB  TYR A 226    12418  12581   8720   -756    702   1444       C  
ATOM   1691  CG  TYR A 226     -17.465 -33.963 -28.130  1.00 91.38           C  
ANISOU 1691  CG  TYR A 226    12649  13009   9061   -810    295   1603       C  
ATOM   1692  CD1 TYR A 226     -17.253 -32.929 -27.227  1.00 85.28           C  
ANISOU 1692  CD1 TYR A 226    11475  12237   8690   -635     78   1677       C  
ATOM   1693  CD2 TYR A 226     -18.287 -33.718 -29.223  1.00 97.60           C  
ANISOU 1693  CD2 TYR A 226    13795  13848   9439  -1029     88   1681       C  
ATOM   1694  CE1 TYR A 226     -17.833 -31.686 -27.412  1.00 90.32           C  
ANISOU 1694  CE1 TYR A 226    12077  12898   9342   -639   -281   1817       C  
ATOM   1695  CE2 TYR A 226     -18.873 -32.480 -29.415  1.00100.70           C  
ANISOU 1695  CE2 TYR A 226    14088  14309   9867  -1042   -286   1862       C  
ATOM   1696  CZ  TYR A 226     -18.643 -31.468 -28.507  1.00 94.52           C  
ANISOU 1696  CZ  TYR A 226    12907  13498   9507   -827   -444   1925       C  
ATOM   1697  OH  TYR A 226     -19.224 -30.235 -28.695  1.00 88.76           O  
ANISOU 1697  OH  TYR A 226    12131  12774   8819   -796   -802   2098       O  
ATOM   1698  N   ASP A 227     -14.803 -37.571 -26.850  1.00 87.36           N  
ANISOU 1698  N   ASP A 227    12081  12139   8973   -381   1592   1268       N  
ATOM   1699  CA  ASP A 227     -14.529 -38.955 -26.477  1.00 87.98           C  
ANISOU 1699  CA  ASP A 227    12274  12087   9069   -267   1870   1129       C  
ATOM   1700  C   ASP A 227     -14.050 -39.063 -25.036  1.00 93.49           C  
ANISOU 1700  C   ASP A 227    12445  12823  10252    -54   1778   1165       C  
ATOM   1701  O   ASP A 227     -14.312 -40.072 -24.371  1.00 96.21           O  
ANISOU 1701  O   ASP A 227    12814  13124  10616      1   1774   1055       O  
ATOM   1702  CB  ASP A 227     -13.496 -39.568 -27.423  1.00 99.27           C  
ANISOU 1702  CB  ASP A 227    14042  13311  10367   -141   2513   1153       C  
ATOM   1703  CG  ASP A 227     -14.067 -39.872 -28.795  1.00 99.32           C  
ANISOU 1703  CG  ASP A 227    14793  13211   9733   -338   2612   1034       C  
ATOM   1704  OD1 ASP A 227     -15.276 -39.637 -29.004  1.00 94.39           O  
ANISOU 1704  OD1 ASP A 227    14358  12685   8822   -619   2115    961       O  
ATOM   1705  OD2 ASP A 227     -13.307 -40.349 -29.663  1.00 99.56           O  
ANISOU 1705  OD2 ASP A 227    15235  13059   9536   -194   3184   1034       O  
ATOM   1706  N   LEU A 228     -13.348 -38.041 -24.538  1.00 95.56           N  
ANISOU 1706  N   LEU A 228    12273  13141  10895     42   1663   1334       N  
ATOM   1707  CA  LEU A 228     -12.922 -38.049 -23.143  1.00 82.88           C  
ANISOU 1707  CA  LEU A 228    10240  11560   9692    217   1462   1366       C  
ATOM   1708  C   LEU A 228     -14.118 -37.962 -22.203  1.00 84.28           C  
ANISOU 1708  C   LEU A 228    10394  11886   9744    210   1017   1231       C  
ATOM   1709  O   LEU A 228     -14.161 -38.654 -21.179  1.00 92.04           O  
ANISOU 1709  O   LEU A 228    11261  12885  10826    342    962   1184       O  
ATOM   1710  CB  LEU A 228     -11.953 -36.897 -22.883  1.00 87.79           C  
ANISOU 1710  CB  LEU A 228    10472  12158  10727    248   1327   1584       C  
ATOM   1711  CG  LEU A 228     -11.515 -36.704 -21.430  1.00 87.26           C  
ANISOU 1711  CG  LEU A 228    10035  12088  11030    386    971   1617       C  
ATOM   1712  CD1 LEU A 228     -10.714 -37.903 -20.946  1.00 84.11           C  
ANISOU 1712  CD1 LEU A 228     9474  11621  10861    566   1258   1674       C  
ATOM   1713  CD2 LEU A 228     -10.720 -35.418 -21.270  1.00 95.71           C  
ANISOU 1713  CD2 LEU A 228    10807  13082  12476    313    687   1827       C  
ATOM   1714  N   GLU A 229     -15.097 -37.118 -22.535  1.00 84.33           N  
ANISOU 1714  N   GLU A 229    10498  12008   9537     88    726   1211       N  
ATOM   1715  CA  GLU A 229     -16.285 -36.996 -21.697  1.00 77.45           C  
ANISOU 1715  CA  GLU A 229     9560  11307   8559    140    386   1144       C  
ATOM   1716  C   GLU A 229     -17.093 -38.288 -21.693  1.00 80.43           C  
ANISOU 1716  C   GLU A 229    10097  11735   8729     42    479   1076       C  
ATOM   1717  O   GLU A 229     -17.629 -38.688 -20.653  1.00 78.74           O  
ANISOU 1717  O   GLU A 229     9739  11632   8548    154    367   1071       O  
ATOM   1718  CB  GLU A 229     -17.145 -35.826 -22.173  1.00 86.48           C  
ANISOU 1718  CB  GLU A 229    10746  12551   9561     69     96   1192       C  
ATOM   1719  CG  GLU A 229     -18.335 -35.523 -21.277  1.00104.20           C  
ANISOU 1719  CG  GLU A 229    12858  14988  11745    220   -194   1183       C  
ATOM   1720  CD  GLU A 229     -19.170 -34.367 -21.790  1.00115.48           C  
ANISOU 1720  CD  GLU A 229    14307  16496  13076    209   -456   1267       C  
ATOM   1721  OE1 GLU A 229     -20.381 -34.562 -22.028  1.00116.75           O  
ANISOU 1721  OE1 GLU A 229    14447  16840  13073    140   -569   1341       O  
ATOM   1722  OE2 GLU A 229     -18.613 -33.263 -21.963  1.00117.67           O  
ANISOU 1722  OE2 GLU A 229    14599  16636  13474    258   -571   1300       O  
ATOM   1723  N   ASP A 230     -17.189 -38.955 -22.846  1.00 96.99           N  
ANISOU 1723  N   ASP A 230    12538  13725  10588   -178    676   1036       N  
ATOM   1724  CA  ASP A 230     -17.909 -40.222 -22.905  1.00114.13           C  
ANISOU 1724  CA  ASP A 230    14931  15857  12576   -340    701    973       C  
ATOM   1725  C   ASP A 230     -17.197 -41.311 -22.115  1.00104.31           C  
ANISOU 1725  C   ASP A 230    13643  14466  11524   -172    955    934       C  
ATOM   1726  O   ASP A 230     -17.847 -42.234 -21.612  1.00101.84           O  
ANISOU 1726  O   ASP A 230    13365  14151  11177   -246    893    934       O  
ATOM   1727  CB  ASP A 230     -18.098 -40.656 -24.359  1.00131.44           C  
ANISOU 1727  CB  ASP A 230    17644  17890  14407   -618    801    903       C  
ATOM   1728  CG  ASP A 230     -19.052 -39.754 -25.115  1.00139.30           C  
ANISOU 1728  CG  ASP A 230    18702  19046  15177   -834    452    983       C  
ATOM   1729  OD1 ASP A 230     -19.555 -38.785 -24.510  1.00137.75           O  
ANISOU 1729  OD1 ASP A 230    18121  19073  15143   -725    182   1095       O  
ATOM   1730  OD2 ASP A 230     -19.301 -40.015 -26.310  1.00144.57           O  
ANISOU 1730  OD2 ASP A 230    19848  19599  15484  -1088    439    939       O  
ATOM   1731  N   ASN A 231     -15.870 -41.226 -21.996  1.00 97.32           N  
ANISOU 1731  N   ASN A 231    12646  13453  10877     45   1227    954       N  
ATOM   1732  CA  ASN A 231     -15.144 -42.190 -21.177  1.00 94.95           C  
ANISOU 1732  CA  ASN A 231    12244  13022  10813    248   1430    969       C  
ATOM   1733  C   ASN A 231     -15.436 -41.983 -19.696  1.00100.79           C  
ANISOU 1733  C   ASN A 231    12636  13941  11718    400   1134   1034       C  
ATOM   1734  O   ASN A 231     -15.618 -42.955 -18.953  1.00108.99           O  
ANISOU 1734  O   ASN A 231    13682  14942  12789    458   1165   1053       O  
ATOM   1735  CB  ASN A 231     -13.643 -42.093 -21.450  1.00 89.81           C  
ANISOU 1735  CB  ASN A 231    11467  12220  10438    453   1779   1057       C  
ATOM   1736  CG  ASN A 231     -13.264 -42.638 -22.813  1.00 92.48           C  
ANISOU 1736  CG  ASN A 231    12241  12338  10560    412   2235    998       C  
ATOM   1737  OD1 ASN A 231     -13.942 -43.511 -23.356  1.00 88.13           O  
ANISOU 1737  OD1 ASN A 231    12171  11641   9675    259   2298    846       O  
ATOM   1738  ND2 ASN A 231     -12.173 -42.128 -23.372  1.00104.02           N  
ANISOU 1738  ND2 ASN A 231    13566  13757  12200    546   2553   1138       N  
ATOM   1739  N   TRP A 232     -15.487 -40.726 -19.248  1.00 97.99           N  
ANISOU 1739  N   TRP A 232    12043  13753  11437    479    851   1072       N  
ATOM   1740  CA  TRP A 232     -15.849 -40.457 -17.860  1.00 98.79           C  
ANISOU 1740  CA  TRP A 232    11946  14011  11580    665    579   1102       C  
ATOM   1741  C   TRP A 232     -17.313 -40.787 -17.601  1.00 96.67           C  
ANISOU 1741  C   TRP A 232    11728  13935  11069    584    481   1118       C  
ATOM   1742  O   TRP A 232     -17.660 -41.290 -16.526  1.00109.16           O  
ANISOU 1742  O   TRP A 232    13229  15611  12637    721    450   1182       O  
ATOM   1743  CB  TRP A 232     -15.560 -38.997 -17.508  1.00100.45           C  
ANISOU 1743  CB  TRP A 232    12012  14272  11883    779    283   1105       C  
ATOM   1744  CG  TRP A 232     -14.101 -38.674 -17.421  1.00 98.82           C  
ANISOU 1744  CG  TRP A 232    11638  13896  12012    842    280   1179       C  
ATOM   1745  CD1 TRP A 232     -13.392 -37.854 -18.248  1.00105.28           C  
ANISOU 1745  CD1 TRP A 232    12386  14615  13002    735    300   1250       C  
ATOM   1746  CD2 TRP A 232     -13.169 -39.169 -16.451  1.00103.19           C  
ANISOU 1746  CD2 TRP A 232    12022  14370  12814   1006    233   1262       C  
ATOM   1747  NE1 TRP A 232     -12.077 -37.804 -17.852  1.00110.51           N  
ANISOU 1747  NE1 TRP A 232    12788  15151  14052    805    271   1396       N  
ATOM   1748  CE2 TRP A 232     -11.914 -38.604 -16.752  1.00106.20           C  
ANISOU 1748  CE2 TRP A 232    12177  14614  13560    975    202   1400       C  
ATOM   1749  CE3 TRP A 232     -13.275 -40.035 -15.358  1.00108.70           C  
ANISOU 1749  CE3 TRP A 232    12722  15104  13474   1168    199   1278       C  
ATOM   1750  CZ2 TRP A 232     -10.773 -38.876 -16.000  1.00112.06           C  
ANISOU 1750  CZ2 TRP A 232    12654  15261  14662   1090     92   1563       C  
ATOM   1751  CZ3 TRP A 232     -12.141 -40.304 -14.612  1.00112.56           C  
ANISOU 1751  CZ3 TRP A 232    13018  15487  14264   1302     92   1410       C  
ATOM   1752  CH2 TRP A 232     -10.907 -39.726 -14.937  1.00114.24           C  
ANISOU 1752  CH2 TRP A 232    12966  15569  14869   1258     18   1554       C  
ATOM   1753  N   GLU A 233     -18.186 -40.511 -18.573  1.00 95.96           N  
ANISOU 1753  N   GLU A 233    11745  13916  10800    357    424   1112       N  
ATOM   1754  CA  GLU A 233     -19.594 -40.862 -18.421  1.00 93.94           C  
ANISOU 1754  CA  GLU A 233    11441  13856  10395    232    310   1214       C  
ATOM   1755  C   GLU A 233     -19.793 -42.372 -18.398  1.00 87.67           C  
ANISOU 1755  C   GLU A 233    10787  12936   9586     46    456   1251       C  
ATOM   1756  O   GLU A 233     -20.753 -42.860 -17.790  1.00 89.54           O  
ANISOU 1756  O   GLU A 233    10886  13332   9805     -5    391   1410       O  
ATOM   1757  CB  GLU A 233     -20.418 -40.234 -19.544  1.00105.52           C  
ANISOU 1757  CB  GLU A 233    12973  15409  11711     -3    142   1245       C  
ATOM   1758  N   THR A 234     -18.903 -43.124 -19.049  1.00 87.89           N  
ANISOU 1758  N   THR A 234    11097  12662   9636    -40    677   1136       N  
ATOM   1759  CA  THR A 234     -18.995 -44.579 -19.010  1.00 89.50           C  
ANISOU 1759  CA  THR A 234    11523  12647   9834   -186    813   1147       C  
ATOM   1760  C   THR A 234     -18.584 -45.117 -17.644  1.00 88.78           C  
ANISOU 1760  C   THR A 234    11236  12568   9928     82    898   1247       C  
ATOM   1761  O   THR A 234     -19.167 -46.090 -17.151  1.00 87.66           O  
ANISOU 1761  O   THR A 234    11124  12392   9791    -26    898   1370       O  
ATOM   1762  CB  THR A 234     -18.130 -45.189 -20.114  1.00 93.72           C  
ANISOU 1762  CB  THR A 234    12495  12813  10300   -259   1085    980       C  
ATOM   1763  OG1 THR A 234     -18.513 -44.639 -21.381  1.00113.53           O  
ANISOU 1763  OG1 THR A 234    15254  15323  12558   -501    991    898       O  
ATOM   1764  CG2 THR A 234     -18.296 -46.701 -20.159  1.00 85.23           C  
ANISOU 1764  CG2 THR A 234    11772  11421   9189   -416   1194    960       C  
ATOM   1765  N   LEU A 235     -17.587 -44.490 -17.014  1.00 90.55           N  
ANISOU 1765  N   LEU A 235    11269  12827  10308    403    928   1230       N  
ATOM   1766  CA  LEU A 235     -17.145 -44.937 -15.696  1.00 91.72           C  
ANISOU 1766  CA  LEU A 235    11270  12989  10591    663    939   1339       C  
ATOM   1767  C   LEU A 235     -18.206 -44.669 -14.635  1.00 97.81           C  
ANISOU 1767  C   LEU A 235    11867  14071  11225    744    769   1481       C  
ATOM   1768  O   LEU A 235     -18.456 -45.519 -13.772  1.00102.75           O  
ANISOU 1768  O   LEU A 235    12481  14711  11850    800    825   1636       O  
ATOM   1769  CB  LEU A 235     -15.832 -44.250 -15.321  1.00 92.10           C  
ANISOU 1769  CB  LEU A 235    11154  12992  10847    931    902   1316       C  
ATOM   1770  CG  LEU A 235     -14.629 -44.488 -16.235  1.00 95.94           C  
ANISOU 1770  CG  LEU A 235    11699  13211  11544    944   1161   1271       C  
ATOM   1771  CD1 LEU A 235     -13.430 -43.681 -15.762  1.00 94.97           C  
ANISOU 1771  CD1 LEU A 235    11282  13097  11706   1154   1033   1347       C  
ATOM   1772  CD2 LEU A 235     -14.288 -45.965 -16.299  1.00100.77           C  
ANISOU 1772  CD2 LEU A 235    12504  13543  12242    976   1452   1309       C  
ATOM   1773  N   ASN A 236     -18.838 -43.495 -14.682  1.00103.03           N  
ANISOU 1773  N   ASN A 236    12404  14975  11766    787    600   1461       N  
ATOM   1774  CA  ASN A 236     -19.831 -43.149 -13.668  1.00110.27           C  
ANISOU 1774  CA  ASN A 236    13162  16199  12534    969    527   1614       C  
ATOM   1775  C   ASN A 236     -21.109 -43.960 -13.842  1.00109.84           C  
ANISOU 1775  C   ASN A 236    13021  16273  12440    705    595   1834       C  
ATOM   1776  O   ASN A 236     -21.726 -44.374 -12.853  1.00117.00           O  
ANISOU 1776  O   ASN A 236    13800  17364  13292    827    676   2062       O  
ATOM   1777  CB  ASN A 236     -20.133 -41.652 -13.718  1.00122.46           C  
ANISOU 1777  CB  ASN A 236    14634  17913  13981   1145    356   1533       C  
ATOM   1778  CG  ASN A 236     -18.927 -40.803 -13.366  1.00130.27           C  
ANISOU 1778  CG  ASN A 236    15705  18756  15034   1368    201   1364       C  
ATOM   1779  OD1 ASN A 236     -17.788 -41.263 -13.433  1.00129.06           O  
ANISOU 1779  OD1 ASN A 236    15591  18384  15060   1331    230   1319       O  
ATOM   1780  ND2 ASN A 236     -19.174 -39.554 -12.986  1.00134.81           N  
ANISOU 1780  ND2 ASN A 236    16302  19429  15492   1604     18   1299       N  
ATOM   1781  N   ASP A 237     -21.526 -44.194 -15.088  1.00104.17           N  
ANISOU 1781  N   ASP A 237    12382  15455  11742    322    542   1804       N  
ATOM   1782  CA  ASP A 237     -22.741 -44.969 -15.322  1.00109.90           C  
ANISOU 1782  CA  ASP A 237    13012  16265  12480    -24    495   2050       C  
ATOM   1783  C   ASP A 237     -22.546 -46.433 -14.948  1.00111.52           C  
ANISOU 1783  C   ASP A 237    13372  16228  12771   -178    619   2151       C  
ATOM   1784  O   ASP A 237     -23.466 -47.073 -14.428  1.00112.71           O  
ANISOU 1784  O   ASP A 237    13339  16512  12975   -323    624   2464       O  
ATOM   1785  CB  ASP A 237     -23.180 -44.839 -16.780  1.00128.24           C  
ANISOU 1785  CB  ASP A 237    15474  18493  14757   -430    304   1977       C  
ATOM   1786  CG  ASP A 237     -23.698 -43.453 -17.111  1.00141.40           C  
ANISOU 1786  CG  ASP A 237    16927  20434  16365   -311    147   1992       C  
ATOM   1787  OD1 ASP A 237     -23.713 -42.591 -16.208  1.00146.67           O  
ANISOU 1787  OD1 ASP A 237    17376  21329  17023    106    205   2028       O  
ATOM   1788  OD2 ASP A 237     -24.090 -43.227 -18.275  1.00144.46           O  
ANISOU 1788  OD2 ASP A 237    17421  20779  16688   -621    -52   1967       O  
ATOM   1789  N   ASN A 238     -21.356 -46.982 -15.205  1.00111.46           N  
ANISOU 1789  N   ASN A 238    13680  15857  12813   -135    739   1934       N  
ATOM   1790  CA  ASN A 238     -21.097 -48.373 -14.844  1.00117.86           C  
ANISOU 1790  CA  ASN A 238    14684  16375  13724   -226    864   2026       C  
ATOM   1791  C   ASN A 238     -20.896 -48.538 -13.343  1.00124.78           C  
ANISOU 1791  C   ASN A 238    15365  17413  14633    123    966   2227       C  
ATOM   1792  O   ASN A 238     -21.210 -49.600 -12.792  1.00133.17           O  
ANISOU 1792  O   ASN A 238    16463  18375  15762     16   1033   2460       O  
ATOM   1793  CB  ASN A 238     -19.882 -48.900 -15.607  1.00112.87           C  
ANISOU 1793  CB  ASN A 238    14446  15293  13145   -202   1019   1761       C  
ATOM   1794  CG  ASN A 238     -20.201 -49.230 -17.051  1.00123.17           C  
ANISOU 1794  CG  ASN A 238    16141  16327  14330   -601    954   1597       C  
ATOM   1795  OD1 ASN A 238     -20.445 -50.386 -17.396  1.00119.78           O  
ANISOU 1795  OD1 ASN A 238    16067  15545  13899   -884    948   1610       O  
ATOM   1796  ND2 ASN A 238     -20.211 -48.211 -17.902  1.00131.54           N  
ANISOU 1796  ND2 ASN A 238    17201  17519  15260   -637    872   1445       N  
ATOM   1797  N   LEU A 239     -20.372 -47.512 -12.667  1.00114.42           N  
ANISOU 1797  N   LEU A 239    13904  16319  13253    521    947   2150       N  
ATOM   1798  CA  LEU A 239     -20.250 -47.576 -11.215  1.00 94.80           C  
ANISOU 1798  CA  LEU A 239    11324  14002  10695    863    992   2332       C  
ATOM   1799  C   LEU A 239     -21.616 -47.625 -10.545  1.00 94.42           C  
ANISOU 1799  C   LEU A 239    11052  14303  10520    843   1054   2663       C  
ATOM   1800  O   LEU A 239     -21.777 -48.284  -9.511  1.00107.61           O  
ANISOU 1800  O   LEU A 239    12708  16040  12138    968   1173   2928       O  
ATOM   1801  CB  LEU A 239     -19.443 -46.383 -10.701  1.00 86.98           C  
ANISOU 1801  CB  LEU A 239    10311  13121   9616   1246    865   2152       C  
ATOM   1802  N   LYS A 240     -22.610 -46.941 -11.118  1.00 91.30           N  
ANISOU 1802  N   LYS A 240    10453  14145  10090    704    994   2705       N  
ATOM   1803  CA  LYS A 240     -23.967 -47.033 -10.593  1.00 99.55           C  
ANISOU 1803  CA  LYS A 240    11181  15545  11099    676   1099   3107       C  
ATOM   1804  C   LYS A 240     -24.593 -48.387 -10.901  1.00109.38           C  
ANISOU 1804  C   LYS A 240    12382  16632  12547    179   1104   3404       C  
ATOM   1805  O   LYS A 240     -25.480 -48.838 -10.169  1.00107.38           O  
ANISOU 1805  O   LYS A 240    11863  16613  12321    154   1248   3843       O  
ATOM   1806  CB  LYS A 240     -24.829 -45.906 -11.162  1.00 96.16           C  
ANISOU 1806  CB  LYS A 240    10492  15404  10641    690   1011   3115       C  
ATOM   1807  N   VAL A 241     -24.151 -49.043 -11.976  1.00120.41           N  
ANISOU 1807  N   VAL A 241    14067  17609  14074   -214    956   3191       N  
ATOM   1808  CA  VAL A 241     -24.649 -50.378 -12.289  1.00129.74           C  
ANISOU 1808  CA  VAL A 241    15347  18515  15432   -715    892   3422       C  
ATOM   1809  C   VAL A 241     -24.124 -51.392 -11.279  1.00131.53           C  
ANISOU 1809  C   VAL A 241    15722  18551  15703   -567   1077   3586       C  
ATOM   1810  O   VAL A 241     -24.846 -52.306 -10.863  1.00139.88           O  
ANISOU 1810  O   VAL A 241    16672  19586  16889   -835   1105   3993       O  
ATOM   1811  CB  VAL A 241     -24.275 -50.762 -13.733  1.00129.03           C  
ANISOU 1811  CB  VAL A 241    15683  17967  15376  -1113    691   3090       C  
ATOM   1812  CG1 VAL A 241     -24.592 -52.226 -14.000  1.00133.14           C  
ANISOU 1812  CG1 VAL A 241    16483  18055  16047  -1604    590   3254       C  
ATOM   1813  CG2 VAL A 241     -25.007 -49.873 -14.723  1.00132.16           C  
ANISOU 1813  CG2 VAL A 241    15927  18571  15718  -1340    450   3034       C  
ATOM   1814  N   ILE A 242     -22.864 -51.242 -10.862  1.00121.45           N  
ANISOU 1814  N   ILE A 242    14666  17132  14349   -156   1178   3325       N  
ATOM   1815  CA  ILE A 242     -22.289 -52.160  -9.882  1.00121.11           C  
ANISOU 1815  CA  ILE A 242    14767  16906  14343     28   1315   3500       C  
ATOM   1816  C   ILE A 242     -23.002 -52.025  -8.543  1.00130.13           C  
ANISOU 1816  C   ILE A 242    15623  18485  15336    263   1464   3921       C  
ATOM   1817  O   ILE A 242     -23.257 -53.022  -7.854  1.00141.63           O  
ANISOU 1817  O   ILE A 242    17099  19859  16855    177   1573   4289       O  
ATOM   1818  CB  ILE A 242     -20.774 -51.916  -9.745  1.00110.58           C  
ANISOU 1818  CB  ILE A 242    13647  15369  13000    423   1332   3180       C  
ATOM   1819  CG1 ILE A 242     -20.077 -52.116 -11.092  1.00110.60           C  
ANISOU 1819  CG1 ILE A 242    13932  14949  13142    241   1303   2822       C  
ATOM   1820  CG2 ILE A 242     -20.173 -52.838  -8.695  1.00105.35           C  
ANISOU 1820  CG2 ILE A 242    13111  14532  12384    640   1424   3405       C  
ATOM   1821  CD1 ILE A 242     -18.584 -51.872 -11.051  1.00107.59           C  
ANISOU 1821  CD1 ILE A 242    13645  14389  12845    620   1358   2592       C  
ATOM   1822  N   GLU A 243     -23.341 -50.793  -8.154  1.00121.88           N  
ANISOU 1822  N   GLU A 243    14352  17887  14071    589   1500   3889       N  
ATOM   1823  CA  GLU A 243     -24.052 -50.584  -6.897  1.00107.29           C  
ANISOU 1823  CA  GLU A 243    12296  16469  12000    901   1723   4278       C  
ATOM   1824  C   GLU A 243     -25.462 -51.159  -6.945  1.00111.14           C  
ANISOU 1824  C   GLU A 243    12413  17158  12657    532   1850   4800       C  
ATOM   1825  O   GLU A 243     -26.003 -51.556  -5.907  1.00108.19           O  
ANISOU 1825  O   GLU A 243    11894  17025  12188    675   2108   5265       O  
ATOM   1826  CB  GLU A 243     -24.097 -49.093  -6.562  1.00100.22           C  
ANISOU 1826  CB  GLU A 243    11337  15932  10810   1372   1739   4077       C  
ATOM   1827  N   LYS A 244     -26.068 -51.214  -8.129  1.00123.32           N  
ANISOU 1827  N   LYS A 244    13794  18611  14451     42   1655   4777       N  
ATOM   1828  CA  LYS A 244     -27.402 -51.772  -8.301  1.00144.89           C  
ANISOU 1828  CA  LYS A 244    16116  21501  17436   -417   1659   5313       C  
ATOM   1829  C   LYS A 244     -27.382 -53.212  -8.795  1.00168.14           C  
ANISOU 1829  C   LYS A 244    19285  23931  20670  -1032   1467   5443       C  
ATOM   1830  O   LYS A 244     -28.448 -53.774  -9.068  1.00167.96           O  
ANISOU 1830  O   LYS A 244    18953  23943  20920  -1549   1354   5894       O  
ATOM   1831  CB  LYS A 244     -28.215 -50.907  -9.271  1.00140.24           C  
ANISOU 1831  CB  LYS A 244    15190  21146  16950   -613   1469   5280       C  
ATOM   1832  CG  LYS A 244     -28.391 -49.464  -8.823  1.00133.93           C  
ANISOU 1832  CG  LYS A 244    14173  20818  15897     -3   1662   5195       C  
ATOM   1833  CD  LYS A 244     -29.151 -49.379  -7.510  1.00132.05           C  
ANISOU 1833  CD  LYS A 244    13585  21054  15533    406   2097   5729       C  
ATOM   1834  CE  LYS A 244     -29.355 -47.934  -7.084  1.00121.10           C  
ANISOU 1834  CE  LYS A 244    12091  20069  13852   1068   2306   5609       C  
ATOM   1835  NZ  LYS A 244     -30.134 -47.832  -5.820  1.00116.55           N  
ANISOU 1835  NZ  LYS A 244    11239  19961  13085   1549   2817   6135       N  
ATOM   1836  N   ALA A 245     -26.205 -53.821  -8.917  1.00182.89           N  
ANISOU 1836  N   ALA A 245    21681  25298  22510   -986   1412   5086       N  
ATOM   1837  CA  ALA A 245     -26.103 -55.188  -9.399  1.00187.85           C  
ANISOU 1837  CA  ALA A 245    22652  25341  23383  -1498   1246   5149       C  
ATOM   1838  C   ALA A 245     -26.487 -56.178  -8.303  1.00182.94           C  
ANISOU 1838  C   ALA A 245    21922  24718  22869  -1560   1430   5732       C  
ATOM   1839  O   ALA A 245     -26.468 -55.865  -7.109  1.00180.09           O  
ANISOU 1839  O   ALA A 245    21365  24750  22312  -1091   1729   5984       O  
ATOM   1840  CB  ALA A 245     -24.688 -55.479  -9.898  1.00190.73           C  
ANISOU 1840  CB  ALA A 245    23603  25170  23697  -1326   1206   4602       C  
ATOM   1841  N   ASP A 246     -26.836 -57.394  -8.728  1.00180.95           N  
ANISOU 1841  N   ASP A 246    21867  23982  22904  -2158   1231   5950       N  
ATOM   1842  CA  ASP A 246     -27.247 -58.442  -7.807  1.00178.36           C  
ANISOU 1842  CA  ASP A 246    21457  23570  22742  -2327   1365   6559       C  
ATOM   1843  C   ASP A 246     -26.484 -59.749  -7.983  1.00179.42           C  
ANISOU 1843  C   ASP A 246    22228  22917  23027  -2526   1248   6440       C  
ATOM   1844  O   ASP A 246     -26.698 -60.677  -7.197  1.00195.25           O  
ANISOU 1844  O   ASP A 246    24240  24774  25174  -2648   1350   6942       O  
ATOM   1845  CB  ASP A 246     -28.753 -58.717  -7.946  1.00181.43           C  
ANISOU 1845  CB  ASP A 246    21311  24182  23442  -2951   1232   7199       C  
ATOM   1846  CG  ASP A 246     -29.603 -57.532  -7.526  1.00181.43           C  
ANISOU 1846  CG  ASP A 246    20599  25002  23334  -2649   1469   7485       C  
ATOM   1847  OD1 ASP A 246     -29.159 -56.761  -6.650  1.00178.79           O  
ANISOU 1847  OD1 ASP A 246    20211  25072  22649  -1936   1835   7383       O  
ATOM   1848  OD2 ASP A 246     -30.715 -57.373  -8.071  1.00185.72           O  
ANISOU 1848  OD2 ASP A 246    20658  25762  24145  -3115   1269   7825       O  
ATOM   1849  N   ASN A 247     -25.609 -59.853  -8.981  1.00168.32           N  
ANISOU 1849  N   ASN A 247    21371  20991  21592  -2528   1075   5824       N  
ATOM   1850  CA  ASN A 247     -24.813 -61.056  -9.175  1.00161.35           C  
ANISOU 1850  CA  ASN A 247    21145  19322  20839  -2597   1028   5675       C  
ATOM   1851  C   ASN A 247     -23.449 -60.664  -9.727  1.00152.03           C  
ANISOU 1851  C   ASN A 247    20370  17898  19495  -2101   1123   5012       C  
ATOM   1852  O   ASN A 247     -23.197 -59.502 -10.056  1.00147.85           O  
ANISOU 1852  O   ASN A 247    19633  17770  18775  -1824   1160   4677       O  
ATOM   1853  CB  ASN A 247     -25.522 -62.060 -10.095  1.00163.15           C  
ANISOU 1853  CB  ASN A 247    21738  18932  21320  -3395    649   5761       C  
ATOM   1854  CG  ASN A 247     -25.970 -61.444 -11.410  1.00162.46           C  
ANISOU 1854  CG  ASN A 247    21709  18864  21155  -3764    327   5394       C  
ATOM   1855  OD1 ASN A 247     -25.286 -60.595 -11.981  1.00159.61           O  
ANISOU 1855  OD1 ASN A 247    21463  18625  20555  -3391    410   4864       O  
ATOM   1856  ND2 ASN A 247     -27.128 -61.873 -11.897  1.00165.39           N  
ANISOU 1856  ND2 ASN A 247    21990  19109  21740  -4532    -76   5722       N  
ATOM   1857  N   ALA A 248     -22.564 -61.658  -9.826  1.00146.35           N  
ANISOU 1857  N   ALA A 248    20218  16501  18888  -1979   1178   4867       N  
ATOM   1858  CA  ALA A 248     -21.208 -61.406 -10.298  1.00135.95           C  
ANISOU 1858  CA  ALA A 248    19227  14936  17490  -1463   1339   4340       C  
ATOM   1859  C   ALA A 248     -21.146 -61.168 -11.801  1.00139.24           C  
ANISOU 1859  C   ALA A 248    20040  15054  17811  -1692   1217   3820       C  
ATOM   1860  O   ALA A 248     -20.164 -60.592 -12.283  1.00132.63           O  
ANISOU 1860  O   ALA A 248    19303  14218  16871  -1267   1391   3408       O  
ATOM   1861  CB  ALA A 248     -20.293 -62.572  -9.919  1.00129.00           C  
ANISOU 1861  CB  ALA A 248    18799  13420  16793  -1192   1483   4408       C  
ATOM   1862  N   ALA A 249     -22.163 -61.597 -12.551  1.00147.98           N  
ANISOU 1862  N   ALA A 249    21378  15904  18944  -2369    903   3865       N  
ATOM   1863  CA  ALA A 249     -22.150 -61.393 -13.996  1.00156.47           C  
ANISOU 1863  CA  ALA A 249    22935  16675  19842  -2610    740   3376       C  
ATOM   1864  C   ALA A 249     -22.340 -59.924 -14.350  1.00154.60           C  
ANISOU 1864  C   ALA A 249    22212  17127  19404  -2496    721   3199       C  
ATOM   1865  O   ALA A 249     -21.660 -59.401 -15.241  1.00145.09           O  
ANISOU 1865  O   ALA A 249    21288  15833  18005  -2273    823   2737       O  
ATOM   1866  CB  ALA A 249     -23.229 -62.250 -14.658  1.00163.04           C  
ANISOU 1866  CB  ALA A 249    24176  17027  20745  -3429    286   3507       C  
ATOM   1867  N   GLN A 250     -23.261 -59.242 -13.664  1.00157.88           N  
ANISOU 1867  N   GLN A 250    21908  18217  19862  -2617    626   3587       N  
ATOM   1868  CA  GLN A 250     -23.475 -57.822 -13.919  1.00155.14           C  
ANISOU 1868  CA  GLN A 250    21104  18499  19344  -2463    611   3449       C  
ATOM   1869  C   GLN A 250     -22.276 -56.987 -13.490  1.00154.58           C  
ANISOU 1869  C   GLN A 250    20886  18685  19164  -1746    938   3190       C  
ATOM   1870  O   GLN A 250     -21.975 -55.966 -14.120  1.00160.40           O  
ANISOU 1870  O   GLN A 250    21559  19642  19744  -1584    945   2876       O  
ATOM   1871  CB  GLN A 250     -24.739 -57.348 -13.203  1.00152.76           C  
ANISOU 1871  CB  GLN A 250    20079  18827  19134  -2669    504   3971       C  
ATOM   1872  CG  GLN A 250     -26.013 -58.011 -13.699  1.00156.34           C  
ANISOU 1872  CG  GLN A 250    20518  19112  19773  -3452    102   4311       C  
ATOM   1873  CD  GLN A 250     -27.108 -58.027 -12.651  1.00156.25           C  
ANISOU 1873  CD  GLN A 250    19782  19609  19976  -3594    143   5013       C  
ATOM   1874  OE1 GLN A 250     -26.873 -57.705 -11.486  1.00155.85           O  
ANISOU 1874  OE1 GLN A 250    19379  19961  19874  -3080    509   5223       O  
ATOM   1875  NE2 GLN A 250     -28.313 -58.406 -13.059  1.00155.94           N  
ANISOU 1875  NE2 GLN A 250    19525  19553  20171  -4294   -237   5411       N  
ATOM   1876  N   VAL A 251     -21.581 -57.401 -12.429  1.00147.67           N  
ANISOU 1876  N   VAL A 251    19955  17770  18382  -1343   1163   3352       N  
ATOM   1877  CA  VAL A 251     -20.388 -56.681 -11.998  1.00133.63           C  
ANISOU 1877  CA  VAL A 251    18039  16185  16549   -718   1377   3151       C  
ATOM   1878  C   VAL A 251     -19.238 -56.929 -12.966  1.00140.91           C  
ANISOU 1878  C   VAL A 251    19431  16608  17500   -529   1524   2733       C  
ATOM   1879  O   VAL A 251     -18.429 -56.032 -13.234  1.00138.01           O  
ANISOU 1879  O   VAL A 251    18932  16422  17083   -188   1631   2484       O  
ATOM   1880  CB  VAL A 251     -20.016 -57.080 -10.558  1.00121.93           C  
ANISOU 1880  CB  VAL A 251    16379  14808  15140   -368   1501   3496       C  
ATOM   1881  CG1 VAL A 251     -18.828 -56.264 -10.066  1.00118.01           C  
ANISOU 1881  CG1 VAL A 251    15706  14532  14598    215   1597   3329       C  
ATOM   1882  CG2 VAL A 251     -21.210 -56.901  -9.634  1.00115.74           C  
ANISOU 1882  CG2 VAL A 251    15184  14512  14281   -527   1452   3951       C  
ATOM   1883  N   LYS A 252     -19.147 -58.146 -13.509  1.00146.56           N  
ANISOU 1883  N   LYS A 252    20719  16666  18301   -735   1551   2672       N  
ATOM   1884  CA  LYS A 252     -18.091 -58.453 -14.468  1.00148.28           C  
ANISOU 1884  CA  LYS A 252    21455  16375  18511   -490   1784   2288       C  
ATOM   1885  C   LYS A 252     -18.275 -57.687 -15.771  1.00142.63           C  
ANISOU 1885  C   LYS A 252    20924  15724  17545   -681   1728   1924       C  
ATOM   1886  O   LYS A 252     -17.287 -57.306 -16.410  1.00148.48           O  
ANISOU 1886  O   LYS A 252    21807  16371  18237   -325   2000   1644       O  
ATOM   1887  CB  LYS A 252     -18.047 -59.957 -14.739  1.00154.54           C  
ANISOU 1887  CB  LYS A 252    22936  16381  19403   -646   1824   2291       C  
ATOM   1888  N   ASP A 253     -19.523 -57.449 -16.179  1.00133.77           N  
ANISOU 1888  N   ASP A 253    19771  14776  16278  -1236   1380   1977       N  
ATOM   1889  CA  ASP A 253     -19.765 -56.700 -17.408  1.00124.20           C  
ANISOU 1889  CA  ASP A 253    18749  13642  14799  -1442   1264   1672       C  
ATOM   1890  C   ASP A 253     -19.424 -55.226 -17.233  1.00126.93           C  
ANISOU 1890  C   ASP A 253    18509  14614  15104  -1108   1350   1627       C  
ATOM   1891  O   ASP A 253     -18.850 -54.605 -18.134  1.00133.34           O  
ANISOU 1891  O   ASP A 253    19498  15410  15754   -962   1486   1337       O  
ATOM   1892  CB  ASP A 253     -21.219 -56.867 -17.847  1.00118.66           C  
ANISOU 1892  CB  ASP A 253    18115  12960  14009  -2150    785   1815       C  
ATOM   1893  N   ALA A 254     -19.764 -54.650 -16.078  1.00121.85           N  
ANISOU 1893  N   ALA A 254    17218  14497  14581   -976   1282   1921       N  
ATOM   1894  CA  ALA A 254     -19.496 -53.233 -15.854  1.00125.63           C  
ANISOU 1894  CA  ALA A 254    17219  15507  15009   -676   1303   1869       C  
ATOM   1895  C   ALA A 254     -18.018 -52.983 -15.585  1.00132.02           C  
ANISOU 1895  C   ALA A 254    17973  16249  15939   -138   1588   1741       C  
ATOM   1896  O   ALA A 254     -17.465 -51.969 -16.028  1.00130.03           O  
ANISOU 1896  O   ALA A 254    17584  16178  15644     43   1643   1570       O  
ATOM   1897  CB  ALA A 254     -20.350 -52.713 -14.699  1.00125.92           C  
ANISOU 1897  CB  ALA A 254    16694  16078  15074   -656   1162   2205       C  
ATOM   1898  N   LEU A 255     -17.360 -53.892 -14.860  1.00137.92           N  
ANISOU 1898  N   LEU A 255    18793  16731  16877    106   1747   1873       N  
ATOM   1899  CA  LEU A 255     -15.944 -53.708 -14.559  1.00141.60           C  
ANISOU 1899  CA  LEU A 255    19121  17143  17538    607   1969   1838       C  
ATOM   1900  C   LEU A 255     -15.079 -53.847 -15.805  1.00142.49           C  
ANISOU 1900  C   LEU A 255    19594  16883  17662    731   2273   1567       C  
ATOM   1901  O   LEU A 255     -14.045 -53.178 -15.916  1.00133.51           O  
ANISOU 1901  O   LEU A 255    18206  15856  16666   1065   2436   1528       O  
ATOM   1902  CB  LEU A 255     -15.499 -54.705 -13.489  1.00139.88           C  
ANISOU 1902  CB  LEU A 255    18894  16722  17533    842   2035   2098       C  
ATOM   1903  N   THR A 256     -15.479 -54.704 -16.747  1.00146.64           N  
ANISOU 1903  N   THR A 256    20729  16954  18031    467   2353   1400       N  
ATOM   1904  CA  THR A 256     -14.735 -54.824 -17.996  1.00142.89           C  
ANISOU 1904  CA  THR A 256    20717  16119  17455    622   2702   1123       C  
ATOM   1905  C   THR A 256     -14.895 -53.574 -18.852  1.00132.43           C  
ANISOU 1905  C   THR A 256    19282  15132  15903    493   2644    955       C  
ATOM   1906  O   THR A 256     -13.940 -53.129 -19.500  1.00137.47           O  
ANISOU 1906  O   THR A 256    19930  15740  16561    791   2980    852       O  
ATOM   1907  CB  THR A 256     -15.192 -56.066 -18.764  1.00142.31           C  
ANISOU 1907  CB  THR A 256    21477  15412  17182    356   2739    950       C  
ATOM   1908  OG1 THR A 256     -15.039 -57.225 -17.936  1.00143.30           O  
ANISOU 1908  OG1 THR A 256    21711  15186  17552    477   2783   1140       O  
ATOM   1909  CG2 THR A 256     -14.368 -56.248 -20.032  1.00141.38           C  
ANISOU 1909  CG2 THR A 256    21958  14882  16878    616   3188    649       C  
ATOM   1910  N   LYS A 257     -16.095 -52.987 -18.860  1.00116.43           N  
ANISOU 1910  N   LYS A 257    17114  13436  13687     68   2238    978       N  
ATOM   1911  CA  LYS A 257     -16.313 -51.759 -19.617  1.00105.28           C  
ANISOU 1911  CA  LYS A 257    15582  12347  12073    -50   2136    859       C  
ATOM   1912  C   LYS A 257     -15.594 -50.574 -18.986  1.00113.00           C  
ANISOU 1912  C   LYS A 257    15919  13748  13267    288   2170    968       C  
ATOM   1913  O   LYS A 257     -15.238 -49.622 -19.690  1.00119.32           O  
ANISOU 1913  O   LYS A 257    16654  14692  13989    336   2241    876       O  
ATOM   1914  CB  LYS A 257     -17.810 -51.474 -19.736  1.00 95.53           C  
ANISOU 1914  CB  LYS A 257    14305  11350  10642   -558   1676    919       C  
ATOM   1915  CG  LYS A 257     -18.578 -52.525 -20.520  1.00102.18           C  
ANISOU 1915  CG  LYS A 257    15811  11753  11261  -1014   1505    819       C  
ATOM   1916  CD  LYS A 257     -20.077 -52.289 -20.446  1.00108.29           C  
ANISOU 1916  CD  LYS A 257    16358  12814  11974  -1531    998   1010       C  
ATOM   1917  CE  LYS A 257     -20.843 -53.390 -21.162  1.00118.60           C  
ANISOU 1917  CE  LYS A 257    18314  13639  13110  -2072    710    959       C  
ATOM   1918  NZ  LYS A 257     -22.316 -53.198 -21.065  1.00119.97           N  
ANISOU 1918  NZ  LYS A 257    18146  14115  13322  -2610    182   1248       N  
ATOM   1919  N   MET A 258     -15.373 -50.609 -17.670  1.00108.96           N  
ANISOU 1919  N   MET A 258    14980  13413  13008    502   2085   1176       N  
ATOM   1920  CA  MET A 258     -14.635 -49.533 -17.017  1.00103.33           C  
ANISOU 1920  CA  MET A 258    13746  13025  12490    795   2028   1270       C  
ATOM   1921  C   MET A 258     -13.141 -49.628 -17.303  1.00105.65           C  
ANISOU 1921  C   MET A 258    13972  13111  13058   1154   2377   1288       C  
ATOM   1922  O   MET A 258     -12.471 -48.601 -17.456  1.00107.69           O  
ANISOU 1922  O   MET A 258    13914  13556  13448   1277   2375   1315       O  
ATOM   1923  CB  MET A 258     -14.891 -49.552 -15.510  1.00102.76           C  
ANISOU 1923  CB  MET A 258    13340  13189  12517    911   1786   1484       C  
ATOM   1924  CG  MET A 258     -16.286 -49.102 -15.113  1.00108.19           C  
ANISOU 1924  CG  MET A 258    13919  14211  12976    663   1498   1544       C  
ATOM   1925  SD  MET A 258     -16.496 -48.977 -13.327  1.00113.23           S  
ANISOU 1925  SD  MET A 258    14237  15156  13629    905   1308   1798       S  
ATOM   1926  CE  MET A 258     -15.262 -47.741 -12.928  1.00109.25           C  
ANISOU 1926  CE  MET A 258    13458  14790  13263   1247   1174   1736       C  
ATOM   1927  N   ARG A 259     -12.604 -50.848 -17.374  1.00105.61           N  
ANISOU 1927  N   ARG A 259    14239  12707  13182   1334   2684   1313       N  
ATOM   1928  CA  ARG A 259     -11.195 -51.011 -17.715  1.00106.39           C  
ANISOU 1928  CA  ARG A 259    14234  12604  13584   1735   3101   1387       C  
ATOM   1929  C   ARG A 259     -10.924 -50.579 -19.150  1.00115.67           C  
ANISOU 1929  C   ARG A 259    15680  13693  14576   1714   3441   1213       C  
ATOM   1930  O   ARG A 259      -9.882 -49.977 -19.437  1.00116.97           O  
ANISOU 1930  O   ARG A 259    15508  13944  14992   1966   3689   1340       O  
ATOM   1931  CB  ARG A 259     -10.766 -52.462 -17.499  1.00106.23           C  
ANISOU 1931  CB  ARG A 259    14506  12129  13726   1985   3388   1457       C  
ATOM   1932  N   ALA A 260     -11.851 -50.874 -20.064  1.00121.39           N  
ANISOU 1932  N   ALA A 260    17013  14250  14862   1396   3436    963       N  
ATOM   1933  CA  ALA A 260     -11.689 -50.437 -21.446  1.00125.23           C  
ANISOU 1933  CA  ALA A 260    17857  14664  15060   1357   3724    794       C  
ATOM   1934  C   ALA A 260     -11.840 -48.926 -21.567  1.00121.01           C  
ANISOU 1934  C   ALA A 260    16887  14584  14507   1197   3466    849       C  
ATOM   1935  O   ALA A 260     -11.146 -48.289 -22.368  1.00120.89           O  
ANISOU 1935  O   ALA A 260    16830  14610  14490   1326   3773    879       O  
ATOM   1936  CB  ALA A 260     -12.697 -51.153 -22.345  1.00124.78           C  
ANISOU 1936  CB  ALA A 260    18631  14284  14497   1005   3654    516       C  
ATOM   1937  N   ALA A 261     -12.740 -48.334 -20.779  1.00115.11           N  
ANISOU 1937  N   ALA A 261    15826  14163  13746    943   2936    889       N  
ATOM   1938  CA  ALA A 261     -12.909 -46.886 -20.811  1.00102.50           C  
ANISOU 1938  CA  ALA A 261    13858  12942  12146    831   2667    937       C  
ATOM   1939  C   ALA A 261     -11.730 -46.168 -20.169  1.00108.22           C  
ANISOU 1939  C   ALA A 261    13989  13815  13314   1121   2700   1151       C  
ATOM   1940  O   ALA A 261     -11.403 -45.043 -20.562  1.00114.29           O  
ANISOU 1940  O   ALA A 261    14535  14749  14141   1089   2655   1210       O  
ATOM   1941  CB  ALA A 261     -14.213 -46.490 -20.118  1.00 91.00           C  
ANISOU 1941  CB  ALA A 261    12262  11765  10549    564   2153    934       C  
ATOM   1942  N   ALA A 262     -11.082 -46.797 -19.185  1.00118.62           N  
ANISOU 1942  N   ALA A 262    15050  15056  14965   1376   2727   1303       N  
ATOM   1943  CA  ALA A 262      -9.925 -46.176 -18.550  1.00120.90           C  
ANISOU 1943  CA  ALA A 262    14762  15461  15714   1607   2663   1552       C  
ATOM   1944  C   ALA A 262      -8.728 -46.125 -19.490  1.00125.73           C  
ANISOU 1944  C   ALA A 262    15259  15936  16576   1818   3181   1697       C  
ATOM   1945  O   ALA A 262      -7.925 -45.188 -19.417  1.00126.91           O  
ANISOU 1945  O   ALA A 262    14924  16232  17063   1858   3099   1917       O  
ATOM   1946  CB  ALA A 262      -9.563 -46.924 -17.267  1.00122.20           C  
ANISOU 1946  CB  ALA A 262    14709  15575  16147   1820   2515   1713       C  
ATOM   1947  N   LEU A 263      -8.591 -47.117 -20.373  1.00134.12           N  
ANISOU 1947  N   LEU A 263    16782  16699  17479   1961   3724   1599       N  
ATOM   1948  CA  LEU A 263      -7.485 -47.105 -21.325  1.00137.27           C  
ANISOU 1948  CA  LEU A 263    17120  16977  18061   2239   4346   1760       C  
ATOM   1949  C   LEU A 263      -7.724 -46.087 -22.434  1.00135.99           C  
ANISOU 1949  C   LEU A 263    17118  16953  17599   2017   4430   1689       C  
ATOM   1950  O   LEU A 263      -6.783 -45.428 -22.893  1.00137.22           O  
ANISOU 1950  O   LEU A 263    16902  17198  18039   2148   4725   1956       O  
ATOM   1951  CB  LEU A 263      -7.279 -48.502 -21.909  1.00141.74           C  
ANISOU 1951  CB  LEU A 263    18257  17123  18474   2534   4940   1645       C  
ATOM   1952  CG  LEU A 263      -6.984 -49.614 -20.899  1.00138.51           C  
ANISOU 1952  CG  LEU A 263    17741  16508  18377   2797   4918   1751       C  
ATOM   1953  CD1 LEU A 263      -6.711 -50.931 -21.610  1.00144.24           C  
ANISOU 1953  CD1 LEU A 263    19112  16739  18952   3136   5561   1629       C  
ATOM   1954  CD2 LEU A 263      -5.819 -49.232 -19.998  1.00136.16           C  
ANISOU 1954  CD2 LEU A 263    16569  16400  18764   3059   4821   2183       C  
ATOM   1955  N   ASP A 264      -8.975 -45.947 -22.880  1.00131.54           N  
ANISOU 1955  N   ASP A 264    17074  16412  16492   1669   4161   1387       N  
ATOM   1956  CA  ASP A 264      -9.293 -44.926 -23.873  1.00130.73           C  
ANISOU 1956  CA  ASP A 264    17130  16455  16086   1438   4147   1344       C  
ATOM   1957  C   ASP A 264      -9.128 -43.527 -23.295  1.00120.46           C  
ANISOU 1957  C   ASP A 264    15193  15467  15110   1300   3700   1545       C  
ATOM   1958  O   ASP A 264      -8.668 -42.612 -23.988  1.00116.38           O  
ANISOU 1958  O   ASP A 264    14530  15040  14647   1258   3846   1708       O  
ATOM   1959  CB  ASP A 264     -10.715 -45.126 -24.400  1.00139.97           C  
ANISOU 1959  CB  ASP A 264    18948  17583  16651   1081   3858   1025       C  
ATOM   1960  CG  ASP A 264     -10.816 -46.271 -25.387  1.00158.92           C  
ANISOU 1960  CG  ASP A 264    22164  19604  18614   1145   4298    806       C  
ATOM   1961  OD1 ASP A 264     -10.571 -47.429 -24.987  1.00166.20           O  
ANISOU 1961  OD1 ASP A 264    23255  20248  19646   1353   4499    755       O  
ATOM   1962  OD2 ASP A 264     -11.143 -46.014 -26.564  1.00164.56           O  
ANISOU 1962  OD2 ASP A 264    23415  20265  18846    993   4419    682       O  
ATOM   1963  N   ALA A 265      -9.499 -43.341 -22.026  1.00116.89           N  
ANISOU 1963  N   ALA A 265    14414  15152  14849   1235   3157   1543       N  
ATOM   1964  CA  ALA A 265      -9.299 -42.047 -21.384  1.00113.37           C  
ANISOU 1964  CA  ALA A 265    13470  14919  14686   1136   2692   1698       C  
ATOM   1965  C   ALA A 265      -7.824 -41.773 -21.122  1.00119.35           C  
ANISOU 1965  C   ALA A 265    13645  15659  16046   1329   2840   2060       C  
ATOM   1966  O   ALA A 265      -7.415 -40.609 -21.050  1.00121.75           O  
ANISOU 1966  O   ALA A 265    13591  16062  16606   1201   2570   2245       O  
ATOM   1967  CB  ALA A 265     -10.091 -41.977 -20.078  1.00104.55           C  
ANISOU 1967  CB  ALA A 265    12272  13927  13527   1076   2120   1586       C  
ATOM   1968  N   GLN A 266      -7.014 -42.824 -20.975  1.00120.39           N  
ANISOU 1968  N   GLN A 266    13654  15642  16447   1629   3240   2201       N  
ATOM   1969  CA  GLN A 266      -5.585 -42.625 -20.758  1.00117.87           C  
ANISOU 1969  CA  GLN A 266    12680  15325  16779   1825   3394   2633       C  
ATOM   1970  C   GLN A 266      -4.875 -42.230 -22.046  1.00126.37           C  
ANISOU 1970  C   GLN A 266    13678  16392  17944   1884   3998   2865       C  
ATOM   1971  O   GLN A 266      -3.877 -41.502 -22.004  1.00128.12           O  
ANISOU 1971  O   GLN A 266    13274  16697  18709   1874   3979   3281       O  
ATOM   1972  CB  GLN A 266      -4.960 -43.890 -20.169  1.00113.55           C  
ANISOU 1972  CB  GLN A 266    11991  14626  16528   2183   3642   2762       C  
ATOM   1973  N   LYS A 267      -5.370 -42.695 -23.192  1.00119.94           N  
ANISOU 1973  N   LYS A 267    16239  16905  12430   3689   -316   3843       N  
ATOM   1974  CA  LYS A 267      -4.778 -42.361 -24.488  1.00130.59           C  
ANISOU 1974  CA  LYS A 267    17445  18199  13975   3707   -318   3706       C  
ATOM   1975  C   LYS A 267      -5.460 -41.126 -25.082  1.00137.75           C  
ANISOU 1975  C   LYS A 267    18232  19097  15010   3324   -377   3372       C  
ATOM   1976  O   LYS A 267      -6.017 -41.145 -26.179  1.00141.44           O  
ANISOU 1976  O   LYS A 267    18813  19256  15673   3190   -267   3225       O  
ATOM   1977  CB  LYS A 267      -4.866 -43.555 -25.430  1.00128.87           C  
ANISOU 1977  CB  LYS A 267    17516  17538  13909   3890   -106   3807       C  
ATOM   1978  N   ALA A 268      -5.404 -40.037 -24.323  1.00133.58           N  
ANISOU 1978  N   ALA A 268    17480  18917  14358   3155   -556   3256       N  
ATOM   1979  CA  ALA A 268      -6.010 -38.778 -24.741  1.00126.91           C  
ANISOU 1979  CA  ALA A 268    16524  18088  13610   2812   -626   2949       C  
ATOM   1980  C   ALA A 268      -4.945 -37.776 -25.172  1.00125.82           C  
ANISOU 1980  C   ALA A 268    16052  18243  13509   2786   -794   2835       C  
ATOM   1981  O   ALA A 268      -3.767 -37.930 -24.849  1.00124.01           O  
ANISOU 1981  O   ALA A 268    15636  18303  13180   3004   -891   2991       O  
ATOM   1982  CB  ALA A 268      -6.859 -38.201 -23.618  1.00116.62           C  
ANISOU 1982  CB  ALA A 268    15249  16918  12145   2609   -691   2864       C  
ATOM   1983  N   ARG A 287       1.599 -39.815 -17.076  1.00146.34           N  
ANISOU 1983  N   ARG A 287    17555  23771  14277   4426  -1755   4441       N  
ATOM   1984  CA  ARG A 287       2.266 -38.866 -16.192  1.00144.75           C  
ANISOU 1984  CA  ARG A 287    17050  24055  13892   4244  -2002   4315       C  
ATOM   1985  C   ARG A 287       1.607 -38.837 -14.819  1.00162.98           C  
ANISOU 1985  C   ARG A 287    19509  26465  15952   4155  -2048   4320       C  
ATOM   1986  O   ARG A 287       2.119 -38.212 -13.889  1.00171.03           O  
ANISOU 1986  O   ARG A 287    20330  27869  16785   4032  -2237   4238       O  
ATOM   1987  CB  ARG A 287       2.262 -37.465 -16.807  1.00136.63           C  
ANISOU 1987  CB  ARG A 287    15813  23168  12933   3909  -2164   4023       C  
ATOM   1988  N   HIS A 288       0.471 -39.512 -14.692  1.00175.92           N  
ANISOU 1988  N   HIS A 288    21502  27758  17583   4205  -1868   4415       N  
ATOM   1989  CA  HIS A 288      -0.252 -39.564 -13.427  1.00189.72           C  
ANISOU 1989  CA  HIS A 288    23414  29576  19095   4128  -1876   4436       C  
ATOM   1990  C   HIS A 288      -0.734 -40.997 -13.216  1.00198.93           C  
ANISOU 1990  C   HIS A 288    24904  30400  20279   4381  -1642   4720       C  
ATOM   1991  O   HIS A 288      -0.278 -41.935 -13.879  1.00207.61           O  
ANISOU 1991  O   HIS A 288    26068  31272  21544   4636  -1506   4896       O  
ATOM   1992  CB  HIS A 288      -1.389 -38.532 -13.411  1.00186.38           C  
ANISOU 1992  CB  HIS A 288    23081  29122  18614   3799  -1920   4176       C  
ATOM   1993  CG  HIS A 288      -1.581 -37.872 -12.081  1.00188.03           C  
ANISOU 1993  CG  HIS A 288    23247  29650  18546   3627  -2066   4055       C  
ATOM   1994  ND1 HIS A 288      -0.718 -36.912 -11.598  1.00189.71           N  
ANISOU 1994  ND1 HIS A 288    23168  30267  18646   3479  -2307   3881       N  
ATOM   1995  CD2 HIS A 288      -2.528 -38.040 -11.128  1.00188.94           C  
ANISOU 1995  CD2 HIS A 288    23580  29736  18472   3574  -1998   4079       C  
ATOM   1996  CE1 HIS A 288      -1.129 -36.512 -10.407  1.00190.85           C  
ANISOU 1996  CE1 HIS A 288    23369  30604  18542   3351  -2384   3791       C  
ATOM   1997  NE2 HIS A 288      -2.225 -37.182 -10.099  1.00190.11           N  
ANISOU 1997  NE2 HIS A 288    23574  30265  18394   3414  -2197   3911       N  
ATOM   1998  N   GLY A 289      -1.671 -41.174 -12.287  1.00195.26           N  
ANISOU 1998  N   GLY A 289    24658  29888  19643   4301  -1585   4759       N  
ATOM   1999  CA  GLY A 289      -2.088 -42.499 -11.877  1.00188.40           C  
ANISOU 1999  CA  GLY A 289    24088  28735  18758   4504  -1382   5033       C  
ATOM   2000  C   GLY A 289      -3.267 -43.077 -12.633  1.00178.30           C  
ANISOU 2000  C   GLY A 289    23156  26948  17643   4460  -1145   5079       C  
ATOM   2001  O   GLY A 289      -4.236 -43.533 -12.020  1.00174.65           O  
ANISOU 2001  O   GLY A 289    22951  26323  17085   4398  -1018   5170       O  
ATOM   2002  N   PHE A 290      -3.202 -43.064 -13.967  1.00171.13           N  
ANISOU 2002  N   PHE A 290    22257  25787  16978   4478  -1078   5016       N  
ATOM   2003  CA  PHE A 290      -4.202 -43.789 -14.744  1.00165.13           C  
ANISOU 2003  CA  PHE A 290    21841  24491  16411   4444   -832   5061       C  
ATOM   2004  C   PHE A 290      -3.965 -45.291 -14.679  1.00174.62           C  
ANISOU 2004  C   PHE A 290    23289  25390  17667   4737   -653   5360       C  
ATOM   2005  O   PHE A 290      -4.918 -46.073 -14.768  1.00172.46           O  
ANISOU 2005  O   PHE A 290    23361  24713  17454   4694   -450   5463       O  
ATOM   2006  CB  PHE A 290      -4.204 -43.306 -16.194  1.00160.31           C  
ANISOU 2006  CB  PHE A 290    21156  23636  16121   4287   -797   4796       C  
ATOM   2007  CG  PHE A 290      -5.381 -42.439 -16.540  1.00157.14           C  
ANISOU 2007  CG  PHE A 290    20798  23065  15842   3872   -764   4463       C  
ATOM   2008  CD1 PHE A 290      -5.326 -41.068 -16.360  1.00156.53           C  
ANISOU 2008  CD1 PHE A 290    20463  23296  15714   3626   -950   4179       C  
ATOM   2009  CD2 PHE A 290      -6.545 -42.998 -17.042  1.00151.66           C  
ANISOU 2009  CD2 PHE A 290    20407  21907  15309   3729   -546   4437       C  
ATOM   2010  CE1 PHE A 290      -6.409 -40.268 -16.676  1.00152.68           C  
ANISOU 2010  CE1 PHE A 290    20023  22652  15336   3280   -912   3883       C  
ATOM   2011  CE2 PHE A 290      -7.632 -42.205 -17.360  1.00146.76           C  
ANISOU 2011  CE2 PHE A 290    19805  21164  14794   3369   -516   4146       C  
ATOM   2012  CZ  PHE A 290      -7.563 -40.838 -17.177  1.00146.28           C  
ANISOU 2012  CZ  PHE A 290    19488  21409  14681   3162   -695   3873       C  
ATOM   2013  N   ASP A 291      -2.707 -45.711 -14.524  1.00185.69           N  
ANISOU 2013  N   ASP A 291    24519  26970  19065   5009   -717   5477       N  
ATOM   2014  CA  ASP A 291      -2.417 -47.115 -14.270  1.00194.73           C  
ANISOU 2014  CA  ASP A 291    25885  27867  20237   5289   -561   5742       C  
ATOM   2015  C   ASP A 291      -2.814 -47.531 -12.861  1.00195.40           C  
ANISOU 2015  C   ASP A 291    26092  28059  20094   5280   -554   5901       C  
ATOM   2016  O   ASP A 291      -3.023 -48.723 -12.615  1.00211.13           O  
ANISOU 2016  O   ASP A 291    28368  29743  22107   5430   -387   6119       O  
ATOM   2017  CB  ASP A 291      -0.931 -47.398 -14.500  1.00199.15           C  
ANISOU 2017  CB  ASP A 291    26199  28630  20839   5596   -628   5819       C  
ATOM   2018  N   ILE A 292      -2.918 -46.576 -11.934  1.00181.27           N  
ANISOU 2018  N   ILE A 292    24102  26690  18081   5103   -732   5791       N  
ATOM   2019  CA  ILE A 292      -3.400 -46.892 -10.594  1.00170.53           C  
ANISOU 2019  CA  ILE A 292    22863  25441  16489   5070   -720   5924       C  
ATOM   2020  C   ILE A 292      -4.885 -47.226 -10.630  1.00169.83           C  
ANISOU 2020  C   ILE A 292    23122  24976  16430   4863   -527   5945       C  
ATOM   2021  O   ILE A 292      -5.338 -48.175  -9.980  1.00160.09           O  
ANISOU 2021  O   ILE A 292    22141  23553  15131   4916   -390   6157       O  
ATOM   2022  CB  ILE A 292      -3.103 -45.730  -9.630  1.00160.57           C  
ANISOU 2022  CB  ILE A 292    21300  24732  14978   4926   -962   5766       C  
ATOM   2023  N   LEU A 293      -5.666 -46.454 -11.389  1.00173.80           N  
ANISOU 2023  N   LEU A 293    23638  25372  17028   4613   -510   5731       N  
ATOM   2024  CA  LEU A 293      -7.081 -46.768 -11.551  1.00178.10           C  
ANISOU 2024  CA  LEU A 293    24494  25556  17619   4401   -311   5745       C  
ATOM   2025  C   LEU A 293      -7.271 -48.055 -12.343  1.00187.89           C  
ANISOU 2025  C   LEU A 293    26056  26243  19091   4517    -85   5916       C  
ATOM   2026  O   LEU A 293      -8.119 -48.885 -11.996  1.00197.51           O  
ANISOU 2026  O   LEU A 293    27574  27170  20301   4440     91   6067       O  
ATOM   2027  CB  LEU A 293      -7.803 -45.605 -12.233  1.00167.43           C  
ANISOU 2027  CB  LEU A 293    23059  24244  16314   4127   -349   5471       C  
ATOM   2028  CG  LEU A 293      -9.248 -45.851 -12.674  1.00161.00           C  
ANISOU 2028  CG  LEU A 293    22508  23010  15655   3834   -135   5383       C  
ATOM   2029  CD1 LEU A 293     -10.132 -46.200 -11.486  1.00162.14           C  
ANISOU 2029  CD1 LEU A 293    22825  23227  15555   3753    -44   5553       C  
ATOM   2030  CD2 LEU A 293      -9.797 -44.642 -13.417  1.00157.03           C  
ANISOU 2030  CD2 LEU A 293    21832  22504  15328   3498   -190   4965       C  
ATOM   2031  N   VAL A 294      -6.486 -48.242 -13.407  1.00170.85           N  
ANISOU 2031  N   VAL A 294    23844  23933  17139   4690    -84   5884       N  
ATOM   2032  CA  VAL A 294      -6.601 -49.454 -14.212  1.00155.56           C  
ANISOU 2032  CA  VAL A 294    22222  21458  15424   4807    127   6011       C  
ATOM   2033  C   VAL A 294      -6.157 -50.672 -13.412  1.00168.31           C  
ANISOU 2033  C   VAL A 294    23995  22986  16968   5051    198   6284       C  
ATOM   2034  O   VAL A 294      -6.740 -51.756 -13.531  1.00168.57           O  
ANISOU 2034  O   VAL A 294    24382  22571  17096   5041    394   6424       O  
ATOM   2035  CB  VAL A 294      -5.795 -49.307 -15.515  1.00137.77           C  
ANISOU 2035  CB  VAL A 294    19851  19107  13387   4954    106   5895       C  
ATOM   2036  N   GLY A 295      -5.121 -50.518 -12.586  1.00171.78           N  
ANISOU 2036  N   GLY A 295    24178  23851  17241   5262     38   6361       N  
ATOM   2037  CA  GLY A 295      -4.671 -51.631 -11.767  1.00176.39           C  
ANISOU 2037  CA  GLY A 295    24894  24390  17735   5511     97   6630       C  
ATOM   2038  C   GLY A 295      -5.661 -51.990 -10.676  1.00181.50           C  
ANISOU 2038  C   GLY A 295    25757  24992  18214   5344    172   6767       C  
ATOM   2039  O   GLY A 295      -5.834 -53.166 -10.345  1.00189.68           O  
ANISOU 2039  O   GLY A 295    27078  25730  19261   5450    318   6992       O  
ATOM   2040  N   GLN A 296      -6.326 -50.984 -10.102  1.00175.61           N  
ANISOU 2040  N   GLN A 296    24878  24544  17303   5079     76   6631       N  
ATOM   2041  CA  GLN A 296      -7.329 -51.254  -9.079  1.00174.86           C  
ANISOU 2041  CA  GLN A 296    24968  24434  17035   4901    158   6747       C  
ATOM   2042  C   GLN A 296      -8.605 -51.826  -9.683  1.00165.44           C  
ANISOU 2042  C   GLN A 296    24128  22728  16005   4663    387   6765       C  
ATOM   2043  O   GLN A 296      -9.324 -52.576  -9.011  1.00180.02           O  
ANISOU 2043  O   GLN A 296    26219  24403  17777   4575    518   6946       O  
ATOM   2044  CB  GLN A 296      -7.626 -49.980  -8.288  1.00173.73           C  
ANISOU 2044  CB  GLN A 296    24571  24783  16655   4703     -7   6573       C  
ATOM   2045  CG  GLN A 296      -6.507 -49.580  -7.337  1.00175.55           C  
ANISOU 2045  CG  GLN A 296    24504  25529  16668   4895   -224   6596       C  
ATOM   2046  CD  GLN A 296      -6.707 -48.201  -6.741  1.00173.12           C  
ANISOU 2046  CD  GLN A 296    23938  25689  16152   4686   -406   6358       C  
ATOM   2047  OE1 GLN A 296      -6.847 -47.215  -7.464  1.00167.99           O  
ANISOU 2047  OE1 GLN A 296    23141  25105  15581   4525   -481   6104       O  
ATOM   2048  NE2 GLN A 296      -6.725 -48.126  -5.416  1.00176.32           N  
ANISOU 2048  NE2 GLN A 296    24297  26412  16284   4686   -477   6432       N  
ATOM   2049  N   ILE A 297      -8.906 -51.487 -10.938  1.00144.59           N  
ANISOU 2049  N   ILE A 297    21513  19845  13581   4541    437   6583       N  
ATOM   2050  CA  ILE A 297     -10.007 -52.145 -11.634  1.00136.14           C  
ANISOU 2050  CA  ILE A 297    20785  18251  12693   4323    659   6600       C  
ATOM   2051  C   ILE A 297      -9.640 -53.591 -11.947  1.00144.70           C  
ANISOU 2051  C   ILE A 297    22164  18884  13931   4526    803   6801       C  
ATOM   2052  O   ILE A 297     -10.478 -54.495 -11.849  1.00133.51           O  
ANISOU 2052  O   ILE A 297    21073  17090  12565   4377    980   6933       O  
ATOM   2053  CB  ILE A 297     -10.384 -51.360 -12.905  1.00124.59           C  
ANISOU 2053  CB  ILE A 297    19261  16667  11411   4145    666   6342       C  
ATOM   2054  CG1 ILE A 297     -11.026 -50.022 -12.534  1.00122.39           C  
ANISOU 2054  CG1 ILE A 297    18757  16777  10969   3899    563   6152       C  
ATOM   2055  CG2 ILE A 297     -11.325 -52.170 -13.786  1.00118.21           C  
ANISOU 2055  CG2 ILE A 297    18812  15279  10825   3951    892   6354       C  
ATOM   2056  CD1 ILE A 297     -11.418 -49.180 -13.730  1.00115.33           C  
ANISOU 2056  CD1 ILE A 297    17781  15790  10248   3711    560   5882       C  
ATOM   2057  N   ASP A 298      -8.379 -53.833 -12.316  1.00165.18           N  
ANISOU 2057  N   ASP A 298    24646  21520  16596   4865    731   6826       N  
ATOM   2058  CA  ASP A 298      -7.921 -55.200 -12.538  1.00168.30           C  
ANISOU 2058  CA  ASP A 298    25310  21525  17111   5107    863   7015       C  
ATOM   2059  C   ASP A 298      -7.937 -56.012 -11.249  1.00163.65           C  
ANISOU 2059  C   ASP A 298    24855  20985  16338   5203    895   7291       C  
ATOM   2060  O   ASP A 298      -8.132 -57.232 -11.290  1.00169.68           O  
ANISOU 2060  O   ASP A 298    25957  21326  17189   5260   1055   7465       O  
ATOM   2061  CB  ASP A 298      -6.518 -55.193 -13.145  1.00170.93           C  
ANISOU 2061  CB  ASP A 298    25445  21972  17529   5468    777   6978       C  
ATOM   2062  N   ASP A 299      -7.734 -55.359 -10.103  1.00151.42           N  
ANISOU 2062  N   ASP A 299    23056  19943  14532   5217    744   7330       N  
ATOM   2063  CA  ASP A 299      -7.837 -56.060  -8.828  1.00142.56           C  
ANISOU 2063  CA  ASP A 299    22059  18893  13215   5283    773   7591       C  
ATOM   2064  C   ASP A 299      -9.284 -56.422  -8.519  1.00142.04           C  
ANISOU 2064  C   ASP A 299    22281  18554  13132   4931    933   7656       C  
ATOM   2065  O   ASP A 299      -9.555 -57.477  -7.933  1.00141.25           O  
ANISOU 2065  O   ASP A 299    22451  18225  12993   4957   1050   7898       O  
ATOM   2066  CB  ASP A 299      -7.245 -55.205  -7.708  1.00138.05           C  
ANISOU 2066  CB  ASP A 299    21136  18952  12363   5373    562   7586       C  
ATOM   2067  N   ALA A 300     -10.228 -55.559  -8.904  1.00146.95           N  
ANISOU 2067  N   ALA A 300    22844  19208  13781   4595    943   7448       N  
ATOM   2068  CA  ALA A 300     -11.638 -55.877  -8.716  1.00161.62           C  
ANISOU 2068  CA  ALA A 300    24952  20819  15638   4235   1108   7497       C  
ATOM   2069  C   ALA A 300     -12.100 -56.960  -9.682  1.00166.42           C  
ANISOU 2069  C   ALA A 300    25925  20793  16513   4140   1304   7546       C  
ATOM   2070  O   ALA A 300     -13.035 -57.707  -9.372  1.00171.16           O  
ANISOU 2070  O   ALA A 300    26798  21118  17116   3913   1456   7688       O  
ATOM   2071  CB  ALA A 300     -12.489 -54.618  -8.881  1.00163.55           C  
ANISOU 2071  CB  ALA A 300    25008  21304  15829   3921   1068   7253       C  
ATOM   2072  N   LEU A 301     -11.464 -57.059 -10.852  1.00164.29           N  
ANISOU 2072  N   LEU A 301    25666  20292  16464   4297   1303   7422       N  
ATOM   2073  CA  LEU A 301     -11.803 -58.123 -11.791  1.00158.75           C  
ANISOU 2073  CA  LEU A 301    25324  18981  16012   4230   1482   7445       C  
ATOM   2074  C   LEU A 301     -11.376 -59.489 -11.271  1.00166.32           C  
ANISOU 2074  C   LEU A 301    26551  19684  16959   4458   1566   7723       C  
ATOM   2075  O   LEU A 301     -11.970 -60.506 -11.646  1.00168.30           O  
ANISOU 2075  O   LEU A 301    27158  19433  17354   4314   1732   7799       O  
ATOM   2076  CB  LEU A 301     -11.162 -57.849 -13.152  1.00147.19           C  
ANISOU 2076  CB  LEU A 301    23792  17370  14765   4368   1456   7230       C  
ATOM   2077  CG  LEU A 301     -11.871 -56.836 -14.052  1.00148.34           C  
ANISOU 2077  CG  LEU A 301    23824  17524  15013   4068   1448   6954       C  
ATOM   2078  CD1 LEU A 301     -11.031 -56.529 -15.281  1.00155.22           C  
ANISOU 2078  CD1 LEU A 301    24587  18323  16065   4265   1398   6766       C  
ATOM   2079  CD2 LEU A 301     -13.238 -57.363 -14.457  1.00147.62           C  
ANISOU 2079  CD2 LEU A 301    24045  16998  15046   3662   1631   6934       C  
ATOM   2080  N   LYS A 302     -10.355 -59.533 -10.411  1.00167.83           N  
ANISOU 2080  N   LYS A 302    26578  20214  16978   4806   1452   7875       N  
ATOM   2081  CA  LYS A 302      -9.922 -60.797  -9.830  1.00163.54           C  
ANISOU 2081  CA  LYS A 302    26278  19463  16399   5049   1528   8158       C  
ATOM   2082  C   LYS A 302     -10.908 -61.332  -8.800  1.00168.29           C  
ANISOU 2082  C   LYS A 302    27089  19993  16860   4802   1619   8373       C  
ATOM   2083  O   LYS A 302     -10.947 -62.545  -8.571  1.00167.00           O  
ANISOU 2083  O   LYS A 302    27244  19475  16733   4875   1739   8595       O  
ATOM   2084  CB  LYS A 302      -8.540 -60.634  -9.194  1.00161.07           C  
ANISOU 2084  CB  LYS A 302    25696  19577  15928   5487   1374   8258       C  
ATOM   2085  N   LEU A 303     -11.705 -60.460  -8.183  1.00174.07           N  
ANISOU 2085  N   LEU A 303    27653  21055  17429   4513   1570   8312       N  
ATOM   2086  CA  LEU A 303     -12.702 -60.883  -7.207  1.00182.60           C  
ANISOU 2086  CA  LEU A 303    28903  22113  18363   4252   1662   8505       C  
ATOM   2087  C   LEU A 303     -14.017 -61.285  -7.861  1.00192.25           C  
ANISOU 2087  C   LEU A 303    30395  22890  19760   3818   1839   8455       C  
ATOM   2088  O   LEU A 303     -14.623 -62.286  -7.464  1.00193.02           O  
ANISOU 2088  O   LEU A 303    30788  22691  19859   3669   1972   8669       O  
ATOM   2089  CB  LEU A 303     -12.955 -59.767  -6.191  1.00177.71           C  
ANISOU 2089  CB  LEU A 303    27973  22084  17465   4151   1537   8457       C  
ATOM   2090  N   ALA A 304     -14.469 -60.526  -8.862  1.00200.71           N  
ANISOU 2090  N   ALA A 304    31365  23917  20978   3601   1840   8179       N  
ATOM   2091  CA  ALA A 304     -15.739 -60.839  -9.509  1.00203.67           C  
ANISOU 2091  CA  ALA A 304    31961  23909  21515   3164   1999   8112       C  
ATOM   2092  C   ALA A 304     -15.666 -62.138 -10.301  1.00206.99           C  
ANISOU 2092  C   ALA A 304    32757  23711  22179   3189   2132   8180       C  
ATOM   2093  O   ALA A 304     -16.687 -62.815 -10.472  1.00212.34           O  
ANISOU 2093  O   ALA A 304    33693  24036  22952   2840   2276   8236       O  
ATOM   2094  CB  ALA A 304     -16.166 -59.685 -10.416  1.00197.70           C  
ANISOU 2094  CB  ALA A 304    30994  23271  20852   2957   1962   7796       C  
ATOM   2095  N   ASN A 305     -14.478 -62.502 -10.788  1.00202.01           N  
ANISOU 2095  N   ASN A 305    32156  22955  21645   3592   2086   8170       N  
ATOM   2096  CA  ASN A 305     -14.309 -63.751 -11.519  1.00191.16           C  
ANISOU 2096  CA  ASN A 305    31148  21001  20482   3667   2213   8222       C  
ATOM   2097  C   ASN A 305     -14.345 -64.975 -10.613  1.00176.03           C  
ANISOU 2097  C   ASN A 305    29519  18880  18486   3736   2300   8551       C  
ATOM   2098  O   ASN A 305     -14.674 -66.068 -11.086  1.00182.49           O  
ANISOU 2098  O   ASN A 305    30698  19172  19466   3635   2437   8611       O  
ATOM   2099  CB  ASN A 305     -12.991 -63.730 -12.295  1.00193.11           C  
ANISOU 2099  CB  ASN A 305    31317  21220  20836   4105   2147   8109       C  
ATOM   2100  N   GLU A 306     -14.024 -64.819  -9.328  1.00170.65           N  
ANISOU 2100  N   GLU A 306    28692  18598  17551   3899   2221   8760       N  
ATOM   2101  CA  GLU A 306     -14.013 -65.929  -8.381  1.00174.19           C  
ANISOU 2101  CA  GLU A 306    29396  18893  17896   3987   2294   9093       C  
ATOM   2102  C   GLU A 306     -15.322 -66.062  -7.615  1.00184.21           C  
ANISOU 2102  C   GLU A 306    30762  20176  19054   3541   2377   9235       C  
ATOM   2103  O   GLU A 306     -15.329 -66.591  -6.495  1.00174.21           O  
ANISOU 2103  O   GLU A 306    29584  19002  17605   3603   2393   9518       O  
ATOM   2104  CB  GLU A 306     -12.841 -65.779  -7.410  1.00166.13           C  
ANISOU 2104  CB  GLU A 306    28172  18297  16654   4445   2163   9257       C  
ATOM   2105  N   GLY A 307     -16.432 -65.600  -8.187  1.00203.08           N  
ANISOU 2105  N   GLY A 307    33128  22491  21542   3093   2434   9051       N  
ATOM   2106  CA  GLY A 307     -17.724 -65.708  -7.547  1.00213.13           C  
ANISOU 2106  CA  GLY A 307    34467  23795  22719   2645   2526   9173       C  
ATOM   2107  C   GLY A 307     -18.001 -64.692  -6.461  1.00216.96           C  
ANISOU 2107  C   GLY A 307    34635  24888  22913   2581   2439   9196       C  
ATOM   2108  O   GLY A 307     -19.115 -64.679  -5.923  1.00215.34           O  
ANISOU 2108  O   GLY A 307    34448  24765  22608   2201   2520   9282       O  
ATOM   2109  N   LYS A 308     -17.034 -63.845  -6.118  1.00214.37           N  
ANISOU 2109  N   LYS A 308    34013  25001  22439   2932   2278   9117       N  
ATOM   2110  CA  LYS A 308     -17.238 -62.827  -5.095  1.00210.61           C  
ANISOU 2110  CA  LYS A 308    33232  25115  21674   2890   2184   9104       C  
ATOM   2111  C   LYS A 308     -17.967 -61.635  -5.704  1.00201.24           C  
ANISOU 2111  C   LYS A 308    31810  24126  20527   2597   2168   8799       C  
ATOM   2112  O   LYS A 308     -17.461 -61.000  -6.635  1.00210.11           O  
ANISOU 2112  O   LYS A 308    32787  25257  21790   2717   2090   8555       O  
ATOM   2113  CB  LYS A 308     -15.901 -62.396  -4.495  1.00211.00           C  
ANISOU 2113  CB  LYS A 308    33051  25565  21554   3364   2007   9128       C  
ATOM   2114  N   VAL A 309     -19.153 -61.334  -5.180  1.00182.41           N  
ANISOU 2114  N   VAL A 309    29384  21911  18013   2219   2247   8818       N  
ATOM   2115  CA  VAL A 309     -19.986 -60.258  -5.693  1.00168.72           C  
ANISOU 2115  CA  VAL A 309    27438  20366  16302   1919   2257   8549       C  
ATOM   2116  C   VAL A 309     -19.976 -59.046  -4.769  1.00170.65           C  
ANISOU 2116  C   VAL A 309    27349  21239  16252   1979   2146   8456       C  
ATOM   2117  O   VAL A 309     -19.908 -57.908  -5.238  1.00161.04           O  
ANISOU 2117  O   VAL A 309    25876  20270  15042   1986   2060   8186       O  
ATOM   2118  CB  VAL A 309     -21.429 -60.753  -5.935  1.00160.34           C  
ANISOU 2118  CB  VAL A 309    26548  19039  15333   1415   2442   8599       C  
ATOM   2119  N   LYS A 310     -20.041 -59.268  -3.455  1.00176.75           N  
ANISOU 2119  N   LYS A 310    28126  22272  16758   2024   2145   8670       N  
ATOM   2120  CA  LYS A 310     -20.067 -58.157  -2.510  1.00184.94           C  
ANISOU 2120  CA  LYS A 310    28864  23905  17500   2074   2044   8569       C  
ATOM   2121  C   LYS A 310     -18.700 -57.507  -2.343  1.00191.63           C  
ANISOU 2121  C   LYS A 310    29484  25063  18264   2498   1828   8466       C  
ATOM   2122  O   LYS A 310     -18.621 -56.308  -2.053  1.00199.59           O  
ANISOU 2122  O   LYS A 310    30198  26523  19114   2529   1711   8255       O  
ATOM   2123  CB  LYS A 310     -20.586 -58.634  -1.153  1.00186.05           C  
ANISOU 2123  CB  LYS A 310    29093  24222  17374   1981   2119   8827       C  
ATOM   2124  N   GLU A 311     -17.619 -58.271  -2.521  1.00192.47           N  
ANISOU 2124  N   GLU A 311    29713  24946  18471   2820   1773   8605       N  
ATOM   2125  CA  GLU A 311     -16.285 -57.708  -2.343  1.00189.73           C  
ANISOU 2125  CA  GLU A 311    29128  24918  18041   3214   1566   8525       C  
ATOM   2126  C   GLU A 311     -15.911 -56.789  -3.500  1.00185.92           C  
ANISOU 2126  C   GLU A 311    28444  24460  17737   3249   1471   8213       C  
ATOM   2127  O   GLU A 311     -15.221 -55.782  -3.301  1.00191.54           O  
ANISOU 2127  O   GLU A 311    28855  25592  18328   3418   1291   8043       O  
ATOM   2128  CB  GLU A 311     -15.257 -58.830  -2.196  1.00188.47           C  
ANISOU 2128  CB  GLU A 311    29147  24528  17934   3560   1551   8775       C  
ATOM   2129  N   ALA A 312     -16.356 -57.118  -4.715  1.00177.46           N  
ANISOU 2129  N   ALA A 312    27536  22942  16949   3079   1587   8129       N  
ATOM   2130  CA  ALA A 312     -16.026 -56.291  -5.870  1.00152.90           C  
ANISOU 2130  CA  ALA A 312    24254  19825  14015   3107   1508   7843       C  
ATOM   2131  C   ALA A 312     -16.734 -54.943  -5.821  1.00149.53           C  
ANISOU 2131  C   ALA A 312    23568  19774  13473   2876   1463   7593       C  
ATOM   2132  O   ALA A 312     -16.196 -53.944  -6.313  1.00155.67           O  
ANISOU 2132  O   ALA A 312    24100  20775  14274   2979   1322   7360       O  
ATOM   2133  CB  ALA A 312     -16.376 -57.028  -7.162  1.00147.57           C  
ANISOU 2133  CB  ALA A 312    23841  18566  13662   2970   1652   7815       C  
ATOM   2134  N   GLN A 313     -17.933 -54.892  -5.236  1.00149.58           N  
ANISOU 2134  N   GLN A 313    23620  19861  13351   2566   1583   7636       N  
ATOM   2135  CA  GLN A 313     -18.657 -53.629  -5.147  1.00147.49           C  
ANISOU 2135  CA  GLN A 313    23111  19964  12965   2361   1557   7395       C  
ATOM   2136  C   GLN A 313     -17.999 -52.670  -4.163  1.00166.32           C  
ANISOU 2136  C   GLN A 313    25210  22916  15070   2566   1362   7304       C  
ATOM   2137  O   GLN A 313     -18.117 -51.449  -4.317  1.00165.24           O  
ANISOU 2137  O   GLN A 313    24825  23091  14867   2512   1268   7038       O  
ATOM   2138  CB  GLN A 313     -20.111 -53.883  -4.749  1.00131.98           C  
ANISOU 2138  CB  GLN A 313    21258  17958  10931   1985   1750   7474       C  
ATOM   2139  N   ALA A 314     -17.307 -53.198  -3.151  1.00177.69           N  
ANISOU 2139  N   ALA A 314    26683  24492  16338   2795   1296   7512       N  
ATOM   2140  CA  ALA A 314     -16.643 -52.334  -2.181  1.00189.51           C  
ANISOU 2140  CA  ALA A 314    27915  26528  17562   2977   1101   7422       C  
ATOM   2141  C   ALA A 314     -15.420 -51.658  -2.788  1.00192.19           C  
ANISOU 2141  C   ALA A 314    28033  27007  17985   3223    893   7238       C  
ATOM   2142  O   ALA A 314     -15.147 -50.485  -2.504  1.00196.99           O  
ANISOU 2142  O   ALA A 314    28369  28035  18443   3243    728   7009       O  
ATOM   2143  CB  ALA A 314     -16.254 -53.137  -0.941  1.00192.91           C  
ANISOU 2143  CB  ALA A 314    28447  27063  17786   3147   1094   7711       C  
ATOM   2144  N   ALA A 315     -14.672 -52.380  -3.625  1.00186.45           N  
ANISOU 2144  N   ALA A 315    27417  25932  17493   3406    897   7327       N  
ATOM   2145  CA  ALA A 315     -13.500 -51.789  -4.262  1.00180.86           C  
ANISOU 2145  CA  ALA A 315    26490  25354  16876   3635    712   7164       C  
ATOM   2146  C   ALA A 315     -13.889 -50.784  -5.339  1.00175.20           C  
ANISOU 2146  C   ALA A 315    25641  24622  16305   3455    691   6863       C  
ATOM   2147  O   ALA A 315     -13.165 -49.808  -5.565  1.00177.43           O  
ANISOU 2147  O   ALA A 315    25655  25198  16561   3552    504   6655       O  
ATOM   2148  CB  ALA A 315     -12.612 -52.884  -4.851  1.00176.68           C  
ANISOU 2148  CB  ALA A 315    26118  24459  16551   3898    743   7345       C  
ATOM   2149  N   ALA A 316     -15.023 -51.001  -6.010  1.00164.20           N  
ANISOU 2149  N   ALA A 316    24427  22899  15063   3182    879   6836       N  
ATOM   2150  CA  ALA A 316     -15.469 -50.059  -7.031  1.00156.84           C  
ANISOU 2150  CA  ALA A 316    23378  21953  14262   3006    874   6560       C  
ATOM   2151  C   ALA A 316     -15.963 -48.755  -6.419  1.00158.05           C  
ANISOU 2151  C   ALA A 316    23285  22580  14185   2862    783   6339       C  
ATOM   2152  O   ALA A 316     -15.770 -47.685  -7.006  1.00154.29           O  
ANISOU 2152  O   ALA A 316    22604  22275  13742   2841    665   6079       O  
ATOM   2153  CB  ALA A 316     -16.564 -50.693  -7.888  1.00154.81           C  
ANISOU 2153  CB  ALA A 316    23378  21220  14224   2741   1104   6598       C  
ATOM   2154  N   GLU A 317     -16.593 -48.821  -5.245  1.00160.53           N  
ANISOU 2154  N   GLU A 317    23624  23110  14262   2764    836   6429       N  
ATOM   2155  CA  GLU A 317     -17.087 -47.619  -4.586  1.00156.17           C  
ANISOU 2155  CA  GLU A 317    22857  23005  13476   2641    761   6207       C  
ATOM   2156  C   GLU A 317     -15.981 -46.824  -3.907  1.00164.14           C  
ANISOU 2156  C   GLU A 317    23622  24452  14291   2851    504   6081       C  
ATOM   2157  O   GLU A 317     -16.180 -45.641  -3.612  1.00168.81           O  
ANISOU 2157  O   GLU A 317    24017  25394  14730   2766    398   5820       O  
ATOM   2158  CB  GLU A 317     -18.159 -47.984  -3.556  1.00147.37           C  
ANISOU 2158  CB  GLU A 317    21852  21973  12170   2466    920   6344       C  
ATOM   2159  N   GLN A 318     -14.825 -47.441  -3.655  1.00165.63           N  
ANISOU 2159  N   GLN A 318    23817  24631  14483   3115    400   6252       N  
ATOM   2160  CA  GLN A 318     -13.736 -46.740  -2.985  1.00162.24           C  
ANISOU 2160  CA  GLN A 318    23143  24631  13869   3296    152   6145       C  
ATOM   2161  C   GLN A 318     -12.963 -45.833  -3.935  1.00161.63           C  
ANISOU 2161  C   GLN A 318    22848  24636  13929   3345    -24   5892       C  
ATOM   2162  O   GLN A 318     -12.409 -44.818  -3.499  1.00166.92           O  
ANISOU 2162  O   GLN A 318    23281  25702  14440   3363   -232   5684       O  
ATOM   2163  CB  GLN A 318     -12.785 -47.745  -2.334  1.00162.60           C  
ANISOU 2163  CB  GLN A 318    23253  24671  13858   3566    112   6433       C  
ATOM   2164  N   LEU A 319     -12.913 -46.175  -5.222  1.00157.07           N  
ANISOU 2164  N   LEU A 319    22352  23687  13640   3352     53   5901       N  
ATOM   2165  CA  LEU A 319     -12.183 -45.373  -6.196  1.00152.70           C  
ANISOU 2165  CA  LEU A 319    21598  23191  13230   3397   -102   5680       C  
ATOM   2166  C   LEU A 319     -12.896 -44.056  -6.471  1.00160.09           C  
ANISOU 2166  C   LEU A 319    22399  24312  14116   3160   -149   5357       C  
ATOM   2167  O   LEU A 319     -12.428 -42.991  -6.056  1.00155.35           O  
ANISOU 2167  O   LEU A 319    21568  24094  13362   3148   -353   5135       O  
ATOM   2168  CB  LEU A 319     -11.992 -46.153  -7.498  1.00143.39           C  
ANISOU 2168  CB  LEU A 319    20569  21545  12370   3476     14   5780       C  
ATOM   2169  CG  LEU A 319     -10.572 -46.651  -7.771  1.00132.36           C  
ANISOU 2169  CG  LEU A 319    19091  20127  11074   3779    -96   5893       C  
ATOM   2170  CD1 LEU A 319      -9.615 -45.476  -7.899  1.00118.76           C  
ANISOU 2170  CD1 LEU A 319    17024  18799   9299   3827   -352   5656       C  
ATOM   2171  CD2 LEU A 319     -10.120 -47.598  -6.672  1.00131.69           C  
ANISOU 2171  CD2 LEU A 319    19091  20105  10842   3973    -84   6168       C  
ATOM   2172  N   LYS A 320     -14.024 -44.118  -7.171  1.00164.73           N  
ANISOU 2172  N   LYS A 320    23122  24607  14860   2947     36   5296       N  
ATOM   2173  CA  LYS A 320     -14.783 -42.919  -7.503  1.00169.12           C  
ANISOU 2173  CA  LYS A 320    23532  25229  15498   2666     10   4898       C  
ATOM   2174  C   LYS A 320     -16.186 -42.978  -6.908  1.00171.18           C  
ANISOU 2174  C   LYS A 320    23906  25501  15633   2458    195   4914       C  
ATOM   2175  O   LYS A 320     -16.353 -42.997  -5.688  1.00171.57           O  
ANISOU 2175  O   LYS A 320    23974  25864  15349   2515    194   5046       O  
ATOM   2176  CB  LYS A 320     -14.861 -42.737  -9.021  1.00166.38           C  
ANISOU 2176  CB  LYS A 320    23157  24509  15550   2537     40   4682       C  
ATOM   2177  N   LYS A1230     -19.392 -31.862 -15.343  1.00 97.88           N  
ANISOU 2177  N   LYS A1230    13402  15510   8279    913   -309   1428       N  
ATOM   2178  CA  LYS A1230     -20.703 -32.427 -15.047  1.00109.80           C  
ANISOU 2178  CA  LYS A1230    14990  17000   9730    851   -102   1532       C  
ATOM   2179  C   LYS A1230     -21.790 -31.745 -15.869  1.00125.15           C  
ANISOU 2179  C   LYS A1230    16887  18817  11846    715    -14   1323       C  
ATOM   2180  O   LYS A1230     -22.803 -32.359 -16.207  1.00134.86           O  
ANISOU 2180  O   LYS A1230    18153  19932  13155    622    159   1418       O  
ATOM   2181  CB  LYS A1230     -21.016 -32.306 -13.554  1.00109.40           C  
ANISOU 2181  CB  LYS A1230    14971  17270   9327    914    -87   1572       C  
ATOM   2182  N   ASN A1231     -21.575 -30.469 -16.190  1.00126.94           N  
ANISOU 2182  N   ASN A1231    17035  19069  12126    700   -137   1043       N  
ATOM   2183  CA  ASN A1231     -22.524 -29.685 -16.970  1.00122.57           C  
ANISOU 2183  CA  ASN A1231    16433  18409  11727    605    -73    834       C  
ATOM   2184  C   ASN A1231     -21.760 -28.862 -18.009  1.00106.32           C  
ANISOU 2184  C   ASN A1231    14313  16194   9891    579   -219    647       C  
ATOM   2185  O   ASN A1231     -21.748 -27.634 -17.997  1.00116.86           O  
ANISOU 2185  O   ASN A1231    15615  17579  11208    574   -308    402       O  
ATOM   2186  CB  ASN A1231     -23.374 -28.799 -16.061  1.00121.11           C  
ANISOU 2186  CB  ASN A1231    16242  18454  11320    628    -34    667       C  
ATOM   2187  CG  ASN A1231     -24.583 -28.226 -16.772  1.00118.32           C  
ANISOU 2187  CG  ASN A1231    15838  18018  11101    557     81    516       C  
ATOM   2188  OD1 ASN A1231     -25.014 -28.746 -17.801  1.00108.07           O  
ANISOU 2188  OD1 ASN A1231    14514  16522  10027    466    166    589       O  
ATOM   2189  ND2 ASN A1231     -25.139 -27.151 -16.225  1.00120.22           N  
ANISOU 2189  ND2 ASN A1231    16068  18417  11194    607     82    304       N  
ATOM   2190  N   LYS A1232     -21.100 -29.558 -18.933  1.00 75.60           N  
ANISOU 2190  N   LYS A1232    10417  12100   6206    566   -237    769       N  
ATOM   2191  CA  LYS A1232     -20.325 -28.897 -19.972  1.00 71.32           C  
ANISOU 2191  CA  LYS A1232     9808  11414   5875    538   -362    628       C  
ATOM   2192  C   LYS A1232     -21.109 -28.844 -21.276  1.00 80.03           C  
ANISOU 2192  C   LYS A1232    10893  12285   7230    439   -263    563       C  
ATOM   2193  O   LYS A1232     -21.783 -29.817 -21.636  1.00 90.61           O  
ANISOU 2193  O   LYS A1232    12278  13510   8641    392   -118    712       O  
ATOM   2194  CB  LYS A1232     -19.001 -29.625 -20.208  1.00 67.61           C  
ANISOU 2194  CB  LYS A1232     9327  10898   5463    610   -451    795       C  
ATOM   2195  N   PRO A1233     -21.044 -27.722 -21.992  1.00 80.70           N  
ANISOU 2195  N   PRO A1233    10920  12299   7445    396   -341    345       N  
ATOM   2196  CA  PRO A1233     -21.743 -27.630 -23.280  1.00 80.10           C  
ANISOU 2196  CA  PRO A1233    10817  12019   7599    311   -260    287       C  
ATOM   2197  C   PRO A1233     -21.190 -28.638 -24.276  1.00 73.28           C  
ANISOU 2197  C   PRO A1233     9964  10955   6923    291   -236    442       C  
ATOM   2198  O   PRO A1233     -19.986 -28.900 -24.323  1.00 68.75           O  
ANISOU 2198  O   PRO A1233     9381  10372   6369    352   -334    515       O  
ATOM   2199  CB  PRO A1233     -21.476 -26.189 -23.728  1.00 85.17           C  
ANISOU 2199  CB  PRO A1233    11409  12633   8318    294   -378     43       C  
ATOM   2200  CG  PRO A1233     -21.130 -25.454 -22.471  1.00 87.42           C  
ANISOU 2200  CG  PRO A1233    11717  13127   8372    351   -478    -62       C  
ATOM   2201  CD  PRO A1233     -20.411 -26.448 -21.613  1.00 83.43           C  
ANISOU 2201  CD  PRO A1233    11234  12750   7715    412   -503    139       C  
ATOM   2202  N   ARG A1234     -22.088 -29.206 -25.078  1.00 76.19           N  
ANISOU 2202  N   ARG A1234    10351  11176   7420    208   -105    489       N  
ATOM   2203  CA  ARG A1234     -21.707 -30.216 -26.053  1.00 82.07           C  
ANISOU 2203  CA  ARG A1234    11139  11710   8333    184    -62    621       C  
ATOM   2204  C   ARG A1234     -22.709 -30.212 -27.196  1.00 83.35           C  
ANISOU 2204  C   ARG A1234    11284  11725   8661     62     31    555       C  
ATOM   2205  O   ARG A1234     -23.919 -30.127 -26.970  1.00 94.50           O  
ANISOU 2205  O   ARG A1234    12678  13207  10019    -11    126    528       O  
ATOM   2206  CB  ARG A1234     -21.633 -31.606 -25.411  1.00 74.49           C  
ANISOU 2206  CB  ARG A1234    10291  10735   7276    219     26    864       C  
ATOM   2207  CG  ARG A1234     -21.296 -32.723 -26.382  1.00 63.19           C  
ANISOU 2207  CG  ARG A1234     8947   9056   6007    206     88    998       C  
ATOM   2208  CD  ARG A1234     -21.058 -34.030 -25.650  1.00 72.34           C  
ANISOU 2208  CD  ARG A1234    10242  10185   7058    273    162   1245       C  
ATOM   2209  NE  ARG A1234     -20.833 -35.139 -26.570  1.00 79.34           N  
ANISOU 2209  NE  ARG A1234    11251  10800   8094    263    239   1364       N  
ATOM   2210  CZ  ARG A1234     -20.478 -36.361 -26.190  1.00 95.95           C  
ANISOU 2210  CZ  ARG A1234    13510  12800  10147    342    308   1587       C  
ATOM   2211  NH1 ARG A1234     -20.302 -36.630 -24.903  1.00105.55           N  
ANISOU 2211  NH1 ARG A1234    14760  14181  11163    433    304   1730       N  
ATOM   2212  NH2 ARG A1234     -20.295 -37.314 -27.094  1.00 97.70           N  
ANISOU 2212  NH2 ARG A1234    13866  12748  10509    337    382   1668       N  
ATOM   2213  N   ASN A1235     -22.196 -30.302 -28.421  1.00 78.29           N  
ANISOU 2213  N   ASN A1235    10635  10903   8209     43      2    533       N  
ATOM   2214  CA  ASN A1235     -23.019 -30.326 -29.629  1.00 89.85           C  
ANISOU 2214  CA  ASN A1235    12080  12228   9830    -73     71    472       C  
ATOM   2215  C   ASN A1235     -22.514 -31.460 -30.515  1.00 97.42           C  
ANISOU 2215  C   ASN A1235    13130  12972  10914    -88    115    591       C  
ATOM   2216  O   ASN A1235     -21.511 -31.306 -31.218  1.00106.59           O  
ANISOU 2216  O   ASN A1235    14273  14047  12179    -25     41    568       O  
ATOM   2217  CB  ASN A1235     -22.970 -28.984 -30.353  1.00 86.29           C  
ANISOU 2217  CB  ASN A1235    11527  11781   9478    -75    -17    276       C  
ATOM   2218  CG  ASN A1235     -23.915 -28.923 -31.538  1.00 66.68           C  
ANISOU 2218  CG  ASN A1235     9010   9198   7129   -183     49    213       C  
ATOM   2219  OD1 ASN A1235     -24.754 -29.804 -31.727  1.00 58.72           O  
ANISOU 2219  OD1 ASN A1235     8040   8148   6125   -280    160    295       O  
ATOM   2220  ND2 ASN A1235     -23.788 -27.872 -32.341  1.00 52.27           N  
ANISOU 2220  ND2 ASN A1235     7113   7341   5407   -177    -22     72       N  
ATOM   2221  N   ASP A1236     -23.209 -32.599 -30.480  1.00 87.49           N  
ANISOU 2221  N   ASP A1236    11975  11625   9641   -174    240    718       N  
ATOM   2222  CA  ASP A1236     -22.818 -33.745 -31.292  1.00 95.15           C  
ANISOU 2222  CA  ASP A1236    13074  12360  10718   -190    296    824       C  
ATOM   2223  C   ASP A1236     -23.091 -33.541 -32.776  1.00100.30           C  
ANISOU 2223  C   ASP A1236    13697  12873  11540   -283    300    707       C  
ATOM   2224  O   ASP A1236     -22.652 -34.365 -33.586  1.00 95.36           O  
ANISOU 2224  O   ASP A1236    13179  12046  11007   -280    335    760       O  
ATOM   2225  CB  ASP A1236     -23.535 -35.003 -30.800  1.00 94.16           C  
ANISOU 2225  CB  ASP A1236    13095  12158  10523   -284    430    989       C  
ATOM   2226  CG  ASP A1236     -23.046 -35.458 -29.439  1.00101.27           C  
ANISOU 2226  CG  ASP A1236    14063  13156  11258   -164    434   1151       C  
ATOM   2227  OD1 ASP A1236     -21.834 -35.326 -29.169  1.00103.16           O  
ANISOU 2227  OD1 ASP A1236    14294  13428  11475     12    343   1186       O  
ATOM   2228  OD2 ASP A1236     -23.873 -35.945 -28.640  1.00107.95           O  
ANISOU 2228  OD2 ASP A1236    14961  14066  11988   -248    527   1252       O  
ATOM   2229  N   ASP A1237     -23.799 -32.479 -33.150  1.00 96.25           N  
ANISOU 2229  N   ASP A1237    13049  12463  11058   -351    268    552       N  
ATOM   2230  CA  ASP A1237     -24.040 -32.155 -34.548  1.00 91.73           C  
ANISOU 2230  CA  ASP A1237    12433  11791  10631   -425    257    442       C  
ATOM   2231  C   ASP A1237     -22.997 -31.205 -35.122  1.00 86.64           C  
ANISOU 2231  C   ASP A1237    11707  11143  10067   -316    142    347       C  
ATOM   2232  O   ASP A1237     -23.129 -30.792 -36.279  1.00 89.12           O  
ANISOU 2232  O   ASP A1237    11976  11394  10493   -362    125    255       O  
ATOM   2233  CB  ASP A1237     -25.437 -31.551 -34.720  1.00 92.75           C  
ANISOU 2233  CB  ASP A1237    12455  12039  10747   -550    292    345       C  
ATOM   2234  CG  ASP A1237     -26.543 -32.556 -34.462  1.00113.84           C  
ANISOU 2234  CG  ASP A1237    15184  14707  13362   -710    413    439       C  
ATOM   2235  OD1 ASP A1237     -26.227 -33.739 -34.216  1.00123.31           O  
ANISOU 2235  OD1 ASP A1237    16538  15772  14544   -734    474    576       O  
ATOM   2236  OD2 ASP A1237     -27.728 -32.163 -34.506  1.00120.15           O  
ANISOU 2236  OD2 ASP A1237    15875  15644  14133   -813    451    384       O  
ATOM   2237  N   ILE A1238     -21.970 -30.847 -34.346  1.00 82.37           N  
ANISOU 2237  N   ILE A1238    11145  10685   9468   -185     61    372       N  
ATOM   2238  CA  ILE A1238     -20.923 -29.972 -34.857  1.00 72.88           C  
ANISOU 2238  CA  ILE A1238     9860   9491   8341   -109    -50    295       C  
ATOM   2239  C   ILE A1238     -20.110 -30.660 -35.945  1.00 78.86           C  
ANISOU 2239  C   ILE A1238    10666  10086   9213    -72    -33    349       C  
ATOM   2240  O   ILE A1238     -19.525 -29.985 -36.800  1.00 80.86           O  
ANISOU 2240  O   ILE A1238    10843  10320   9559    -55    -94    277       O  
ATOM   2241  CB  ILE A1238     -20.012 -29.490 -33.710  1.00 65.97           C  
ANISOU 2241  CB  ILE A1238     8942   8767   7358     -2   -149    313       C  
ATOM   2242  CG1 ILE A1238     -19.153 -28.307 -34.161  1.00 53.42           C  
ANISOU 2242  CG1 ILE A1238     7244   7215   5836     22   -273    203       C  
ATOM   2243  CG2 ILE A1238     -19.125 -30.621 -33.207  1.00 51.97           C  
ANISOU 2243  CG2 ILE A1238     7246   6972   5529    105   -132    487       C  
ATOM   2244  CD1 ILE A1238     -19.953 -27.090 -34.569  1.00 60.18           C  
ANISOU 2244  CD1 ILE A1238     8042   8084   6738    -54   -296     40       C  
ATOM   2245  N   PHE A1239     -20.069 -31.995 -35.947  1.00 76.26           N  
ANISOU 2245  N   PHE A1239    10473   9631   8872    -56     57    478       N  
ATOM   2246  CA  PHE A1239     -19.341 -32.708 -36.989  1.00 74.35           C  
ANISOU 2246  CA  PHE A1239    10301   9221   8725      1     91    521       C  
ATOM   2247  C   PHE A1239     -20.085 -32.667 -38.316  1.00 82.95           C  
ANISOU 2247  C   PHE A1239    11405  10196   9918   -128    136    421       C  
ATOM   2248  O   PHE A1239     -19.454 -32.652 -39.379  1.00 71.28           O  
ANISOU 2248  O   PHE A1239     9920   8636   8528    -85    127    391       O  
ATOM   2249  CB  PHE A1239     -19.086 -34.150 -36.553  1.00 61.71           C  
ANISOU 2249  CB  PHE A1239     8878   7493   7075     72    179    686       C  
ATOM   2250  CG  PHE A1239     -18.326 -34.262 -35.262  1.00 79.64           C  
ANISOU 2250  CG  PHE A1239    11135   9895   9229    217    133    807       C  
ATOM   2251  CD1 PHE A1239     -16.944 -34.178 -35.248  1.00 81.95           C  
ANISOU 2251  CD1 PHE A1239    11363  10249   9526    394     63    864       C  
ATOM   2252  CD2 PHE A1239     -18.994 -34.442 -34.062  1.00 88.55           C  
ANISOU 2252  CD2 PHE A1239    12301  11113  10232    176    158    868       C  
ATOM   2253  CE1 PHE A1239     -16.241 -34.276 -34.063  1.00 77.72           C  
ANISOU 2253  CE1 PHE A1239    10797   9864   8868    526      7    978       C  
ATOM   2254  CE2 PHE A1239     -18.296 -34.541 -32.873  1.00 85.97           C  
ANISOU 2254  CE2 PHE A1239    11961  10925   9778    311    109    981       C  
ATOM   2255  CZ  PHE A1239     -16.918 -34.458 -32.873  1.00 86.48           C  
ANISOU 2255  CZ  PHE A1239    11959  11054   9846    486     28   1035       C  
ATOM   2256  N   LYS A1240     -21.419 -32.645 -38.279  1.00 84.72           N  
ANISOU 2256  N   LYS A1240    11634  10434  10120   -284    183    372       N  
ATOM   2257  CA  LYS A1240     -22.184 -32.444 -39.504  1.00 72.66           C  
ANISOU 2257  CA  LYS A1240    10085   8851   8674   -412    204    269       C  
ATOM   2258  C   LYS A1240     -22.021 -31.025 -40.031  1.00 70.28           C  
ANISOU 2258  C   LYS A1240     9622   8655   8428   -387    111    150       C  
ATOM   2259  O   LYS A1240     -22.070 -30.806 -41.247  1.00 79.89           O  
ANISOU 2259  O   LYS A1240    10817   9813   9724   -425    106     83       O  
ATOM   2260  CB  LYS A1240     -23.661 -32.754 -39.261  1.00 71.94           C  
ANISOU 2260  CB  LYS A1240    10007   8795   8533   -587    273    260       C  
ATOM   2261  CG  LYS A1240     -23.929 -34.165 -38.764  1.00 77.42           C  
ANISOU 2261  CG  LYS A1240    10878   9366   9174   -652    374    385       C  
ATOM   2262  CD  LYS A1240     -25.409 -34.381 -38.497  1.00 72.79           C  
ANISOU 2262  CD  LYS A1240    10270   8854   8532   -853    438    381       C  
ATOM   2263  CE  LYS A1240     -25.677 -35.783 -37.976  1.00 78.39           C  
ANISOU 2263  CE  LYS A1240    11172   9425   9190   -947    543    518       C  
ATOM   2264  NZ  LYS A1240     -27.120 -35.998 -37.680  1.00 97.15           N  
ANISOU 2264  NZ  LYS A1240    13504  11902  11505  -1168    609    528       N  
ATOM   2265  N   ILE A1241     -21.825 -30.054 -39.137  1.00 57.77           N  
ANISOU 2265  N   ILE A1241     7940   7217   6794   -326     37    121       N  
ATOM   2266  CA  ILE A1241     -21.613 -28.675 -39.566  1.00 61.89           C  
ANISOU 2266  CA  ILE A1241     8340   7809   7369   -304    -52     13       C  
ATOM   2267  C   ILE A1241     -20.249 -28.529 -40.228  1.00 76.25           C  
ANISOU 2267  C   ILE A1241    10136   9573   9262   -220   -105     30       C  
ATOM   2268  O   ILE A1241     -20.121 -27.922 -41.298  1.00 82.74           O  
ANISOU 2268  O   ILE A1241    10905  10364  10168   -240   -130    -31       O  
ATOM   2269  CB  ILE A1241     -21.768 -27.715 -38.373  1.00 66.83           C  
ANISOU 2269  CB  ILE A1241     8901   8584   7910   -269   -113    -35       C  
ATOM   2270  CG1 ILE A1241     -23.170 -27.836 -37.771  1.00 78.89           C  
ANISOU 2270  CG1 ILE A1241    10428  10192   9354   -339    -45    -48       C  
ATOM   2271  CG2 ILE A1241     -21.485 -26.282 -38.799  1.00 63.40           C  
ANISOU 2271  CG2 ILE A1241     8376   8181   7534   -250   -205   -146       C  
ATOM   2272  CD1 ILE A1241     -23.391 -26.961 -36.556  1.00 90.19           C  
ANISOU 2272  CD1 ILE A1241    11815  11774  10678   -286    -88   -102       C  
ATOM   2273  N   ILE A1242     -19.208 -29.082 -39.599  1.00 80.51           N  
ANISOU 2273  N   ILE A1242    10705  10120   9763   -119   -119    127       N  
ATOM   2274  CA  ILE A1242     -17.876 -29.061 -40.198  1.00 82.33           C  
ANISOU 2274  CA  ILE A1242    10895  10333  10055    -27   -158    164       C  
ATOM   2275  C   ILE A1242     -17.882 -29.805 -41.527  1.00 77.29           C  
ANISOU 2275  C   ILE A1242    10328   9546   9492    -34    -77    174       C  
ATOM   2276  O   ILE A1242     -17.201 -29.411 -42.482  1.00 69.88           O  
ANISOU 2276  O   ILE A1242     9328   8598   8625     -5   -100    153       O  
ATOM   2277  CB  ILE A1242     -16.843 -29.649 -39.218  1.00 85.03           C  
ANISOU 2277  CB  ILE A1242    11248  10738  10323    101   -181    285       C  
ATOM   2278  CG1 ILE A1242     -16.758 -28.794 -37.952  1.00 71.33           C  
ANISOU 2278  CG1 ILE A1242     9435   9169   8496     98   -278    255       C  
ATOM   2279  CG2 ILE A1242     -15.475 -29.764 -39.874  1.00 78.81           C  
ANISOU 2279  CG2 ILE A1242    10398   9954   9590    212   -204    343       C  
ATOM   2280  CD1 ILE A1242     -15.784 -29.323 -36.922  1.00 57.85           C  
ANISOU 2280  CD1 ILE A1242     7723   7564   6693    222   -316    377       C  
ATOM   2281  N   MET A1243     -18.661 -30.886 -41.612  1.00 85.14           N  
ANISOU 2281  N   MET A1243    11460  10423  10464    -85     20    204       N  
ATOM   2282  CA  MET A1243     -18.772 -31.626 -42.865  1.00 81.54           C  
ANISOU 2282  CA  MET A1243    11102   9815  10065   -112     96    191       C  
ATOM   2283  C   MET A1243     -19.432 -30.784 -43.949  1.00 75.75           C  
ANISOU 2283  C   MET A1243    10290   9103   9389   -220     72     73       C  
ATOM   2284  O   MET A1243     -18.999 -30.801 -45.107  1.00 70.61           O  
ANISOU 2284  O   MET A1243     9641   8396   8792   -198     86     48       O  
ATOM   2285  CB  MET A1243     -19.558 -32.918 -42.638  1.00 89.10           C  
ANISOU 2285  CB  MET A1243    12240  10635  10979   -183    197    238       C  
ATOM   2286  CG  MET A1243     -19.711 -33.786 -43.876  1.00102.85           C  
ANISOU 2286  CG  MET A1243    14122  12196  12761   -228    277    209       C  
ATOM   2287  SD  MET A1243     -18.157 -34.543 -44.385  1.00121.90           S  
ANISOU 2287  SD  MET A1243    16625  14492  15198     -4    320    288       S  
ATOM   2288  CE  MET A1243     -17.777 -35.531 -42.941  1.00124.90           C  
ANISOU 2288  CE  MET A1243    17130  14823  15502    114    361    450       C  
ATOM   2289  N   ALA A1244     -20.478 -30.034 -43.592  1.00 69.57           N  
ANISOU 2289  N   ALA A1244     9435   8411   8586   -321     41      8       N  
ATOM   2290  CA  ALA A1244     -21.195 -29.243 -44.585  1.00 62.06           C  
ANISOU 2290  CA  ALA A1244     8410   7492   7680   -406     19    -88       C  
ATOM   2291  C   ALA A1244     -20.391 -28.029 -45.032  1.00 63.51           C  
ANISOU 2291  C   ALA A1244     8478   7732   7921   -341    -62   -121       C  
ATOM   2292  O   ALA A1244     -20.486 -27.623 -46.195  1.00 67.43           O  
ANISOU 2292  O   ALA A1244     8941   8213   8467   -369    -67   -165       O  
ATOM   2293  CB  ALA A1244     -22.551 -28.806 -44.032  1.00 59.03           C  
ANISOU 2293  CB  ALA A1244     7973   7207   7248   -502     17   -136       C  
ATOM   2294  N   ILE A1245     -19.601 -27.440 -44.133  1.00 68.58           N  
ANISOU 2294  N   ILE A1245     9062   8446   8552   -268   -128    -97       N  
ATOM   2295  CA  ILE A1245     -18.837 -26.246 -44.482  1.00 66.53           C  
ANISOU 2295  CA  ILE A1245     8698   8234   8346   -241   -209   -126       C  
ATOM   2296  C   ILE A1245     -17.779 -26.568 -45.531  1.00 70.90           C  
ANISOU 2296  C   ILE A1245     9241   8742   8955   -188   -190    -80       C  
ATOM   2297  O   ILE A1245     -17.583 -25.809 -46.488  1.00 71.22           O  
ANISOU 2297  O   ILE A1245     9222   8787   9053   -210   -214   -109       O  
ATOM   2298  CB  ILE A1245     -18.214 -25.626 -43.217  1.00 64.59           C  
ANISOU 2298  CB  ILE A1245     8402   8080   8059   -200   -291   -119       C  
ATOM   2299  CG1 ILE A1245     -19.299 -24.989 -42.345  1.00 65.90           C  
ANISOU 2299  CG1 ILE A1245     8569   8301   8168   -243   -311   -192       C  
ATOM   2300  CG2 ILE A1245     -17.147 -24.606 -43.583  1.00 58.11           C  
ANISOU 2300  CG2 ILE A1245     7486   7296   7296   -193   -374   -127       C  
ATOM   2301  CD1 ILE A1245     -18.770 -24.363 -41.074  1.00 65.57           C  
ANISOU 2301  CD1 ILE A1245     8500   8350   8063   -211   -393   -207       C  
ATOM   2302  N   VAL A1246     -17.089 -27.699 -45.377  1.00 67.30           N  
ANISOU 2302  N   VAL A1246     8848   8246   8476   -104   -138      2       N  
ATOM   2303  CA  VAL A1246     -16.020 -28.050 -46.307  1.00 68.05           C  
ANISOU 2303  CA  VAL A1246     8928   8318   8609    -19   -107     52       C  
ATOM   2304  C   VAL A1246     -16.596 -28.449 -47.661  1.00 73.55           C  
ANISOU 2304  C   VAL A1246     9699   8918   9330    -65    -34      4       C  
ATOM   2305  O   VAL A1246     -16.122 -28.001 -48.712  1.00 80.00           O  
ANISOU 2305  O   VAL A1246    10457   9752  10187    -53    -35     -5       O  
ATOM   2306  CB  VAL A1246     -15.141 -29.166 -45.716  1.00 66.50           C  
ANISOU 2306  CB  VAL A1246     8788   8107   8372    119    -64    158       C  
ATOM   2307  CG1 VAL A1246     -14.052 -29.560 -46.702  1.00 66.50           C  
ANISOU 2307  CG1 VAL A1246     8767   8097   8401    237    -16    210       C  
ATOM   2308  CG2 VAL A1246     -14.536 -28.720 -44.394  1.00 66.93           C  
ANISOU 2308  CG2 VAL A1246     8752   8294   8385    160   -152    206       C  
ATOM   2309  N   LEU A1247     -17.627 -29.297 -47.657  1.00 72.98           N  
ANISOU 2309  N   LEU A1247     9755   8752   9223   -131     28    -26       N  
ATOM   2310  CA  LEU A1247     -18.199 -29.766 -48.915  1.00 69.61           C  
ANISOU 2310  CA  LEU A1247     9410   8240   8799   -193     88    -82       C  
ATOM   2311  C   LEU A1247     -18.933 -28.654 -49.654  1.00 80.81           C  
ANISOU 2311  C   LEU A1247    10730   9732  10243   -291     37   -157       C  
ATOM   2312  O   LEU A1247     -19.048 -28.703 -50.884  1.00 83.79           O  
ANISOU 2312  O   LEU A1247    11125  10087  10624   -316     63   -194       O  
ATOM   2313  CB  LEU A1247     -19.136 -30.946 -48.662  1.00 55.95           C  
ANISOU 2313  CB  LEU A1247     7842   6397   7021   -276    159    -94       C  
ATOM   2314  CG  LEU A1247     -18.490 -32.206 -48.083  1.00 48.37           C  
ANISOU 2314  CG  LEU A1247     7031   5317   6032   -170    229    -10       C  
ATOM   2315  CD1 LEU A1247     -19.507 -33.333 -47.977  1.00 46.61           C  
ANISOU 2315  CD1 LEU A1247     6990   4954   5766   -294    302    -27       C  
ATOM   2316  CD2 LEU A1247     -17.295 -32.634 -48.922  1.00 46.24           C  
ANISOU 2316  CD2 LEU A1247     6800   4990   5778    -15    277     22       C  
ATOM   2317  N   PHE A1248     -19.437 -27.650 -48.932  1.00 75.62           N  
ANISOU 2317  N   PHE A1248     9977   9162   9591   -333    -33   -179       N  
ATOM   2318  CA  PHE A1248     -20.096 -26.531 -49.597  1.00 69.69           C  
ANISOU 2318  CA  PHE A1248     9141   8474   8865   -392    -80   -236       C  
ATOM   2319  C   PHE A1248     -19.089 -25.678 -50.357  1.00 76.28           C  
ANISOU 2319  C   PHE A1248     9897   9332   9753   -339   -115   -213       C  
ATOM   2320  O   PHE A1248     -19.394 -25.162 -51.438  1.00 91.23           O  
ANISOU 2320  O   PHE A1248    11762  11241  11661   -369   -120   -237       O  
ATOM   2321  CB  PHE A1248     -20.857 -25.684 -48.578  1.00 67.74           C  
ANISOU 2321  CB  PHE A1248     8834   8300   8605   -419   -133   -267       C  
ATOM   2322  CG  PHE A1248     -21.829 -24.720 -49.193  1.00 76.24           C  
ANISOU 2322  CG  PHE A1248     9845   9433   9691   -463   -164   -321       C  
ATOM   2323  CD1 PHE A1248     -23.092 -25.140 -49.576  1.00 72.61           C  
ANISOU 2323  CD1 PHE A1248     9393   9009   9187   -544   -130   -356       C  
ATOM   2324  CD2 PHE A1248     -21.485 -23.391 -49.381  1.00 86.40           C  
ANISOU 2324  CD2 PHE A1248    11064  10741  11024   -426   -227   -329       C  
ATOM   2325  CE1 PHE A1248     -23.991 -24.256 -50.140  1.00 73.57           C  
ANISOU 2325  CE1 PHE A1248     9438   9210   9307   -559   -161   -392       C  
ATOM   2326  CE2 PHE A1248     -22.381 -22.502 -49.944  1.00 75.11           C  
ANISOU 2326  CE2 PHE A1248     9587   9352   9598   -437   -250   -363       C  
ATOM   2327  CZ  PHE A1248     -23.636 -22.935 -50.323  1.00 72.25           C  
ANISOU 2327  CZ  PHE A1248     9215   9050   9187   -490   -218   -392       C  
ATOM   2328  N   PHE A1249     -17.883 -25.517 -49.808  1.00 75.35           N  
ANISOU 2328  N   PHE A1249     9737   9235   9659   -267   -142   -156       N  
ATOM   2329  CA  PHE A1249     -16.840 -24.787 -50.518  1.00 70.42           C  
ANISOU 2329  CA  PHE A1249     9025   8649   9082   -236   -168   -117       C  
ATOM   2330  C   PHE A1249     -16.281 -25.599 -51.677  1.00 73.53           C  
ANISOU 2330  C   PHE A1249     9455   9015   9467   -181    -88    -87       C  
ATOM   2331  O   PHE A1249     -15.883 -25.028 -52.699  1.00 83.14           O  
ANISOU 2331  O   PHE A1249    10616  10265  10709   -183    -87    -71       O  
ATOM   2332  CB  PHE A1249     -15.719 -24.401 -49.550  1.00 57.69           C  
ANISOU 2332  CB  PHE A1249     7334   7099   7485   -195   -228    -64       C  
ATOM   2333  CG  PHE A1249     -14.578 -23.667 -50.198  1.00 58.71           C  
ANISOU 2333  CG  PHE A1249     7355   7289   7664   -190   -256    -11       C  
ATOM   2334  CD1 PHE A1249     -14.610 -22.288 -50.330  1.00 58.55           C  
ANISOU 2334  CD1 PHE A1249     7274   7282   7690   -273   -328    -31       C  
ATOM   2335  CD2 PHE A1249     -13.467 -24.353 -50.665  1.00 67.35           C  
ANISOU 2335  CD2 PHE A1249     8411   8427   8753   -100   -203     67       C  
ATOM   2336  CE1 PHE A1249     -13.561 -21.610 -50.922  1.00 68.86           C  
ANISOU 2336  CE1 PHE A1249     8480   8643   9039   -296   -350     31       C  
ATOM   2337  CE2 PHE A1249     -12.416 -23.680 -51.259  1.00 60.26           C  
ANISOU 2337  CE2 PHE A1249     7389   7615   7893   -106   -221    129       C  
ATOM   2338  CZ  PHE A1249     -12.463 -22.307 -51.387  1.00 63.58           C  
ANISOU 2338  CZ  PHE A1249     7748   8048   8363   -221   -297    113       C  
ATOM   2339  N   PHE A1250     -16.246 -26.925 -51.541  1.00 68.66           N  
ANISOU 2339  N   PHE A1250     8948   8332   8810   -126    -15    -77       N  
ATOM   2340  CA  PHE A1250     -15.637 -27.770 -52.563  1.00 78.43           C  
ANISOU 2340  CA  PHE A1250    10246   9527  10026    -45     72    -57       C  
ATOM   2341  C   PHE A1250     -16.576 -27.977 -53.748  1.00 83.46           C  
ANISOU 2341  C   PHE A1250    10963  10116  10630   -124    110   -135       C  
ATOM   2342  O   PHE A1250     -16.220 -27.682 -54.893  1.00 83.87           O  
ANISOU 2342  O   PHE A1250    10983  10206  10678   -105    132   -134       O  
ATOM   2343  CB  PHE A1250     -15.230 -29.114 -51.951  1.00 82.03           C  
ANISOU 2343  CB  PHE A1250    10821   9901  10446     60    140    -16       C  
ATOM   2344  CG  PHE A1250     -14.492 -30.014 -52.900  1.00 81.10           C  
ANISOU 2344  CG  PHE A1250    10785   9730  10300    185    240      3       C  
ATOM   2345  CD1 PHE A1250     -13.139 -29.833 -53.137  1.00 84.72           C  
ANISOU 2345  CD1 PHE A1250    11130  10287  10771    324    255     86       C  
ATOM   2346  CD2 PHE A1250     -15.148 -31.046 -53.549  1.00 78.00           C  
ANISOU 2346  CD2 PHE A1250    10583   9195   9860    160    320    -65       C  
ATOM   2347  CE1 PHE A1250     -12.456 -30.662 -54.007  1.00 86.89           C  
ANISOU 2347  CE1 PHE A1250    11480  10526  11009    468    360    103       C  
ATOM   2348  CE2 PHE A1250     -14.471 -31.878 -54.421  1.00 78.53           C  
ANISOU 2348  CE2 PHE A1250    10752   9197   9888    291    420    -63       C  
ATOM   2349  CZ  PHE A1250     -13.123 -31.685 -54.650  1.00 80.86           C  
ANISOU 2349  CZ  PHE A1250    10932   9597  10194    461    446     23       C  
ATOM   2350  N   PHE A1251     -17.784 -28.482 -53.488  1.00 77.19           N  
ANISOU 2350  N   PHE A1251    10264   9261   9804   -222    117   -198       N  
ATOM   2351  CA  PHE A1251     -18.716 -28.796 -54.566  1.00 50.70           C  
ANISOU 2351  CA  PHE A1251     6982   5879   6401   -317    144   -277       C  
ATOM   2352  C   PHE A1251     -19.269 -27.561 -55.263  1.00 70.93           C  
ANISOU 2352  C   PHE A1251     9424   8550   8974   -381     80   -299       C  
ATOM   2353  O   PHE A1251     -19.862 -27.696 -56.339  1.00 88.16           O  
ANISOU 2353  O   PHE A1251    11641  10748  11107   -442     93   -352       O  
ATOM   2354  CB  PHE A1251     -19.872 -29.644 -54.033  1.00 46.99           C  
ANISOU 2354  CB  PHE A1251     6624   5340   5891   -433    162   -328       C  
ATOM   2355  CG  PHE A1251     -19.515 -31.086 -53.820  1.00 60.74           C  
ANISOU 2355  CG  PHE A1251     8550   6926   7600   -391    249   -320       C  
ATOM   2356  CD1 PHE A1251     -19.420 -31.953 -54.896  1.00 56.05           C  
ANISOU 2356  CD1 PHE A1251     8104   6234   6957   -389    320   -374       C  
ATOM   2357  CD2 PHE A1251     -19.277 -31.577 -52.547  1.00 80.99           C  
ANISOU 2357  CD2 PHE A1251    11160   9436  10176   -344    262   -258       C  
ATOM   2358  CE1 PHE A1251     -19.093 -33.282 -54.708  1.00 59.07           C  
ANISOU 2358  CE1 PHE A1251     8692   6440   7311   -336    408   -370       C  
ATOM   2359  CE2 PHE A1251     -18.950 -32.906 -52.352  1.00 88.99           C  
ANISOU 2359  CE2 PHE A1251    12365  10286  11160   -289    348   -235       C  
ATOM   2360  CZ  PHE A1251     -18.857 -33.759 -53.434  1.00 80.18           C  
ANISOU 2360  CZ  PHE A1251    11413   9047  10005   -282    423   -293       C  
ATOM   2361  N   SER A1252     -19.098 -26.370 -54.688  1.00 73.09           N  
ANISOU 2361  N   SER A1252     9573   8893   9304   -368      9   -261       N  
ATOM   2362  CA  SER A1252     -19.571 -25.164 -55.360  1.00 82.25           C  
ANISOU 2362  CA  SER A1252    10642  10130  10478   -405    -45   -267       C  
ATOM   2363  C   SER A1252     -18.562 -24.663 -56.384  1.00 78.15           C  
ANISOU 2363  C   SER A1252    10073   9643   9975   -349    -32   -213       C  
ATOM   2364  O   SER A1252     -18.949 -24.156 -57.443  1.00 91.62           O  
ANISOU 2364  O   SER A1252    11756  11398  11656   -375    -40   -218       O  
ATOM   2365  CB  SER A1252     -19.875 -24.071 -54.335  1.00 94.15           C  
ANISOU 2365  CB  SER A1252    12070  11669  12034   -414   -120   -258       C  
ATOM   2366  OG  SER A1252     -18.734 -23.774 -53.549  1.00109.37           O  
ANISOU 2366  OG  SER A1252    13960  13586  14011   -359   -143   -207       O  
ATOM   2367  N   TRP A1253     -17.267 -24.801 -56.093  1.00 62.49           N  
ANISOU 2367  N   TRP A1253     8062   7655   8025   -271    -10   -151       N  
ATOM   2368  CA  TRP A1253     -16.223 -24.292 -56.972  1.00 63.40           C  
ANISOU 2368  CA  TRP A1253     8104   7828   8155   -224      8    -82       C  
ATOM   2369  C   TRP A1253     -15.632 -25.345 -57.898  1.00 72.99           C  
ANISOU 2369  C   TRP A1253     9386   9039   9309   -143    108    -81       C  
ATOM   2370  O   TRP A1253     -15.061 -24.980 -58.932  1.00 86.52           O  
ANISOU 2370  O   TRP A1253    11050  10819  11005   -114    139    -37       O  
ATOM   2371  CB  TRP A1253     -15.090 -23.668 -56.147  1.00 70.43           C  
ANISOU 2371  CB  TRP A1253     8888   8759   9113   -197    -33     -6       C  
ATOM   2372  CG  TRP A1253     -15.472 -22.394 -55.462  1.00 77.84           C  
ANISOU 2372  CG  TRP A1253     9771   9696  10108   -274   -129     -9       C  
ATOM   2373  CD1 TRP A1253     -15.767 -22.229 -54.140  1.00 76.24           C  
ANISOU 2373  CD1 TRP A1253     9575   9468   9925   -296   -187    -41       C  
ATOM   2374  CD2 TRP A1253     -15.603 -21.102 -56.067  1.00 87.02           C  
ANISOU 2374  CD2 TRP A1253    10886  10872  11307   -331   -173     18       C  
ATOM   2375  NE1 TRP A1253     -16.072 -20.914 -53.884  1.00 81.52           N  
ANISOU 2375  NE1 TRP A1253    10210  10126  10638   -356   -262    -50       N  
ATOM   2376  CE2 TRP A1253     -15.979 -20.202 -55.051  1.00 85.54           C  
ANISOU 2376  CE2 TRP A1253    10691  10646  11163   -378   -255     -9       C  
ATOM   2377  CE3 TRP A1253     -15.439 -20.620 -57.369  1.00 91.76           C  
ANISOU 2377  CE3 TRP A1253    11459  11508  11897   -339   -146     68       C  
ATOM   2378  CZ2 TRP A1253     -16.193 -18.847 -55.296  1.00 92.28           C  
ANISOU 2378  CZ2 TRP A1253    11530  11470  12061   -428   -308      9       C  
ATOM   2379  CZ3 TRP A1253     -15.652 -19.276 -57.610  1.00 95.30           C  
ANISOU 2379  CZ3 TRP A1253    11881  11938  12389   -395   -201    102       C  
ATOM   2380  CH2 TRP A1253     -16.025 -18.404 -56.579  1.00 95.80           C  
ANISOU 2380  CH2 TRP A1253    11956  11937  12506   -436   -281     71       C  
ATOM   2381  N   ILE A1254     -15.754 -26.627 -57.568  1.00 70.34           N  
ANISOU 2381  N   ILE A1254     9173   8619   8932   -102    165   -125       N  
ATOM   2382  CA  ILE A1254     -15.109 -27.682 -58.350  1.00 62.44           C  
ANISOU 2382  CA  ILE A1254     8267   7587   7870      4    270   -131       C  
ATOM   2383  C   ILE A1254     -15.726 -27.853 -59.740  1.00 74.06           C  
ANISOU 2383  C   ILE A1254     9816   9065   9259    -43    305   -203       C  
ATOM   2384  O   ILE A1254     -15.035 -28.366 -60.631  1.00 75.78           O  
ANISOU 2384  O   ILE A1254    10081   9294   9417     56    391   -200       O  
ATOM   2385  CB  ILE A1254     -15.093 -29.015 -57.577  1.00 53.77           C  
ANISOU 2385  CB  ILE A1254     7317   6361   6753     65    324   -155       C  
ATOM   2386  CG1 ILE A1254     -13.930 -29.888 -58.052  1.00 56.37           C  
ANISOU 2386  CG1 ILE A1254     7704   6672   7042    247    432   -118       C  
ATOM   2387  CG2 ILE A1254     -16.397 -29.780 -57.732  1.00 56.29           C  
ANISOU 2387  CG2 ILE A1254     7802   6568   7017    -53    335   -264       C  
ATOM   2388  CD1 ILE A1254     -12.579 -29.218 -57.939  1.00 66.40           C  
ANISOU 2388  CD1 ILE A1254     8784   8091   8356    358    427      2       C  
ATOM   2389  N   PRO A1255     -16.981 -27.458 -60.011  1.00 68.84           N  
ANISOU 2389  N   PRO A1255     9163   8416   8575   -177    246   -265       N  
ATOM   2390  CA  PRO A1255     -17.404 -27.457 -61.422  1.00 71.67           C  
ANISOU 2390  CA  PRO A1255     9562   8828   8842   -213    267   -315       C  
ATOM   2391  C   PRO A1255     -16.755 -26.350 -62.231  1.00 75.94           C  
ANISOU 2391  C   PRO A1255     9970   9493   9390   -171    259   -227       C  
ATOM   2392  O   PRO A1255     -16.367 -26.577 -63.384  1.00 84.17           O  
ANISOU 2392  O   PRO A1255    11045  10587  10350   -121    322   -231       O  
ATOM   2393  CB  PRO A1255     -18.929 -27.285 -61.338  1.00 70.68           C  
ANISOU 2393  CB  PRO A1255     9447   8717   8691   -363    194   -387       C  
ATOM   2394  CG  PRO A1255     -19.287 -27.707 -59.967  1.00 69.86           C  
ANISOU 2394  CG  PRO A1255     9374   8527   8644   -399    174   -400       C  
ATOM   2395  CD  PRO A1255     -18.146 -27.243 -59.129  1.00 74.12           C  
ANISOU 2395  CD  PRO A1255     9826   9062   9272   -292    172   -305       C  
ATOM   2396  N   HIS A1256     -16.616 -25.153 -61.655  1.00 66.02           N  
ANISOU 2396  N   HIS A1256     8578   8281   8227   -195    187   -146       N  
ATOM   2397  CA  HIS A1256     -16.043 -24.036 -62.398  1.00 63.62           C  
ANISOU 2397  CA  HIS A1256     8160   8074   7936   -183    177    -49       C  
ATOM   2398  C   HIS A1256     -14.535 -24.174 -62.560  1.00 68.13           C  
ANISOU 2398  C   HIS A1256     8669   8696   8522    -81    250     36       C  
ATOM   2399  O   HIS A1256     -13.983 -23.742 -63.578  1.00 75.14           O  
ANISOU 2399  O   HIS A1256     9501   9678   9369    -55    291    104       O  
ATOM   2400  CB  HIS A1256     -16.385 -22.717 -61.703  1.00 68.61           C  
ANISOU 2400  CB  HIS A1256     8700   8706   8664   -249     79      1       C  
ATOM   2401  CG  HIS A1256     -15.756 -21.517 -62.339  1.00 74.00           C  
ANISOU 2401  CG  HIS A1256     9286   9455   9377   -256     68    115       C  
ATOM   2402  ND1 HIS A1256     -14.526 -21.028 -61.952  1.00 82.22           N  
ANISOU 2402  ND1 HIS A1256    10231  10517  10490   -246     72    208       N  
ATOM   2403  CD2 HIS A1256     -16.186 -20.706 -63.334  1.00 79.64           C  
ANISOU 2403  CD2 HIS A1256     9984  10222  10053   -282     52    160       C  
ATOM   2404  CE1 HIS A1256     -14.226 -19.969 -62.682  1.00 85.61           C  
ANISOU 2404  CE1 HIS A1256    10600  10996  10933   -282     64    306       C  
ATOM   2405  NE2 HIS A1256     -15.216 -19.752 -63.529  1.00 84.02           N  
ANISOU 2405  NE2 HIS A1256    10451  10808  10664   -293     54    283       N  
ATOM   2406  N   GLN A1257     -13.854 -24.768 -61.579  1.00 69.68           N  
ANISOU 2406  N   GLN A1257     8861   8850   8765    -17    269     47       N  
ATOM   2407  CA  GLN A1257     -12.402 -24.877 -61.635  1.00 72.80           C  
ANISOU 2407  CA  GLN A1257     9161   9329   9172     91    332    142       C  
ATOM   2408  C   GLN A1257     -11.924 -25.959 -62.594  1.00 81.22           C  
ANISOU 2408  C   GLN A1257    10314  10415  10132    226    459    116       C  
ATOM   2409  O   GLN A1257     -10.775 -25.900 -63.046  1.00 81.74           O  
ANISOU 2409  O   GLN A1257    10279  10598  10180    324    529    206       O  
ATOM   2410  CB  GLN A1257     -11.837 -25.141 -60.238  1.00 75.70           C  
ANISOU 2410  CB  GLN A1257     9483   9669   9609    130    301    172       C  
ATOM   2411  CG  GLN A1257     -12.052 -24.001 -59.252  1.00 82.99           C  
ANISOU 2411  CG  GLN A1257    10314  10590  10627     10    181    200       C  
ATOM   2412  CD  GLN A1257     -11.317 -22.734 -59.648  1.00 87.23           C  
ANISOU 2412  CD  GLN A1257    10700  11232  11212    -55    149    304       C  
ATOM   2413  OE1 GLN A1257     -10.326 -22.777 -60.378  1.00 81.81           O  
ANISOU 2413  OE1 GLN A1257     9926  10658  10499      5    218    386       O  
ATOM   2414  NE2 GLN A1257     -11.801 -21.595 -59.166  1.00 89.31           N  
ANISOU 2414  NE2 GLN A1257    10937  11454  11542   -177     50    304       N  
ATOM   2415  N   ILE A1258     -12.767 -26.940 -62.915  1.00 87.01           N  
ANISOU 2415  N   ILE A1258    11232  11041  10787    228    494     -6       N  
ATOM   2416  CA  ILE A1258     -12.370 -27.979 -63.859  1.00 87.56           C  
ANISOU 2416  CA  ILE A1258    11424  11102  10742    356    617    -56       C  
ATOM   2417  C   ILE A1258     -12.450 -27.463 -65.290  1.00 78.38           C  
ANISOU 2417  C   ILE A1258    10237  10057   9487    334    646    -50       C  
ATOM   2418  O   ILE A1258     -11.511 -27.624 -66.078  1.00 74.71           O  
ANISOU 2418  O   ILE A1258     9738   9693   8954    461    746     -1       O  
ATOM   2419  CB  ILE A1258     -13.228 -29.242 -63.661  1.00 81.44           C  
ANISOU 2419  CB  ILE A1258    10883  10148   9913    340    641   -197       C  
ATOM   2420  CG1 ILE A1258     -12.846 -29.941 -62.355  1.00 76.34           C  
ANISOU 2420  CG1 ILE A1258    10276   9393   9336    419    651   -173       C  
ATOM   2421  CG2 ILE A1258     -13.070 -30.188 -64.843  1.00 66.35           C  
ANISOU 2421  CG2 ILE A1258     9140   8209   7863    436    757   -283       C  
ATOM   2422  CD1 ILE A1258     -13.639 -31.199 -62.080  1.00 70.66           C  
ANISOU 2422  CD1 ILE A1258     9801   8473   8573    390    682   -293       C  
ATOM   2423  N   PHE A1259     -13.571 -26.833 -65.650  1.00 66.38           N  
ANISOU 2423  N   PHE A1259     8727   8544   7952    185    562    -91       N  
ATOM   2424  CA  PHE A1259     -13.692 -26.244 -66.978  1.00 68.96           C  
ANISOU 2424  CA  PHE A1259     9021   8997   8182    163    576    -67       C  
ATOM   2425  C   PHE A1259     -12.772 -25.045 -67.160  1.00 78.27           C  
ANISOU 2425  C   PHE A1259    10005  10311   9421    175    575    101       C  
ATOM   2426  O   PHE A1259     -12.430 -24.710 -68.299  1.00 98.24           O  
ANISOU 2426  O   PHE A1259    12499  12965  11861    204    629    156       O  
ATOM   2427  CB  PHE A1259     -15.144 -25.849 -67.250  1.00 69.26           C  
ANISOU 2427  CB  PHE A1259     9102   9028   8186     15    478   -136       C  
ATOM   2428  CG  PHE A1259     -16.061 -27.024 -67.442  1.00 80.27           C  
ANISOU 2428  CG  PHE A1259    10685  10332   9483    -32    487   -302       C  
ATOM   2429  CD1 PHE A1259     -16.135 -27.666 -68.667  1.00 86.31           C  
ANISOU 2429  CD1 PHE A1259    11572  11139  10084     -5    552   -386       C  
ATOM   2430  CD2 PHE A1259     -16.843 -27.489 -66.398  1.00 75.19           C  
ANISOU 2430  CD2 PHE A1259    10104   9564   8902   -116    431   -374       C  
ATOM   2431  CE1 PHE A1259     -16.974 -28.750 -68.849  1.00 84.92           C  
ANISOU 2431  CE1 PHE A1259    11585  10867   9813    -80    554   -550       C  
ATOM   2432  CE2 PHE A1259     -17.684 -28.572 -66.573  1.00 65.70           C  
ANISOU 2432  CE2 PHE A1259     9078   8274   7611   -194    439   -520       C  
ATOM   2433  CZ  PHE A1259     -17.749 -29.203 -67.800  1.00 82.37           C  
ANISOU 2433  CZ  PHE A1259    11319  10413   9564   -185    496   -613       C  
ATOM   2434  N   THR A1260     -12.368 -24.391 -66.068  1.00 72.08           N  
ANISOU 2434  N   THR A1260     9101   9508   8778    138    513    183       N  
ATOM   2435  CA  THR A1260     -11.310 -23.392 -66.160  1.00 68.97           C  
ANISOU 2435  CA  THR A1260     8528   9234   8443    133    520    341       C  
ATOM   2436  C   THR A1260      -9.991 -24.039 -66.561  1.00 61.69           C  
ANISOU 2436  C   THR A1260     7547   8427   7467    287    648    399       C  
ATOM   2437  O   THR A1260      -9.255 -23.506 -67.399  1.00 51.09           O  
ANISOU 2437  O   THR A1260     6094   7236   6084    304    707    511       O  
ATOM   2438  CB  THR A1260     -11.166 -22.653 -64.828  1.00 63.69           C  
ANISOU 2438  CB  THR A1260     7764   8512   7924     48    419    391       C  
ATOM   2439  OG1 THR A1260     -12.356 -21.898 -64.566  1.00 76.98           O  
ANISOU 2439  OG1 THR A1260     9492  10108   9649    -72    313    351       O  
ATOM   2440  CG2 THR A1260      -9.968 -21.714 -64.858  1.00 51.55           C  
ANISOU 2440  CG2 THR A1260     6042   7097   6448     15    424    549       C  
ATOM   2441  N   PHE A1261      -9.682 -25.199 -65.975  1.00 54.96           N  
ANISOU 2441  N   PHE A1261     6767   7509   6605    410    700    334       N  
ATOM   2442  CA  PHE A1261      -8.485 -25.936 -66.363  1.00 64.75           C  
ANISOU 2442  CA  PHE A1261     7966   8857   7778    602    834    381       C  
ATOM   2443  C   PHE A1261      -8.595 -26.471 -67.785  1.00 75.40           C  
ANISOU 2443  C   PHE A1261     9432  10254   8964    691    947    320       C  
ATOM   2444  O   PHE A1261      -7.584 -26.565 -68.490  1.00 68.74           O  
ANISOU 2444  O   PHE A1261     8500   9570   8047    823   1062    400       O  
ATOM   2445  CB  PHE A1261      -8.236 -27.077 -65.376  1.00 70.15           C  
ANISOU 2445  CB  PHE A1261     8734   9433   8487    733    862    327       C  
ATOM   2446  CG  PHE A1261      -7.008 -27.888 -65.678  1.00 70.08           C  
ANISOU 2446  CG  PHE A1261     8687   9529   8409    972   1005    381       C  
ATOM   2447  CD1 PHE A1261      -5.750 -27.414 -65.344  1.00 69.27           C  
ANISOU 2447  CD1 PHE A1261     8337   9624   8357   1033   1022    540       C  
ATOM   2448  CD2 PHE A1261      -7.113 -29.128 -66.286  1.00 64.38           C  
ANISOU 2448  CD2 PHE A1261     8179   8716   7567   1139   1125    269       C  
ATOM   2449  CE1 PHE A1261      -4.619 -28.160 -65.617  1.00 69.89           C  
ANISOU 2449  CE1 PHE A1261     8357   9832   8365   1278   1160    601       C  
ATOM   2450  CE2 PHE A1261      -5.986 -29.878 -66.562  1.00 66.53           C  
ANISOU 2450  CE2 PHE A1261     8427   9082   7769   1395   1269    318       C  
ATOM   2451  CZ  PHE A1261      -4.737 -29.393 -66.227  1.00 68.81           C  
ANISOU 2451  CZ  PHE A1261     8443   9594   8107   1477   1289    490       C  
ATOM   2452  N   LEU A1262      -9.806 -26.827 -68.221  1.00 79.88           N  
ANISOU 2452  N   LEU A1262    10188  10702   9459    618    915    179       N  
ATOM   2453  CA  LEU A1262      -9.999 -27.249 -69.604  1.00 71.37           C  
ANISOU 2453  CA  LEU A1262     9229   9680   8207    674   1002    107       C  
ATOM   2454  C   LEU A1262      -9.821 -26.086 -70.571  1.00 72.54           C  
ANISOU 2454  C   LEU A1262     9235  10015   8313    609    999    230       C  
ATOM   2455  O   LEU A1262      -9.411 -26.293 -71.719  1.00 85.06           O  
ANISOU 2455  O   LEU A1262    10841  11727   9751    704   1107    237       O  
ATOM   2456  CB  LEU A1262     -11.381 -27.880 -69.775  1.00 70.88           C  
ANISOU 2456  CB  LEU A1262     9390   9466   8077    576    948    -74       C  
ATOM   2457  CG  LEU A1262     -11.484 -29.404 -69.653  1.00 76.63           C  
ANISOU 2457  CG  LEU A1262    10357  10026   8734    680   1026   -230       C  
ATOM   2458  CD1 LEU A1262     -10.788 -29.914 -68.399  1.00 69.54           C  
ANISOU 2458  CD1 LEU A1262     9437   9031   7956    789   1049   -185       C  
ATOM   2459  CD2 LEU A1262     -12.941 -29.838 -69.669  1.00 86.24           C  
ANISOU 2459  CD2 LEU A1262    11756  11104   9908    511    942   -392       C  
ATOM   2460  N   ASP A1263     -10.124 -24.863 -70.129  1.00 65.22           N  
ANISOU 2460  N   ASP A1263     8179   9099   7505    453    883    328       N  
ATOM   2461  CA  ASP A1263      -9.868 -23.691 -70.957  1.00 70.70           C  
ANISOU 2461  CA  ASP A1263     8742   9946   8174    387    883    474       C  
ATOM   2462  C   ASP A1263      -8.374 -23.457 -71.148  1.00 82.26           C  
ANISOU 2462  C   ASP A1263    10025  11584   9645    475    988    631       C  
ATOM   2463  O   ASP A1263      -7.955 -22.950 -72.195  1.00 97.77           O  
ANISOU 2463  O   ASP A1263    11917  13713  11520    483   1057    737       O  
ATOM   2464  CB  ASP A1263     -10.527 -22.459 -70.336  1.00 77.37           C  
ANISOU 2464  CB  ASP A1263     9521  10721   9155    212    739    539       C  
ATOM   2465  CG  ASP A1263     -10.141 -21.172 -71.038  1.00 95.73           C  
ANISOU 2465  CG  ASP A1263    11720  13171  11483    138    739    717       C  
ATOM   2466  OD1 ASP A1263     -10.581 -20.965 -72.187  1.00102.87           O  
ANISOU 2466  OD1 ASP A1263    12673  14156  12257    139    763    731       O  
ATOM   2467  OD2 ASP A1263      -9.396 -20.368 -70.440  1.00103.54           O  
ANISOU 2467  OD2 ASP A1263    12565  14177  12598     70    713    847       O  
ATOM   2468  N   VAL A1264      -7.560 -23.822 -70.155  1.00 68.62           N  
ANISOU 2468  N   VAL A1264     8211   9847   8016    542   1003    659       N  
ATOM   2469  CA  VAL A1264      -6.117 -23.640 -70.272  1.00 73.53           C  
ANISOU 2469  CA  VAL A1264     8627  10671   8641    626   1099    815       C  
ATOM   2470  C   VAL A1264      -5.533 -24.629 -71.273  1.00 83.05           C  
ANISOU 2470  C   VAL A1264     9884  11998   9671    848   1273    783       C  
ATOM   2471  O   VAL A1264      -4.608 -24.298 -72.025  1.00 86.68           O  
ANISOU 2471  O   VAL A1264    10192  12681  10062    904   1377    917       O  
ATOM   2472  CB  VAL A1264      -5.451 -23.770 -68.890  1.00 81.09           C  
ANISOU 2472  CB  VAL A1264     9467  11607   9738    640   1051    854       C  
ATOM   2473  CG1 VAL A1264      -3.955 -23.509 -68.991  1.00 75.51           C  
ANISOU 2473  CG1 VAL A1264     8507  11152   9034    705   1137   1030       C  
ATOM   2474  CG2 VAL A1264      -6.097 -22.816 -67.900  1.00 83.68           C  
ANISOU 2474  CG2 VAL A1264     9775  11801  10219    427    881    860       C  
ATOM   2475  N   LEU A1265      -6.060 -25.856 -71.302  1.00 81.29           N  
ANISOU 2475  N   LEU A1265     9886  11631   9368    974   1313    603       N  
ATOM   2476  CA  LEU A1265      -5.560 -26.854 -72.243  1.00 83.48           C  
ANISOU 2476  CA  LEU A1265    10261  11991   9468   1201   1483    543       C  
ATOM   2477  C   LEU A1265      -5.813 -26.429 -73.684  1.00 86.44           C  
ANISOU 2477  C   LEU A1265    10664  12500   9680   1169   1536    556       C  
ATOM   2478  O   LEU A1265      -4.989 -26.690 -74.569  1.00 96.77           O  
ANISOU 2478  O   LEU A1265    11925  13995  10849   1332   1689    605       O  
ATOM   2479  CB  LEU A1265      -6.202 -28.212 -71.960  1.00 69.45           C  
ANISOU 2479  CB  LEU A1265     8764   9981   7641   1304   1501    334       C  
ATOM   2480  CG  LEU A1265      -5.779 -28.899 -70.660  1.00 65.46           C  
ANISOU 2480  CG  LEU A1265     8259   9359   7253   1409   1494    330       C  
ATOM   2481  CD1 LEU A1265      -6.507 -30.222 -70.487  1.00 60.35           C  
ANISOU 2481  CD1 LEU A1265     7926   8454   6549   1485   1517    128       C  
ATOM   2482  CD2 LEU A1265      -4.272 -29.105 -70.634  1.00 64.41           C  
ANISOU 2482  CD2 LEU A1265     7936   9433   7105   1638   1626    470       C  
ATOM   2483  N   ILE A1266      -6.947 -25.774 -73.940  1.00 78.45           N  
ANISOU 2483  N   ILE A1266     9722  11412   8671    973   1415    518       N  
ATOM   2484  CA  ILE A1266      -7.206 -25.250 -75.276  1.00 73.41           C  
ANISOU 2484  CA  ILE A1266     9095  10921   7878    935   1449    557       C  
ATOM   2485  C   ILE A1266      -6.293 -24.068 -75.572  1.00 74.14           C  
ANISOU 2485  C   ILE A1266     8932  11227   8011    880   1482    801       C  
ATOM   2486  O   ILE A1266      -5.877 -23.865 -76.719  1.00 74.56           O  
ANISOU 2486  O   ILE A1266     8943  11478   7910    938   1590    880       O  
ATOM   2487  CB  ILE A1266      -8.690 -24.865 -75.421  1.00 72.30           C  
ANISOU 2487  CB  ILE A1266     9085  10659   7729    755   1303    465       C  
ATOM   2488  CG1 ILE A1266      -9.590 -26.015 -74.966  1.00 70.38           C  
ANISOU 2488  CG1 ILE A1266     9071  10202   7467    764   1259    235       C  
ATOM   2489  CG2 ILE A1266      -9.005 -24.488 -76.860  1.00 60.99           C  
ANISOU 2489  CG2 ILE A1266     7687   9388   6099    743   1339    491       C  
ATOM   2490  CD1 ILE A1266     -11.067 -25.680 -74.990  1.00 57.80           C  
ANISOU 2490  CD1 ILE A1266     7572   8518   5872    583   1109    148       C  
ATOM   2491  N   GLN A1267      -5.958 -23.278 -74.549  1.00 77.33           N  
ANISOU 2491  N   GLN A1267     9169  11599   8615    757   1393    923       N  
ATOM   2492  CA  GLN A1267      -5.107 -22.111 -74.758  1.00 75.65           C  
ANISOU 2492  CA  GLN A1267     8722  11565   8455    659   1413   1156       C  
ATOM   2493  C   GLN A1267      -3.668 -22.517 -75.054  1.00 80.47           C  
ANISOU 2493  C   GLN A1267     9159  12416   8998    827   1580   1263       C  
ATOM   2494  O   GLN A1267      -3.015 -21.922 -75.919  1.00 82.02           O  
ANISOU 2494  O   GLN A1267     9215  12834   9114    812   1671   1427       O  
ATOM   2495  CB  GLN A1267      -5.169 -21.199 -73.532  1.00 74.15           C  
ANISOU 2495  CB  GLN A1267     8428  11255   8489    468   1263   1230       C  
ATOM   2496  CG  GLN A1267      -4.302 -19.957 -73.629  1.00 85.73           C  
ANISOU 2496  CG  GLN A1267     9672  12871  10030    321   1267   1465       C  
ATOM   2497  CD  GLN A1267      -4.385 -19.094 -72.385  1.00 99.71           C  
ANISOU 2497  CD  GLN A1267    11376  14498  12012    126   1114   1509       C  
ATOM   2498  OE1 GLN A1267      -5.136 -19.393 -71.457  1.00106.13           O  
ANISOU 2498  OE1 GLN A1267    12304  15112  12910    112   1007   1367       O  
ATOM   2499  NE2 GLN A1267      -3.609 -18.016 -72.360  1.00104.31           N  
ANISOU 2499  NE2 GLN A1267    11778  15183  12672    -35   1106   1703       N  
ATOM   2500  N   LEU A1268      -3.157 -23.529 -74.349  1.00 91.23           N  
ANISOU 2500  N   LEU A1268    10523  13752  10388    997   1628   1184       N  
ATOM   2501  CA  LEU A1268      -1.782 -23.967 -74.560  1.00 92.16           C  
ANISOU 2501  CA  LEU A1268    10459  14118  10441   1192   1790   1289       C  
ATOM   2502  C   LEU A1268      -1.601 -24.705 -75.879  1.00 94.70           C  
ANISOU 2502  C   LEU A1268    10885  14574  10522   1409   1970   1232       C  
ATOM   2503  O   LEU A1268      -0.485 -24.737 -76.408  1.00104.53           O  
ANISOU 2503  O   LEU A1268    11946  16092  11678   1546   2123   1365       O  
ATOM   2504  CB  LEU A1268      -1.330 -24.862 -73.406  1.00 81.11           C  
ANISOU 2504  CB  LEU A1268     9045  12646   9130   1342   1788   1228       C  
ATOM   2505  CG  LEU A1268      -1.276 -24.225 -72.017  1.00 84.52           C  
ANISOU 2505  CG  LEU A1268     9344  12993   9777   1160   1625   1291       C  
ATOM   2506  CD1 LEU A1268      -0.843 -25.248 -70.978  1.00100.84           C  
ANISOU 2506  CD1 LEU A1268    11415  15006  11892   1347   1637   1231       C  
ATOM   2507  CD2 LEU A1268      -0.342 -23.026 -72.014  1.00 74.95           C  
ANISOU 2507  CD2 LEU A1268     7824  12017   8637    992   1613   1524       C  
ATOM   2508  N   GLY A1269      -2.663 -25.295 -76.418  1.00 71.94           N  
ANISOU 2508  N   GLY A1269     8286  11523   7524   1439   1957   1036       N  
ATOM   2509  CA  GLY A1269      -2.569 -26.089 -77.622  1.00 79.81           C  
ANISOU 2509  CA  GLY A1269     9428  12619   8278   1645   2118    940       C  
ATOM   2510  C   GLY A1269      -2.611 -27.585 -77.410  1.00 85.39           C  
ANISOU 2510  C   GLY A1269    10364  13169   8912   1887   2198    731       C  
ATOM   2511  O   GLY A1269      -2.372 -28.332 -78.366  1.00 91.56           O  
ANISOU 2511  O   GLY A1269    11276  14032   9483   2093   2353    643       O  
ATOM   2512  N   ILE A1270      -2.898 -28.046 -76.191  1.00 79.68           N  
ANISOU 2512  N   ILE A1270     9709  12216   8347   1871   2102    651       N  
ATOM   2513  CA  ILE A1270      -2.995 -29.480 -75.943  1.00 84.30           C  
ANISOU 2513  CA  ILE A1270    10548  12610   8873   2089   2175    458       C  
ATOM   2514  C   ILE A1270      -4.202 -30.065 -76.663  1.00 89.44           C  
ANISOU 2514  C   ILE A1270    11532  13071   9378   2033   2150    226       C  
ATOM   2515  O   ILE A1270      -4.168 -31.216 -77.115  1.00 97.68           O  
ANISOU 2515  O   ILE A1270    12818  14024  10271   2236   2270     61       O  
ATOM   2516  CB  ILE A1270      -3.049 -29.755 -74.428  1.00 84.43           C  
ANISOU 2516  CB  ILE A1270    10551  12433   9094   2063   2071    452       C  
ATOM   2517  CG1 ILE A1270      -1.932 -28.998 -73.707  1.00 87.70           C  
ANISOU 2517  CG1 ILE A1270    10608  13063   9650   2058   2059    687       C  
ATOM   2518  CG2 ILE A1270      -2.941 -31.246 -74.149  1.00 69.34           C  
ANISOU 2518  CG2 ILE A1270     8889  10333   7125   2322   2171    296       C  
ATOM   2519  CD1 ILE A1270      -0.539 -29.410 -74.132  1.00105.35           C  
ANISOU 2519  CD1 ILE A1270    12678  15568  11782   2349   2255    800       C  
ATOM   2520  N   ILE A1271      -5.279 -29.292 -76.788  1.00 92.43           N  
ANISOU 2520  N   ILE A1271    11934  13393   9792   1763   1994    207       N  
ATOM   2521  CA  ILE A1271      -6.483 -29.716 -77.493  1.00100.21           C  
ANISOU 2521  CA  ILE A1271    13193  14249  10634   1669   1945      3       C  
ATOM   2522  C   ILE A1271      -6.967 -28.557 -78.354  1.00112.02           C  
ANISOU 2522  C   ILE A1271    14582  15917  12062   1489   1874     99       C  
ATOM   2523  O   ILE A1271      -7.072 -27.423 -77.876  1.00106.56           O  
ANISOU 2523  O   ILE A1271    13693  15267  11528   1318   1762    260       O  
ATOM   2524  CB  ILE A1271      -7.589 -30.176 -76.522  1.00 90.35           C  
ANISOU 2524  CB  ILE A1271    12122  12701   9509   1519   1797   -149       C  
ATOM   2525  CG1 ILE A1271      -7.703 -29.208 -75.342  1.00 98.65           C  
ANISOU 2525  CG1 ILE A1271    12957  13722  10805   1348   1650     -2       C  
ATOM   2526  CG2 ILE A1271      -7.320 -31.593 -76.037  1.00 84.49           C  
ANISOU 2526  CG2 ILE A1271    11600  11751   8752   1713   1890   -296       C  
ATOM   2527  CD1 ILE A1271      -8.689 -29.650 -74.282  1.00105.51           C  
ANISOU 2527  CD1 ILE A1271    13969  14323  11796   1219   1521   -128       C  
ATOM   2528  N   ARG A1272      -7.252 -28.841 -79.625  1.00126.79           N  
ANISOU 2528  N   ARG A1272    16598  17886  13692   1534   1942      2       N  
ATOM   2529  CA  ARG A1272      -7.706 -27.827 -80.569  1.00122.11           C  
ANISOU 2529  CA  ARG A1272    15925  17476  12996   1394   1889     98       C  
ATOM   2530  C   ARG A1272      -9.023 -28.199 -81.238  1.00127.88           C  
ANISOU 2530  C   ARG A1272    16895  18131  13562   1278   1797   -104       C  
ATOM   2531  O   ARG A1272      -9.418 -27.547 -82.211  1.00146.02           O  
ANISOU 2531  O   ARG A1272    19165  20603  15715   1203   1769    -49       O  
ATOM   2532  CB  ARG A1272      -6.634 -27.574 -81.633  1.00112.06           C  
ANISOU 2532  CB  ARG A1272    14529  16498  11552   1556   2067    236       C  
ATOM   2533  N   ASP A1273      -9.709 -29.226 -80.743  1.00111.97           N  
ANISOU 2533  N   ASP A1273    15109  15873  11560   1253   1748   -329       N  
ATOM   2534  CA  ASP A1273     -10.970 -29.646 -81.338  1.00101.16           C  
ANISOU 2534  CA  ASP A1273    13960  14444  10032   1115   1652   -532       C  
ATOM   2535  C   ASP A1273     -12.068 -28.640 -81.013  1.00 88.97           C  
ANISOU 2535  C   ASP A1273    12299  12907   8599    869   1451   -455       C  
ATOM   2536  O   ASP A1273     -12.215 -28.214 -79.864  1.00 99.70           O  
ANISOU 2536  O   ASP A1273    13542  14143  10197    782   1360   -374       O  
ATOM   2537  CB  ASP A1273     -11.351 -31.036 -80.827  1.00108.06           C  
ANISOU 2537  CB  ASP A1273    15115  15039  10904   1134   1661   -782       C  
ATOM   2538  CG  ASP A1273     -12.601 -31.585 -81.490  1.00129.13           C  
ANISOU 2538  CG  ASP A1273    18023  17656  13387    970   1568  -1011       C  
ATOM   2539  OD1 ASP A1273     -13.039 -31.018 -82.514  1.00143.88           O  
ANISOU 2539  OD1 ASP A1273    19852  19736  15079    896   1524   -991       O  
ATOM   2540  OD2 ASP A1273     -13.147 -32.587 -80.983  1.00131.49           O  
ANISOU 2540  OD2 ASP A1273    18546  17706  13708    907   1537  -1206       O  
ATOM   2541  N   CYS A1274     -12.838 -28.256 -82.033  1.00 81.36           N  
ANISOU 2541  N   CYS A1274    11366  12099   7449    771   1385   -478       N  
ATOM   2542  CA  CYS A1274     -13.973 -27.367 -81.828  1.00 81.10           C  
ANISOU 2542  CA  CYS A1274    11236  12089   7489    567   1197   -414       C  
ATOM   2543  C   CYS A1274     -15.172 -28.070 -81.207  1.00 75.48           C  
ANISOU 2543  C   CYS A1274    10673  11189   6819    408   1066   -618       C  
ATOM   2544  O   CYS A1274     -16.142 -27.397 -80.842  1.00 80.88           O  
ANISOU 2544  O   CYS A1274    11262  11880   7587    251    911   -569       O  
ATOM   2545  CB  CYS A1274     -14.395 -26.720 -83.151  1.00115.65           C  
ANISOU 2545  CB  CYS A1274    15583  16722  11635    534   1167   -352       C  
ATOM   2546  SG  CYS A1274     -13.333 -25.367 -83.715  1.00132.63           S  
ANISOU 2546  SG  CYS A1274    17492  19108  13795    629   1261    -24       S  
ATOM   2547  N   ARG A1275     -15.134 -29.398 -81.083  1.00 73.89           N  
ANISOU 2547  N   ARG A1275    10702  10817   6555    445   1129   -837       N  
ATOM   2548  CA  ARG A1275     -16.218 -30.114 -80.421  1.00 81.63           C  
ANISOU 2548  CA  ARG A1275    11826  11604   7587    271   1015  -1019       C  
ATOM   2549  C   ARG A1275     -16.086 -30.032 -78.905  1.00 84.84           C  
ANISOU 2549  C   ARG A1275    12143  11810   8282    253    982   -946       C  
ATOM   2550  O   ARG A1275     -17.069 -29.774 -78.202  1.00 82.54           O  
ANISOU 2550  O   ARG A1275    11800  11459   8104     80    841   -954       O  
ATOM   2551  CB  ARG A1275     -16.244 -31.573 -80.881  1.00 79.58           C  
ANISOU 2551  CB  ARG A1275    11883  11208   7147    300   1097  -1283       C  
ATOM   2552  N   ILE A1276     -14.875 -30.249 -78.384  1.00 89.51           N  
ANISOU 2552  N   ILE A1276    12706  12320   8983    437   1111   -871       N  
ATOM   2553  CA  ILE A1276     -14.652 -30.114 -76.950  1.00 97.88           C  
ANISOU 2553  CA  ILE A1276    13667  13221  10302    432   1079   -786       C  
ATOM   2554  C   ILE A1276     -14.656 -28.653 -76.522  1.00 96.95           C  
ANISOU 2554  C   ILE A1276    13274  13221  10342    368    988   -566       C  
ATOM   2555  O   ILE A1276     -14.920 -28.354 -75.353  1.00104.24           O  
ANISOU 2555  O   ILE A1276    14115  14030  11461    293    906   -517       O  
ATOM   2556  CB  ILE A1276     -13.340 -30.809 -76.536  1.00106.57           C  
ANISOU 2556  CB  ILE A1276    14811  14227  11456    660   1239   -767       C  
ATOM   2557  CG1 ILE A1276     -12.165 -30.313 -77.382  1.00111.51           C  
ANISOU 2557  CG1 ILE A1276    15302  15076  11992    843   1370   -625       C  
ATOM   2558  CG2 ILE A1276     -13.481 -32.320 -76.649  1.00112.70           C  
ANISOU 2558  CG2 ILE A1276    15904  14798  12119    715   1316   -996       C  
ATOM   2559  CD1 ILE A1276     -11.366 -29.191 -76.747  1.00112.10           C  
ANISOU 2559  CD1 ILE A1276    15082  15256  12253    868   1360   -377       C  
ATOM   2560  N   ALA A1277     -14.361 -27.730 -77.440  1.00 90.08           N  
ANISOU 2560  N   ALA A1277    12274  12568   9385    396   1005   -429       N  
ATOM   2561  CA  ALA A1277     -14.488 -26.313 -77.126  1.00 80.82           C  
ANISOU 2561  CA  ALA A1277    10881  11479   8349    318    912   -227       C  
ATOM   2562  C   ALA A1277     -15.944 -25.889 -76.998  1.00 83.75           C  
ANISOU 2562  C   ALA A1277    11250  11843   8727    142    745   -270       C  
ATOM   2563  O   ALA A1277     -16.231 -24.892 -76.326  1.00 86.79           O  
ANISOU 2563  O   ALA A1277    11492  12211   9271     76    654   -142       O  
ATOM   2564  CB  ALA A1277     -13.789 -25.469 -78.192  1.00 70.06           C  
ANISOU 2564  CB  ALA A1277     9399  10340   6879    391    985    -56       C  
ATOM   2565  N   ASP A1278     -16.865 -26.625 -77.623  1.00 84.18           N  
ANISOU 2565  N   ASP A1278    11459  11919   8606     66    705   -448       N  
ATOM   2566  CA  ASP A1278     -18.282 -26.305 -77.499  1.00 86.30           C  
ANISOU 2566  CA  ASP A1278    11703  12217   8868   -101    545   -490       C  
ATOM   2567  C   ASP A1278     -18.816 -26.710 -76.131  1.00 94.50           C  
ANISOU 2567  C   ASP A1278    12761  13058  10089   -193    479   -564       C  
ATOM   2568  O   ASP A1278     -19.522 -25.935 -75.475  1.00 88.59           O  
ANISOU 2568  O   ASP A1278    11886  12312   9461   -272    369   -488       O  
ATOM   2569  CB  ASP A1278     -19.071 -26.990 -78.616  1.00 82.42           C  
ANISOU 2569  CB  ASP A1278    11358  11842   8117   -176    515   -660       C  
ATOM   2570  CG  ASP A1278     -20.564 -26.756 -78.503  1.00 87.50           C  
ANISOU 2570  CG  ASP A1278    11955  12555   8736   -354    347   -708       C  
ATOM   2571  OD1 ASP A1278     -20.997 -25.592 -78.638  1.00 89.38           O  
ANISOU 2571  OD1 ASP A1278    12026  12934   9002   -360    263   -548       O  
ATOM   2572  OD2 ASP A1278     -21.306 -27.736 -78.281  1.00 92.11           O  
ANISOU 2572  OD2 ASP A1278    12671  13055   9271   -487    302   -899       O  
ATOM   2573  N   ILE A1279     -18.485 -27.923 -75.679  1.00105.17           N  
ANISOU 2573  N   ILE A1279    14275  14230  11453   -171    552   -708       N  
ATOM   2574  CA  ILE A1279     -18.946 -28.377 -74.373  1.00110.94           C  
ANISOU 2574  CA  ILE A1279    15036  14771  12344   -257    502   -767       C  
ATOM   2575  C   ILE A1279     -18.308 -27.571 -73.247  1.00 98.46           C  
ANISOU 2575  C   ILE A1279    13290  13129  10992   -190    500   -600       C  
ATOM   2576  O   ILE A1279     -18.875 -27.484 -72.152  1.00104.07           O  
ANISOU 2576  O   ILE A1279    13960  13743  11840   -273    425   -602       O  
ATOM   2577  CB  ILE A1279     -18.683 -29.887 -74.204  1.00114.73           C  
ANISOU 2577  CB  ILE A1279    15760  15056  12776   -236    592   -946       C  
ATOM   2578  CG1 ILE A1279     -19.422 -30.434 -72.980  1.00123.04           C  
ANISOU 2578  CG1 ILE A1279    16867  15927  13956   -369    528  -1018       C  
ATOM   2579  CG2 ILE A1279     -17.194 -30.172 -74.097  1.00109.38           C  
ANISOU 2579  CG2 ILE A1279    15106  14312  12142    -15    744   -883       C  
ATOM   2580  CD1 ILE A1279     -20.921 -30.235 -73.032  1.00126.32           C  
ANISOU 2580  CD1 ILE A1279    17240  16432  14323   -590    384  -1079       C  
ATOM   2581  N   VAL A1280     -17.146 -26.963 -73.491  1.00 84.96           N  
ANISOU 2581  N   VAL A1280    11477  11487   9316    -52    579   -455       N  
ATOM   2582  CA  VAL A1280     -16.553 -26.072 -72.500  1.00 73.10           C  
ANISOU 2582  CA  VAL A1280     9808   9951   8017    -20    560   -296       C  
ATOM   2583  C   VAL A1280     -17.244 -24.714 -72.516  1.00 85.58           C  
ANISOU 2583  C   VAL A1280    11244  11623   9650   -105    445   -177       C  
ATOM   2584  O   VAL A1280     -17.537 -24.142 -71.460  1.00 87.01           O  
ANISOU 2584  O   VAL A1280    11344  11726   9990   -154    370   -127       O  
ATOM   2585  CB  VAL A1280     -15.037 -25.945 -72.739  1.00 61.24           C  
ANISOU 2585  CB  VAL A1280     8236   8504   6529    135    685   -180       C  
ATOM   2586  CG1 VAL A1280     -14.461 -24.797 -71.924  1.00 63.84           C  
ANISOU 2586  CG1 VAL A1280     8374   8840   7044    125    646     -1       C  
ATOM   2587  CG2 VAL A1280     -14.336 -27.248 -72.388  1.00 71.61           C  
ANISOU 2587  CG2 VAL A1280     9681   9697   7832    254    794   -280       C  
ATOM   2588  N   ASP A1281     -17.525 -24.182 -73.708  1.00 83.15           N  
ANISOU 2588  N   ASP A1281    10912  11480   9201   -109    434   -128       N  
ATOM   2589  CA  ASP A1281     -18.197 -22.892 -73.810  1.00 78.94           C  
ANISOU 2589  CA  ASP A1281    10260  11029   8704   -160    332     -2       C  
ATOM   2590  C   ASP A1281     -19.659 -22.959 -73.386  1.00 76.62           C  
ANISOU 2590  C   ASP A1281     9977  10724   8412   -269    208    -95       C  
ATOM   2591  O   ASP A1281     -20.235 -21.923 -73.038  1.00 66.45           O  
ANISOU 2591  O   ASP A1281     8588   9453   7205   -289    123      4       O  
ATOM   2592  CB  ASP A1281     -18.090 -22.354 -75.238  1.00 75.08           C  
ANISOU 2592  CB  ASP A1281     9750  10732   8045   -121    359     90       C  
ATOM   2593  CG  ASP A1281     -16.749 -21.701 -75.517  1.00 90.93           C  
ANISOU 2593  CG  ASP A1281    11673  12780  10096    -36    458    264       C  
ATOM   2594  OD1 ASP A1281     -16.266 -20.941 -74.652  1.00101.02           O  
ANISOU 2594  OD1 ASP A1281    12854  13968  11561    -46    442    381       O  
ATOM   2595  OD2 ASP A1281     -16.176 -21.949 -76.598  1.00101.82           O  
ANISOU 2595  OD2 ASP A1281    13080  14292  11314     32    552    283       O  
ATOM   2596  N   THR A1282     -20.271 -24.142 -73.408  1.00 81.81           N  
ANISOU 2596  N   THR A1282    10755  11352   8978   -339    201   -277       N  
ATOM   2597  CA  THR A1282     -21.647 -24.284 -72.946  1.00 89.75           C  
ANISOU 2597  CA  THR A1282    11749  12369   9985   -463     89   -362       C  
ATOM   2598  C   THR A1282     -21.730 -24.501 -71.441  1.00 79.02           C  
ANISOU 2598  C   THR A1282    10379  10834   8810   -496     73   -389       C  
ATOM   2599  O   THR A1282     -22.665 -24.014 -70.796  1.00 70.35           O  
ANISOU 2599  O   THR A1282     9196   9755   7778   -555    -18   -372       O  
ATOM   2600  CB  THR A1282     -22.341 -25.445 -73.665  1.00 95.05           C  
ANISOU 2600  CB  THR A1282    12556  13095  10464   -568     78   -547       C  
ATOM   2601  OG1 THR A1282     -21.541 -26.628 -73.558  1.00106.95           O  
ANISOU 2601  OG1 THR A1282    14232  14447  11958   -538    187   -663       O  
ATOM   2602  CG2 THR A1282     -22.564 -25.113 -75.128  1.00 99.84           C  
ANISOU 2602  CG2 THR A1282    13152  13921  10861   -554     59   -524       C  
ATOM   2603  N   ALA A1283     -20.769 -25.226 -70.868  1.00 72.04           N  
ANISOU 2603  N   ALA A1283     9577   9795   8000   -445    163   -424       N  
ATOM   2604  CA  ALA A1283     -20.784 -25.516 -69.441  1.00 68.00           C  
ANISOU 2604  CA  ALA A1283     9067   9125   7645   -468    152   -446       C  
ATOM   2605  C   ALA A1283     -20.240 -24.375 -68.592  1.00 56.33           C  
ANISOU 2605  C   ALA A1283     7453   7614   6337   -405    131   -299       C  
ATOM   2606  O   ALA A1283     -20.447 -24.381 -67.374  1.00 70.83           O  
ANISOU 2606  O   ALA A1283     9268   9352   8293   -432     98   -307       O  
ATOM   2607  CB  ALA A1283     -19.987 -26.790 -69.155  1.00 65.45           C  
ANISOU 2607  CB  ALA A1283     8897   8651   7321   -422    255   -534       C  
ATOM   2608  N   MET A1284     -19.555 -23.399 -69.198  1.00 59.73           N  
ANISOU 2608  N   MET A1284     7800   8121   6774   -333    148   -165       N  
ATOM   2609  CA  MET A1284     -19.011 -22.296 -68.407  1.00 75.44           C  
ANISOU 2609  CA  MET A1284     9680  10061   8923   -301    124    -34       C  
ATOM   2610  C   MET A1284     -20.107 -21.427 -67.802  1.00 76.61           C  
ANISOU 2610  C   MET A1284     9766  10207   9137   -349     17    -12       C  
ATOM   2611  O   MET A1284     -20.007 -21.091 -66.608  1.00 69.88           O  
ANISOU 2611  O   MET A1284     8880   9252   8418   -354    -12      2       O  
ATOM   2612  CB  MET A1284     -18.031 -21.478 -69.253  1.00 92.78           C  
ANISOU 2612  CB  MET A1284    11812  12336  11104   -240    173    111       C  
ATOM   2613  CG  MET A1284     -17.106 -20.588 -68.437  1.00100.42           C  
ANISOU 2613  CG  MET A1284    12688  13233  12233   -227    170    234       C  
ATOM   2614  SD  MET A1284     -15.968 -21.536 -67.407  1.00 91.43           S  
ANISOU 2614  SD  MET A1284    11555  12005  11179   -183    237    192       S  
ATOM   2615  CE  MET A1284     -15.043 -22.425 -68.657  1.00 87.90           C  
ANISOU 2615  CE  MET A1284    11149  11663  10584    -84    373    187       C  
ATOM   2616  N   PRO A1285     -21.156 -21.022 -68.531  1.00 74.23           N  
ANISOU 2616  N   PRO A1285     9441  10024   8740   -373    -43     -7       N  
ATOM   2617  CA  PRO A1285     -22.244 -20.288 -67.863  1.00 83.06           C  
ANISOU 2617  CA  PRO A1285    10494  11148   9916   -389   -134      8       C  
ATOM   2618  C   PRO A1285     -22.976 -21.115 -66.821  1.00 80.18           C  
ANISOU 2618  C   PRO A1285    10151  10732   9582   -459   -159   -117       C  
ATOM   2619  O   PRO A1285     -23.532 -20.549 -65.873  1.00 77.30           O  
ANISOU 2619  O   PRO A1285     9733  10333   9305   -452   -209   -103       O  
ATOM   2620  CB  PRO A1285     -23.170 -19.895 -69.024  1.00 85.12           C  
ANISOU 2620  CB  PRO A1285    10719  11588  10033   -384   -185     40       C  
ATOM   2621  CG  PRO A1285     -22.302 -19.921 -70.226  1.00 80.96           C  
ANISOU 2621  CG  PRO A1285    10226  11124   9412   -349   -120     97       C  
ATOM   2622  CD  PRO A1285     -21.349 -21.049 -69.992  1.00 73.16           C  
ANISOU 2622  CD  PRO A1285     9320  10043   8435   -363    -32      8       C  
ATOM   2623  N   ILE A1286     -22.993 -22.441 -66.969  1.00 83.83           N  
ANISOU 2623  N   ILE A1286    10702  11180   9968   -524   -118   -237       N  
ATOM   2624  CA  ILE A1286     -23.654 -23.291 -65.983  1.00 83.56           C  
ANISOU 2624  CA  ILE A1286    10702  11085   9961   -610   -132   -342       C  
ATOM   2625  C   ILE A1286     -22.868 -23.309 -64.679  1.00 82.56           C  
ANISOU 2625  C   ILE A1286    10587  10800   9982   -568   -100   -320       C  
ATOM   2626  O   ILE A1286     -23.443 -23.199 -63.589  1.00 81.35           O  
ANISOU 2626  O   ILE A1286    10399  10614   9896   -596   -137   -336       O  
ATOM   2627  CB  ILE A1286     -23.848 -24.710 -66.548  1.00 83.47           C  
ANISOU 2627  CB  ILE A1286    10818  11071   9826   -704    -93   -475       C  
ATOM   2628  CG1 ILE A1286     -24.781 -24.682 -67.760  1.00 83.64           C  
ANISOU 2628  CG1 ILE A1286    10815  11280   9683   -773   -147   -511       C  
ATOM   2629  CG2 ILE A1286     -24.387 -25.645 -65.476  1.00 84.28           C  
ANISOU 2629  CG2 ILE A1286    10978  11077   9967   -805    -92   -566       C  
ATOM   2630  CD1 ILE A1286     -26.187 -24.229 -67.436  1.00 89.48           C  
ANISOU 2630  CD1 ILE A1286    11430  12159  10409   -843   -244   -508       C  
ATOM   2631  N   THR A1287     -21.542 -23.443 -64.766  1.00 80.90           N  
ANISOU 2631  N   THR A1287    10414  10513   9811   -496    -32   -278       N  
ATOM   2632  CA  THR A1287     -20.724 -23.521 -63.560  1.00 75.29           C  
ANISOU 2632  CA  THR A1287     9703   9681   9222   -456     -9   -253       C  
ATOM   2633  C   THR A1287     -20.682 -22.193 -62.815  1.00 71.57           C  
ANISOU 2633  C   THR A1287     9132   9198   8862   -429    -71   -167       C  
ATOM   2634  O   THR A1287     -20.575 -22.181 -61.583  1.00 86.59           O  
ANISOU 2634  O   THR A1287    11027  11025  10849   -430    -88   -176       O  
ATOM   2635  CB  THR A1287     -19.307 -23.971 -63.915  1.00 71.84           C  
ANISOU 2635  CB  THR A1287     9303   9207   8785   -374     77   -219       C  
ATOM   2636  OG1 THR A1287     -18.733 -23.056 -64.857  1.00 77.69           O  
ANISOU 2636  OG1 THR A1287     9974  10034   9511   -330     86   -119       O  
ATOM   2637  CG2 THR A1287     -19.326 -25.368 -64.517  1.00 66.27           C  
ANISOU 2637  CG2 THR A1287     8739   8473   7970   -380    149   -323       C  
ATOM   2638  N   ILE A1288     -20.758 -21.072 -63.535  1.00 66.42           N  
ANISOU 2638  N   ILE A1288     8419   8611   8205   -405   -102    -84       N  
ATOM   2639  CA  ILE A1288     -20.770 -19.770 -62.876  1.00 66.56           C  
ANISOU 2639  CA  ILE A1288     8379   8587   8326   -381   -158    -11       C  
ATOM   2640  C   ILE A1288     -22.056 -19.589 -62.078  1.00 68.61           C  
ANISOU 2640  C   ILE A1288     8620   8854   8593   -396   -217    -68       C  
ATOM   2641  O   ILE A1288     -22.048 -19.019 -60.980  1.00 72.15           O  
ANISOU 2641  O   ILE A1288     9056   9229   9129   -380   -249    -64       O  
ATOM   2642  CB  ILE A1288     -20.573 -18.647 -63.912  1.00 69.16           C  
ANISOU 2642  CB  ILE A1288     8673   8963   8640   -348   -169    104       C  
ATOM   2643  CG1 ILE A1288     -19.186 -18.752 -64.549  1.00 75.56           C  
ANISOU 2643  CG1 ILE A1288     9480   9780   9451   -337   -100    177       C  
ATOM   2644  CG2 ILE A1288     -20.761 -17.279 -63.273  1.00 57.89           C  
ANISOU 2644  CG2 ILE A1288     7224   7460   7311   -324   -228    169       C  
ATOM   2645  CD1 ILE A1288     -18.923 -17.712 -65.615  1.00 84.19           C  
ANISOU 2645  CD1 ILE A1288    10545  10924  10519   -318    -97    307       C  
ATOM   2646  N   CYS A1289     -23.177 -20.084 -62.606  1.00 71.91           N  
ANISOU 2646  N   CYS A1289     9031   9380   8910   -431   -233   -124       N  
ATOM   2647  CA  CYS A1289     -24.445 -20.018 -61.889  1.00 78.86           C  
ANISOU 2647  CA  CYS A1289     9869  10312   9783   -448   -279   -173       C  
ATOM   2648  C   CYS A1289     -24.472 -20.905 -60.652  1.00 83.08           C  
ANISOU 2648  C   CYS A1289    10438  10775  10355   -500   -258   -250       C  
ATOM   2649  O   CYS A1289     -25.403 -20.786 -59.849  1.00 97.85           O  
ANISOU 2649  O   CYS A1289    12263  12685  12229   -509   -286   -281       O  
ATOM   2650  CB  CYS A1289     -25.598 -20.402 -62.819  1.00 81.01           C  
ANISOU 2650  CB  CYS A1289    10103  10754   9924   -497   -305   -208       C  
ATOM   2651  SG  CYS A1289     -25.893 -19.235 -64.165  1.00 91.78           S  
ANISOU 2651  SG  CYS A1289    11408  12243  11222   -412   -346    -99       S  
ATOM   2652  N   ILE A1290     -23.491 -21.784 -60.483  1.00 77.51           N  
ANISOU 2652  N   ILE A1290     9807   9977   9668   -522   -204   -273       N  
ATOM   2653  CA  ILE A1290     -23.400 -22.648 -59.311  1.00 68.97           C  
ANISOU 2653  CA  ILE A1290     8773   8816   8618   -557   -179   -324       C  
ATOM   2654  C   ILE A1290     -22.414 -22.098 -58.291  1.00 76.59           C  
ANISOU 2654  C   ILE A1290     9729   9687   9686   -494   -184   -278       C  
ATOM   2655  O   ILE A1290     -22.712 -22.035 -57.098  1.00 99.46           O  
ANISOU 2655  O   ILE A1290    12617  12557  12617   -495   -203   -298       O  
ATOM   2656  CB  ILE A1290     -23.023 -24.085 -59.737  1.00 62.41           C  
ANISOU 2656  CB  ILE A1290     8050   7935   7728   -606   -113   -380       C  
ATOM   2657  CG1 ILE A1290     -24.193 -24.750 -60.465  1.00 54.72           C  
ANISOU 2657  CG1 ILE A1290     7098   7050   6643   -717   -121   -455       C  
ATOM   2658  CG2 ILE A1290     -22.590 -24.908 -58.532  1.00 58.02           C  
ANISOU 2658  CG2 ILE A1290     7561   7267   7217   -608    -76   -398       C  
ATOM   2659  CD1 ILE A1290     -23.912 -26.170 -60.902  1.00 55.74           C  
ANISOU 2659  CD1 ILE A1290     7374   7100   6706   -779    -56   -529       C  
ATOM   2660  N   ALA A1291     -21.230 -21.685 -58.748  1.00 75.11           N  
ANISOU 2660  N   ALA A1291     9535   9466   9537   -446   -169   -213       N  
ATOM   2661  CA  ALA A1291     -20.210 -21.189 -57.830  1.00 71.67           C  
ANISOU 2661  CA  ALA A1291     9078   8964   9190   -412   -184   -169       C  
ATOM   2662  C   ALA A1291     -20.617 -19.854 -57.219  1.00 69.07           C  
ANISOU 2662  C   ALA A1291     8708   8618   8917   -401   -252   -153       C  
ATOM   2663  O   ALA A1291     -20.542 -19.670 -55.999  1.00 89.16           O  
ANISOU 2663  O   ALA A1291    11255  11119  11501   -398   -280   -176       O  
ATOM   2664  CB  ALA A1291     -18.870 -21.064 -58.555  1.00 64.74           C  
ANISOU 2664  CB  ALA A1291     8178   8087   8331   -382   -149    -94       C  
ATOM   2665  N   TYR A1292     -21.057 -18.911 -58.052  1.00 64.65           N  
ANISOU 2665  N   TYR A1292     8125   8087   8350   -384   -277   -113       N  
ATOM   2666  CA  TYR A1292     -21.372 -17.571 -57.577  1.00 58.64           C  
ANISOU 2666  CA  TYR A1292     7358   7279   7644   -351   -332    -92       C  
ATOM   2667  C   TYR A1292     -22.747 -17.469 -56.932  1.00 67.87           C  
ANISOU 2667  C   TYR A1292     8518   8489   8781   -319   -356   -155       C  
ATOM   2668  O   TYR A1292     -23.020 -16.471 -56.257  1.00 71.97           O  
ANISOU 2668  O   TYR A1292     9052   8954   9341   -270   -393   -159       O  
ATOM   2669  CB  TYR A1292     -21.253 -16.570 -58.729  1.00 63.92           C  
ANISOU 2669  CB  TYR A1292     8020   7948   8318   -328   -342     -2       C  
ATOM   2670  CG  TYR A1292     -19.822 -16.337 -59.160  1.00 71.21           C  
ANISOU 2670  CG  TYR A1292     8937   8832   9289   -365   -321     78       C  
ATOM   2671  CD1 TYR A1292     -19.194 -17.202 -60.047  1.00 63.64           C  
ANISOU 2671  CD1 TYR A1292     7959   7944   8279   -378   -262    103       C  
ATOM   2672  CD2 TYR A1292     -19.094 -15.262 -58.667  1.00 74.25           C  
ANISOU 2672  CD2 TYR A1292     9335   9115   9760   -393   -358    126       C  
ATOM   2673  CE1 TYR A1292     -17.885 -16.997 -60.438  1.00 66.67           C  
ANISOU 2673  CE1 TYR A1292     8310   8326   8697   -402   -233    187       C  
ATOM   2674  CE2 TYR A1292     -17.784 -15.049 -59.053  1.00 74.50           C  
ANISOU 2674  CE2 TYR A1292     9335   9141   9832   -450   -340    210       C  
ATOM   2675  CZ  TYR A1292     -17.185 -15.920 -59.938  1.00 73.72           C  
ANISOU 2675  CZ  TYR A1292     9190   9141   9680   -447   -274    247       C  
ATOM   2676  OH  TYR A1292     -15.881 -15.713 -60.325  1.00 80.67           O  
ANISOU 2676  OH  TYR A1292    10013  10047  10590   -493   -245    341       O  
ATOM   2677  N   PHE A1293     -23.617 -18.464 -57.118  1.00 64.69           N  
ANISOU 2677  N   PHE A1293     8095   8183   8301   -349   -333   -204       N  
ATOM   2678  CA  PHE A1293     -24.861 -18.490 -56.357  1.00 74.91           C  
ANISOU 2678  CA  PHE A1293     9355   9546   9561   -332   -346   -258       C  
ATOM   2679  C   PHE A1293     -24.626 -19.000 -54.941  1.00 83.06           C  
ANISOU 2679  C   PHE A1293    10415  10527  10615   -355   -335   -308       C  
ATOM   2680  O   PHE A1293     -25.191 -18.463 -53.982  1.00 96.90           O  
ANISOU 2680  O   PHE A1293    12157  12288  12374   -306   -353   -337       O  
ATOM   2681  CB  PHE A1293     -25.904 -19.352 -57.069  1.00 72.04           C  
ANISOU 2681  CB  PHE A1293     8947   9325   9100   -390   -332   -287       C  
ATOM   2682  CG  PHE A1293     -27.180 -19.523 -56.294  1.00 77.02           C  
ANISOU 2682  CG  PHE A1293     9514  10063   9686   -396   -336   -332       C  
ATOM   2683  CD1 PHE A1293     -28.091 -18.484 -56.195  1.00 85.06           C  
ANISOU 2683  CD1 PHE A1293    10462  11163  10692   -292   -367   -312       C  
ATOM   2684  CD2 PHE A1293     -27.472 -20.725 -55.669  1.00 74.09           C  
ANISOU 2684  CD2 PHE A1293     9156   9715   9280   -497   -302   -385       C  
ATOM   2685  CE1 PHE A1293     -29.267 -18.638 -55.483  1.00 84.82           C  
ANISOU 2685  CE1 PHE A1293    10351  11266  10611   -284   -362   -346       C  
ATOM   2686  CE2 PHE A1293     -28.646 -20.885 -54.956  1.00 79.09           C  
ANISOU 2686  CE2 PHE A1293     9715  10470   9865   -517   -299   -413       C  
ATOM   2687  CZ  PHE A1293     -29.544 -19.840 -54.864  1.00 81.21           C  
ANISOU 2687  CZ  PHE A1293     9889  10850  10117   -408   -327   -395       C  
ATOM   2688  N   ASN A1294     -23.793 -20.033 -54.794  1.00 68.14           N  
ANISOU 2688  N   ASN A1294     8569   8591   8731   -411   -300   -314       N  
ATOM   2689  CA  ASN A1294     -23.451 -20.523 -53.464  1.00 66.77           C  
ANISOU 2689  CA  ASN A1294     8426   8373   8571   -420   -292   -341       C  
ATOM   2690  C   ASN A1294     -22.538 -19.552 -52.729  1.00 78.57           C  
ANISOU 2690  C   ASN A1294     9931   9790  10133   -377   -335   -324       C  
ATOM   2691  O   ASN A1294     -22.582 -19.475 -51.496  1.00 83.67           O  
ANISOU 2691  O   ASN A1294    10590  10425  10776   -363   -351   -357       O  
ATOM   2692  CB  ASN A1294     -22.792 -21.898 -53.565  1.00 61.18           C  
ANISOU 2692  CB  ASN A1294     7772   7629   7844   -467   -240   -338       C  
ATOM   2693  CG  ASN A1294     -23.732 -22.957 -54.104  1.00 71.45           C  
ANISOU 2693  CG  ASN A1294     9095   8982   9073   -544   -199   -375       C  
ATOM   2694  OD1 ASN A1294     -24.949 -22.858 -53.952  1.00 77.60           O  
ANISOU 2694  OD1 ASN A1294     9827   9849   9809   -578   -210   -405       O  
ATOM   2695  ND2 ASN A1294     -23.171 -23.980 -54.737  1.00 86.21           N  
ANISOU 2695  ND2 ASN A1294    11036  10800  10920   -573   -151   -376       N  
ATOM   2696  N   ASN A1295     -21.708 -18.806 -53.462  1.00 67.27           N  
ANISOU 2696  N   ASN A1295     8495   8312   8752   -368   -356   -273       N  
ATOM   2697  CA  ASN A1295     -20.819 -17.845 -52.819  1.00 61.40           C  
ANISOU 2697  CA  ASN A1295     7763   7494   8072   -364   -405   -259       C  
ATOM   2698  C   ASN A1295     -21.585 -16.643 -52.284  1.00 60.69           C  
ANISOU 2698  C   ASN A1295     7702   7366   7993   -316   -448   -298       C  
ATOM   2699  O   ASN A1295     -21.225 -16.100 -51.233  1.00 79.57           O  
ANISOU 2699  O   ASN A1295    10127   9700  10404   -317   -489   -335       O  
ATOM   2700  CB  ASN A1295     -19.734 -17.396 -53.797  1.00 63.77           C  
ANISOU 2700  CB  ASN A1295     8045   7763   8421   -391   -408   -180       C  
ATOM   2701  CG  ASN A1295     -18.681 -16.527 -53.140  1.00 88.27           C  
ANISOU 2701  CG  ASN A1295    11152  10800  11588   -431   -463   -162       C  
ATOM   2702  OD1 ASN A1295     -17.747 -17.030 -52.516  1.00 94.02           O  
ANISOU 2702  OD1 ASN A1295    11851  11550  12321   -459   -470   -154       O  
ATOM   2703  ND2 ASN A1295     -18.826 -15.214 -53.278  1.00107.49           N  
ANISOU 2703  ND2 ASN A1295    13625  13152  14064   -437   -505   -151       N  
ATOM   2704  N   CYS A1296     -22.638 -16.215 -52.983  1.00 71.70           N  
ANISOU 2704  N   CYS A1296     9084   8794   9363   -264   -440   -292       N  
ATOM   2705  CA  CYS A1296     -23.460 -15.111 -52.502  1.00 88.13           C  
ANISOU 2705  CA  CYS A1296    11198  10844  11445   -178   -467   -326       C  
ATOM   2706  C   CYS A1296     -24.320 -15.496 -51.306  1.00 81.64           C  
ANISOU 2706  C   CYS A1296    10365  10091  10565   -140   -453   -404       C  
ATOM   2707  O   CYS A1296     -24.851 -14.604 -50.636  1.00 87.74           O  
ANISOU 2707  O   CYS A1296    11176  10830  11330    -53   -470   -448       O  
ATOM   2708  CB  CYS A1296     -24.348 -14.583 -53.631  1.00 98.13           C  
ANISOU 2708  CB  CYS A1296    12438  12157  12691   -107   -460   -278       C  
ATOM   2709  SG  CYS A1296     -23.460 -13.644 -54.895  1.00107.54           S  
ANISOU 2709  SG  CYS A1296    13669  13244  13946   -123   -478   -172       S  
ATOM   2710  N   LEU A1297     -24.474 -16.788 -51.028  1.00 70.53           N  
ANISOU 2710  N   LEU A1297     8917   8771   9111   -197   -417   -418       N  
ATOM   2711  CA  LEU A1297     -25.169 -17.258 -49.839  1.00 66.48           C  
ANISOU 2711  CA  LEU A1297     8392   8330   8537   -183   -395   -474       C  
ATOM   2712  C   LEU A1297     -24.216 -17.609 -48.705  1.00 66.08           C  
ANISOU 2712  C   LEU A1297     8389   8226   8491   -221   -410   -497       C  
ATOM   2713  O   LEU A1297     -24.672 -18.023 -47.634  1.00 68.82           O  
ANISOU 2713  O   LEU A1297     8736   8633   8779   -210   -390   -534       O  
ATOM   2714  CB  LEU A1297     -26.038 -18.474 -50.179  1.00 58.87           C  
ANISOU 2714  CB  LEU A1297     7364   7495   7509   -241   -344   -467       C  
ATOM   2715  CG  LEU A1297     -27.212 -18.220 -51.126  1.00 71.89           C  
ANISOU 2715  CG  LEU A1297     8934   9259   9121   -210   -337   -452       C  
ATOM   2716  CD1 LEU A1297     -27.943 -19.517 -51.440  1.00 63.97           C  
ANISOU 2716  CD1 LEU A1297     7875   8380   8052   -319   -297   -453       C  
ATOM   2717  CD2 LEU A1297     -28.163 -17.196 -50.527  1.00 70.18           C  
ANISOU 2717  CD2 LEU A1297     8686   9102   8877    -80   -343   -479       C  
ATOM   2718  N   ASN A1298     -22.903 -17.454 -48.915  1.00 61.22           N  
ANISOU 2718  N   ASN A1298     7801   7523   7935   -263   -444   -465       N  
ATOM   2719  CA  ASN A1298     -21.947 -17.783 -47.858  1.00 67.43           C  
ANISOU 2719  CA  ASN A1298     8612   8292   8716   -294   -469   -475       C  
ATOM   2720  C   ASN A1298     -22.018 -16.815 -46.683  1.00 80.11           C  
ANISOU 2720  C   ASN A1298    10271   9866  10301   -257   -518   -548       C  
ATOM   2721  O   ASN A1298     -22.028 -17.283 -45.531  1.00 73.13           O  
ANISOU 2721  O   ASN A1298     9399   9034   9354   -253   -518   -581       O  
ATOM   2722  CB  ASN A1298     -20.534 -17.868 -48.443  1.00 57.52           C  
ANISOU 2722  CB  ASN A1298     7341   6991   7522   -348   -492   -412       C  
ATOM   2723  CG  ASN A1298     -20.052 -19.295 -48.596  1.00 69.88           C  
ANISOU 2723  CG  ASN A1298     8885   8600   9066   -366   -442   -363       C  
ATOM   2724  OD1 ASN A1298     -20.803 -20.243 -48.367  1.00 75.39           O  
ANISOU 2724  OD1 ASN A1298     9596   9339   9711   -361   -391   -374       O  
ATOM   2725  ND2 ASN A1298     -18.795 -19.456 -48.986  1.00 85.88           N  
ANISOU 2725  ND2 ASN A1298    10882  10617  11131   -387   -452   -303       N  
ATOM   2726  N   PRO A1299     -22.054 -15.489 -46.874  1.00 80.43           N  
ANISOU 2726  N   PRO A1299    10361   9815  10382   -228   -560   -579       N  
ATOM   2727  CA  PRO A1299     -22.192 -14.606 -45.703  1.00 75.94           C  
ANISOU 2727  CA  PRO A1299     9874   9203   9778   -186   -601   -672       C  
ATOM   2728  C   PRO A1299     -23.479 -14.828 -44.930  1.00 78.91           C  
ANISOU 2728  C   PRO A1299    10245   9676  10061    -89   -550   -729       C  
ATOM   2729  O   PRO A1299     -23.530 -14.533 -43.729  1.00 83.27           O  
ANISOU 2729  O   PRO A1299    10853  10237  10547    -56   -569   -808       O  
ATOM   2730  CB  PRO A1299     -22.137 -13.199 -46.316  1.00 80.51           C  
ANISOU 2730  CB  PRO A1299    10530   9635  10424   -165   -636   -681       C  
ATOM   2731  CG  PRO A1299     -21.413 -13.373 -47.598  1.00 78.92           C  
ANISOU 2731  CG  PRO A1299    10277   9409  10300   -241   -636   -579       C  
ATOM   2732  CD  PRO A1299     -21.844 -14.711 -48.109  1.00 82.60           C  
ANISOU 2732  CD  PRO A1299    10644  10007  10732   -236   -572   -528       C  
ATOM   2733  N   LEU A1300     -24.522 -15.343 -45.582  1.00 74.62           N  
ANISOU 2733  N   LEU A1300     9628   9226   9498    -49   -487   -692       N  
ATOM   2734  CA  LEU A1300     -25.779 -15.601 -44.889  1.00 70.54           C  
ANISOU 2734  CA  LEU A1300     9074   8840   8889     31   -431   -731       C  
ATOM   2735  C   LEU A1300     -25.729 -16.907 -44.105  1.00 76.92           C  
ANISOU 2735  C   LEU A1300     9846   9751   9630    -38   -396   -713       C  
ATOM   2736  O   LEU A1300     -26.259 -16.985 -42.991  1.00 81.18           O  
ANISOU 2736  O   LEU A1300    10391  10374  10080      9   -369   -758       O  
ATOM   2737  CB  LEU A1300     -26.933 -15.622 -45.892  1.00 72.14           C  
ANISOU 2737  CB  LEU A1300     9190   9132   9088     82   -386   -691       C  
ATOM   2738  CG  LEU A1300     -28.341 -15.760 -45.312  1.00 77.20           C  
ANISOU 2738  CG  LEU A1300     9756   9944   9631    170   -325   -718       C  
ATOM   2739  CD1 LEU A1300     -28.648 -14.598 -44.381  1.00 83.75           C  
ANISOU 2739  CD1 LEU A1300    10665  10737  10419    322   -330   -803       C  
ATOM   2740  CD2 LEU A1300     -29.374 -15.848 -46.425  1.00 82.62           C  
ANISOU 2740  CD2 LEU A1300    10329  10751  10312    197   -297   -664       C  
ATOM   2741  N   PHE A1301     -25.095 -17.939 -44.667  1.00 83.72           N  
ANISOU 2741  N   PHE A1301    10681  10603  10527   -138   -388   -644       N  
ATOM   2742  CA  PHE A1301     -25.023 -19.225 -43.979  1.00 86.33           C  
ANISOU 2742  CA  PHE A1301    11003  11001  10799   -195   -348   -611       C  
ATOM   2743  C   PHE A1301     -24.093 -19.158 -42.773  1.00 84.34           C  
ANISOU 2743  C   PHE A1301    10807  10728  10511   -190   -392   -633       C  
ATOM   2744  O   PHE A1301     -24.417 -19.688 -41.704  1.00 82.96           O  
ANISOU 2744  O   PHE A1301    10640  10636  10245   -181   -362   -637       O  
ATOM   2745  CB  PHE A1301     -24.567 -20.316 -44.948  1.00 92.41           C  
ANISOU 2745  CB  PHE A1301    11758  11740  11614   -280   -322   -537       C  
ATOM   2746  CG  PHE A1301     -25.559 -20.618 -46.035  1.00 94.16           C  
ANISOU 2746  CG  PHE A1301    11925  12014  11839   -312   -279   -522       C  
ATOM   2747  CD1 PHE A1301     -25.158 -21.252 -47.200  1.00 98.12           C  
ANISOU 2747  CD1 PHE A1301    12430  12469  12384   -374   -267   -480       C  
ATOM   2748  CD2 PHE A1301     -26.894 -20.273 -45.893  1.00 93.65           C  
ANISOU 2748  CD2 PHE A1301    11797  12065  11720   -275   -252   -551       C  
ATOM   2749  CE1 PHE A1301     -26.067 -21.534 -48.202  1.00 93.97           C  
ANISOU 2749  CE1 PHE A1301    11854  12006  11842   -418   -240   -475       C  
ATOM   2750  CE2 PHE A1301     -27.808 -20.552 -46.893  1.00 89.82           C  
ANISOU 2750  CE2 PHE A1301    11239  11662  11225   -315   -225   -533       C  
ATOM   2751  CZ  PHE A1301     -27.393 -21.184 -48.048  1.00 87.79           C  
ANISOU 2751  CZ  PHE A1301    10996  11354  11008   -397   -225   -499       C  
ATOM   2752  N   TYR A1302     -22.932 -18.515 -42.927  1.00 83.30           N  
ANISOU 2752  N   TYR A1302    10707  10503  10441   -206   -466   -640       N  
ATOM   2753  CA  TYR A1302     -22.015 -18.369 -41.801  1.00 73.09           C  
ANISOU 2753  CA  TYR A1302     9453   9216   9104   -215   -528   -665       C  
ATOM   2754  C   TYR A1302     -22.623 -17.530 -40.686  1.00 81.74           C  
ANISOU 2754  C   TYR A1302    10605  10342  10112   -150   -544   -769       C  
ATOM   2755  O   TYR A1302     -22.280 -17.714 -39.513  1.00 78.20           O  
ANISOU 2755  O   TYR A1302    10185   9955   9574   -147   -571   -794       O  
ATOM   2756  CB  TYR A1302     -20.698 -17.748 -42.268  1.00 63.94           C  
ANISOU 2756  CB  TYR A1302     8297   7971   8027   -271   -609   -652       C  
ATOM   2757  CG  TYR A1302     -19.697 -18.743 -42.810  1.00 81.04           C  
ANISOU 2757  CG  TYR A1302    10406  10151  10234   -314   -601   -549       C  
ATOM   2758  CD1 TYR A1302     -18.774 -19.354 -41.971  1.00 79.58           C  
ANISOU 2758  CD1 TYR A1302    10205  10031   9999   -322   -634   -509       C  
ATOM   2759  CD2 TYR A1302     -19.669 -19.066 -44.160  1.00 92.75           C  
ANISOU 2759  CD2 TYR A1302    11854  11593  11793   -330   -558   -489       C  
ATOM   2760  CE1 TYR A1302     -17.855 -20.262 -42.460  1.00 74.51           C  
ANISOU 2760  CE1 TYR A1302     9514   9406   9390   -326   -617   -409       C  
ATOM   2761  CE2 TYR A1302     -18.753 -19.973 -44.659  1.00 83.44           C  
ANISOU 2761  CE2 TYR A1302    10637  10425  10641   -344   -538   -403       C  
ATOM   2762  CZ  TYR A1302     -17.848 -20.568 -43.804  1.00 70.53           C  
ANISOU 2762  CZ  TYR A1302     8987   8849   8964   -333   -564   -361       C  
ATOM   2763  OH  TYR A1302     -16.934 -21.471 -44.295  1.00 55.46           O  
ANISOU 2763  OH  TYR A1302     7040   6956   7077   -312   -535   -268       O  
ATOM   2764  N   GLY A1303     -23.523 -16.606 -41.028  1.00 82.50           N  
ANISOU 2764  N   GLY A1303    10721  10404  10221    -81   -526   -829       N  
ATOM   2765  CA  GLY A1303     -24.157 -15.796 -40.003  1.00 74.48           C  
ANISOU 2765  CA  GLY A1303     9772   9413   9114     12   -526   -936       C  
ATOM   2766  C   GLY A1303     -25.114 -16.592 -39.137  1.00 68.19           C  
ANISOU 2766  C   GLY A1303     8933   8782   8195     60   -446   -929       C  
ATOM   2767  O   GLY A1303     -25.179 -16.389 -37.922  1.00 77.45           O  
ANISOU 2767  O   GLY A1303    10158  10015   9255    105   -452   -997       O  
ATOM   2768  N   PHE A1304     -25.864 -17.513 -39.745  1.00 68.22           N  
ANISOU 2768  N   PHE A1304     8844   8868   8209     36   -369   -847       N  
ATOM   2769  CA  PHE A1304     -26.829 -18.313 -39.001  1.00 75.64           C  
ANISOU 2769  CA  PHE A1304     9731   9972   9036     51   -284   -822       C  
ATOM   2770  C   PHE A1304     -26.175 -19.278 -38.021  1.00 71.39           C  
ANISOU 2770  C   PHE A1304     9221   9479   8424     -8   -285   -774       C  
ATOM   2771  O   PHE A1304     -26.880 -19.851 -37.183  1.00 78.79           O  
ANISOU 2771  O   PHE A1304    10135  10550   9250      3   -216   -752       O  
ATOM   2772  CB  PHE A1304     -27.729 -19.085 -39.968  1.00 81.44           C  
ANISOU 2772  CB  PHE A1304    10362  10776   9804     -2   -213   -745       C  
ATOM   2773  CG  PHE A1304     -28.720 -18.220 -40.694  1.00 95.91           C  
ANISOU 2773  CG  PHE A1304    12136  12645  11660     87   -195   -779       C  
ATOM   2774  CD1 PHE A1304     -29.089 -16.987 -40.182  1.00 93.98           C  
ANISOU 2774  CD1 PHE A1304    11935  12399  11375    238   -203   -870       C  
ATOM   2775  CD2 PHE A1304     -29.284 -18.640 -41.888  1.00101.84           C  
ANISOU 2775  CD2 PHE A1304    12797  13433  12463     31   -170   -720       C  
ATOM   2776  CE1 PHE A1304     -30.000 -16.188 -40.846  1.00 90.31           C  
ANISOU 2776  CE1 PHE A1304    11420  11968  10926    353   -182   -886       C  
ATOM   2777  CE2 PHE A1304     -30.197 -17.845 -42.557  1.00100.20           C  
ANISOU 2777  CE2 PHE A1304    12522  13286  12265    130   -159   -736       C  
ATOM   2778  CZ  PHE A1304     -30.555 -16.618 -42.034  1.00 95.18           C  
ANISOU 2778  CZ  PHE A1304    11925  12646  11593    302   -162   -811       C  
ATOM   2779  N   LEU A1305     -24.857 -19.478 -38.105  1.00 65.77           N  
ANISOU 2779  N   LEU A1305     8549   8674   7765    -65   -358   -745       N  
ATOM   2780  CA  LEU A1305     -24.175 -20.296 -37.108  1.00 65.52           C  
ANISOU 2780  CA  LEU A1305     8545   8697   7651    -90   -369   -692       C  
ATOM   2781  C   LEU A1305     -24.124 -19.600 -35.755  1.00 71.07           C  
ANISOU 2781  C   LEU A1305     9305   9474   8224    -26   -408   -784       C  
ATOM   2782  O   LEU A1305     -24.198 -20.263 -34.714  1.00 79.54           O  
ANISOU 2782  O   LEU A1305    10390  10659   9173    -16   -379   -745       O  
ATOM   2783  CB  LEU A1305     -22.763 -20.639 -37.584  1.00 52.47           C  
ANISOU 2783  CB  LEU A1305     6897   6957   6082   -145   -438   -631       C  
ATOM   2784  CG  LEU A1305     -22.669 -21.568 -38.796  1.00 50.34           C  
ANISOU 2784  CG  LEU A1305     6594   6621   5914   -199   -389   -535       C  
ATOM   2785  CD1 LEU A1305     -21.221 -21.746 -39.226  1.00 48.01           C  
ANISOU 2785  CD1 LEU A1305     6292   6261   5689   -220   -452   -481       C  
ATOM   2786  CD2 LEU A1305     -23.309 -22.914 -38.486  1.00 45.04           C  
ANISOU 2786  CD2 LEU A1305     5929   6004   5180   -226   -293   -448       C  
ATOM   2787  N   GLY A1306     -24.002 -18.273 -35.747  1.00 52.29           N  
ANISOU 2787  N   GLY A1306     6978   7028   5862     17   -472   -906       N  
ATOM   2788  CA  GLY A1306     -24.000 -17.530 -34.498  1.00 68.32           C  
ANISOU 2788  CA  GLY A1306     9088   9112   7757     78   -510  -1021       C  
ATOM   2789  C   GLY A1306     -25.408 -17.397 -33.949  1.00 77.41           C  
ANISOU 2789  C   GLY A1306    10233  10382   8797    187   -407  -1066       C  
ATOM   2790  O   GLY A1306     -26.335 -17.011 -34.669  1.00 66.99           O  
ANISOU 2790  O   GLY A1306     8874   9046   7533    244   -348  -1081       O  
ATOM   2791  N   LYS A1307     -25.572 -17.722 -32.664  1.00 83.91           N  
ANISOU 2791  N   LYS A1307    11081  11349   9451    224   -382  -1079       N  
ATOM   2792  CA  LYS A1307     -26.892 -17.652 -32.047  1.00 82.12           C  
ANISOU 2792  CA  LYS A1307    10830  11273   9097    332   -271  -1111       C  
ATOM   2793  C   LYS A1307     -27.383 -16.216 -31.923  1.00 79.65           C  
ANISOU 2793  C   LYS A1307    10598  10909   8755    468   -277  -1276       C  
ATOM   2794  O   LYS A1307     -28.588 -15.963 -32.034  1.00 70.60           O  
ANISOU 2794  O   LYS A1307     9399   9850   7577    580   -179  -1293       O  
ATOM   2795  CB  LYS A1307     -26.868 -18.325 -30.675  1.00 72.63           C  
ANISOU 2795  CB  LYS A1307     9646  10244   7707    340   -241  -1077       C  
ATOM   2796  N   LYS A1308     -26.473 -15.266 -31.694  1.00 82.61           N  
ANISOU 2796  N   LYS A1308    11103  11145   9139    461   -391  -1397       N  
ATOM   2797  CA  LYS A1308     -26.881 -13.870 -31.581  1.00 87.42           C  
ANISOU 2797  CA  LYS A1308    11834  11657   9724    591   -397  -1563       C  
ATOM   2798  C   LYS A1308     -27.253 -13.292 -32.941  1.00 87.93           C  
ANISOU 2798  C   LYS A1308    11876  11573   9962    624   -384  -1545       C  
ATOM   2799  O   LYS A1308     -28.190 -12.492 -33.045  1.00100.20           O  
ANISOU 2799  O   LYS A1308    13463  13114  11494    788   -320  -1617       O  
ATOM   2800  CB  LYS A1308     -25.768 -13.049 -30.930  1.00 93.09           C  
ANISOU 2800  CB  LYS A1308    12717  12256  10396    536   -531  -1701       C  
ATOM   2801  N   PHE A1309     -26.530 -13.683 -33.994  1.00 87.88           N  
ANISOU 2801  N   PHE A1309    11810  11463  10117    486   -439  -1444       N  
ATOM   2802  CA  PHE A1309     -26.872 -13.223 -35.337  1.00 73.64           C  
ANISOU 2802  CA  PHE A1309     9974   9539   8465    512   -425  -1408       C  
ATOM   2803  C   PHE A1309     -28.240 -13.740 -35.760  1.00 68.30           C  
ANISOU 2803  C   PHE A1309     9155   9024   7773    602   -303  -1330       C  
ATOM   2804  O   PHE A1309     -29.022 -13.014 -36.384  1.00 63.83           O  
ANISOU 2804  O   PHE A1309     8582   8426   7246    727   -265  -1350       O  
ATOM   2805  CB  PHE A1309     -25.796 -13.665 -36.332  1.00 75.33           C  
ANISOU 2805  CB  PHE A1309    10144   9646   8831    344   -498  -1308       C  
ATOM   2806  CG  PHE A1309     -25.984 -13.115 -37.721  1.00101.29           C  
ANISOU 2806  CG  PHE A1309    13416  12803  12265    359   -497  -1270       C  
ATOM   2807  CD1 PHE A1309     -26.791 -13.767 -38.641  1.00103.71           C  
ANISOU 2807  CD1 PHE A1309    13587  13198  12619    374   -422  -1166       C  
ATOM   2808  CD2 PHE A1309     -25.343 -11.951 -38.110  1.00114.24           C  
ANISOU 2808  CD2 PHE A1309    15183  14237  13989    343   -574  -1334       C  
ATOM   2809  CE1 PHE A1309     -26.961 -13.265 -39.917  1.00105.89           C  
ANISOU 2809  CE1 PHE A1309    13847  13376  13011    393   -427  -1125       C  
ATOM   2810  CE2 PHE A1309     -25.509 -11.444 -39.386  1.00115.74           C  
ANISOU 2810  CE2 PHE A1309    15364  14309  14302    362   -569  -1282       C  
ATOM   2811  CZ  PHE A1309     -26.319 -12.102 -40.290  1.00108.78           C  
ANISOU 2811  CZ  PHE A1309    14340  13536  13456    397   -497  -1176       C  
ATOM   2812  N   LYS A1310     -28.545 -14.997 -35.428  1.00 64.69           N  
ANISOU 2812  N   LYS A1310     8580   8744   7253    535   -243  -1232       N  
ATOM   2813  CA  LYS A1310     -29.859 -15.550 -35.737  1.00 58.23           C  
ANISOU 2813  CA  LYS A1310     7612   8108   6404    582   -130  -1157       C  
ATOM   2814  C   LYS A1310     -30.964 -14.806 -35.000  1.00 78.55           C  
ANISOU 2814  C   LYS A1310    10189  10811   8845    784    -50  -1244       C  
ATOM   2815  O   LYS A1310     -32.102 -14.748 -35.480  1.00 79.13           O  
ANISOU 2815  O   LYS A1310    10139  11014   8914    874     29  -1207       O  
ATOM   2816  CB  LYS A1310     -29.892 -17.038 -35.386  1.00 65.24           C  
ANISOU 2816  CB  LYS A1310     8410   9136   7242    447    -82  -1039       C  
ATOM   2817  CG  LYS A1310     -31.129 -17.773 -35.874  1.00 81.43           C  
ANISOU 2817  CG  LYS A1310    10295  11363   9281    422     21   -943       C  
ATOM   2818  CD  LYS A1310     -31.317 -19.089 -35.135  1.00 84.29           C  
ANISOU 2818  CD  LYS A1310    10608  11870   9549    308     87   -845       C  
ATOM   2819  CE  LYS A1310     -30.084 -19.970 -35.238  1.00 81.68           C  
ANISOU 2819  CE  LYS A1310    10351  11401   9283    162     25   -776       C  
ATOM   2820  NZ  LYS A1310     -30.259 -21.247 -34.494  1.00 87.15           N  
ANISOU 2820  NZ  LYS A1310    11025  12207   9882     65     95   -667       N  
ATOM   2821  N   ARG A1311     -30.650 -14.225 -33.840  1.00 89.94           N  
ANISOU 2821  N   ARG A1311    11766  12238  10169    864    -69  -1364       N  
ATOM   2822  CA  ARG A1311     -31.659 -13.506 -33.070  1.00 90.73           C  
ANISOU 2822  CA  ARG A1311    11889  12461  10124   1081     17  -1460       C  
ATOM   2823  C   ARG A1311     -32.029 -12.188 -33.742  1.00 83.14           C  
ANISOU 2823  C   ARG A1311    11006  11352   9234   1256     11  -1544       C  
ATOM   2824  O   ARG A1311     -33.214 -11.863 -33.881  1.00 90.74           O  
ANISOU 2824  O   ARG A1311    11878  12452  10147   1440    109  -1538       O  
ATOM   2825  CB  ARG A1311     -31.159 -13.265 -31.646  1.00 91.62           C  
ANISOU 2825  CB  ARG A1311    12147  12590  10074   1112     -7  -1578       C  
ATOM   2826  N   TYR A1312     -31.027 -11.414 -34.166  1.00 78.05           N  
ANISOU 2826  N   TYR A1312    10525  10431   8700   1206   -100  -1611       N  
ATOM   2827  CA  TYR A1312     -31.309 -10.141 -34.821  1.00 87.76           C  
ANISOU 2827  CA  TYR A1312    11863  11480  10003   1367   -107  -1678       C  
ATOM   2828  C   TYR A1312     -31.897 -10.338 -36.212  1.00 87.91           C  
ANISOU 2828  C   TYR A1312    11722  11532  10148   1378    -78  -1542       C  
ATOM   2829  O   TYR A1312     -32.697  -9.511 -36.667  1.00 82.69           O  
ANISOU 2829  O   TYR A1312    11069  10852   9496   1583    -31  -1556       O  
ATOM   2830  CB  TYR A1312     -30.040  -9.292 -34.907  1.00 84.68           C  
ANISOU 2830  CB  TYR A1312    11694  10782   9698   1270   -234  -1773       C  
ATOM   2831  CG  TYR A1312     -29.527  -8.794 -33.575  1.00 89.77           C  
ANISOU 2831  CG  TYR A1312    12532  11372  10206   1283   -276  -1942       C  
ATOM   2832  CD1 TYR A1312     -30.166  -7.757 -32.907  1.00 83.44           C  
ANISOU 2832  CD1 TYR A1312    11894  10522   9288   1514   -222  -2097       C  
ATOM   2833  CD2 TYR A1312     -28.394  -9.348 -32.995  1.00 95.27           C  
ANISOU 2833  CD2 TYR A1312    13250  12072  10876   1073   -371  -1950       C  
ATOM   2834  CE1 TYR A1312     -29.697  -7.295 -31.692  1.00 87.73           C  
ANISOU 2834  CE1 TYR A1312    12630  11014   9687   1518   -265  -2269       C  
ATOM   2835  CE2 TYR A1312     -27.918  -8.892 -31.780  1.00 98.48           C  
ANISOU 2835  CE2 TYR A1312    13828  12452  11139   1072   -422  -2109       C  
ATOM   2836  CZ  TYR A1312     -28.573  -7.866 -31.134  1.00 93.49           C  
ANISOU 2836  CZ  TYR A1312    13369  11764  10387   1286   -371  -2275       C  
ATOM   2837  OH  TYR A1312     -28.101  -7.409 -29.925  1.00 89.53           O  
ANISOU 2837  OH  TYR A1312    13055  11237   9726   1278   -426  -2450       O  
ATOM   2838  N   PHE A1313     -31.514 -11.415 -36.902  1.00 78.77           N  
ANISOU 2838  N   PHE A1313    10426  10425   9077   1171   -107  -1412       N  
ATOM   2839  CA  PHE A1313     -32.016 -11.645 -38.253  1.00 66.61           C  
ANISOU 2839  CA  PHE A1313     8742   8924   7644   1158    -92  -1293       C  
ATOM   2840  C   PHE A1313     -33.515 -11.918 -38.246  1.00 78.22           C  
ANISOU 2840  C   PHE A1313    10022  10678   9021   1298     22  -1241       C  
ATOM   2841  O   PHE A1313     -34.246 -11.421 -39.111  1.00100.70           O  
ANISOU 2841  O   PHE A1313    12796  13559  11907   1428     45  -1198       O  
ATOM   2842  CB  PHE A1313     -31.260 -12.804 -38.902  1.00 74.82           C  
ANISOU 2842  CB  PHE A1313     9697   9956   8775    907   -140  -1184       C  
ATOM   2843  CG  PHE A1313     -31.507 -12.941 -40.379  1.00 83.30           C  
ANISOU 2843  CG  PHE A1313    10667  11022   9961    868   -149  -1082       C  
ATOM   2844  CD1 PHE A1313     -32.533 -13.742 -40.855  1.00 90.78           C  
ANISOU 2844  CD1 PHE A1313    11417  12198  10876    848    -83   -991       C  
ATOM   2845  CD2 PHE A1313     -30.709 -12.272 -41.292  1.00 82.53           C  
ANISOU 2845  CD2 PHE A1313    10667  10700   9989    837   -225  -1074       C  
ATOM   2846  CE1 PHE A1313     -32.760 -13.869 -42.213  1.00 93.06           C  
ANISOU 2846  CE1 PHE A1313    11613  12496  11248    806   -101   -907       C  
ATOM   2847  CE2 PHE A1313     -30.931 -12.395 -42.650  1.00 88.28           C  
ANISOU 2847  CE2 PHE A1313    11303  11437  10801    808   -232   -978       C  
ATOM   2848  CZ  PHE A1313     -31.957 -13.195 -43.111  1.00 90.57           C  
ANISOU 2848  CZ  PHE A1313    11402  11961  11049    796   -174   -900       C  
ATOM   2849  N   LEU A1314     -33.993 -12.702 -37.277  1.00 73.43           N  
ANISOU 2849  N   LEU A1314     9323  10294   8285   1274     94  -1232       N  
ATOM   2850  CA  LEU A1314     -35.416 -13.003 -37.200  1.00 84.42           C  
ANISOU 2850  CA  LEU A1314    10507  11991   9576   1384    207  -1174       C  
ATOM   2851  C   LEU A1314     -36.231 -11.828 -36.676  1.00 91.22           C  
ANISOU 2851  C   LEU A1314    11415  12908  10337   1698    276  -1268       C  
ATOM   2852  O   LEU A1314     -37.447 -11.791 -36.891  1.00 98.53           O  
ANISOU 2852  O   LEU A1314    12155  14081  11201   1843    363  -1212       O  
ATOM   2853  CB  LEU A1314     -35.648 -14.234 -36.323  1.00 87.63           C  
ANISOU 2853  CB  LEU A1314    10805  12617   9873   1240    270  -1119       C  
ATOM   2854  CG  LEU A1314     -35.009 -15.535 -36.815  1.00 91.08           C  
ANISOU 2854  CG  LEU A1314    11194  13017  10394    950    225  -1013       C  
ATOM   2855  CD1 LEU A1314     -35.348 -16.687 -35.882  1.00104.09           C  
ANISOU 2855  CD1 LEU A1314    12757  14870  11923    831    302   -948       C  
ATOM   2856  CD2 LEU A1314     -35.444 -15.846 -38.239  1.00 91.50           C  
ANISOU 2856  CD2 LEU A1314    11105  13106  10553    870    210   -919       C  
ATOM   2857  N   GLN A1315     -35.596 -10.872 -35.994  1.00 87.30           N  
ANISOU 2857  N   GLN A1315    11161  12193   9814   1810    241  -1411       N  
ATOM   2858  CA  GLN A1315     -36.321  -9.688 -35.545  1.00 95.04           C  
ANISOU 2858  CA  GLN A1315    12233  13178  10702   2132    311  -1516       C  
ATOM   2859  C   GLN A1315     -36.624  -8.753 -36.709  1.00 99.14           C  
ANISOU 2859  C   GLN A1315    12777  13559  11332   2294    291  -1487       C  
ATOM   2860  O   GLN A1315     -37.683  -8.115 -36.739  1.00 97.80           O  
ANISOU 2860  O   GLN A1315    12548  13518  11093   2579    379  -1490       O  
ATOM   2861  CB  GLN A1315     -35.526  -8.957 -34.462  1.00105.49           C  
ANISOU 2861  CB  GLN A1315    13839  14288  11953   2180    272  -1695       C  
ATOM   2862  CG  GLN A1315     -35.489  -9.673 -33.122  1.00113.43           C  
ANISOU 2862  CG  GLN A1315    14825  15484  12791   2115    317  -1735       C  
ATOM   2863  CD  GLN A1315     -34.843  -8.837 -32.034  1.00126.81           C  
ANISOU 2863  CD  GLN A1315    16800  16999  14383   2194    280  -1931       C  
ATOM   2864  OE1 GLN A1315     -34.433  -7.701 -32.269  1.00129.07           O  
ANISOU 2864  OE1 GLN A1315    17311  17000  14730   2288    223  -2044       O  
ATOM   2865  NE2 GLN A1315     -34.751  -9.397 -30.833  1.00130.71           N  
ANISOU 2865  NE2 GLN A1315    17294  17659  14712   2147    311  -1970       N  
ATOM   2866  N   LEU A1316     -35.706  -8.655 -37.674  1.00103.61           N  
ANISOU 2866  N   LEU A1316    13426  13875  12064   2130    182  -1449       N  
ATOM   2867  CA  LEU A1316     -35.950  -7.821 -38.846  1.00 96.93           C  
ANISOU 2867  CA  LEU A1316    12606  12900  11323   2267    161  -1396       C  
ATOM   2868  C   LEU A1316     -37.086  -8.367 -39.700  1.00 98.53           C  
ANISOU 2868  C   LEU A1316    12510  13410  11516   2317    217  -1246       C  
ATOM   2869  O   LEU A1316     -37.843  -7.589 -40.292  1.00113.77           O  
ANISOU 2869  O   LEU A1316    14409  15370  13448   2563    251  -1209       O  
ATOM   2870  CB  LEU A1316     -34.676  -7.697 -39.682  1.00 87.14           C  
ANISOU 2870  CB  LEU A1316    11503  11357  10251   2051     38  -1373       C  
ATOM   2871  CG  LEU A1316     -33.722  -6.555 -39.329  1.00 85.02           C  
ANISOU 2871  CG  LEU A1316    11556  10720  10027   2077    -28  -1505       C  
ATOM   2872  CD1 LEU A1316     -32.447  -6.652 -40.148  1.00 84.51           C  
ANISOU 2872  CD1 LEU A1316    11563  10426  10119   1816   -143  -1454       C  
ATOM   2873  CD2 LEU A1316     -34.402  -5.212 -39.552  1.00 82.21           C  
ANISOU 2873  CD2 LEU A1316    11344  10230   9662   2398     19  -1546       C  
ATOM   2874  N   LEU A1317     -37.225  -9.691 -39.775  1.00 94.79           N  
ANISOU 2874  N   LEU A1317    11823  13166  11028   2087    224  -1158       N  
ATOM   2875  CA  LEU A1317     -38.279 -10.282 -40.589  1.00 98.46           C  
ANISOU 2875  CA  LEU A1317    12000  13936  11476   2082    263  -1024       C  
ATOM   2876  C   LEU A1317     -39.621 -10.301 -39.868  1.00112.51           C  
ANISOU 2876  C   LEU A1317    13590  16067  13093   2286    388  -1016       C  
ATOM   2877  O   LEU A1317     -40.669 -10.234 -40.520  1.00117.76           O  
ANISOU 2877  O   LEU A1317    14036  16980  13727   2410    427   -923       O  
ATOM   2878  CB  LEU A1317     -37.887 -11.701 -41.005  1.00 85.18           C  
ANISOU 2878  CB  LEU A1317    10190  12331   9843   1735    222   -939       C  
ATOM   2879  CG  LEU A1317     -36.586 -11.828 -41.801  1.00 76.54           C  
ANISOU 2879  CG  LEU A1317     9242  10940   8901   1532    110   -928       C  
ATOM   2880  CD1 LEU A1317     -36.339 -13.273 -42.205  1.00 76.68           C  
ANISOU 2880  CD1 LEU A1317     9134  11052   8948   1229     90   -847       C  
ATOM   2881  CD2 LEU A1317     -36.610 -10.921 -43.022  1.00 77.05           C  
ANISOU 2881  CD2 LEU A1317     9343  10877   9056   1656     63   -885       C  
ATOM   2882  N   LYS A1318     -39.613 -10.389 -38.542  1.00117.16           N  
ANISOU 2882  N   LYS A1318    14243  16707  13567   2325    451  -1105       N  
ATOM   2883  CA  LYS A1318     -40.851 -10.413 -37.769  1.00108.66           C  
ANISOU 2883  CA  LYS A1318    12984  15983  12319   2523    585  -1097       C  
ATOM   2884  C   LYS A1318     -41.499  -9.033 -37.724  1.00104.31           C  
ANISOU 2884  C   LYS A1318    12507  15411  11715   2936    644  -1158       C  
ATOM   2885  O   LYS A1318     -40.829  -8.029 -37.485  1.00 99.78           O  
ANISOU 2885  O   LYS A1318    12231  14504  11176   3074    609  -1281       O  
ATOM   2886  CB  LYS A1318     -40.587 -10.917 -36.348  1.00 90.08           C  
ANISOU 2886  CB  LYS A1318    10696  13687   9843   2444    638  -1172       C  
TER    2887      LYS A1318                                                      
ATOM   2888  N   GLN D   1     -24.882 -12.311 -20.106  1.00129.76           N  
ANISOU 2888  N   GLN D   1    14555  16225  18524     44  -1049  -3636       N  
ATOM   2889  CA  GLN D   1     -23.451 -12.045 -20.008  1.00130.17           C  
ANISOU 2889  CA  GLN D   1    15033  16322  18105     84   -947  -3023       C  
ATOM   2890  C   GLN D   1     -22.799 -12.883 -18.915  1.00126.46           C  
ANISOU 2890  C   GLN D   1    14601  16396  17051   -111   -189  -2776       C  
ATOM   2891  O   GLN D   1     -23.446 -13.265 -17.940  1.00136.37           O  
ANISOU 2891  O   GLN D   1    15473  18050  18291   -331    216  -3191       O  
ATOM   2892  CB  GLN D   1     -23.200 -10.558 -19.748  1.00134.64           C  
ANISOU 2892  CB  GLN D   1    15388  16749  19019    277  -1451  -3300       C  
ATOM   2893  CG  GLN D   1     -23.336  -9.685 -20.983  1.00138.43           C  
ANISOU 2893  CG  GLN D   1    16186  16545  19868    417  -2359  -3239       C  
ATOM   2894  CD  GLN D   1     -22.265  -9.976 -22.016  1.00143.18           C  
ANISOU 2894  CD  GLN D   1    17547  16937  19919    267  -2397  -2430       C  
ATOM   2895  OE1 GLN D   1     -22.547 -10.071 -23.211  1.00154.23           O  
ANISOU 2895  OE1 GLN D   1    19344  17872  21384    199  -2848  -2242       O  
ATOM   2896  NE2 GLN D   1     -21.025 -10.117 -21.560  1.00134.11           N  
ANISOU 2896  NE2 GLN D   1    16578  16160  18218    187  -1928  -2004       N  
ATOM   2897  N   VAL D   2     -21.512 -13.164 -19.088  1.00112.69           N  
ANISOU 2897  N   VAL D   2    13334  14671  14810    -76    -39  -2140       N  
ATOM   2898  CA  VAL D   2     -20.728 -13.936 -18.132  1.00102.40           C  
ANISOU 2898  CA  VAL D   2    12172  13766  12969   -198    509  -1850       C  
ATOM   2899  C   VAL D   2     -19.708 -12.980 -17.526  1.00 99.96           C  
ANISOU 2899  C   VAL D   2    11789  13631  12561    -87    475  -1768       C  
ATOM   2900  O   VAL D   2     -18.704 -12.637 -18.161  1.00 95.21           O  
ANISOU 2900  O   VAL D   2    11480  12897  11799     42    287  -1392       O  
ATOM   2901  CB  VAL D   2     -20.050 -15.144 -18.787  1.00 92.85           C  
ANISOU 2901  CB  VAL D   2    11513  12443  11323   -183    666  -1287       C  
ATOM   2902  CG1 VAL D   2     -19.302 -15.962 -17.745  1.00 89.26           C  
ANISOU 2902  CG1 VAL D   2    11240  12298  10377   -275   1071  -1041       C  
ATOM   2903  CG2 VAL D   2     -21.080 -16.002 -19.508  1.00 94.26           C  
ANISOU 2903  CG2 VAL D   2    11799  12392  11624   -290    633  -1354       C  
ATOM   2904  N   GLN D   3     -19.961 -12.546 -16.296  1.00 98.22           N  
ANISOU 2904  N   GLN D   3    11167  13751  12401   -195    679  -2156       N  
ATOM   2905  CA  GLN D   3     -19.093 -11.599 -15.616  1.00 98.42           C  
ANISOU 2905  CA  GLN D   3    11084  13954  12358   -107    647  -2132       C  
ATOM   2906  C   GLN D   3     -18.017 -12.329 -14.816  1.00 82.39           C  
ANISOU 2906  C   GLN D   3     9330  12229   9747   -194   1060  -1706       C  
ATOM   2907  O   GLN D   3     -18.167 -13.495 -14.442  1.00 76.97           O  
ANISOU 2907  O   GLN D   3     8846  11656   8742   -390   1373  -1567       O  
ATOM   2908  CB  GLN D   3     -19.908 -10.692 -14.694  1.00114.59           C  
ANISOU 2908  CB  GLN D   3    12528  16213  14797   -165    618  -2847       C  
ATOM   2909  CG  GLN D   3     -21.021  -9.935 -15.401  1.00126.91           C  
ANISOU 2909  CG  GLN D   3    13748  17428  17044     -2     79  -3407       C  
ATOM   2910  CD  GLN D   3     -21.864  -9.111 -14.447  1.00138.08           C  
ANISOU 2910  CD  GLN D   3    14452  19105  18906    -17     54  -4285       C  
ATOM   2911  OE1 GLN D   3     -21.573  -9.031 -13.254  1.00138.26           O  
ANISOU 2911  OE1 GLN D   3    14266  19596  18672   -201    477  -4440       O  
ATOM   2912  NE2 GLN D   3     -22.917  -8.494 -14.970  1.00143.75           N  
ANISOU 2912  NE2 GLN D   3    14784  19522  20312    178   -480  -4923       N  
ATOM   2913  N   LEU D   4     -16.920 -11.620 -14.558  1.00 72.56           N  
ANISOU 2913  N   LEU D   4     8125  11077   8366    -63    985  -1504       N  
ATOM   2914  CA  LEU D   4     -15.787 -12.160 -13.816  1.00 71.34           C  
ANISOU 2914  CA  LEU D   4     8199  11174   7731    -75   1255  -1142       C  
ATOM   2915  C   LEU D   4     -15.381 -11.160 -12.744  1.00 92.62           C  
ANISOU 2915  C   LEU D   4    10622  14143  10424   -108   1296  -1322       C  
ATOM   2916  O   LEU D   4     -14.962 -10.042 -13.063  1.00 90.20           O  
ANISOU 2916  O   LEU D   4    10206  13762  10303     35   1013  -1353       O  
ATOM   2917  CB  LEU D   4     -14.606 -12.457 -14.745  1.00 69.22           C  
ANISOU 2917  CB  LEU D   4     8269  10787   7243    140   1136   -693       C  
ATOM   2918  CG  LEU D   4     -14.839 -13.477 -15.862  1.00 71.54           C  
ANISOU 2918  CG  LEU D   4     8859  10825   7499    191   1098   -512       C  
ATOM   2919  CD1 LEU D   4     -13.585 -13.641 -16.706  1.00 67.64           C  
ANISOU 2919  CD1 LEU D   4     8584  10338   6777    364   1027   -220       C  
ATOM   2920  CD2 LEU D   4     -15.279 -14.813 -15.287  1.00 70.06           C  
ANISOU 2920  CD2 LEU D   4     8870  10652   7099     65   1337   -454       C  
ATOM   2921  N   GLN D   5     -15.504 -11.560 -11.482  1.00114.18           N  
ANISOU 2921  N   GLN D   5    13305  17177  12902   -360   1619  -1428       N  
ATOM   2922  CA  GLN D   5     -15.117 -10.729 -10.351  1.00113.66           C  
ANISOU 2922  CA  GLN D   5    13009  17408  12769   -444   1709  -1601       C  
ATOM   2923  C   GLN D   5     -13.746 -11.165  -9.850  1.00108.89           C  
ANISOU 2923  C   GLN D   5    12747  16916  11711   -379   1776  -1116       C  
ATOM   2924  O   GLN D   5     -13.512 -12.357  -9.627  1.00117.71           O  
ANISOU 2924  O   GLN D   5    14238  18004  12482   -477   1884   -831       O  
ATOM   2925  CB  GLN D   5     -16.147 -10.823  -9.224  1.00110.50           C  
ANISOU 2925  CB  GLN D   5    12321  17331  12333   -868   2029  -2108       C  
ATOM   2926  N   GLU D   6     -12.848 -10.201  -9.676  1.00 99.48           N  
ANISOU 2926  N   GLU D   6    11440  15818  10539   -213   1646  -1050       N  
ATOM   2927  CA  GLU D   6     -11.482 -10.465  -9.253  1.00100.01           C  
ANISOU 2927  CA  GLU D   6    11737  16010  10253    -99   1651   -672       C  
ATOM   2928  C   GLU D   6     -11.240  -9.904  -7.857  1.00 99.71           C  
ANISOU 2928  C   GLU D   6    11567  16267  10050   -292   1783   -799       C  
ATOM   2929  O   GLU D   6     -11.907  -8.966  -7.414  1.00100.87           O  
ANISOU 2929  O   GLU D   6    11367  16538  10422   -427   1825  -1207       O  
ATOM   2930  CB  GLU D   6     -10.478  -9.861 -10.240  1.00 98.56           C  
ANISOU 2930  CB  GLU D   6    11544  15764  10139    181   1418   -479       C  
ATOM   2931  CG  GLU D   6     -10.765 -10.189 -11.695  1.00108.96           C  
ANISOU 2931  CG  GLU D   6    12977  16814  11607    286   1278   -411       C  
ATOM   2932  CD  GLU D   6      -9.714  -9.630 -12.632  1.00107.79           C  
ANISOU 2932  CD  GLU D   6    12861  16700  11394    390   1101   -250       C  
ATOM   2933  OE1 GLU D   6      -8.579  -9.386 -12.173  1.00110.60           O  
ANISOU 2933  OE1 GLU D   6    13171  17316  11537    449   1135   -143       O  
ATOM   2934  OE2 GLU D   6     -10.024  -9.431 -13.825  1.00102.49           O  
ANISOU 2934  OE2 GLU D   6    12274  15817  10851    352    923   -250       O  
ATOM   2935  N   SER D   7     -10.265 -10.494  -7.170  1.00 90.47           N  
ANISOU 2935  N   SER D   7    10676  15191   8507   -288   1799   -488       N  
ATOM   2936  CA  SER D   7      -9.904 -10.082  -5.820  1.00 90.77           C  
ANISOU 2936  CA  SER D   7    10688  15491   8310   -506   1898   -534       C  
ATOM   2937  C   SER D   7      -8.558 -10.696  -5.468  1.00 91.98           C  
ANISOU 2937  C   SER D   7    11169  15631   8150   -327   1729   -135       C  
ATOM   2938  O   SER D   7      -8.109 -11.655  -6.103  1.00 90.38           O  
ANISOU 2938  O   SER D   7    11225  15220   7896    -88   1567    100       O  
ATOM   2939  CB  SER D   7     -10.968 -10.499  -4.798  1.00 93.10           C  
ANISOU 2939  CB  SER D   7    11042  15939   8392  -1046   2173   -791       C  
ATOM   2940  OG  SER D   7     -11.190 -11.898  -4.837  1.00 96.40           O  
ANISOU 2940  OG  SER D   7    11933  16176   8521  -1228   2168   -544       O  
ATOM   2941  N   GLY D   8      -7.919 -10.128  -4.446  1.00 91.11           N  
ANISOU 2941  N   GLY D   8    11018  15733   7865   -419   1728   -117       N  
ATOM   2942  CA  GLY D   8      -6.656 -10.627  -3.939  1.00 92.43           C  
ANISOU 2942  CA  GLY D   8    11460  15890   7770   -254   1502    190       C  
ATOM   2943  C   GLY D   8      -5.472  -9.712  -4.164  1.00 92.09           C  
ANISOU 2943  C   GLY D   8    11125  16025   7840     68   1379    221       C  
ATOM   2944  O   GLY D   8      -4.378 -10.017  -3.672  1.00110.65           O  
ANISOU 2944  O   GLY D   8    13612  18414  10018    228   1170    394       O  
ATOM   2945  N   GLY D   9      -5.647  -8.607  -4.885  1.00 77.31           N  
ANISOU 2945  N   GLY D   9     8889  14245   6241    134   1443     46       N  
ATOM   2946  CA  GLY D   9      -4.536  -7.719  -5.148  1.00 82.31           C  
ANISOU 2946  CA  GLY D   9     9295  15070   6907    316   1327     82       C  
ATOM   2947  C   GLY D   9      -4.103  -6.944  -3.918  1.00 91.68           C  
ANISOU 2947  C   GLY D   9    10407  16477   7949    166   1340     60       C  
ATOM   2948  O   GLY D   9      -4.815  -6.844  -2.918  1.00 92.22           O  
ANISOU 2948  O   GLY D   9    10533  16580   7928   -124   1479    -61       O  
ATOM   2949  N   GLY D  10      -2.903  -6.383  -4.002  1.00 88.66           N  
ANISOU 2949  N   GLY D  10     9877  16294   7517    318   1215    138       N  
ATOM   2950  CA  GLY D  10      -2.364  -5.606  -2.904  1.00 79.96           C  
ANISOU 2950  CA  GLY D  10     8701  15403   6275    197   1199    137       C  
ATOM   2951  C   GLY D  10      -0.895  -5.325  -3.113  1.00 88.62           C  
ANISOU 2951  C   GLY D  10     9645  16739   7289    394   1044    230       C  
ATOM   2952  O   GLY D  10      -0.243  -5.889  -3.998  1.00 89.44           O  
ANISOU 2952  O   GLY D  10     9683  16885   7416    623    967    246       O  
ATOM   2953  N   LEU D  11      -0.379  -4.432  -2.273  1.00100.98           N  
ANISOU 2953  N   LEU D  11    11111  18504   8751    277   1016    228       N  
ATOM   2954  CA  LEU D  11       1.021  -4.028  -2.307  1.00 97.03           C  
ANISOU 2954  CA  LEU D  11    10417  18301   8151    392    886    269       C  
ATOM   2955  C   LEU D  11       1.790  -4.802  -1.243  1.00 92.97           C  
ANISOU 2955  C   LEU D  11    10043  17816   7465    538    717    377       C  
ATOM   2956  O   LEU D  11       1.467  -4.718  -0.053  1.00 93.63           O  
ANISOU 2956  O   LEU D  11    10334  17838   7403    341    721    446       O  
ATOM   2957  CB  LEU D  11       1.156  -2.521  -2.088  1.00 97.84           C  
ANISOU 2957  CB  LEU D  11    10362  18568   8244    159    886    212       C  
ATOM   2958  CG  LEU D  11       2.552  -1.945  -1.829  1.00104.30           C  
ANISOU 2958  CG  LEU D  11    10988  19742   8899    162    778    246       C  
ATOM   2959  CD1 LEU D  11       3.546  -2.383  -2.892  1.00102.01           C  
ANISOU 2959  CD1 LEU D  11    10483  19702   8573    308    746    179       C  
ATOM   2960  CD2 LEU D  11       2.486  -0.428  -1.761  1.00111.52           C  
ANISOU 2960  CD2 LEU D  11    11838  20727   9809   -122    732    205       C  
ATOM   2961  N   VAL D  12       2.807  -5.549  -1.674  1.00 84.93           N  
ANISOU 2961  N   VAL D  12     8915  16889   6467    865    527    341       N  
ATOM   2962  CA  VAL D  12       3.622  -6.365  -0.787  1.00 81.60           C  
ANISOU 2962  CA  VAL D  12     8643  16402   5957   1094    193    400       C  
ATOM   2963  C   VAL D  12       5.088  -6.145  -1.140  1.00 91.08           C  
ANISOU 2963  C   VAL D  12     9400  17989   7215   1359     38    191       C  
ATOM   2964  O   VAL D  12       5.431  -5.747  -2.256  1.00 91.79           O  
ANISOU 2964  O   VAL D  12     9121  18383   7374   1357    213     -9       O  
ATOM   2965  CB  VAL D  12       3.252  -7.866  -0.878  1.00 83.63           C  
ANISOU 2965  CB  VAL D  12     9263  16257   6255   1310    -37    457       C  
ATOM   2966  CG1 VAL D  12       3.743  -8.462  -2.189  1.00 84.31           C  
ANISOU 2966  CG1 VAL D  12     9053  16422   6558   1690    -89    218       C  
ATOM   2967  CG2 VAL D  12       3.794  -8.641   0.318  1.00 97.46           C  
ANISOU 2967  CG2 VAL D  12    11404  17763   7863   1411   -514    598       C  
ATOM   2968  N   ALA D  13       5.956  -6.395  -0.162  1.00112.37           N  
ANISOU 2968  N   ALA D  13    12143  20697   9854   1524   -307    208       N  
ATOM   2969  CA  ALA D  13       7.387  -6.247  -0.368  1.00109.64           C  
ANISOU 2969  CA  ALA D  13    11309  20756   9593   1796   -492    -82       C  
ATOM   2970  C   ALA D  13       7.906  -7.322  -1.322  1.00 96.22           C  
ANISOU 2970  C   ALA D  13     9348  19079   8131   2256   -682   -438       C  
ATOM   2971  O   ALA D  13       7.197  -8.260  -1.700  1.00101.63           O  
ANISOU 2971  O   ALA D  13    10324  19384   8906   2396   -747   -385       O  
ATOM   2972  CB  ALA D  13       8.129  -6.313   0.966  1.00118.42           C  
ANISOU 2972  CB  ALA D  13    12568  21799  10626   1895   -907      7       C  
ATOM   2973  N   ALA D  14       9.170  -7.174  -1.712  1.00 99.02           N  
ANISOU 2973  N   ALA D  14     9110  19925   8590   2473   -766   -868       N  
ATOM   2974  CA  ALA D  14       9.784  -8.117  -2.637  1.00 99.32           C  
ANISOU 2974  CA  ALA D  14     8750  20105   8883   2920   -927  -1380       C  
ATOM   2975  C   ALA D  14       9.989  -9.470  -1.968  1.00106.45           C  
ANISOU 2975  C   ALA D  14     9964  20456  10025   3488  -1627  -1432       C  
ATOM   2976  O   ALA D  14      10.452  -9.555  -0.827  1.00129.67           O  
ANISOU 2976  O   ALA D  14    13115  23188  12965   3621  -2095  -1309       O  
ATOM   2977  CB  ALA D  14      11.118  -7.574  -3.145  1.00102.69           C  
ANISOU 2977  CB  ALA D  14     8378  21301   9338   2937   -818  -1950       C  
ATOM   2978  N   GLY D  15       9.642 -10.533  -2.688  1.00105.38           N  
ANISOU 2978  N   GLY D  15     9920  20038  10082   3798  -1764  -1605       N  
ATOM   2979  CA  GLY D  15       9.766 -11.880  -2.175  1.00109.99           C  
ANISOU 2979  CA  GLY D  15    10901  19992  10897   4325  -2533  -1653       C  
ATOM   2980  C   GLY D  15       8.595 -12.370  -1.355  1.00108.18           C  
ANISOU 2980  C   GLY D  15    11631  19030  10444   4058  -2725   -997       C  
ATOM   2981  O   GLY D  15       8.683 -13.457  -0.772  1.00112.83           O  
ANISOU 2981  O   GLY D  15    12733  19006  11132   4373  -3471   -936       O  
ATOM   2982  N   GLY D  16       7.503 -11.612  -1.293  1.00102.39           N  
ANISOU 2982  N   GLY D  16    11163  18337   9405   3453  -2122   -556       N  
ATOM   2983  CA  GLY D  16       6.352 -11.996  -0.500  1.00111.13           C  
ANISOU 2983  CA  GLY D  16    13089  18890  10243   3072  -2193    -33       C  
ATOM   2984  C   GLY D  16       5.479 -13.045  -1.157  1.00112.88           C  
ANISOU 2984  C   GLY D  16    13677  18689  10523   3139  -2243     24       C  
ATOM   2985  O   GLY D  16       5.981 -13.938  -1.847  1.00104.65           O  
ANISOU 2985  O   GLY D  16    12472  17516   9773   3666  -2607   -319       O  
ATOM   2986  N   SER D  17       4.168 -12.948  -0.949  1.00115.67           N  
ANISOU 2986  N   SER D  17    14486  18849  10613   2607  -1883    393       N  
ATOM   2987  CA  SER D  17       3.237 -13.923  -1.498  1.00119.61           C  
ANISOU 2987  CA  SER D  17    15382  18945  11118   2578  -1907    487       C  
ATOM   2988  C   SER D  17       1.841 -13.320  -1.537  1.00111.90           C  
ANISOU 2988  C   SER D  17    14535  18056   9926   1966  -1262    715       C  
ATOM   2989  O   SER D  17       1.478 -12.503  -0.687  1.00125.38           O  
ANISOU 2989  O   SER D  17    16317  19924  11398   1510  -1005    874       O  
ATOM   2990  CB  SER D  17       3.234 -15.218  -0.678  1.00135.96           C  
ANISOU 2990  CB  SER D  17    18267  20334  13058   2627  -2686    706       C  
ATOM   2991  OG  SER D  17       2.255 -16.124  -1.155  1.00147.71           O  
ANISOU 2991  OG  SER D  17    20201  21432  14490   2497  -2690    836       O  
ATOM   2992  N   LEU D  18       1.066 -13.737  -2.536  1.00100.69           N  
ANISOU 2992  N   LEU D  18    13107  16534   8617   1981  -1030    665       N  
ATOM   2993  CA  LEU D  18      -0.319 -13.312  -2.679  1.00 87.99           C  
ANISOU 2993  CA  LEU D  18    11585  14960   6888   1473   -503    786       C  
ATOM   2994  C   LEU D  18      -1.124 -14.461  -3.270  1.00 88.90           C  
ANISOU 2994  C   LEU D  18    12080  14680   7020   1478   -596    848       C  
ATOM   2995  O   LEU D  18      -0.571 -15.457  -3.744  1.00 91.71           O  
ANISOU 2995  O   LEU D  18    12555  14767   7525   1924  -1026    764       O  
ATOM   2996  CB  LEU D  18      -0.441 -12.060  -3.555  1.00 83.45           C  
ANISOU 2996  CB  LEU D  18    10388  14824   6496   1445      5    597       C  
ATOM   2997  CG  LEU D  18      -0.036 -10.715  -2.950  1.00 81.92           C  
ANISOU 2997  CG  LEU D  18     9883  15005   6240   1261    191    572       C  
ATOM   2998  CD1 LEU D  18      -0.124  -9.613  -3.994  1.00 85.15           C  
ANISOU 2998  CD1 LEU D  18     9809  15724   6819   1226    532    405       C  
ATOM   2999  CD2 LEU D  18      -0.909 -10.389  -1.752  1.00 82.06           C  
ANISOU 2999  CD2 LEU D  18    10209  14964   6006    747    341    716       C  
ATOM   3000  N   ARG D  19      -2.446 -14.310  -3.238  1.00 86.97           N  
ANISOU 3000  N   ARG D  19    11989  14410   6643    984   -207    933       N  
ATOM   3001  CA  ARG D  19      -3.359 -15.304  -3.798  1.00 87.58           C  
ANISOU 3001  CA  ARG D  19    12413  14154   6708    889   -221    994       C  
ATOM   3002  C   ARG D  19      -4.506 -14.566  -4.474  1.00 91.11           C  
ANISOU 3002  C   ARG D  19    12512  14819   7285    622    345    857       C  
ATOM   3003  O   ARG D  19      -5.381 -14.020  -3.795  1.00 90.56           O  
ANISOU 3003  O   ARG D  19    12452  14898   7061    113    653    827       O  
ATOM   3004  CB  ARG D  19      -3.881 -16.254  -2.719  1.00 91.99           C  
ANISOU 3004  CB  ARG D  19    13767  14337   6849    405   -517   1263       C  
ATOM   3005  CG  ARG D  19      -4.764 -17.373  -3.250  1.00 93.37           C  
ANISOU 3005  CG  ARG D  19    14379  14136   6960    261   -599   1350       C  
ATOM   3006  CD  ARG D  19      -5.248 -18.275  -2.125  1.00112.42           C  
ANISOU 3006  CD  ARG D  19    17679  16190   8845   -383   -926   1644       C  
ATOM   3007  NE  ARG D  19      -6.045 -19.394  -2.621  1.00123.34           N  
ANISOU 3007  NE  ARG D  19    19547  17188  10128   -561  -1060   1749       N  
ATOM   3008  CZ  ARG D  19      -5.549 -20.588  -2.928  1.00134.78           C  
ANISOU 3008  CZ  ARG D  19    21507  18075  11626   -182  -1749   1879       C  
ATOM   3009  NH1 ARG D  19      -4.252 -20.825  -2.789  1.00143.87           N  
ANISOU 3009  NH1 ARG D  19    22693  19001  12970    435  -2382   1855       N  
ATOM   3010  NH2 ARG D  19      -6.349 -21.547  -3.373  1.00134.47           N  
ANISOU 3010  NH2 ARG D  19    21925  17694  11473   -401  -1846   1982       N  
ATOM   3011  N   LEU D  20      -4.500 -14.550  -5.804  1.00 90.47           N  
ANISOU 3011  N   LEU D  20    12117  14761   7496    950    445    716       N  
ATOM   3012  CA  LEU D  20      -5.546 -13.896  -6.576  1.00 77.95           C  
ANISOU 3012  CA  LEU D  20    10249  13282   6084    756    837    583       C  
ATOM   3013  C   LEU D  20      -6.691 -14.865  -6.832  1.00 78.87           C  
ANISOU 3013  C   LEU D  20    10722  13097   6147    531    874    637       C  
ATOM   3014  O   LEU D  20      -6.470 -16.028  -7.182  1.00 80.83           O  
ANISOU 3014  O   LEU D  20    11312  13041   6360    743    591    744       O  
ATOM   3015  CB  LEU D  20      -4.992 -13.379  -7.904  1.00 75.62           C  
ANISOU 3015  CB  LEU D  20     9535  13148   6050   1094    892    434       C  
ATOM   3016  CG  LEU D  20      -3.790 -12.436  -7.827  1.00 82.82           C  
ANISOU 3016  CG  LEU D  20    10077  14412   6978   1256    868    349       C  
ATOM   3017  CD1 LEU D  20      -3.331 -12.038  -9.221  1.00 77.63           C  
ANISOU 3017  CD1 LEU D  20     9093  13941   6460   1406    946    187       C  
ATOM   3018  CD2 LEU D  20      -4.123 -11.206  -7.000  1.00 95.18           C  
ANISOU 3018  CD2 LEU D  20    11491  16169   8503    937   1041    341       C  
ATOM   3019  N   SER D  21      -7.917 -14.379  -6.657  1.00 87.74           N  
ANISOU 3019  N   SER D  21    11737  14313   7286    108   1196    506       N  
ATOM   3020  CA  SER D  21      -9.115 -15.178  -6.863  1.00100.84           C  
ANISOU 3020  CA  SER D  21    13657  15773   8886   -201   1296    492       C  
ATOM   3021  C   SER D  21      -9.950 -14.583  -7.988  1.00 93.72           C  
ANISOU 3021  C   SER D  21    12354  14903   8353   -135   1505    260       C  
ATOM   3022  O   SER D  21      -9.907 -13.376  -8.245  1.00 96.07           O  
ANISOU 3022  O   SER D  21    12218  15390   8894    -47   1596     76       O  
ATOM   3023  CB  SER D  21      -9.956 -15.263  -5.582  1.00111.72           C  
ANISOU 3023  CB  SER D  21    15254  17276   9919   -876   1487    431       C  
ATOM   3024  OG  SER D  21      -9.221 -15.857  -4.527  1.00138.64           O  
ANISOU 3024  OG  SER D  21    19172  20580  12925  -1028   1204    698       O  
ATOM   3025  N   CYS D  22     -10.711 -15.446  -8.660  1.00 88.42           N  
ANISOU 3025  N   CYS D  22    11888  13992   7717   -195   1505    280       N  
ATOM   3026  CA  CYS D  22     -11.591 -15.005  -9.740  1.00 87.10           C  
ANISOU 3026  CA  CYS D  22    11414  13782   7898   -156   1625     68       C  
ATOM   3027  C   CYS D  22     -12.687 -16.047  -9.913  1.00 81.28           C  
ANISOU 3027  C   CYS D  22    10959  12846   7077   -446   1691     59       C  
ATOM   3028  O   CYS D  22     -12.414 -17.157 -10.381  1.00 78.36           O  
ANISOU 3028  O   CYS D  22    10987  12197   6590   -292   1505    293       O  
ATOM   3029  CB  CYS D  22     -10.813 -14.809 -11.035  1.00 96.45           C  
ANISOU 3029  CB  CYS D  22    12482  14877   9288    296   1466    145       C  
ATOM   3030  SG  CYS D  22     -11.861 -14.433 -12.459  1.00116.15           S  
ANISOU 3030  SG  CYS D  22    14786  17197  12149    294   1477    -31       S  
ATOM   3031  N   ALA D  23     -13.913 -15.690  -9.544  1.00 84.33           N  
ANISOU 3031  N   ALA D  23    11111  13393   7539   -865   1936   -269       N  
ATOM   3032  CA  ALA D  23     -15.067 -16.567  -9.678  1.00 87.47           C  
ANISOU 3032  CA  ALA D  23    11693  13691   7850  -1241   2054   -361       C  
ATOM   3033  C   ALA D  23     -15.967 -16.068 -10.799  1.00 95.92           C  
ANISOU 3033  C   ALA D  23    12358  14682   9405  -1089   2070   -662       C  
ATOM   3034  O   ALA D  23     -16.199 -14.862 -10.933  1.00 98.49           O  
ANISOU 3034  O   ALA D  23    12188  15136  10098   -966   2066   -991       O  
ATOM   3035  CB  ALA D  23     -15.856 -16.645  -8.369  1.00 93.84           C  
ANISOU 3035  CB  ALA D  23    12508  14822   8324  -1955   2347   -620       C  
ATOM   3036  N   ALA D  24     -16.471 -17.000 -11.603  1.00 96.44           N  
ANISOU 3036  N   ALA D  24    12682  14483   9479  -1096   2010   -548       N  
ATOM   3037  CA  ALA D  24     -17.336 -16.669 -12.725  1.00 95.92           C  
ANISOU 3037  CA  ALA D  24    12322  14270   9853   -966   1953   -792       C  
ATOM   3038  C   ALA D  24     -18.792 -16.633 -12.281  1.00 95.42           C  
ANISOU 3038  C   ALA D  24    11939  14420   9895  -1449   2189  -1299       C  
ATOM   3039  O   ALA D  24     -19.253 -17.512 -11.546  1.00 87.12           O  
ANISOU 3039  O   ALA D  24    11147  13508   8448  -1967   2405  -1301       O  
ATOM   3040  CB  ALA D  24     -17.161 -17.679 -13.859  1.00100.89           C  
ANISOU 3040  CB  ALA D  24    13358  14528  10447   -737   1779   -461       C  
ATOM   3041  N   SER D  25     -19.512 -15.610 -12.734  1.00100.72           N  
ANISOU 3041  N   SER D  25    12056  15117  11097  -1314   2101  -1773       N  
ATOM   3042  CA  SER D  25     -20.917 -15.433 -12.404  1.00 98.53           C  
ANISOU 3042  CA  SER D  25    11293  15088  11056  -1688   2285  -2444       C  
ATOM   3043  C   SER D  25     -21.705 -15.116 -13.667  1.00 90.77           C  
ANISOU 3043  C   SER D  25    10058  13784  10648  -1399   1970  -2691       C  
ATOM   3044  O   SER D  25     -21.172 -14.549 -14.626  1.00 80.31           O  
ANISOU 3044  O   SER D  25     8821  12103   9590   -945   1587  -2455       O  
ATOM   3045  CB  SER D  25     -21.116 -14.316 -11.370  1.00 94.98           C  
ANISOU 3045  CB  SER D  25    10267  15051  10769  -1821   2423  -3025       C  
ATOM   3046  OG  SER D  25     -22.488 -14.143 -11.062  1.00108.13           O  
ANISOU 3046  OG  SER D  25    11343  17034  12707  -2175   2613  -3836       O  
ATOM   3047  N   GLY D  26     -22.982 -15.488 -13.657  1.00 89.38           N  
ANISOU 3047  N   GLY D  26     9588  13748  10623  -1733   2117  -3187       N  
ATOM   3048  CA  GLY D  26     -23.856 -15.229 -14.783  1.00 94.14           C  
ANISOU 3048  CA  GLY D  26     9929  14039  11802  -1490   1772  -3494       C  
ATOM   3049  C   GLY D  26     -23.825 -16.266 -15.880  1.00108.54           C  
ANISOU 3049  C   GLY D  26    12299  15460  13481  -1415   1653  -2965       C  
ATOM   3050  O   GLY D  26     -24.244 -15.967 -17.004  1.00109.60           O  
ANISOU 3050  O   GLY D  26    12368  15215  14059  -1130   1257  -3040       O  
ATOM   3051  N   ASN D  27     -23.346 -17.473 -15.597  1.00113.77           N  
ANISOU 3051  N   ASN D  27    13536  16149  13541  -1667   1916  -2448       N  
ATOM   3052  CA  ASN D  27     -23.268 -18.542 -16.581  1.00115.39           C  
ANISOU 3052  CA  ASN D  27    14284  15972  13586  -1586   1800  -1973       C  
ATOM   3053  C   ASN D  27     -24.195 -19.683 -16.183  1.00120.08           C  
ANISOU 3053  C   ASN D  27    15031  16726  13866  -2172   2088  -2090       C  
ATOM   3054  O   ASN D  27     -24.276 -20.051 -15.007  1.00120.29           O  
ANISOU 3054  O   ASN D  27    15126  17122  13456  -2697   2415  -2177       O  
ATOM   3055  CB  ASN D  27     -21.833 -19.059 -16.719  1.00113.29           C  
ANISOU 3055  CB  ASN D  27    14621  15509  12917  -1313   1729  -1289       C  
ATOM   3056  CG  ASN D  27     -21.272 -19.578 -15.410  1.00115.50           C  
ANISOU 3056  CG  ASN D  27    15177  16047  12660  -1626   1973  -1106       C  
ATOM   3057  OD1 ASN D  27     -21.578 -19.054 -14.339  1.00116.56           O  
ANISOU 3057  OD1 ASN D  27    14978  16571  12739  -1954   2200  -1457       O  
ATOM   3058  ND2 ASN D  27     -20.448 -20.616 -15.490  1.00113.56           N  
ANISOU 3058  ND2 ASN D  27    15559  15566  12022  -1533   1874   -592       N  
ATOM   3059  N   ILE D  28     -24.896 -20.238 -17.172  1.00115.70           N  
ANISOU 3059  N   ILE D  28    14576  15896  13489  -2155   1951  -2085       N  
ATOM   3060  CA  ILE D  28     -25.783 -21.364 -16.904  1.00113.26           C  
ANISOU 3060  CA  ILE D  28    14466  15714  12852  -2758   2198  -2167       C  
ATOM   3061  C   ILE D  28     -25.004 -22.675 -16.884  1.00117.40           C  
ANISOU 3061  C   ILE D  28    15879  15960  12768  -2848   2169  -1452       C  
ATOM   3062  O   ILE D  28     -25.355 -23.600 -16.142  1.00129.78           O  
ANISOU 3062  O   ILE D  28    17813  17681  13817  -3489   2373  -1389       O  
ATOM   3063  CB  ILE D  28     -26.923 -21.400 -17.936  1.00109.96           C  
ANISOU 3063  CB  ILE D  28    13754  15120  12907  -2714   2033  -2513       C  
ATOM   3064  CG1 ILE D  28     -27.627 -20.044 -17.999  1.00112.19           C  
ANISOU 3064  CG1 ILE D  28    13164  15566  13898  -2501   1876  -3277       C  
ATOM   3065  CG2 ILE D  28     -27.924 -22.495 -17.598  1.00110.62           C  
ANISOU 3065  CG2 ILE D  28    13968  15423  12640  -3433   2328  -2682       C  
ATOM   3066  CD1 ILE D  28     -28.771 -19.994 -18.988  1.00112.39           C  
ANISOU 3066  CD1 ILE D  28    12856  15377  14470  -2415   1599  -3692       C  
ATOM   3067  N   PHE D  29     -23.941 -22.776 -17.675  1.00107.42           N  
ANISOU 3067  N   PHE D  29    14984  14291  11540  -2257   1880   -959       N  
ATOM   3068  CA  PHE D  29     -23.139 -23.985 -17.778  1.00 99.68           C  
ANISOU 3068  CA  PHE D  29    14779  12984  10111  -2186   1735   -390       C  
ATOM   3069  C   PHE D  29     -21.725 -23.714 -17.277  1.00 94.07           C  
ANISOU 3069  C   PHE D  29    14235  12279   9230  -1831   1635   -106       C  
ATOM   3070  O   PHE D  29     -21.342 -22.574 -17.004  1.00 90.27           O  
ANISOU 3070  O   PHE D  29    13297  12031   8971  -1627   1692   -287       O  
ATOM   3071  CB  PHE D  29     -23.113 -24.503 -19.222  1.00 99.57           C  
ANISOU 3071  CB  PHE D  29    15017  12528  10288  -1803   1484   -173       C  
ATOM   3072  CG  PHE D  29     -24.468 -24.876 -19.754  1.00 98.29           C  
ANISOU 3072  CG  PHE D  29    14750  12313  10284  -2139   1533   -413       C  
ATOM   3073  CD1 PHE D  29     -25.309 -23.911 -20.285  1.00 91.20           C  
ANISOU 3073  CD1 PHE D  29    13220  11506   9925  -2066   1510   -865       C  
ATOM   3074  CD2 PHE D  29     -24.902 -26.190 -19.719  1.00 99.88           C  
ANISOU 3074  CD2 PHE D  29    15505  12338  10107  -2531   1530   -208       C  
ATOM   3075  CE1 PHE D  29     -26.556 -24.250 -20.770  1.00 86.90           C  
ANISOU 3075  CE1 PHE D  29    12525  10921   9571  -2349   1515  -1146       C  
ATOM   3076  CE2 PHE D  29     -26.149 -26.536 -20.204  1.00 96.97           C  
ANISOU 3076  CE2 PHE D  29    15016  11956   9871  -2873   1589   -449       C  
ATOM   3077  CZ  PHE D  29     -26.977 -25.565 -20.730  1.00 89.30           C  
ANISOU 3077  CZ  PHE D  29    13338  11120   9470  -2768   1598   -938       C  
ATOM   3078  N   ASP D  30     -20.948 -24.788 -17.158  1.00104.89           N  
ANISOU 3078  N   ASP D  30    16269  13360  10223  -1744   1426    310       N  
ATOM   3079  CA  ASP D  30     -19.599 -24.682 -16.622  1.00109.78           C  
ANISOU 3079  CA  ASP D  30    17061  13967  10682  -1406   1268    533       C  
ATOM   3080  C   ASP D  30     -18.686 -23.932 -17.585  1.00 91.42           C  
ANISOU 3080  C   ASP D  30    14406  11614   8715   -736   1168    521       C  
ATOM   3081  O   ASP D  30     -18.770 -24.097 -18.805  1.00100.18           O  
ANISOU 3081  O   ASP D  30    15516  12515  10032   -474   1075    529       O  
ATOM   3082  CB  ASP D  30     -19.027 -26.071 -16.338  1.00123.35           C  
ANISOU 3082  CB  ASP D  30    19584  15293  11990  -1416    919    903       C  
ATOM   3083  CG  ASP D  30     -19.711 -26.756 -15.172  1.00128.13           C  
ANISOU 3083  CG  ASP D  30    20668  15936  12078  -2228    957    988       C  
ATOM   3084  OD1 ASP D  30     -20.153 -26.050 -14.242  1.00131.72           O  
ANISOU 3084  OD1 ASP D  30    20797  16831  12419  -2713   1282    761       O  
ATOM   3085  OD2 ASP D  30     -19.802 -28.002 -15.183  1.00129.12           O  
ANISOU 3085  OD2 ASP D  30    21524  15656  11879  -2433    643   1258       O  
ATOM   3086  N   VAL D  31     -17.809 -23.100 -17.022  1.00 90.80           N  
ANISOU 3086  N   VAL D  31    14072  11773   8655   -538   1195    494       N  
ATOM   3087  CA  VAL D  31     -16.826 -22.386 -17.826  1.00 79.16           C  
ANISOU 3087  CA  VAL D  31    12326  10343   7408    -28   1115    478       C  
ATOM   3088  C   VAL D  31     -15.780 -23.369 -18.336  1.00 79.07           C  
ANISOU 3088  C   VAL D  31    12688  10089   7267    386    860    649       C  
ATOM   3089  O   VAL D  31     -15.328 -24.262 -17.606  1.00 93.83           O  
ANISOU 3089  O   VAL D  31    14976  11795   8880    410    651    801       O  
ATOM   3090  CB  VAL D  31     -16.184 -21.257 -17.002  1.00 76.09           C  
ANISOU 3090  CB  VAL D  31    11576  10292   7042     16   1209    390       C  
ATOM   3091  CG1 VAL D  31     -15.173 -20.494 -17.837  1.00 84.82           C  
ANISOU 3091  CG1 VAL D  31    12428  11490   8308    415   1139    364       C  
ATOM   3092  CG2 VAL D  31     -17.254 -20.317 -16.472  1.00 75.23           C  
ANISOU 3092  CG2 VAL D  31    11054  10418   7112   -355   1419    103       C  
ATOM   3093  N   ASP D  32     -15.392 -23.212 -19.601  1.00 81.88           N  
ANISOU 3093  N   ASP D  32    12908  10408   7795    689    826    576       N  
ATOM   3094  CA  ASP D  32     -14.482 -24.154 -20.241  1.00 85.26           C  
ANISOU 3094  CA  ASP D  32    13582  10660   8154   1092    612    580       C  
ATOM   3095  C   ASP D  32     -13.057 -23.994 -19.722  1.00 87.54           C  
ANISOU 3095  C   ASP D  32    13732  11151   8379   1451    498    498       C  
ATOM   3096  O   ASP D  32     -12.538 -24.884 -19.039  1.00 98.41           O  
ANISOU 3096  O   ASP D  32    15439  12327   9627   1640    202    557       O  
ATOM   3097  CB  ASP D  32     -14.520 -23.977 -21.761  1.00 76.58           C  
ANISOU 3097  CB  ASP D  32    12349   9551   7196   1189    672    457       C  
ATOM   3098  CG  ASP D  32     -13.955 -25.172 -22.502  1.00 98.55           C  
ANISOU 3098  CG  ASP D  32    15406  12116   9923   1527    477    375       C  
ATOM   3099  OD1 ASP D  32     -14.624 -26.226 -22.528  1.00108.21           O  
ANISOU 3099  OD1 ASP D  32    17051  12969  11096   1466    320    495       O  
ATOM   3100  OD2 ASP D  32     -12.844 -25.058 -23.061  1.00110.63           O  
ANISOU 3100  OD2 ASP D  32    16712  13869  11453   1829    476    137       O  
ATOM   3101  N   ILE D  33     -12.415 -22.872 -20.042  1.00 85.98           N  
ANISOU 3101  N   ILE D  33    11166  10859  10642  -1413  -3121   -383       N  
ATOM   3102  CA  ILE D  33     -11.027 -22.618 -19.673  1.00 87.44           C  
ANISOU 3102  CA  ILE D  33    11635  10854  10733  -1081  -2678   -600       C  
ATOM   3103  C   ILE D  33     -10.926 -21.221 -19.078  1.00 93.50           C  
ANISOU 3103  C   ILE D  33    12169  11927  11431   -665  -2458   -468       C  
ATOM   3104  O   ILE D  33     -11.565 -20.282 -19.565  1.00109.97           O  
ANISOU 3104  O   ILE D  33    14156  14248  13380   -568  -2613   -366       O  
ATOM   3105  CB  ILE D  33     -10.081 -22.763 -20.886  1.00106.12           C  
ANISOU 3105  CB  ILE D  33    14654  12886  12780  -1111  -2658   -967       C  
ATOM   3106  CG1 ILE D  33     -10.185 -24.165 -21.487  1.00127.43           C  
ANISOU 3106  CG1 ILE D  33    17732  15196  15491  -1515  -2844  -1139       C  
ATOM   3107  CG2 ILE D  33      -8.640 -22.468 -20.492  1.00 73.22           C  
ANISOU 3107  CG2 ILE D  33    10676   8586   8556   -772  -2203  -1080       C  
ATOM   3108  CD1 ILE D  33      -9.367 -24.352 -22.746  1.00139.94           C  
ANISOU 3108  CD1 ILE D  33    20039  16431  16703  -1511  -2802  -1490       C  
ATOM   3109  N   MET D  34     -10.125 -21.086 -18.021  1.00 85.06           N  
ANISOU 3109  N   MET D  34    11040  10842  10438   -428  -2100   -456       N  
ATOM   3110  CA  MET D  34      -9.882 -19.802 -17.381  1.00 84.16           C  
ANISOU 3110  CA  MET D  34    10838  10925  10214    -76  -1877   -388       C  
ATOM   3111  C   MET D  34      -8.384 -19.603 -17.191  1.00 79.13           C  
ANISOU 3111  C   MET D  34    10498  10112   9456     48  -1602   -581       C  
ATOM   3112  O   MET D  34      -7.629 -20.566 -17.027  1.00 75.84           O  
ANISOU 3112  O   MET D  34    10176   9505   9135    -51  -1484   -642       O  
ATOM   3113  CB  MET D  34     -10.600 -19.701 -16.029  1.00 87.91           C  
ANISOU 3113  CB  MET D  34    10875  11650  10879     76  -1749    -84       C  
ATOM   3114  CG  MET D  34     -12.076 -20.066 -16.078  1.00 99.81           C  
ANISOU 3114  CG  MET D  34    11965  13370  12586    -59  -1994    231       C  
ATOM   3115  SD  MET D  34     -12.927 -19.870 -14.500  1.00 98.50           S  
ANISOU 3115  SD  MET D  34    11285  13521  12620    226  -1752    662       S  
ATOM   3116  CE  MET D  34     -12.779 -18.103 -14.252  1.00 91.68           C  
ANISOU 3116  CE  MET D  34    10618  12774  11443    708  -1490    636       C  
ATOM   3117  N   GLY D  35      -7.962 -18.344 -17.214  1.00 70.03           N  
ANISOU 3117  N   GLY D  35     9479   9023   8105    262  -1493   -631       N  
ATOM   3118  CA  GLY D  35      -6.560 -18.025 -17.074  1.00 63.16           C  
ANISOU 3118  CA  GLY D  35     8839   8032   7127    331  -1282   -747       C  
ATOM   3119  C   GLY D  35      -6.358 -16.630 -16.523  1.00 64.86           C  
ANISOU 3119  C   GLY D  35     9108   8349   7188    523  -1168   -727       C  
ATOM   3120  O   GLY D  35      -7.310 -15.950 -16.135  1.00 72.18           O  
ANISOU 3120  O   GLY D  35     9916   9419   8089    670  -1182   -621       O  
ATOM   3121  N   TRP D  36      -5.094 -16.210 -16.498  1.00 60.67           N  
ANISOU 3121  N   TRP D  36     8774   7724   6553    519  -1040   -799       N  
ATOM   3122  CA  TRP D  36      -4.704 -14.913 -15.959  1.00 65.96           C  
ANISOU 3122  CA  TRP D  36     9587   8417   7060    612   -952   -808       C  
ATOM   3123  C   TRP D  36      -3.791 -14.197 -16.942  1.00 65.33           C  
ANISOU 3123  C   TRP D  36     9780   8194   6848    594   -936   -892       C  
ATOM   3124  O   TRP D  36      -2.852 -14.797 -17.475  1.00 64.27           O  
ANISOU 3124  O   TRP D  36     9686   7979   6753    508   -889   -891       O  
ATOM   3125  CB  TRP D  36      -3.997 -15.062 -14.606  1.00 68.94           C  
ANISOU 3125  CB  TRP D  36     9878   8871   7444    545   -847   -736       C  
ATOM   3126  CG  TRP D  36      -4.908 -15.440 -13.478  1.00 72.15           C  
ANISOU 3126  CG  TRP D  36    10059   9435   7920    630   -813   -625       C  
ATOM   3127  CD1 TRP D  36      -5.191 -16.701 -13.041  1.00 65.55           C  
ANISOU 3127  CD1 TRP D  36     8935   8678   7292    577   -803   -506       C  
ATOM   3128  CD2 TRP D  36      -5.651 -14.548 -12.638  1.00 68.64           C  
ANISOU 3128  CD2 TRP D  36     9683   9067   7331    816   -737   -591       C  
ATOM   3129  NE1 TRP D  36      -6.065 -16.649 -11.982  1.00 63.66           N  
ANISOU 3129  NE1 TRP D  36     8528   8600   7061    713   -738   -374       N  
ATOM   3130  CE2 TRP D  36      -6.363 -15.339 -11.716  1.00 60.43           C  
ANISOU 3130  CE2 TRP D  36     8348   8193   6419    886   -679   -424       C  
ATOM   3131  CE3 TRP D  36      -5.783 -13.157 -12.578  1.00 67.34           C  
ANISOU 3131  CE3 TRP D  36     9839   8813   6934    958   -673   -669       C  
ATOM   3132  CZ2 TRP D  36      -7.196 -14.786 -10.745  1.00 62.08           C  
ANISOU 3132  CZ2 TRP D  36     8564   8511   6511   1128   -540   -317       C  
ATOM   3133  CZ3 TRP D  36      -6.611 -12.610 -11.613  1.00 69.34           C  
ANISOU 3133  CZ3 TRP D  36    10157   9129   7060   1200   -525   -593       C  
ATOM   3134  CH2 TRP D  36      -7.307 -13.423 -10.710  1.00 68.59           C  
ANISOU 3134  CH2 TRP D  36     9755   9231   7077   1301   -450   -411       C  
ATOM   3135  N   TYR D  37      -4.068 -12.915 -17.172  1.00 66.35           N  
ANISOU 3135  N   TYR D  37    10100   8281   6827    710   -931   -925       N  
ATOM   3136  CA  TYR D  37      -3.235 -12.050 -17.994  1.00 58.78           C  
ANISOU 3136  CA  TYR D  37     9397   7184   5752    699   -896   -963       C  
ATOM   3137  C   TYR D  37      -2.790 -10.851 -17.170  1.00 77.09           C  
ANISOU 3137  C   TYR D  37    11914   9424   7954    666   -826   -968       C  
ATOM   3138  O   TYR D  37      -3.524 -10.372 -16.301  1.00 84.64           O  
ANISOU 3138  O   TYR D  37    12919  10398   8841    773   -787   -980       O  
ATOM   3139  CB  TYR D  37      -3.986 -11.558 -19.239  1.00 61.70           C  
ANISOU 3139  CB  TYR D  37     9884   7525   6033    857   -962   -986       C  
ATOM   3140  CG  TYR D  37      -4.368 -12.640 -20.224  1.00 77.71           C  
ANISOU 3140  CG  TYR D  37    11840   9593   8095    824  -1089  -1017       C  
ATOM   3141  CD1 TYR D  37      -5.457 -13.468 -19.988  1.00 70.24           C  
ANISOU 3141  CD1 TYR D  37    10666   8773   7251    793  -1226   -987       C  
ATOM   3142  CD2 TYR D  37      -3.652 -12.818 -21.401  1.00 76.89           C  
ANISOU 3142  CD2 TYR D  37    11934   9383   7898    812  -1070  -1063       C  
ATOM   3143  CE1 TYR D  37      -5.813 -14.453 -20.889  1.00 75.23           C  
ANISOU 3143  CE1 TYR D  37    11310   9392   7882    683  -1391  -1040       C  
ATOM   3144  CE2 TYR D  37      -4.001 -13.798 -22.308  1.00 62.77           C  
ANISOU 3144  CE2 TYR D  37    10206   7577   6065    766  -1189  -1134       C  
ATOM   3145  CZ  TYR D  37      -5.082 -14.612 -22.047  1.00 70.85           C  
ANISOU 3145  CZ  TYR D  37    11044   8694   7180    669  -1374  -1142       C  
ATOM   3146  OH  TYR D  37      -5.435 -15.591 -22.946  1.00 78.90           O  
ANISOU 3146  OH  TYR D  37    12197   9651   8129    546  -1541  -1237       O  
ATOM   3147  N   ARG D  38      -1.583 -10.362 -17.447  1.00 78.21           N  
ANISOU 3147  N   ARG D  38    12195   9461   8059    513   -802   -939       N  
ATOM   3148  CA  ARG D  38      -1.074  -9.162 -16.801  1.00 80.30           C  
ANISOU 3148  CA  ARG D  38    12722   9593   8194    388   -788   -954       C  
ATOM   3149  C   ARG D  38      -0.501  -8.219 -17.849  1.00 70.78           C  
ANISOU 3149  C   ARG D  38    11735   8211   6949    372   -758   -918       C  
ATOM   3150  O   ARG D  38      -0.061  -8.646 -18.920  1.00 67.18           O  
ANISOU 3150  O   ARG D  38    11181   7780   6562    407   -734   -840       O  
ATOM   3151  CB  ARG D  38      -0.004  -9.483 -15.743  1.00 75.26           C  
ANISOU 3151  CB  ARG D  38    11984   9045   7567     86   -845   -872       C  
ATOM   3152  CG  ARG D  38       1.373  -9.815 -16.297  1.00 75.34           C  
ANISOU 3152  CG  ARG D  38    11835   9099   7691   -110   -852   -679       C  
ATOM   3153  CD  ARG D  38       2.437  -9.637 -15.224  1.00 87.22           C  
ANISOU 3153  CD  ARG D  38    13288  10697   9157   -465   -962   -539       C  
ATOM   3154  NE  ARG D  38       3.766 -10.037 -15.679  1.00 88.49           N  
ANISOU 3154  NE  ARG D  38    13187  10970   9465   -628   -943   -238       N  
ATOM   3155  CZ  ARG D  38       4.351 -11.185 -15.355  1.00 94.65           C  
ANISOU 3155  CZ  ARG D  38    13604  11976  10384   -652   -896    -16       C  
ATOM   3156  NH1 ARG D  38       3.726 -12.050 -14.568  1.00103.90           N  
ANISOU 3156  NH1 ARG D  38    14640  13269  11567   -560   -889    -90       N  
ATOM   3157  NH2 ARG D  38       5.563 -11.467 -15.813  1.00 97.78           N  
ANISOU 3157  NH2 ARG D  38    13755  12479  10918   -739   -822    331       N  
ATOM   3158  N   GLN D  39      -0.516  -6.927 -17.528  1.00 67.37           N  
ANISOU 3158  N   GLN D  39    11644   7568   6385    337   -731   -969       N  
ATOM   3159  CA  GLN D  39      -0.018  -5.885 -18.421  1.00 82.41           C  
ANISOU 3159  CA  GLN D  39    13787   9262   8263    313   -685   -911       C  
ATOM   3160  C   GLN D  39       0.874  -4.947 -17.622  1.00 94.79           C  
ANISOU 3160  C   GLN D  39    15638  10628   9752    -40   -745   -907       C  
ATOM   3161  O   GLN D  39       0.381  -4.152 -16.814  1.00 82.74           O  
ANISOU 3161  O   GLN D  39    14476   8902   8060    -32   -716  -1048       O  
ATOM   3162  CB  GLN D  39      -1.170  -5.120 -19.075  1.00 96.15           C  
ANISOU 3162  CB  GLN D  39    15731  10879   9921    669   -574   -957       C  
ATOM   3163  CG  GLN D  39      -0.719  -4.021 -20.023  1.00106.15           C  
ANISOU 3163  CG  GLN D  39    17251  11916  11165    684   -496   -869       C  
ATOM   3164  CD  GLN D  39      -1.869  -3.414 -20.802  1.00114.19           C  
ANISOU 3164  CD  GLN D  39    18388  12886  12113   1085   -378   -842       C  
ATOM   3165  OE1 GLN D  39      -3.001  -3.895 -20.738  1.00121.17           O  
ANISOU 3165  OE1 GLN D  39    19104  13954  12982   1335   -383   -856       O  
ATOM   3166  NE2 GLN D  39      -1.584  -2.352 -21.546  1.00111.48           N  
ANISOU 3166  NE2 GLN D  39    18299  12315  11742   1141   -273   -748       N  
ATOM   3167  N   ALA D  40       2.182  -5.041 -17.845  1.00116.73           N  
ANISOU 3167  N   ALA D  40    18269  13451  12633   -355   -824   -718       N  
ATOM   3168  CA  ALA D  40       3.120  -4.155 -17.178  1.00120.03           C  
ANISOU 3168  CA  ALA D  40    18920  13697  12987   -797   -956   -661       C  
ATOM   3169  C   ALA D  40       2.999  -2.738 -17.743  1.00125.14           C  
ANISOU 3169  C   ALA D  40    20016  13959  13571   -777   -875   -697       C  
ATOM   3170  O   ALA D  40       2.561  -2.552 -18.883  1.00125.87           O  
ANISOU 3170  O   ALA D  40    20101  14004  13719   -446   -717   -655       O  
ATOM   3171  CB  ALA D  40       4.548  -4.667 -17.346  1.00121.21           C  
ANISOU 3171  CB  ALA D  40    18684  14059  13310  -1127  -1058   -333       C  
ATOM   3172  N   PRO D  41       3.368  -1.722 -16.964  1.00127.19           N  
ANISOU 3172  N   PRO D  41    20712  13924  13692  -1135   -982   -772       N  
ATOM   3173  CA  PRO D  41       3.291  -0.345 -17.472  1.00132.31           C  
ANISOU 3173  CA  PRO D  41    21845  14133  14295  -1133   -877   -795       C  
ATOM   3174  C   PRO D  41       4.250  -0.127 -18.633  1.00136.71           C  
ANISOU 3174  C   PRO D  41    22167  14704  15073  -1265   -869   -477       C  
ATOM   3175  O   PRO D  41       5.438  -0.449 -18.551  1.00143.12           O  
ANISOU 3175  O   PRO D  41    22664  15697  16018  -1672  -1041   -219       O  
ATOM   3176  CB  PRO D  41       3.670   0.504 -16.253  1.00133.23           C  
ANISOU 3176  CB  PRO D  41    22504  13925  14193  -1609  -1050   -950       C  
ATOM   3177  CG  PRO D  41       4.443  -0.419 -15.369  1.00125.43           C  
ANISOU 3177  CG  PRO D  41    21150  13305  13203  -2003  -1326   -864       C  
ATOM   3178  CD  PRO D  41       3.814  -1.765 -15.560  1.00123.18           C  
ANISOU 3178  CD  PRO D  41    20341  13440  13023  -1562  -1208   -854       C  
ATOM   3179  N   GLY D  42       3.721   0.425 -19.722  1.00133.60           N  
ANISOU 3179  N   GLY D  42    21900  14148  14714   -890   -649   -441       N  
ATOM   3180  CA  GLY D  42       4.504   0.685 -20.910  1.00130.22           C  
ANISOU 3180  CA  GLY D  42    21288  13726  14466   -918   -579   -125       C  
ATOM   3181  C   GLY D  42       4.808  -0.528 -21.762  1.00116.67           C  
ANISOU 3181  C   GLY D  42    19021  12436  12874   -692   -522     71       C  
ATOM   3182  O   GLY D  42       5.547  -0.400 -22.746  1.00116.37           O  
ANISOU 3182  O   GLY D  42    18815  12436  12965   -682   -426    377       O  
ATOM   3183  N   LYS D  43       4.266  -1.695 -21.422  1.00108.48           N  
ANISOU 3183  N   LYS D  43    17737  11690  11792   -500   -550    -80       N  
ATOM   3184  CA  LYS D  43       4.512  -2.922 -22.162  1.00 99.16           C  
ANISOU 3184  CA  LYS D  43    16142  10842  10693   -286   -476     60       C  
ATOM   3185  C   LYS D  43       3.182  -3.545 -22.566  1.00 89.23           C  
ANISOU 3185  C   LYS D  43    14890   9694   9319    158   -412   -176       C  
ATOM   3186  O   LYS D  43       2.118  -3.188 -22.054  1.00 79.67           O  
ANISOU 3186  O   LYS D  43    13883   8385   8001    286   -433   -397       O  
ATOM   3187  CB  LYS D  43       5.341  -3.917 -21.338  1.00 97.40           C  
ANISOU 3187  CB  LYS D  43    15560  10877  10569   -568   -594    182       C  
ATOM   3188  CG  LYS D  43       6.705  -3.390 -20.925  1.00 97.08           C  
ANISOU 3188  CG  LYS D  43    15412  10820  10656  -1069   -719    506       C  
ATOM   3189  CD  LYS D  43       7.469  -4.415 -20.102  1.00103.59           C  
ANISOU 3189  CD  LYS D  43    15823  11967  11572  -1307   -834    694       C  
ATOM   3190  CE  LYS D  43       8.828  -3.881 -19.680  1.00116.58           C  
ANISOU 3190  CE  LYS D  43    17289  13661  13346  -1862  -1017   1095       C  
ATOM   3191  NZ  LYS D  43       9.586  -4.869 -18.865  1.00118.35           N  
ANISOU 3191  NZ  LYS D  43    17053  14259  13657  -2079  -1132   1359       N  
ATOM   3192  N   GLU D  44       3.255  -4.490 -23.498  1.00 92.58           N  
ANISOU 3192  N   GLU D  44    15103  10322   9753    387   -329    -96       N  
ATOM   3193  CA  GLU D  44       2.063  -5.163 -23.987  1.00100.97           C  
ANISOU 3193  CA  GLU D  44    16161  11506  10697    720   -334   -287       C  
ATOM   3194  C   GLU D  44       1.609  -6.238 -23.004  1.00 93.46           C  
ANISOU 3194  C   GLU D  44    15020  10711   9778    653   -447   -453       C  
ATOM   3195  O   GLU D  44       2.386  -6.747 -22.191  1.00 96.53           O  
ANISOU 3195  O   GLU D  44    15231  11173  10273    412   -480   -383       O  
ATOM   3196  CB  GLU D  44       2.320  -5.783 -25.361  1.00100.03           C  
ANISOU 3196  CB  GLU D  44    16003  11494  10511    954   -220   -176       C  
ATOM   3197  N   ARG D  45       0.326  -6.579 -23.087  1.00 82.76           N  
ANISOU 3197  N   ARG D  45    13669   9433   8341    865   -510   -622       N  
ATOM   3198  CA  ARG D  45      -0.235  -7.612 -22.231  1.00 71.99           C  
ANISOU 3198  CA  ARG D  45    12109   8216   7027    824   -606   -746       C  
ATOM   3199  C   ARG D  45       0.328  -8.978 -22.610  1.00 71.65           C  
ANISOU 3199  C   ARG D  45    11889   8289   7045    795   -583   -709       C  
ATOM   3200  O   ARG D  45       0.662  -9.239 -23.769  1.00 89.09           O  
ANISOU 3200  O   ARG D  45    14178  10486   9185    919   -505   -651       O  
ATOM   3201  CB  ARG D  45      -1.762  -7.616 -22.337  1.00 68.67           C  
ANISOU 3201  CB  ARG D  45    11683   7875   6532   1046   -683   -847       C  
ATOM   3202  CG  ARG D  45      -2.465  -8.481 -21.302  1.00 77.53           C  
ANISOU 3202  CG  ARG D  45    12591   9136   7732   1004   -767   -926       C  
ATOM   3203  CD  ARG D  45      -3.978  -8.346 -21.395  1.00 74.06           C  
ANISOU 3203  CD  ARG D  45    12082   8807   7249   1226   -833   -918       C  
ATOM   3204  NE  ARG D  45      -4.422  -6.973 -21.165  1.00 80.23           N  
ANISOU 3204  NE  ARG D  45    13073   9462   7951   1410   -712   -865       N  
ATOM   3205  CZ  ARG D  45      -5.696  -6.606 -21.071  1.00 82.97           C  
ANISOU 3205  CZ  ARG D  45    13356   9899   8268   1670   -687   -768       C  
ATOM   3206  NH1 ARG D  45      -6.659  -7.510 -21.184  1.00 87.28           N  
ANISOU 3206  NH1 ARG D  45    13585  10701   8875   1712   -836   -700       N  
ATOM   3207  NH2 ARG D  45      -6.008  -5.334 -20.862  1.00 82.02           N  
ANISOU 3207  NH2 ARG D  45    13493   9604   8066   1887   -502   -701       N  
ATOM   3208  N   GLU D  46       0.443  -9.853 -21.612  1.00 78.19           N  
ANISOU 3208  N   GLU D  46    12516   9210   7984    660   -618   -730       N  
ATOM   3209  CA  GLU D  46       0.978 -11.190 -21.818  1.00 81.18           C  
ANISOU 3209  CA  GLU D  46    12752   9651   8440    656   -544   -674       C  
ATOM   3210  C   GLU D  46       0.203 -12.185 -20.967  1.00 76.72           C  
ANISOU 3210  C   GLU D  46    12014   9179   7959    618   -635   -783       C  
ATOM   3211  O   GLU D  46      -0.438 -11.824 -19.977  1.00 81.72           O  
ANISOU 3211  O   GLU D  46    12577   9866   8606    566   -725   -842       O  
ATOM   3212  CB  GLU D  46       2.474 -11.260 -21.482  1.00 96.29           C  
ANISOU 3212  CB  GLU D  46    14522  11596  10469    509   -414   -416       C  
ATOM   3213  CG  GLU D  46       2.810 -10.860 -20.054  1.00101.75           C  
ANISOU 3213  CG  GLU D  46    15068  12362  11229    244   -518   -355       C  
ATOM   3214  CD  GLU D  46       4.270 -11.083 -19.716  1.00108.47           C  
ANISOU 3214  CD  GLU D  46    15684  13324  12205     57   -441    -20       C  
ATOM   3215  OE1 GLU D  46       4.955 -11.799 -20.476  1.00112.22           O  
ANISOU 3215  OE1 GLU D  46    16064  13824  12750    205   -242    179       O  
ATOM   3216  OE2 GLU D  46       4.735 -10.541 -18.691  1.00111.97           O  
ANISOU 3216  OE2 GLU D  46    16050  13834  12657   -234   -576     70       O  
ATOM   3217  N   LEU D  47       0.271 -13.452 -21.369  1.00 67.88           N  
ANISOU 3217  N   LEU D  47    10862   8048   6883    661   -578   -796       N  
ATOM   3218  CA  LEU D  47      -0.382 -14.524 -20.633  1.00 69.53           C  
ANISOU 3218  CA  LEU D  47    10900   8311   7208    604   -644   -860       C  
ATOM   3219  C   LEU D  47       0.520 -15.003 -19.503  1.00 70.14           C  
ANISOU 3219  C   LEU D  47    10738   8472   7441    493   -533   -685       C  
ATOM   3220  O   LEU D  47       1.714 -15.242 -19.708  1.00 67.25           O  
ANISOU 3220  O   LEU D  47    10337   8095   7120    501   -358   -491       O  
ATOM   3221  CB  LEU D  47      -0.722 -15.685 -21.568  1.00 61.60           C  
ANISOU 3221  CB  LEU D  47    10048   7189   6168    660   -640   -963       C  
ATOM   3222  CG  LEU D  47      -1.337 -16.929 -20.921  1.00 60.96           C  
ANISOU 3222  CG  LEU D  47     9817   7104   6240    565   -697  -1006       C  
ATOM   3223  CD1 LEU D  47      -2.702 -16.614 -20.327  1.00 63.89           C  
ANISOU 3223  CD1 LEU D  47    10005   7618   6652    502   -929  -1061       C  
ATOM   3224  CD2 LEU D  47      -1.433 -18.067 -21.926  1.00 66.34           C  
ANISOU 3224  CD2 LEU D  47    10782   7573   6853    577   -669  -1122       C  
ATOM   3225  N   VAL D  48      -0.053 -15.142 -18.308  1.00 78.65           N  
ANISOU 3225  N   VAL D  48    11628   9665   8591    412   -622   -701       N  
ATOM   3226  CA  VAL D  48       0.701 -15.586 -17.141  1.00 79.61           C  
ANISOU 3226  CA  VAL D  48    11508   9918   8823    299   -554   -518       C  
ATOM   3227  C   VAL D  48       0.504 -17.084 -16.950  1.00 77.43           C  
ANISOU 3227  C   VAL D  48    11082   9627   8712    339   -465   -472       C  
ATOM   3228  O   VAL D  48       1.472 -17.852 -16.941  1.00 67.15           O  
ANISOU 3228  O   VAL D  48     9681   8320   7513    361   -281   -272       O  
ATOM   3229  CB  VAL D  48       0.283 -14.812 -15.878  1.00 73.77           C  
ANISOU 3229  CB  VAL D  48    10718   9303   8008    204   -674   -549       C  
ATOM   3230  CG1 VAL D  48       1.040 -15.331 -14.667  1.00 79.12           C  
ANISOU 3230  CG1 VAL D  48    11151  10161   8751     67   -643   -347       C  
ATOM   3231  CG2 VAL D  48       0.523 -13.325 -16.067  1.00 66.89           C  
ANISOU 3231  CG2 VAL D  48    10088   8359   6970    147   -737   -605       C  
ATOM   3232  N   ALA D  49      -0.748 -17.506 -16.796  1.00 80.02           N  
ANISOU 3232  N   ALA D  49    11380   9941   9081    353   -577   -610       N  
ATOM   3233  CA  ALA D  49      -1.056 -18.912 -16.586  1.00 77.89           C  
ANISOU 3233  CA  ALA D  49    10993   9610   8990    344   -515   -570       C  
ATOM   3234  C   ALA D  49      -2.489 -19.175 -17.022  1.00 68.96           C  
ANISOU 3234  C   ALA D  49     9909   8418   7875    314   -705   -732       C  
ATOM   3235  O   ALA D  49      -3.315 -18.261 -17.094  1.00 68.94           O  
ANISOU 3235  O   ALA D  49     9912   8510   7772    339   -862   -804       O  
ATOM   3236  CB  ALA D  49      -0.854 -19.321 -15.123  1.00 89.59           C  
ANISOU 3236  CB  ALA D  49    12164  11279  10596    300   -454   -379       C  
ATOM   3237  N   SER D  50      -2.770 -20.444 -17.311  1.00 64.25           N  
ANISOU 3237  N   SER D  50     9348   7655   7410    253   -687   -751       N  
ATOM   3238  CA  SER D  50      -4.105 -20.872 -17.701  1.00 71.85           C  
ANISOU 3238  CA  SER D  50    10316   8567   8418    129   -921   -851       C  
ATOM   3239  C   SER D  50      -4.294 -22.319 -17.274  1.00 69.94           C  
ANISOU 3239  C   SER D  50     9985   8177   8411     13   -859   -777       C  
ATOM   3240  O   SER D  50      -3.362 -23.124 -17.358  1.00 67.21           O  
ANISOU 3240  O   SER D  50     9784   7631   8122     63   -617   -738       O  
ATOM   3241  CB  SER D  50      -4.326 -20.730 -19.211  1.00 82.76           C  
ANISOU 3241  CB  SER D  50    12070   9781   9593     94  -1067  -1050       C  
ATOM   3242  OG  SER D  50      -3.442 -21.566 -19.938  1.00 85.24           O  
ANISOU 3242  OG  SER D  50    12731   9801   9855    122   -875  -1122       O  
ATOM   3243  N   ILE D  51      -5.500 -22.642 -16.814  1.00 64.43           N  
ANISOU 3243  N   ILE D  51     9038   7574   7868   -121  -1047   -708       N  
ATOM   3244  CA  ILE D  51      -5.829 -23.989 -16.363  1.00 66.28           C  
ANISOU 3244  CA  ILE D  51     9162   7658   8365   -270  -1013   -606       C  
ATOM   3245  C   ILE D  51      -7.197 -24.364 -16.917  1.00 69.18           C  
ANISOU 3245  C   ILE D  51     9505   7979   8800   -544  -1361   -642       C  
ATOM   3246  O   ILE D  51      -8.133 -23.558 -16.894  1.00 81.03           O  
ANISOU 3246  O   ILE D  51    10774   9752  10262   -547  -1578   -568       O  
ATOM   3247  CB  ILE D  51      -5.793 -24.098 -14.822  1.00 76.79           C  
ANISOU 3247  CB  ILE D  51    10064   9228   9885   -168   -848   -341       C  
ATOM   3248  CG1 ILE D  51      -6.176 -25.509 -14.368  1.00 73.46           C  
ANISOU 3248  CG1 ILE D  51     9509   8637   9767   -318   -795   -194       C  
ATOM   3249  CG2 ILE D  51      -6.692 -23.049 -14.176  1.00 70.18           C  
ANISOU 3249  CG2 ILE D  51     8930   8739   8995    -83   -977   -240       C  
ATOM   3250  CD1 ILE D  51      -6.029 -25.730 -12.880  1.00 75.01           C  
ANISOU 3250  CD1 ILE D  51     9306   9068  10128   -187   -594     97       C  
ATOM   3251  N   THR D  52      -7.306 -25.586 -17.431  1.00 74.80           N  
ANISOU 3251  N   THR D  52    10476   8337   9609   -781  -1412   -727       N  
ATOM   3252  CA  THR D  52      -8.542 -26.064 -18.024  1.00 82.34           C  
ANISOU 3252  CA  THR D  52    11448   9216  10620  -1152  -1809   -753       C  
ATOM   3253  C   THR D  52      -9.366 -26.823 -16.985  1.00 85.43           C  
ANISOU 3253  C   THR D  52    11380   9688  11390  -1322  -1852   -458       C  
ATOM   3254  O   THR D  52      -8.939 -27.043 -15.849  1.00 93.50           O  
ANISOU 3254  O   THR D  52    12130  10796  12599  -1125  -1550   -265       O  
ATOM   3255  CB  THR D  52      -8.247 -26.945 -19.237  1.00 92.09           C  
ANISOU 3255  CB  THR D  52    13339   9961  11692  -1377  -1881  -1045       C  
ATOM   3256  OG1 THR D  52      -7.597 -28.149 -18.809  1.00 80.53           O  
ANISOU 3256  OG1 THR D  52    12057   8121  10422  -1369  -1562  -1022       O  
ATOM   3257  CG2 THR D  52      -7.343 -26.213 -20.217  1.00 86.30           C  
ANISOU 3257  CG2 THR D  52    13047   9163  10581  -1139  -1759  -1282       C  
ATOM   3258  N   ASP D  53     -10.572 -27.234 -17.384  1.00 81.43           N  
ANISOU 3258  N   ASP D  53    10766   9179  10995  -1711  -2252   -383       N  
ATOM   3259  CA  ASP D  53     -11.444 -27.983 -16.487  1.00 87.86           C  
ANISOU 3259  CA  ASP D  53    11111  10071  12202  -1914  -2319    -44       C  
ATOM   3260  C   ASP D  53     -10.889 -29.361 -16.152  1.00 99.30           C  
ANISOU 3260  C   ASP D  53    12793  11064  13874  -2036  -2083    -68       C  
ATOM   3261  O   ASP D  53     -11.331 -29.972 -15.173  1.00111.31           O  
ANISOU 3261  O   ASP D  53    13901  12647  15744  -2096  -2000    250       O  
ATOM   3262  CB  ASP D  53     -12.838 -28.117 -17.101  1.00109.26           C  
ANISOU 3262  CB  ASP D  53    13633  12892  14988  -2372  -2853     95       C  
ATOM   3263  CG  ASP D  53     -12.799 -28.619 -18.532  1.00133.58           C  
ANISOU 3263  CG  ASP D  53    17368  15570  17815  -2777  -3185   -268       C  
ATOM   3264  OD1 ASP D  53     -11.856 -28.254 -19.265  1.00136.22           O  
ANISOU 3264  OD1 ASP D  53    18237  15720  17801  -2568  -3033   -618       O  
ATOM   3265  OD2 ASP D  53     -13.710 -29.378 -18.923  1.00146.31           O  
ANISOU 3265  OD2 ASP D  53    18980  17051  19560  -3319  -3606   -188       O  
ATOM   3266  N   GLY D  54      -9.937 -29.862 -16.936  1.00 96.53           N  
ANISOU 3266  N   GLY D  54    13098  10250  13330  -2032  -1928   -397       N  
ATOM   3267  CA  GLY D  54      -9.339 -31.154 -16.669  1.00 91.44           C  
ANISOU 3267  CA  GLY D  54    12741   9121  12880  -2073  -1623   -401       C  
ATOM   3268  C   GLY D  54      -8.192 -31.085 -15.683  1.00 84.04           C  
ANISOU 3268  C   GLY D  54    11616   8298  12016  -1592  -1094   -236       C  
ATOM   3269  O   GLY D  54      -7.899 -32.065 -14.991  1.00 85.29           O  
ANISOU 3269  O   GLY D  54    11720   8239  12447  -1558   -810    -49       O  
ATOM   3270  N   GLY D  55      -7.534 -29.932 -15.610  1.00 79.84           N  
ANISOU 3270  N   GLY D  55    10983   8111  11243  -1243   -975   -275       N  
ATOM   3271  CA  GLY D  55      -6.428 -29.725 -14.690  1.00 80.51           C  
ANISOU 3271  CA  GLY D  55    10859   8382  11350   -848   -559    -92       C  
ATOM   3272  C   GLY D  55      -5.094 -29.428 -15.344  1.00 93.52           C  
ANISOU 3272  C   GLY D  55    12906   9891  12737   -581   -291   -249       C  
ATOM   3273  O   GLY D  55      -4.116 -29.185 -14.623  1.00 98.64           O  
ANISOU 3273  O   GLY D  55    13343  10747  13390   -291     10    -51       O  
ATOM   3274  N   SER D  56      -4.993 -29.436 -16.671  1.00102.96           N  
ANISOU 3274  N   SER D  56    14657  10771  13691   -668   -388   -556       N  
ATOM   3275  CA  SER D  56      -3.726 -29.143 -17.328  1.00 95.78           C  
ANISOU 3275  CA  SER D  56    14108   9746  12538   -370    -87   -644       C  
ATOM   3276  C   SER D  56      -3.420 -27.653 -17.239  1.00 91.03           C  
ANISOU 3276  C   SER D  56    13242   9606  11740   -202   -176   -630       C  
ATOM   3277  O   SER D  56      -4.267 -26.813 -17.557  1.00 91.74           O  
ANISOU 3277  O   SER D  56    13252   9900  11704   -341   -529   -762       O  
ATOM   3278  CB  SER D  56      -3.768 -29.593 -18.787  1.00 97.99           C  
ANISOU 3278  CB  SER D  56    15125   9540  12566   -490   -148   -980       C  
ATOM   3279  OG  SER D  56      -3.950 -30.995 -18.883  1.00106.38           O  
ANISOU 3279  OG  SER D  56    16558  10078  13783   -656    -30  -1019       O  
ATOM   3280  N   THR D  57      -2.204 -27.328 -16.808  1.00 87.28           N  
ANISOU 3280  N   THR D  57    12628   9289  11244     86    145   -433       N  
ATOM   3281  CA  THR D  57      -1.782 -25.951 -16.606  1.00 83.96           C  
ANISOU 3281  CA  THR D  57    11980   9262  10659    202     76   -391       C  
ATOM   3282  C   THR D  57      -0.665 -25.592 -17.576  1.00 81.57           C  
ANISOU 3282  C   THR D  57    12007   8842  10144    403    289   -424       C  
ATOM   3283  O   THR D  57       0.135 -26.444 -17.974  1.00 91.04           O  
ANISOU 3283  O   THR D  57    13469   9753  11370    572    635   -334       O  
ATOM   3284  CB  THR D  57      -1.309 -25.720 -15.164  1.00 78.35           C  
ANISOU 3284  CB  THR D  57    10770   8919  10083    293    193    -77       C  
ATOM   3285  OG1 THR D  57      -0.276 -26.659 -14.841  1.00 70.47           O  
ANISOU 3285  OG1 THR D  57     9737   7806   9231    461    571    196       O  
ATOM   3286  CG2 THR D  57      -2.465 -25.892 -14.191  1.00 76.72           C  
ANISOU 3286  CG2 THR D  57    10229   8881  10042    150      3    -18       C  
ATOM   3287  N   ASN D  58      -0.620 -24.315 -17.953  1.00 72.71           N  
ANISOU 3287  N   ASN D  58    10876   7933   8818    415    120   -517       N  
ATOM   3288  CA  ASN D  58       0.403 -23.796 -18.857  1.00 72.87           C  
ANISOU 3288  CA  ASN D  58    11146   7899   8644    604    306   -499       C  
ATOM   3289  C   ASN D  58       0.873 -22.455 -18.311  1.00 73.44           C  
ANISOU 3289  C   ASN D  58    10899   8343   8662    610    221   -362       C  
ATOM   3290  O   ASN D  58       0.098 -21.495 -18.269  1.00 76.25           O  
ANISOU 3290  O   ASN D  58    11203   8848   8918    498    -67   -520       O  
ATOM   3291  CB  ASN D  58      -0.133 -23.650 -20.281  1.00 67.52           C  
ANISOU 3291  CB  ASN D  58    10966   6980   7709    571    156   -817       C  
ATOM   3292  N   TYR D  59       2.134 -22.389 -17.896  1.00 79.39           N  
ANISOU 3292  N   TYR D  59    11450   9236   9479    730    470    -39       N  
ATOM   3293  CA  TYR D  59       2.713 -21.184 -17.322  1.00 84.24           C  
ANISOU 3293  CA  TYR D  59    11794  10173  10039    657    365    118       C  
ATOM   3294  C   TYR D  59       3.652 -20.516 -18.318  1.00 80.73           C  
ANISOU 3294  C   TYR D  59    11512   9695   9466    774    500    217       C  
ATOM   3295  O   TYR D  59       4.124 -21.133 -19.277  1.00 84.70           O  
ANISOU 3295  O   TYR D  59    12276   9970   9937    987    778    266       O  
ATOM   3296  CB  TYR D  59       3.477 -21.499 -16.031  1.00 75.36           C  
ANISOU 3296  CB  TYR D  59    10247   9316   9071    624    466    488       C  
ATOM   3297  CG  TYR D  59       2.636 -22.124 -14.942  1.00 73.89           C  
ANISOU 3297  CG  TYR D  59     9863   9204   9008    538    370    457       C  
ATOM   3298  CD1 TYR D  59       2.596 -23.502 -14.774  1.00 79.92           C  
ANISOU 3298  CD1 TYR D  59    10596   9803   9967    643    597    578       C  
ATOM   3299  CD2 TYR D  59       1.888 -21.337 -14.078  1.00 72.44           C  
ANISOU 3299  CD2 TYR D  59     9552   9229   8741    383     95    333       C  
ATOM   3300  CE1 TYR D  59       1.831 -24.078 -13.778  1.00 84.85           C  
ANISOU 3300  CE1 TYR D  59    11011  10500  10728    568    525    597       C  
ATOM   3301  CE2 TYR D  59       1.119 -21.904 -13.079  1.00 74.05           C  
ANISOU 3301  CE2 TYR D  59     9560   9523   9052    349     48    356       C  
ATOM   3302  CZ  TYR D  59       1.094 -23.274 -12.934  1.00 84.44           C  
ANISOU 3302  CZ  TYR D  59    10790  10703  10589    428    251    499       C  
ATOM   3303  OH  TYR D  59       0.331 -23.844 -11.941  1.00 88.85           O  
ANISOU 3303  OH  TYR D  59    11127  11355  11277    395    219    567       O  
ATOM   3304  N   ALA D  60       3.918 -19.237 -18.074  1.00 86.14           N  
ANISOU 3304  N   ALA D  60     9598  13967   9166    430    188  -1513       N  
ATOM   3305  CA  ALA D  60       4.905 -18.510 -18.852  1.00 82.90           C  
ANISOU 3305  CA  ALA D  60     8950  13905   8644    272    494  -1658       C  
ATOM   3306  C   ALA D  60       6.307 -18.791 -18.320  1.00 97.01           C  
ANISOU 3306  C   ALA D  60    10291  15752  10815    394    441  -1833       C  
ATOM   3307  O   ALA D  60       6.491 -19.269 -17.198  1.00113.38           O  
ANISOU 3307  O   ALA D  60    12319  17563  13196    553    102  -1745       O  
ATOM   3308  CB  ALA D  60       4.618 -17.008 -18.824  1.00 70.26           C  
ANISOU 3308  CB  ALA D  60     7567  12408   6722    -44    581  -1352       C  
ATOM   3309  N   ASP D  61       7.307 -18.485 -19.149  1.00100.29           N  
ANISOU 3309  N   ASP D  61    10370  16526  11209    288    770  -2079       N  
ATOM   3310  CA  ASP D  61       8.689 -18.771 -18.780  1.00106.23           C  
ANISOU 3310  CA  ASP D  61    10580  17388  12396    419    745  -2300       C  
ATOM   3311  C   ASP D  61       9.203 -17.856 -17.676  1.00109.77           C  
ANISOU 3311  C   ASP D  61    10971  17801  12934    233    524  -1988       C  
ATOM   3312  O   ASP D  61      10.162 -18.219 -16.987  1.00107.01           O  
ANISOU 3312  O   ASP D  61    10233  17402  13026    383    298  -2073       O  
ATOM   3313  CB  ASP D  61       9.593 -18.659 -20.008  1.00113.94           C  
ANISOU 3313  CB  ASP D  61    11166  18820  13305    307   1239  -2681       C  
ATOM   3314  CG  ASP D  61       9.166 -19.584 -21.131  1.00128.91           C  
ANISOU 3314  CG  ASP D  61    13153  20751  15074    472   1476  -3045       C  
ATOM   3315  OD1 ASP D  61       8.539 -20.624 -20.840  1.00133.42           O  
ANISOU 3315  OD1 ASP D  61    13897  20964  15832    791   1190  -3099       O  
ATOM   3316  OD2 ASP D  61       9.459 -19.271 -22.304  1.00137.82           O  
ANISOU 3316  OD2 ASP D  61    14222  22260  15884    242   1941  -3275       O  
ATOM   3317  N   SER D  62       8.591 -16.688 -17.490  1.00113.43           N  
ANISOU 3317  N   SER D  62    11825  18260  13013    -79    543  -1641       N  
ATOM   3318  CA  SER D  62       9.048 -15.732 -16.491  1.00111.96           C  
ANISOU 3318  CA  SER D  62    11665  18025  12850   -295    346  -1362       C  
ATOM   3319  C   SER D  62       8.446 -15.968 -15.111  1.00117.61           C  
ANISOU 3319  C   SER D  62    12699  18329  13659   -176    -80  -1110       C  
ATOM   3320  O   SER D  62       8.922 -15.373 -14.138  1.00135.60           O  
ANISOU 3320  O   SER D  62    15006  20520  15995   -325   -308   -917       O  
ATOM   3321  CB  SER D  62       8.730 -14.303 -16.945  1.00104.68           C  
ANISOU 3321  CB  SER D  62    11050  17251  11474   -694    555  -1133       C  
ATOM   3322  OG  SER D  62       7.336 -14.125 -17.131  1.00109.52           O  
ANISOU 3322  OG  SER D  62    12157  17670  11784   -673    545   -968       O  
ATOM   3323  N   VAL D  63       7.420 -16.810 -15.000  1.00 96.44           N  
ANISOU 3323  N   VAL D  63    10279  15403  10962     38   -189  -1107       N  
ATOM   3324  CA  VAL D  63       6.774 -17.067 -13.717  1.00 81.49           C  
ANISOU 3324  CA  VAL D  63     8722  13151   9088     82   -534   -873       C  
ATOM   3325  C   VAL D  63       6.756 -18.564 -13.440  1.00 82.53           C  
ANISOU 3325  C   VAL D  63     8772  13043   9541    380   -807  -1011       C  
ATOM   3326  O   VAL D  63       6.107 -19.023 -12.493  1.00 71.80           O  
ANISOU 3326  O   VAL D  63     7732  11382   8168    395  -1085   -832       O  
ATOM   3327  CB  VAL D  63       5.349 -16.486 -13.682  1.00 72.78           C  
ANISOU 3327  CB  VAL D  63     8085  11951   7616    -30   -419   -667       C  
ATOM   3328  CG1 VAL D  63       5.376 -14.986 -13.937  1.00 83.07           C  
ANISOU 3328  CG1 VAL D  63     9516  13408   8639   -299   -225   -528       C  
ATOM   3329  CG2 VAL D  63       4.463 -17.192 -14.696  1.00 75.80           C  
ANISOU 3329  CG2 VAL D  63     8512  12362   7927    112   -262   -806       C  
ATOM   3330  N   LYS D  64       7.466 -19.334 -14.261  1.00 92.21           N  
ANISOU 3330  N   LYS D  64     9595  14393  11049    602   -724  -1344       N  
ATOM   3331  CA  LYS D  64       7.518 -20.778 -14.076  1.00 85.68           C  
ANISOU 3331  CA  LYS D  64     8696  13283  10575    921  -1023  -1512       C  
ATOM   3332  C   LYS D  64       8.269 -21.118 -12.795  1.00 97.03           C  
ANISOU 3332  C   LYS D  64    10058  14447  12361    982  -1536  -1381       C  
ATOM   3333  O   LYS D  64       9.333 -20.557 -12.517  1.00101.89           O  
ANISOU 3333  O   LYS D  64    10344  15208  13161    913  -1599  -1384       O  
ATOM   3334  CB  LYS D  64       8.188 -21.442 -15.278  1.00 84.71           C  
ANISOU 3334  CB  LYS D  64     8138  13355  10693   1170   -779  -1967       C  
ATOM   3335  N   GLY D  65       7.710 -22.041 -12.011  1.00107.03           N  
ANISOU 3335  N   GLY D  65    11651  15310  13704   1068  -1938  -1244       N  
ATOM   3336  CA  GLY D  65       8.288 -22.432 -10.745  1.00114.96           C  
ANISOU 3336  CA  GLY D  65    12716  15988  14974   1076  -2512  -1064       C  
ATOM   3337  C   GLY D  65       7.936 -21.544  -9.572  1.00106.62           C  
ANISOU 3337  C   GLY D  65    12086  14860  13564    708  -2641   -673       C  
ATOM   3338  O   GLY D  65       8.144 -21.951  -8.423  1.00111.34           O  
ANISOU 3338  O   GLY D  65    12919  15131  14253    636  -3152   -465       O  
ATOM   3339  N   ARG D  66       7.409 -20.347  -9.820  1.00 91.25           N  
ANISOU 3339  N   ARG D  66    10286  13180  11206    467  -2217   -576       N  
ATOM   3340  CA  ARG D  66       7.025 -19.413  -8.770  1.00 78.37           C  
ANISOU 3340  CA  ARG D  66     9078  11485   9216    136  -2266   -271       C  
ATOM   3341  C   ARG D  66       5.519 -19.333  -8.578  1.00 86.11           C  
ANISOU 3341  C   ARG D  66    10532  12390   9796      6  -2049   -134       C  
ATOM   3342  O   ARG D  66       5.032 -19.435  -7.447  1.00 85.74           O  
ANISOU 3342  O   ARG D  66    10911  12117   9550   -187  -2251     81       O  
ATOM   3343  CB  ARG D  66       7.579 -18.017  -9.087  1.00 71.76           C  
ANISOU 3343  CB  ARG D  66     8069  10950   8246    -45  -1992   -268       C  
ATOM   3344  CG  ARG D  66       9.092 -17.955  -9.194  1.00 83.80           C  
ANISOU 3344  CG  ARG D  66     9069  12605  10165      6  -2179   -387       C  
ATOM   3345  CD  ARG D  66       9.519 -16.758 -10.023  1.00 86.51           C  
ANISOU 3345  CD  ARG D  66     9167  13329  10374   -167  -1771   -456       C  
ATOM   3346  NE  ARG D  66       8.883 -15.527  -9.565  1.00 85.24           N  
ANISOU 3346  NE  ARG D  66     9478  13146   9762   -475  -1640   -219       N  
ATOM   3347  CZ  ARG D  66       8.875 -14.391 -10.254  1.00 92.91           C  
ANISOU 3347  CZ  ARG D  66    10444  14357  10501   -668  -1298   -213       C  
ATOM   3348  NH1 ARG D  66       9.465 -14.329 -11.440  1.00 97.06           N  
ANISOU 3348  NH1 ARG D  66    10530  15208  11141   -644  -1014   -414       N  
ATOM   3349  NH2 ARG D  66       8.271 -13.319  -9.760  1.00 95.19           N  
ANISOU 3349  NH2 ARG D  66    11193  14543  10430   -897  -1238    -20       N  
ATOM   3350  N   PHE D  67       4.765 -19.151  -9.658  1.00 86.37           N  
ANISOU 3350  N   PHE D  67    10495  12620   9702     83  -1642   -257       N  
ATOM   3351  CA  PHE D  67       3.316 -19.061  -9.579  1.00 79.52           C  
ANISOU 3351  CA  PHE D  67     9966  11714   8533    -15  -1433   -152       C  
ATOM   3352  C   PHE D  67       2.694 -20.448  -9.683  1.00 74.52           C  
ANISOU 3352  C   PHE D  67     9410  10888   8017    102  -1593   -192       C  
ATOM   3353  O   PHE D  67       3.237 -21.348 -10.329  1.00 76.40           O  
ANISOU 3353  O   PHE D  67     9399  11082   8547    332  -1729   -383       O  
ATOM   3354  CB  PHE D  67       2.757 -18.160 -10.684  1.00 76.90           C  
ANISOU 3354  CB  PHE D  67     9544  11648   8026    -10  -1010   -228       C  
ATOM   3355  CG  PHE D  67       3.102 -16.701 -10.526  1.00 77.34           C  
ANISOU 3355  CG  PHE D  67     9649  11831   7906   -179   -861   -144       C  
ATOM   3356  CD1 PHE D  67       3.843 -16.254  -9.443  1.00 88.21           C  
ANISOU 3356  CD1 PHE D  67    11141  13105   9267   -335  -1076    -24       C  
ATOM   3357  CD2 PHE D  67       2.670 -15.774 -11.460  1.00 84.99           C  
ANISOU 3357  CD2 PHE D  67    10599  12982   8711   -208   -561   -169       C  
ATOM   3358  CE1 PHE D  67       4.157 -14.914  -9.304  1.00 89.47           C  
ANISOU 3358  CE1 PHE D  67    11391  13346   9259   -514   -967     48       C  
ATOM   3359  CE2 PHE D  67       2.978 -14.433 -11.325  1.00 86.28           C  
ANISOU 3359  CE2 PHE D  67    10862  13205   8717   -378   -471    -82       C  
ATOM   3360  CZ  PHE D  67       3.722 -14.003 -10.245  1.00 87.86           C  
ANISOU 3360  CZ  PHE D  67    11173  13303   8908   -530   -661     17       C  
ATOM   3361  N   THR D  68       1.542 -20.610  -9.036  1.00 72.52           N  
ANISOU 3361  N   THR D  68     9503  10518   7534    -71  -1563    -29       N  
ATOM   3362  CA  THR D  68       0.809 -21.874  -9.050  1.00 75.50           C  
ANISOU 3362  CA  THR D  68    10016  10702   7969    -56  -1719    -17       C  
ATOM   3363  C   THR D  68      -0.671 -21.558  -9.212  1.00 81.55           C  
ANISOU 3363  C   THR D  68    10913  11587   8486   -195  -1386     48       C  
ATOM   3364  O   THR D  68      -1.294 -21.011  -8.296  1.00 91.04           O  
ANISOU 3364  O   THR D  68    12356  12793   9443   -425  -1260    198       O  
ATOM   3365  CB  THR D  68       1.058 -22.678  -7.774  1.00 76.41           C  
ANISOU 3365  CB  THR D  68    10447  10484   8100   -216  -2166    169       C  
ATOM   3366  OG1 THR D  68       2.451 -23.002  -7.676  1.00 98.79           O  
ANISOU 3366  OG1 THR D  68    13090  13184  11261    -38  -2545     98       O  
ATOM   3367  CG2 THR D  68       0.244 -23.963  -7.789  1.00 71.25           C  
ANISOU 3367  CG2 THR D  68     9988   9608   7477   -266  -2341    212       C  
ATOM   3368  N   ILE D  69      -1.229 -21.900 -10.368  1.00 73.16           N  
ANISOU 3368  N   ILE D  69     9682  10623   7494    -59  -1248    -86       N  
ATOM   3369  CA  ILE D  69      -2.631 -21.643 -10.667  1.00 68.52           C  
ANISOU 3369  CA  ILE D  69     9130  10154   6753   -161   -988    -37       C  
ATOM   3370  C   ILE D  69      -3.437 -22.899 -10.366  1.00 67.57           C  
ANISOU 3370  C   ILE D  69     9176   9845   6654   -296  -1168     40       C  
ATOM   3371  O   ILE D  69      -2.963 -24.029 -10.532  1.00 67.87           O  
ANISOU 3371  O   ILE D  69     9254   9668   6866   -211  -1481    -19       O  
ATOM   3372  CB  ILE D  69      -2.817 -21.182 -12.130  1.00 77.19           C  
ANISOU 3372  CB  ILE D  69     9990  11465   7876      4   -783   -189       C  
ATOM   3373  CG1 ILE D  69      -4.244 -20.682 -12.366  1.00 82.76           C  
ANISOU 3373  CG1 ILE D  69    10690  12286   8471    -86   -566   -113       C  
ATOM   3374  CG2 ILE D  69      -2.469 -22.300 -13.104  1.00 66.51           C  
ANISOU 3374  CG2 ILE D  69     8537  10041   6691    167   -945   -376       C  
ATOM   3375  CD1 ILE D  69      -4.473 -20.130 -13.756  1.00 57.53           C  
ANISOU 3375  CD1 ILE D  69     7334   9262   5262     29   -442   -209       C  
ATOM   3376  N   SER D  70      -4.665 -22.697  -9.894  1.00 61.85           N  
ANISOU 3376  N   SER D  70     8542   9189   5769   -517   -973    163       N  
ATOM   3377  CA  SER D  70      -5.567 -23.795  -9.581  1.00 69.20           C  
ANISOU 3377  CA  SER D  70     9624   9987   6682   -741  -1097    265       C  
ATOM   3378  C   SER D  70      -6.995 -23.322  -9.805  1.00 77.55           C  
ANISOU 3378  C   SER D  70    10528  11267   7672   -860   -768    289       C  
ATOM   3379  O   SER D  70      -7.246 -22.143 -10.068  1.00 77.16           O  
ANISOU 3379  O   SER D  70    10301  11421   7598   -747   -486    234       O  
ATOM   3380  CB  SER D  70      -5.372 -24.290  -8.144  1.00 85.21           C  
ANISOU 3380  CB  SER D  70    12014  11805   8559  -1036  -1292    452       C  
ATOM   3381  OG  SER D  70      -5.637 -23.259  -7.210  1.00 90.44           O  
ANISOU 3381  OG  SER D  70    12773  12612   8977  -1214   -995    523       O  
ATOM   3382  N   ARG D  71      -7.937 -24.255  -9.698  1.00 86.13           N  
ANISOU 3382  N   ARG D  71    11671  12294   8759  -1095   -838    375       N  
ATOM   3383  CA  ARG D  71      -9.338 -23.916  -9.898  1.00 82.73           C  
ANISOU 3383  CA  ARG D  71    11014  12086   8335  -1221   -555    392       C  
ATOM   3384  C   ARG D  71     -10.217 -24.929  -9.181  1.00 85.45           C  
ANISOU 3384  C   ARG D  71    11505  12364   8598  -1637   -604    544       C  
ATOM   3385  O   ARG D  71      -9.813 -26.067  -8.929  1.00 80.48           O  
ANISOU 3385  O   ARG D  71    11167  11465   7948  -1786   -952    633       O  
ATOM   3386  CB  ARG D  71      -9.698 -23.857 -11.387  1.00 66.86           C  
ANISOU 3386  CB  ARG D  71     8733  10167   6504   -995   -603    279       C  
ATOM   3387  CG  ARG D  71      -9.584 -25.183 -12.117  1.00 65.65           C  
ANISOU 3387  CG  ARG D  71     8687   9812   6445  -1009   -956    249       C  
ATOM   3388  CD  ARG D  71     -10.019 -25.045 -13.567  1.00 82.38           C  
ANISOU 3388  CD  ARG D  71    10595  12039   8667   -847   -988    137       C  
ATOM   3389  NE  ARG D  71     -11.452 -24.791 -13.693  1.00 85.29           N  
ANISOU 3389  NE  ARG D  71    10718  12588   9101  -1015   -858    222       N  
ATOM   3390  CZ  ARG D  71     -12.068 -24.538 -14.844  1.00 83.48           C  
ANISOU 3390  CZ  ARG D  71    10291  12463   8964   -929   -918    178       C  
ATOM   3391  NH1 ARG D  71     -11.375 -24.501 -15.974  1.00 74.01           N  
ANISOU 3391  NH1 ARG D  71     9172  11221   7727   -717  -1059     44       N  
ATOM   3392  NH2 ARG D  71     -13.376 -24.320 -14.865  1.00 77.62           N  
ANISOU 3392  NH2 ARG D  71     9265  11877   8350  -1076   -841    261       N  
ATOM   3393  N   ASP D  72     -11.430 -24.488  -8.855  1.00 83.74           N  
ANISOU 3393  N   ASP D  72    11074  12390   8355  -1832   -255    565       N  
ATOM   3394  CA  ASP D  72     -12.461 -25.329  -8.256  1.00 93.16           C  
ANISOU 3394  CA  ASP D  72    12312  13616   9470  -2294   -203    700       C  
ATOM   3395  C   ASP D  72     -13.641 -25.361  -9.219  1.00 94.65           C  
ANISOU 3395  C   ASP D  72    12066  13994   9903  -2272   -136    655       C  
ATOM   3396  O   ASP D  72     -14.380 -24.377  -9.334  1.00 91.49           O  
ANISOU 3396  O   ASP D  72    11282  13858   9623  -2154    201    561       O  
ATOM   3397  CB  ASP D  72     -12.877 -24.798  -6.884  1.00105.16           C  
ANISOU 3397  CB  ASP D  72    13924  15303  10731  -2608    209    737       C  
ATOM   3398  CG  ASP D  72     -13.832 -25.728  -6.159  1.00118.29           C  
ANISOU 3398  CG  ASP D  72    15689  17016  12240  -3188    290    893       C  
ATOM   3399  OD1 ASP D  72     -14.038 -26.866  -6.632  1.00123.23           O  
ANISOU 3399  OD1 ASP D  72    16393  17475  12953  -3358    -62   1010       O  
ATOM   3400  OD2 ASP D  72     -14.380 -25.320  -5.113  1.00122.47           O  
ANISOU 3400  OD2 ASP D  72    16242  17753  12539  -3503    719    886       O  
ATOM   3401  N   ASN D  73     -13.814 -26.490  -9.911  1.00102.93           N  
ANISOU 3401  N   ASN D  73    13184  14877  11050  -2378   -498    716       N  
ATOM   3402  CA  ASN D  73     -14.863 -26.598 -10.920  1.00101.92           C  
ANISOU 3402  CA  ASN D  73    12681  14891  11152  -2379   -539    690       C  
ATOM   3403  C   ASN D  73     -16.261 -26.511 -10.324  1.00107.14           C  
ANISOU 3403  C   ASN D  73    13002  15840  11867  -2752   -209    758       C  
ATOM   3404  O   ASN D  73     -17.218 -26.248 -11.061  1.00101.90           O  
ANISOU 3404  O   ASN D  73    11894  15364  11458  -2701   -178    719       O  
ATOM   3405  CB  ASN D  73     -14.713 -27.907 -11.696  1.00 97.04           C  
ANISOU 3405  CB  ASN D  73    12296  13991  10584  -2465  -1019    728       C  
ATOM   3406  CG  ASN D  73     -13.408 -27.983 -12.464  1.00 96.74           C  
ANISOU 3406  CG  ASN D  73    12489  13717  10551  -2054  -1288    582       C  
ATOM   3407  OD1 ASN D  73     -12.873 -26.965 -12.903  1.00101.08           O  
ANISOU 3407  OD1 ASN D  73    12895  14387  11122  -1695  -1139    455       O  
ATOM   3408  ND2 ASN D  73     -12.888 -29.193 -12.630  1.00108.40           N  
ANISOU 3408  ND2 ASN D  73    14318  14849  12019  -2115  -1682    585       N  
ATOM   3409  N   ALA D  74     -16.404 -26.724  -9.015  1.00114.56           N  
ANISOU 3409  N   ALA D  74    14129  16828  12571  -3146     34    852       N  
ATOM   3410  CA  ALA D  74     -17.721 -26.643  -8.392  1.00118.98           C  
ANISOU 3410  CA  ALA D  74    14330  17717  13162  -3542    441    875       C  
ATOM   3411  C   ALA D  74     -18.216 -25.202  -8.341  1.00116.26           C  
ANISOU 3411  C   ALA D  74    13488  17687  13000  -3221    912    668       C  
ATOM   3412  O   ALA D  74     -19.372 -24.920  -8.680  1.00121.98           O  
ANISOU 3412  O   ALA D  74    13644  18677  14026  -3240   1097    601       O  
ATOM   3413  CB  ALA D  74     -17.677 -27.250  -6.990  1.00127.22           C  
ANISOU 3413  CB  ALA D  74    15791  18730  13818  -4109    599   1026       C  
ATOM   3414  N   LYS D  75     -17.355 -24.277  -7.924  1.00111.56           N  
ANISOU 3414  N   LYS D  75    13089  17039  12259  -2918   1073    560       N  
ATOM   3415  CA  LYS D  75     -17.717 -22.872  -7.798  1.00109.36           C  
ANISOU 3415  CA  LYS D  75    12437  16977  12138  -2592   1488    346       C  
ATOM   3416  C   LYS D  75     -17.286 -22.034  -8.994  1.00113.18           C  
ANISOU 3416  C   LYS D  75    12764  17362  12877  -2024   1243    260       C  
ATOM   3417  O   LYS D  75     -17.539 -20.824  -9.004  1.00115.51           O  
ANISOU 3417  O   LYS D  75    12787  17762  13340  -1708   1493     94       O  
ATOM   3418  CB  LYS D  75     -17.114 -22.286  -6.516  1.00102.60           C  
ANISOU 3418  CB  LYS D  75    11941  16119  10924  -2675   1836    273       C  
ATOM   3419  N   ASN D  76     -16.652 -22.644  -9.996  1.00113.88           N  
ANISOU 3419  N   ASN D  76    13046  17238  12984  -1906    764    355       N  
ATOM   3420  CA  ASN D  76     -16.160 -21.937 -11.180  1.00110.51           C  
ANISOU 3420  CA  ASN D  76    12557  16725  12709  -1457    525    292       C  
ATOM   3421  C   ASN D  76     -15.248 -20.777 -10.788  1.00103.80           C  
ANISOU 3421  C   ASN D  76    11887  15824  11730  -1171    700    193       C  
ATOM   3422  O   ASN D  76     -15.390 -19.647 -11.260  1.00110.50           O  
ANISOU 3422  O   ASN D  76    12529  16711  12747   -853    759    101       O  
ATOM   3423  CB  ASN D  76     -17.319 -21.458 -12.057  1.00106.10           C  
ANISOU 3423  CB  ASN D  76    11470  16319  12525  -1308    485    252       C  
ATOM   3424  CG  ASN D  76     -18.001 -22.595 -12.792  1.00105.96           C  
ANISOU 3424  CG  ASN D  76    11332  16297  12632  -1555    160    366       C  
ATOM   3425  OD1 ASN D  76     -19.205 -22.809 -12.650  1.00107.59           O  
ANISOU 3425  OD1 ASN D  76    11119  16693  13067  -1770    264    386       O  
ATOM   3426  ND2 ASN D  76     -17.232 -23.332 -13.585  1.00100.62           N  
ANISOU 3426  ND2 ASN D  76    11011  15406  11815  -1536   -228    417       N  
ATOM   3427  N   THR D  77     -14.298 -21.072  -9.905  1.00 85.31           N  
ANISOU 3427  N   THR D  77     9963  13362   9090  -1310    729    230       N  
ATOM   3428  CA  THR D  77     -13.337 -20.097  -9.416  1.00 80.16           C  
ANISOU 3428  CA  THR D  77     9538  12641   8278  -1120    850    159       C  
ATOM   3429  C   THR D  77     -11.930 -20.554  -9.774  1.00 71.65           C  
ANISOU 3429  C   THR D  77     8798  11354   7072  -1035    502    216       C  
ATOM   3430  O   THR D  77     -11.663 -21.754  -9.886  1.00 69.33           O  
ANISOU 3430  O   THR D  77     8668  10933   6741  -1193    234    302       O  
ATOM   3431  CB  THR D  77     -13.462 -19.911  -7.894  1.00 80.62           C  
ANISOU 3431  CB  THR D  77     9784  12758   8088  -1390   1211    133       C  
ATOM   3432  OG1 THR D  77     -14.846 -19.818  -7.536  1.00 82.51           O  
ANISOU 3432  OG1 THR D  77     9661  13231   8460  -1546   1571     55       O  
ATOM   3433  CG2 THR D  77     -12.751 -18.643  -7.441  1.00 70.69           C  
ANISOU 3433  CG2 THR D  77     8695  11452   6714  -1175   1375     21       C  
ATOM   3434  N   VAL D  78     -11.032 -19.590  -9.966  1.00 64.39           N  
ANISOU 3434  N   VAL D  78     7964  10390   6113   -783    501    154       N  
ATOM   3435  CA  VAL D  78      -9.635 -19.860 -10.284  1.00 65.47           C  
ANISOU 3435  CA  VAL D  78     8328  10379   6170   -682    231    167       C  
ATOM   3436  C   VAL D  78      -8.759 -19.075  -9.319  1.00 75.09           C  
ANISOU 3436  C   VAL D  78     9780  11544   7208   -689    335    159       C  
ATOM   3437  O   VAL D  78      -8.970 -17.874  -9.118  1.00 70.21           O  
ANISOU 3437  O   VAL D  78     9113  10991   6574   -587    565     92       O  
ATOM   3438  CB  VAL D  78      -9.298 -19.501 -11.743  1.00 78.30           C  
ANISOU 3438  CB  VAL D  78     9803  12030   7917   -418     83    104       C  
ATOM   3439  CG1 VAL D  78      -7.794 -19.483 -11.957  1.00 80.37           C  
ANISOU 3439  CG1 VAL D  78    10227  12208   8104   -309    -71     65       C  
ATOM   3440  CG2 VAL D  78      -9.944 -20.496 -12.679  1.00 83.11           C  
ANISOU 3440  CG2 VAL D  78    10290  12641   8648   -456   -108    112       C  
ATOM   3441  N   TYR D  79      -7.781 -19.753  -8.726  1.00 84.52           N  
ANISOU 3441  N   TYR D  79    11242  12585   8285   -807    118    225       N  
ATOM   3442  CA  TYR D  79      -6.882 -19.160  -7.746  1.00 82.96           C  
ANISOU 3442  CA  TYR D  79    11306  12310   7905   -873    125    248       C  
ATOM   3443  C   TYR D  79      -5.469 -19.127  -8.310  1.00 83.24           C  
ANISOU 3443  C   TYR D  79    11333  12265   8029   -685   -148    224       C  
ATOM   3444  O   TYR D  79      -4.981 -20.134  -8.833  1.00 95.20           O  
ANISOU 3444  O   TYR D  79    12803  13688   9680   -620   -419    219       O  
ATOM   3445  CB  TYR D  79      -6.913 -19.946  -6.434  1.00 77.86           C  
ANISOU 3445  CB  TYR D  79    11000  11542   7043  -1225     49    372       C  
ATOM   3446  CG  TYR D  79      -8.309 -20.221  -5.922  1.00 76.45           C  
ANISOU 3446  CG  TYR D  79    10796  11483   6767  -1488    344    389       C  
ATOM   3447  CD1 TYR D  79      -8.968 -19.304  -5.114  1.00 89.41           C  
ANISOU 3447  CD1 TYR D  79    12473  13261   8236  -1601    766    302       C  
ATOM   3448  CD2 TYR D  79      -8.969 -21.399  -6.249  1.00 77.02           C  
ANISOU 3448  CD2 TYR D  79    10795  11538   6931  -1636    217    466       C  
ATOM   3449  CE1 TYR D  79     -10.245 -19.552  -4.646  1.00 99.06           C  
ANISOU 3449  CE1 TYR D  79    13596  14646   9395  -1853   1100    276       C  
ATOM   3450  CE2 TYR D  79     -10.246 -21.656  -5.786  1.00 95.47           C  
ANISOU 3450  CE2 TYR D  79    13055  14026   9193  -1930    506    485       C  
ATOM   3451  CZ  TYR D  79     -10.879 -20.729  -4.985  1.00100.47           C  
ANISOU 3451  CZ  TYR D  79    13661  14841   9671  -2036    971    382       C  
ATOM   3452  OH  TYR D  79     -12.150 -20.980  -4.521  1.00 96.69           O  
ANISOU 3452  OH  TYR D  79    13034  14563   9142  -2339   1322    361       O  
ATOM   3453  N   LEU D  80      -4.818 -17.971  -8.206  1.00 77.77           N  
ANISOU 3453  N   LEU D  80    10670  11605   7275   -606    -67    188       N  
ATOM   3454  CA  LEU D  80      -3.441 -17.788  -8.656  1.00 75.70           C  
ANISOU 3454  CA  LEU D  80    10350  11319   7095   -481   -271    160       C  
ATOM   3455  C   LEU D  80      -2.577 -17.526  -7.427  1.00 91.84           C  
ANISOU 3455  C   LEU D  80    12665  13236   8993   -649   -412    240       C  
ATOM   3456  O   LEU D  80      -2.565 -16.414  -6.891  1.00 96.23           O  
ANISOU 3456  O   LEU D  80    13370  13807   9388   -720   -252    239       O  
ATOM   3457  CB  LEU D  80      -3.338 -16.646  -9.663  1.00 71.82           C  
ANISOU 3457  CB  LEU D  80     9683  10965   6639   -318   -115     85       C  
ATOM   3458  CG  LEU D  80      -1.945 -16.404 -10.250  1.00 70.43           C  
ANISOU 3458  CG  LEU D  80     9392  10836   6533   -244   -252     40       C  
ATOM   3459  CD1 LEU D  80      -1.524 -17.565 -11.141  1.00 57.24           C  
ANISOU 3459  CD1 LEU D  80     7517   9192   5041   -119   -404    -57       C  
ATOM   3460  CD2 LEU D  80      -1.894 -15.088 -11.011  1.00 77.32           C  
ANISOU 3460  CD2 LEU D  80    10211  11821   7347   -200    -93     19       C  
ATOM   3461  N   ALA D  81      -1.858 -18.553  -6.983  1.00 96.05           N  
ANISOU 3461  N   ALA D  81    13290  13610   9593   -714   -757    308       N  
ATOM   3462  CA  ALA D  81      -0.981 -18.449  -5.822  1.00 76.78           C  
ANISOU 3462  CA  ALA D  81    11126  11014   7033   -899  -1010    417       C  
ATOM   3463  C   ALA D  81       0.378 -17.931  -6.280  1.00 81.31           C  
ANISOU 3463  C   ALA D  81    11477  11631   7788   -753  -1174    361       C  
ATOM   3464  O   ALA D  81       1.160 -18.670  -6.888  1.00 77.68           O  
ANISOU 3464  O   ALA D  81    10754  11146   7614   -576  -1412    295       O  
ATOM   3465  CB  ALA D  81      -0.850 -19.797  -5.120  1.00 81.40           C  
ANISOU 3465  CB  ALA D  81    11932  11360   7636  -1048  -1392    546       C  
ATOM   3466  N   MET D  82       0.656 -16.664  -5.992  1.00 81.15           N  
ANISOU 3466  N   MET D  82    11548  11674   7613   -837  -1036    367       N  
ATOM   3467  CA  MET D  82       1.915 -16.031  -6.360  1.00 79.68           C  
ANISOU 3467  CA  MET D  82    11154  11556   7563   -786  -1163    336       C  
ATOM   3468  C   MET D  82       2.881 -16.098  -5.185  1.00 81.93           C  
ANISOU 3468  C   MET D  82    11658  11661   7809   -986  -1557    464       C  
ATOM   3469  O   MET D  82       2.531 -15.712  -4.065  1.00 69.73           O  
ANISOU 3469  O   MET D  82    10549   9992   5955  -1235  -1559    563       O  
ATOM   3470  CB  MET D  82       1.689 -14.578  -6.783  1.00 83.05           C  
ANISOU 3470  CB  MET D  82    11593  12114   7848   -798   -851    292       C  
ATOM   3471  CG  MET D  82       0.772 -14.421  -7.987  1.00 94.66           C  
ANISOU 3471  CG  MET D  82    12868  13734   9364   -614   -547    196       C  
ATOM   3472  SD  MET D  82       0.639 -12.718  -8.568  1.00 98.23           S  
ANISOU 3472  SD  MET D  82    13367  14262   9694   -627   -311    178       S  
ATOM   3473  CE  MET D  82      -0.123 -11.929  -7.154  1.00 94.00           C  
ANISOU 3473  CE  MET D  82    13283  13535   8897   -767   -188    202       C  
ATOM   3474  N   ALA D  83       4.090 -16.594  -5.443  1.00 90.84           N  
ANISOU 3474  N   ALA D  83    12479  12778   9258   -884  -1894    445       N  
ATOM   3475  CA  ALA D  83       5.116 -16.716  -4.418  1.00 86.59           C  
ANISOU 3475  CA  ALA D  83    12074  12055   8772  -1052  -2375    579       C  
ATOM   3476  C   ALA D  83       6.444 -16.231  -4.978  1.00100.05           C  
ANISOU 3476  C   ALA D  83    13321  13914  10778   -976  -2494    503       C  
ATOM   3477  O   ALA D  83       6.675 -16.273  -6.190  1.00113.58           O  
ANISOU 3477  O   ALA D  83    14578  15854  12722   -757  -2265    326       O  
ATOM   3478  CB  ALA D  83       5.250 -18.161  -3.918  1.00 80.91           C  
ANISOU 3478  CB  ALA D  83    11434  11073   8234  -1010  -2831    660       C  
ATOM   3479  N   SER D  84       7.316 -15.774  -4.078  1.00100.25           N  
ANISOU 3479  N   SER D  84    13481  13831  10778  -1202  -2851    637       N  
ATOM   3480  CA  SER D  84       8.617 -15.215  -4.443  1.00 99.26           C  
ANISOU 3480  CA  SER D  84    12916  13866  10933  -1218  -2989    592       C  
ATOM   3481  C   SER D  84       8.455 -14.080  -5.452  1.00 92.04           C  
ANISOU 3481  C   SER D  84    11835  13245   9892  -1236  -2482    484       C  
ATOM   3482  O   SER D  84       9.044 -14.082  -6.535  1.00 94.21           O  
ANISOU 3482  O   SER D  84    11585  13778  10434  -1099  -2317    330       O  
ATOM   3483  CB  SER D  84       9.553 -16.300  -4.979  1.00104.96           C  
ANISOU 3483  CB  SER D  84    13040  14617  12222   -926  -3277    460       C  
ATOM   3484  OG  SER D  84      10.800 -15.752  -5.368  1.00116.72           O  
ANISOU 3484  OG  SER D  84    14015  16324  14010   -961  -3346    386       O  
ATOM   3485  N   LEU D  85       7.637 -13.098  -5.081  1.00 83.84           N  
ANISOU 3485  N   LEU D  85    11274  12150   8432  -1421  -2236    556       N  
ATOM   3486  CA  LEU D  85       7.311 -12.007  -5.988  1.00 80.54           C  
ANISOU 3486  CA  LEU D  85    10810  11921   7871  -1440  -1818    488       C  
ATOM   3487  C   LEU D  85       8.521 -11.115  -6.231  1.00 86.74           C  
ANISOU 3487  C   LEU D  85    11355  12849   8753  -1652  -1918    517       C  
ATOM   3488  O   LEU D  85       9.276 -10.793  -5.310  1.00 74.21           O  
ANISOU 3488  O   LEU D  85     9903  11138   7154  -1889  -2272    636       O  
ATOM   3489  CB  LEU D  85       6.151 -11.183  -5.430  1.00 79.02           C  
ANISOU 3489  CB  LEU D  85    11183  11569   7271  -1542  -1586    529       C  
ATOM   3490  CG  LEU D  85       4.780 -11.856  -5.501  1.00 86.98           C  
ANISOU 3490  CG  LEU D  85    12327  12533   8190  -1349  -1339    470       C  
ATOM   3491  CD1 LEU D  85       3.716 -10.995  -4.843  1.00 83.17           C  
ANISOU 3491  CD1 LEU D  85    12331  11910   7360  -1443  -1094    462       C  
ATOM   3492  CD2 LEU D  85       4.414 -12.146  -6.948  1.00108.50           C  
ANISOU 3492  CD2 LEU D  85    14661  15472  11093  -1102  -1075    353       C  
ATOM   3493  N   LYS D  86       8.698 -10.718  -7.485  1.00101.55           N  
ANISOU 3493  N   LYS D  86    12894  14992  10700  -1615  -1617    420       N  
ATOM   3494  CA  LYS D  86       9.777  -9.853  -7.927  1.00 95.10           C  
ANISOU 3494  CA  LYS D  86    11810  14376   9949  -1870  -1623    442       C  
ATOM   3495  C   LYS D  86       9.235  -8.486  -8.326  1.00 97.54           C  
ANISOU 3495  C   LYS D  86    12487  14661   9911  -2067  -1369    512       C  
ATOM   3496  O   LYS D  86       8.047  -8.345  -8.638  1.00 97.90           O  
ANISOU 3496  O   LYS D  86    12818  14616   9765  -1911  -1128    487       O  
ATOM   3497  CB  LYS D  86      10.514 -10.483  -9.118  1.00 80.31           C  
ANISOU 3497  CB  LYS D  86     9256  12855   8405  -1738  -1457    258       C  
ATOM   3498  CG  LYS D  86      11.142 -11.833  -8.818  1.00 92.41           C  
ANISOU 3498  CG  LYS D  86    10364  14375  10373  -1485  -1741    144       C  
ATOM   3499  CD  LYS D  86      11.826 -12.405 -10.049  1.00 99.15           C  
ANISOU 3499  CD  LYS D  86    10539  15584  11549  -1322  -1493   -118       C  
ATOM   3500  CE  LYS D  86      12.408 -13.781  -9.770  1.00116.13           C  
ANISOU 3500  CE  LYS D  86    12265  17657  14202   -993  -1807   -275       C  
ATOM   3501  NZ  LYS D  86      13.044 -14.369 -10.981  1.00128.78           N  
ANISOU 3501  NZ  LYS D  86    13199  19602  16130   -791  -1505   -611       N  
ATOM   3502  N   PRO D  87      10.077  -7.448  -8.322  1.00101.55           N  
ANISOU 3502  N   PRO D  87    12999  15224  10360  -2418  -1459    609       N  
ATOM   3503  CA  PRO D  87       9.605  -6.127  -8.769  1.00108.94           C  
ANISOU 3503  CA  PRO D  87    14322  16083  10987  -2615  -1276    688       C  
ATOM   3504  C   PRO D  87       9.186  -6.093 -10.228  1.00111.99           C  
ANISOU 3504  C   PRO D  87    14526  16695  11329  -2531   -923    620       C  
ATOM   3505  O   PRO D  87       8.492  -5.153 -10.635  1.00112.67           O  
ANISOU 3505  O   PRO D  87    14997  16644  11171  -2602   -809    691       O  
ATOM   3506  CB  PRO D  87      10.811  -5.213  -8.507  1.00103.70           C  
ANISOU 3506  CB  PRO D  87    13619  15462  10319  -3062  -1500    814       C  
ATOM   3507  CG  PRO D  87      11.986  -6.134  -8.449  1.00 97.41           C  
ANISOU 3507  CG  PRO D  87    12170  14928   9912  -3060  -1674    752       C  
ATOM   3508  CD  PRO D  87      11.469  -7.401  -7.842  1.00 96.82           C  
ANISOU 3508  CD  PRO D  87    12083  14717   9989  -2671  -1789    668       C  
ATOM   3509  N   GLU D  88       9.583  -7.083 -11.031  1.00113.06           N  
ANISOU 3509  N   GLU D  88    14121  17145  11692  -2382   -774    474       N  
ATOM   3510  CA  GLU D  88       9.139  -7.144 -12.417  1.00104.13           C  
ANISOU 3510  CA  GLU D  88    12881  16226  10457  -2325   -442    393       C  
ATOM   3511  C   GLU D  88       7.682  -7.571 -12.539  1.00 96.41           C  
ANISOU 3511  C   GLU D  88    12187  15059   9387  -1983   -345    357       C  
ATOM   3512  O   GLU D  88       7.056  -7.304 -13.570  1.00112.82           O  
ANISOU 3512  O   GLU D  88    14368  17199  11301  -1976   -153    358       O  
ATOM   3513  CB  GLU D  88      10.026  -8.101 -13.219  1.00105.44           C  
ANISOU 3513  CB  GLU D  88    12395  16786  10882  -2268   -277    186       C  
ATOM   3514  CG  GLU D  88      11.453  -7.614 -13.443  1.00123.50           C  
ANISOU 3514  CG  GLU D  88    14275  19376  13275  -2651   -262    186       C  
ATOM   3515  CD  GLU D  88      12.348  -7.815 -12.233  1.00129.14           C  
ANISOU 3515  CD  GLU D  88    14772  19999  14295  -2681   -638    225       C  
ATOM   3516  OE1 GLU D  88      11.867  -8.349 -11.212  1.00130.80           O  
ANISOU 3516  OE1 GLU D  88    15210  19899  14587  -2426   -912    261       O  
ATOM   3517  OE2 GLU D  88      13.537  -7.440 -12.306  1.00134.09           O  
ANISOU 3517  OE2 GLU D  88    15003  20871  15072  -2998   -676    231       O  
ATOM   3518  N   ASP D  89       7.131  -8.221 -11.515  1.00 83.92           N  
ANISOU 3518  N   ASP D  89    10739  13252   7895  -1740   -491    340       N  
ATOM   3519  CA  ASP D  89       5.750  -8.687 -11.545  1.00 79.93           C  
ANISOU 3519  CA  ASP D  89    10439  12596   7334  -1449   -390    301       C  
ATOM   3520  C   ASP D  89       4.739  -7.584 -11.264  1.00 70.04           C  
ANISOU 3520  C   ASP D  89     9674  11079   5860  -1469   -359    397       C  
ATOM   3521  O   ASP D  89       3.538  -7.870 -11.209  1.00 64.68           O  
ANISOU 3521  O   ASP D  89     9128  10279   5168  -1235   -270    358       O  
ATOM   3522  CB  ASP D  89       5.557  -9.824 -10.537  1.00 97.09           C  
ANISOU 3522  CB  ASP D  89    12584  14643   9661  -1252   -545    254       C  
ATOM   3523  CG  ASP D  89       6.325 -11.075 -10.915  1.00112.31           C  
ANISOU 3523  CG  ASP D  89    14034  16758  11880  -1116   -604    118       C  
ATOM   3524  OD1 ASP D  89       6.958 -11.084 -11.991  1.00117.79           O  
ANISOU 3524  OD1 ASP D  89    14385  17724  12646  -1158   -448     15       O  
ATOM   3525  OD2 ASP D  89       6.294 -12.050 -10.135  1.00112.56           O  
ANISOU 3525  OD2 ASP D  89    14053  16652  12062   -978   -808    103       O  
ATOM   3526  N   THR D  90       5.185  -6.342 -11.085  1.00 66.28           N  
ANISOU 3526  N   THR D  90     9447  10496   5240  -1735   -440    506       N  
ATOM   3527  CA  THR D  90       4.274  -5.231 -10.829  1.00 70.31           C  
ANISOU 3527  CA  THR D  90    10431  10698   5586  -1716   -440    560       C  
ATOM   3528  C   THR D  90       3.469  -4.937 -12.089  1.00 79.64           C  
ANISOU 3528  C   THR D  90    11631  11904   6726  -1614   -321    581       C  
ATOM   3529  O   THR D  90       3.993  -4.368 -13.052  1.00 85.01           O  
ANISOU 3529  O   THR D  90    12297  12700   7303  -1857   -326    674       O  
ATOM   3530  CB  THR D  90       5.053  -3.998 -10.381  1.00 68.75           C  
ANISOU 3530  CB  THR D  90    10529  10343   5249  -2056   -610    672       C  
ATOM   3531  OG1 THR D  90       5.802  -4.306  -9.199  1.00 74.54           O  
ANISOU 3531  OG1 THR D  90    11263  11045   6015  -2175   -782    668       O  
ATOM   3532  CG2 THR D  90       4.102  -2.847 -10.084  1.00 70.03           C  
ANISOU 3532  CG2 THR D  90    11209  10120   5281  -1983   -629    681       C  
ATOM   3533  N   ALA D  91       2.196  -5.324 -12.084  1.00 69.75           N  
ANISOU 3533  N   ALA D  91    10416  10545   5541  -1298   -234    508       N  
ATOM   3534  CA  ALA D  91       1.324  -5.119 -13.232  1.00 66.59           C  
ANISOU 3534  CA  ALA D  91    10031  10135   5134  -1179   -198    539       C  
ATOM   3535  C   ALA D  91      -0.121  -5.273 -12.780  1.00 69.69           C  
ANISOU 3535  C   ALA D  91    10496  10331   5654   -838   -143    452       C  
ATOM   3536  O   ALA D  91      -0.401  -5.627 -11.632  1.00 69.61           O  
ANISOU 3536  O   ALA D  91    10517  10241   5691   -731    -72    355       O  
ATOM   3537  CB  ALA D  91       1.650  -6.099 -14.364  1.00 71.41           C  
ANISOU 3537  CB  ALA D  91    10292  11084   5756  -1205   -106    508       C  
ATOM   3538  N   VAL D  92      -1.037  -4.998 -13.702  1.00 74.27           N  
ANISOU 3538  N   VAL D  92    11097  10841   6282   -701   -184    490       N  
ATOM   3539  CA  VAL D  92      -2.465  -5.188 -13.479  1.00 70.25           C  
ANISOU 3539  CA  VAL D  92    10536  10195   5961   -372   -134    398       C  
ATOM   3540  C   VAL D  92      -2.847  -6.550 -14.039  1.00 61.44           C  
ANISOU 3540  C   VAL D  92     9081   9336   4927   -275    -60    357       C  
ATOM   3541  O   VAL D  92      -2.690  -6.803 -15.239  1.00 81.10           O  
ANISOU 3541  O   VAL D  92    11489  11975   7352   -360   -130    425       O  
ATOM   3542  CB  VAL D  92      -3.293  -4.069 -14.129  1.00 72.24           C  
ANISOU 3542  CB  VAL D  92    10990  10168   6291   -252   -313    471       C  
ATOM   3543  CG1 VAL D  92      -4.779  -4.350 -13.969  1.00 65.95           C  
ANISOU 3543  CG1 VAL D  92    10010   9279   5770    108   -260    353       C  
ATOM   3544  CG2 VAL D  92      -2.933  -2.728 -13.517  1.00 67.76           C  
ANISOU 3544  CG2 VAL D  92    10812   9280   5655   -336   -413    489       C  
ATOM   3545  N   TYR D  93      -3.345  -7.427 -13.174  1.00 67.21           N  
ANISOU 3545  N   TYR D  93     9663  10108   5765   -138     78    243       N  
ATOM   3546  CA  TYR D  93      -3.663  -8.798 -13.544  1.00 71.22           C  
ANISOU 3546  CA  TYR D  93     9893  10815   6352    -74    121    201       C  
ATOM   3547  C   TYR D  93      -5.139  -8.911 -13.904  1.00 80.14           C  
ANISOU 3547  C   TYR D  93    10893  11888   7667    138    119    178       C  
ATOM   3548  O   TYR D  93      -6.008  -8.530 -13.114  1.00 67.42           O  
ANISOU 3548  O   TYR D  93     9293  10142   6183    284    221    102       O  
ATOM   3549  CB  TYR D  93      -3.309  -9.761 -12.410  1.00 63.45           C  
ANISOU 3549  CB  TYR D  93     8854   9887   5366   -114    209    131       C  
ATOM   3550  CG  TYR D  93      -1.820  -9.979 -12.259  1.00 61.80           C  
ANISOU 3550  CG  TYR D  93     8646   9774   5063   -297    135    154       C  
ATOM   3551  CD1 TYR D  93      -1.009  -9.006 -11.688  1.00 60.39           C  
ANISOU 3551  CD1 TYR D  93     8674   9500   4773   -453     89    198       C  
ATOM   3552  CD2 TYR D  93      -1.224 -11.155 -12.694  1.00 67.21           C  
ANISOU 3552  CD2 TYR D  93     9101  10630   5805   -307     92    111       C  
ATOM   3553  CE1 TYR D  93       0.353  -9.199 -11.553  1.00 64.12           C  
ANISOU 3553  CE1 TYR D  93     9071  10078   5214   -631     -6    221       C  
ATOM   3554  CE2 TYR D  93       0.137 -11.358 -12.562  1.00 71.36           C  
ANISOU 3554  CE2 TYR D  93     9537  11248   6329   -433     16     99       C  
ATOM   3555  CZ  TYR D  93       0.920 -10.377 -11.991  1.00 69.26           C  
ANISOU 3555  CZ  TYR D  93     9424  10918   5973   -603    -36    164       C  
ATOM   3556  OH  TYR D  93       2.275 -10.574 -11.858  1.00 74.82           O  
ANISOU 3556  OH  TYR D  93     9968  11733   6728   -740   -138    154       O  
ATOM   3557  N   TYR D  94      -5.411  -9.431 -15.097  1.00 87.27           N  
ANISOU 3557  N   TYR D  94    11664  12907   8589    142      8    223       N  
ATOM   3558  CA  TYR D  94      -6.762  -9.583 -15.611  1.00 75.39           C  
ANISOU 3558  CA  TYR D  94    10003  11361   7280    310    -76    230       C  
ATOM   3559  C   TYR D  94      -7.160 -11.053 -15.610  1.00 72.56           C  
ANISOU 3559  C   TYR D  94     9413  11166   6991    312    -23    170       C  
ATOM   3560  O   TYR D  94      -6.328 -11.940 -15.825  1.00 74.44           O  
ANISOU 3560  O   TYR D  94     9641  11540   7105    196    -11    141       O  
ATOM   3561  CB  TYR D  94      -6.881  -9.019 -17.030  1.00 61.89           C  
ANISOU 3561  CB  TYR D  94     8397   9613   5506    263   -329    359       C  
ATOM   3562  CG  TYR D  94      -6.504  -7.560 -17.152  1.00 63.56           C  
ANISOU 3562  CG  TYR D  94     8898   9616   5634    213   -453    459       C  
ATOM   3563  CD1 TYR D  94      -7.467  -6.564 -17.059  1.00 66.01           C  
ANISOU 3563  CD1 TYR D  94     9263   9645   6173    424   -610    486       C  
ATOM   3564  CD2 TYR D  94      -5.185  -7.179 -17.363  1.00 63.27           C  
ANISOU 3564  CD2 TYR D  94     9068   9649   5322    -50   -430    519       C  
ATOM   3565  CE1 TYR D  94      -7.127  -5.229 -17.170  1.00 75.02           C  
ANISOU 3565  CE1 TYR D  94    10730  10527   7250    376   -780    583       C  
ATOM   3566  CE2 TYR D  94      -4.835  -5.847 -17.475  1.00 69.39           C  
ANISOU 3566  CE2 TYR D  94    10152  10212   6002   -156   -573    636       C  
ATOM   3567  CZ  TYR D  94      -5.810  -4.876 -17.378  1.00 79.89           C  
ANISOU 3567  CZ  TYR D  94    11604  11210   7542     58   -768    675       C  
ATOM   3568  OH  TYR D  94      -5.467  -3.548 -17.490  1.00 86.93           O  
ANISOU 3568  OH  TYR D  94    12859  11822   8349    -48   -965    796       O  
ATOM   3569  N   CYS D  95      -8.442 -11.302 -15.369  1.00 79.60           N  
ANISOU 3569  N   CYS D  95    10104  12030   8111    445     -1    138       N  
ATOM   3570  CA  CYS D  95      -8.996 -12.649 -15.372  1.00 86.94           C  
ANISOU 3570  CA  CYS D  95    10831  13083   9121    407     15    105       C  
ATOM   3571  C   CYS D  95      -9.773 -12.873 -16.662  1.00 87.01           C  
ANISOU 3571  C   CYS D  95    10718  13115   9227    435   -231    171       C  
ATOM   3572  O   CYS D  95     -10.590 -12.034 -17.054  1.00102.10           O  
ANISOU 3572  O   CYS D  95    12556  14922  11314    564   -371    223       O  
ATOM   3573  CB  CYS D  95      -9.904 -12.869 -14.161  1.00 95.80           C  
ANISOU 3573  CB  CYS D  95    11790  14204  10405    446    234     27       C  
ATOM   3574  SG  CYS D  95     -10.605 -14.530 -14.051  1.00106.36           S  
ANISOU 3574  SG  CYS D  95    12920  15674  11820    309    239     24       S  
ATOM   3575  N   ALA D  96      -9.515 -14.002 -17.316  1.00 75.23           N  
ANISOU 3575  N   ALA D  96     9225  11728   7632    319   -321    161       N  
ATOM   3576  CA  ALA D  96     -10.163 -14.346 -18.572  1.00 67.11           C  
ANISOU 3576  CA  ALA D  96     8152  10720   6625    286   -581    216       C  
ATOM   3577  C   ALA D  96     -10.801 -15.722 -18.459  1.00 62.09           C  
ANISOU 3577  C   ALA D  96     7350  10145   6097    218   -608    173       C  
ATOM   3578  O   ALA D  96     -10.337 -16.579 -17.703  1.00 62.06           O  
ANISOU 3578  O   ALA D  96     7363  10166   6051    157   -463    101       O  
ATOM   3579  CB  ALA D  96      -9.171 -14.323 -19.740  1.00 65.42           C  
ANISOU 3579  CB  ALA D  96     8191  10564   6101    156   -681    218       C  
ATOM   3580  N   ALA D  97     -11.872 -15.927 -19.223  1.00 80.33           N  
ANISOU 3580  N   ALA D  97     9521  12450   8550    204   -849    237       N  
ATOM   3581  CA  ALA D  97     -12.609 -17.181 -19.180  1.00 84.97           C  
ANISOU 3581  CA  ALA D  97     9950  13079   9256     94   -922    221       C  
ATOM   3582  C   ALA D  97     -13.293 -17.417 -20.518  1.00 85.79           C  
ANISOU 3582  C   ALA D  97    10059  13170   9367     16  -1291    293       C  
ATOM   3583  O   ALA D  97     -13.670 -16.472 -21.216  1.00 84.34           O  
ANISOU 3583  O   ALA D  97     9882  12933   9231     82  -1506    393       O  
ATOM   3584  CB  ALA D  97     -13.642 -17.185 -18.048  1.00 79.37           C  
ANISOU 3584  CB  ALA D  97     8906  12404   8849    121   -748    226       C  
ATOM   3585  N   VAL D  98     -13.450 -18.692 -20.865  1.00 83.95           N  
ANISOU 3585  N   VAL D  98     9868  12949   9079   -142  -1410    249       N  
ATOM   3586  CA  VAL D  98     -14.116 -19.113 -22.093  1.00 87.29           C  
ANISOU 3586  CA  VAL D  98    10345  13349   9473   -273  -1787    304       C  
ATOM   3587  C   VAL D  98     -15.339 -19.931 -21.705  1.00 93.09           C  
ANISOU 3587  C   VAL D  98    10761  14099  10510   -388  -1899    356       C  
ATOM   3588  O   VAL D  98     -15.217 -20.940 -20.999  1.00 88.06           O  
ANISOU 3588  O   VAL D  98    10122  13460   9876   -495  -1756    292       O  
ATOM   3589  CB  VAL D  98     -13.181 -19.925 -23.003  1.00 76.85           C  
ANISOU 3589  CB  VAL D  98     9411  12012   7776   -397  -1846    165       C  
ATOM   3590  CG1 VAL D  98     -13.937 -20.428 -24.224  1.00 72.70           C  
ANISOU 3590  CG1 VAL D  98     9002  11446   7176   -579  -2251    211       C  
ATOM   3591  CG2 VAL D  98     -11.983 -19.086 -23.419  1.00 71.21           C  
ANISOU 3591  CG2 VAL D  98     8954  11341   6761   -341  -1691    109       C  
ATOM   3592  N   ALA D  99     -16.512 -19.502 -22.166  1.00 62.72           N  
ANISOU 3592  N   ALA D  99     7791   7793   8246   -255  -1646    418       N  
ATOM   3593  CA  ALA D  99     -17.761 -20.181 -21.850  1.00 65.47           C  
ANISOU 3593  CA  ALA D  99     7982   8512   8380   -165  -1357    138       C  
ATOM   3594  C   ALA D  99     -18.631 -20.245 -23.095  1.00 59.33           C  
ANISOU 3594  C   ALA D  99     6720   8374   7449    -88  -1202     93       C  
ATOM   3595  O   ALA D  99     -18.861 -19.222 -23.746  1.00 67.56           O  
ANISOU 3595  O   ALA D  99     7731   9549   8390    150  -1293    263       O  
ATOM   3596  CB  ALA D  99     -18.509 -19.469 -20.717  1.00 63.57           C  
ANISOU 3596  CB  ALA D  99     8142   8076   7934    210  -1373    113       C  
ATOM   3597  N   TYR D 100     -19.118 -21.458 -23.422  1.00 57.22           N  
ANISOU 3597  N   TYR D 100     6098   8468   7176   -296  -1025   -132       N  
ATOM   3598  CA  TYR D 100     -19.969 -21.681 -24.579  1.00 68.63           C  
ANISOU 3598  CA  TYR D 100     7100  10494   8482   -255   -956   -223       C  
ATOM   3599  C   TYR D 100     -21.426 -21.836 -24.156  1.00 74.41           C  
ANISOU 3599  C   TYR D 100     7619  11554   9100   -147   -807   -293       C  
ATOM   3600  O   TYR D 100     -21.714 -22.315 -23.055  1.00 83.49           O  
ANISOU 3600  O   TYR D 100     8864  12556  10304   -216   -692   -319       O  
ATOM   3601  CB  TYR D 100     -19.532 -22.936 -25.342  1.00 63.52           C  
ANISOU 3601  CB  TYR D 100     6222   9998   7914   -539   -972   -430       C  
ATOM   3602  CG  TYR D 100     -18.095 -22.910 -25.815  1.00 59.40           C  
ANISOU 3602  CG  TYR D 100     5815   9277   7477   -588  -1052   -310       C  
ATOM   3603  CD1 TYR D 100     -17.738 -22.242 -26.979  1.00 76.79           C  
ANISOU 3603  CD1 TYR D 100     7875  11755   9546   -395  -1090   -114       C  
ATOM   3604  CD2 TYR D 100     -17.098 -23.565 -25.103  1.00 44.20           C  
ANISOU 3604  CD2 TYR D 100     4098   6934   5762   -807  -1074   -334       C  
ATOM   3605  CE1 TYR D 100     -16.426 -22.219 -27.417  1.00 73.33           C  
ANISOU 3605  CE1 TYR D 100     7452  11222   9187   -409  -1117    106       C  
ATOM   3606  CE2 TYR D 100     -15.784 -23.549 -25.534  1.00 57.60           C  
ANISOU 3606  CE2 TYR D 100     5820   8512   7553   -827  -1127   -152       C  
ATOM   3607  CZ  TYR D 100     -15.454 -22.874 -26.691  1.00 68.69           C  
ANISOU 3607  CZ  TYR D 100     7033  10238   8827   -623  -1133     93       C  
ATOM   3608  OH  TYR D 100     -14.147 -22.855 -27.123  1.00 63.71           O  
ANISOU 3608  OH  TYR D 100     6343   9572   8291   -614  -1142    380       O  
ATOM   3609  N   PRO D 101     -22.371 -21.431 -25.009  1.00 80.89           N  
ANISOU 3609  N   PRO D 101     8115  12860   9760     41   -796   -269       N  
ATOM   3610  CA  PRO D 101     -23.791 -21.629 -24.685  1.00 76.75           C  
ANISOU 3610  CA  PRO D 101     7265  12733   9165    131   -654   -259       C  
ATOM   3611  C   PRO D 101     -24.218 -23.080 -24.840  1.00 78.52           C  
ANISOU 3611  C   PRO D 101     7119  13146   9571   -289   -674   -423       C  
ATOM   3612  O   PRO D 101     -23.395 -23.947 -25.153  1.00 72.09           O  
ANISOU 3612  O   PRO D 101     6380  12112   8897   -597   -799   -607       O  
ATOM   3613  CB  PRO D 101     -24.516 -20.723 -25.692  1.00 67.55           C  
ANISOU 3613  CB  PRO D 101     5863  12004   7798    447   -704   -168       C  
ATOM   3614  CG  PRO D 101     -23.451 -19.828 -26.271  1.00 77.36           C  
ANISOU 3614  CG  PRO D 101     7417  12985   8993    579   -848    -70       C  
ATOM   3615  CD  PRO D 101     -22.193 -20.628 -26.228  1.00 77.34           C  
ANISOU 3615  CD  PRO D 101     7580  12629   9177    231   -909   -168       C  
ATOM   3616  N   ASP D 102     -25.502 -23.357 -24.626  1.00 82.43           N  
ANISOU 3616  N   ASP D 102     7203  14036  10081   -292   -583   -325       N  
ATOM   3617  CA  ASP D 102     -26.013 -24.707 -24.816  1.00 86.00           C  
ANISOU 3617  CA  ASP D 102     7265  14633  10776   -744   -705   -420       C  
ATOM   3618  C   ASP D 102     -26.102 -25.031 -26.301  1.00 99.15           C  
ANISOU 3618  C   ASP D 102     8710  16541  12420   -862  -1016   -646       C  
ATOM   3619  O   ASP D 102     -26.452 -24.174 -27.118  1.00114.18           O  
ANISOU 3619  O   ASP D 102    10505  18769  14108   -559  -1055   -607       O  
ATOM   3620  CB  ASP D 102     -27.386 -24.858 -24.163  1.00 90.70           C  
ANISOU 3620  CB  ASP D 102     7396  15626  11440   -728   -534   -128       C  
ATOM   3621  CG  ASP D 102     -27.841 -26.303 -24.094  1.00102.67           C  
ANISOU 3621  CG  ASP D 102     8530  17165  13314  -1285   -704   -123       C  
ATOM   3622  OD1 ASP D 102     -27.012 -27.203 -24.346  1.00104.04           O  
ANISOU 3622  OD1 ASP D 102     8924  16950  13656  -1639   -934   -398       O  
ATOM   3623  OD2 ASP D 102     -29.029 -26.540 -23.790  1.00113.79           O  
ANISOU 3623  OD2 ASP D 102     9406  18976  14852  -1360   -630    190       O  
ATOM   3624  N   ILE D 103     -25.799 -26.282 -26.641  1.00 92.08           N  
ANISOU 3624  N   ILE D 103     7788  15474  11722  -1262  -1267   -891       N  
ATOM   3625  CA  ILE D 103     -25.684 -26.734 -28.027  1.00 81.60           C  
ANISOU 3625  CA  ILE D 103     6493  14193  10320  -1284  -1586  -1162       C  
ATOM   3626  C   ILE D 103     -24.756 -25.771 -28.759  1.00 74.18           C  
ANISOU 3626  C   ILE D 103     5757  13373   9054   -922  -1538  -1220       C  
ATOM   3627  O   ILE D 103     -25.204 -25.029 -29.646  1.00 77.27           O  
ANISOU 3627  O   ILE D 103     6021  14121   9217   -640  -1580  -1164       O  
ATOM   3628  CB  ILE D 103     -27.060 -26.831 -28.708  1.00 74.50           C  
ANISOU 3628  CB  ILE D 103     5248  13594   9464  -1291  -1768  -1079       C  
ATOM   3629  CG1 ILE D 103     -28.061 -27.530 -27.788  1.00 73.75           C  
ANISOU 3629  CG1 ILE D 103     4833  13452   9736  -1612  -1750   -835       C  
ATOM   3630  CG2 ILE D 103     -26.958 -27.593 -30.022  1.00 70.18           C  
ANISOU 3630  CG2 ILE D 103     4849  12947   8871  -1345  -2168  -1385       C  
ATOM   3631  CD1 ILE D 103     -27.701 -28.966 -27.473  1.00 71.46           C  
ANISOU 3631  CD1 ILE D 103     4718  12640   9793  -2031  -1978   -965       C  
ATOM   3632  N   PRO D 104     -23.466 -25.733 -28.417  1.00 64.60           N  
ANISOU 3632  N   PRO D 104     4930  11771   7843   -896  -1418  -1234       N  
ATOM   3633  CA  PRO D 104     -22.579 -24.696 -28.965  1.00 64.31           C  
ANISOU 3633  CA  PRO D 104     5102  11754   7580   -558  -1322  -1095       C  
ATOM   3634  C   PRO D 104     -22.204 -24.996 -30.410  1.00 72.60           C  
ANISOU 3634  C   PRO D 104     6117  13082   8384   -405  -1504  -1288       C  
ATOM   3635  O   PRO D 104     -21.660 -26.058 -30.718  1.00 78.76           O  
ANISOU 3635  O   PRO D 104     7009  13737   9180   -524  -1649  -1563       O  
ATOM   3636  CB  PRO D 104     -21.356 -24.756 -28.041  1.00 50.90           C  
ANISOU 3636  CB  PRO D 104     3758   9538   6043   -657  -1192  -1010       C  
ATOM   3637  CG  PRO D 104     -21.324 -26.170 -27.572  1.00 50.27           C  
ANISOU 3637  CG  PRO D 104     3693   9223   6183  -1016  -1286  -1259       C  
ATOM   3638  CD  PRO D 104     -22.759 -26.630 -27.485  1.00 53.26           C  
ANISOU 3638  CD  PRO D 104     3724   9860   6653  -1191  -1384  -1313       C  
ATOM   3639  N   THR D 105     -22.500 -24.050 -31.298  1.00 69.81           N  
ANISOU 3639  N   THR D 105     5642  13116   7765    -83  -1503  -1142       N  
ATOM   3640  CA  THR D 105     -22.028 -24.123 -32.674  1.00 71.62           C  
ANISOU 3640  CA  THR D 105     5880  13667   7665    186  -1614  -1239       C  
ATOM   3641  C   THR D 105     -20.592 -23.638 -32.821  1.00 71.29           C  
ANISOU 3641  C   THR D 105     6041  13496   7550    370  -1423   -969       C  
ATOM   3642  O   THR D 105     -20.078 -23.610 -33.945  1.00 83.17           O  
ANISOU 3642  O   THR D 105     7534  15329   8736    674  -1434   -944       O  
ATOM   3643  CB  THR D 105     -22.944 -23.310 -33.594  1.00 85.20           C  
ANISOU 3643  CB  THR D 105     7372  15881   9120    468  -1690  -1138       C  
ATOM   3644  OG1 THR D 105     -22.953 -21.940 -33.176  1.00 95.13           O  
ANISOU 3644  OG1 THR D 105     8636  17105  10405    634  -1491   -728       O  
ATOM   3645  CG2 THR D 105     -24.364 -23.856 -33.549  1.00 86.72           C  
ANISOU 3645  CG2 THR D 105     7401  16093   9454    266  -1849  -1317       C  
ATOM   3646  N   TYR D 106     -19.946 -23.256 -31.715  1.00 68.65           N  
ANISOU 3646  N   TYR D 106     5874  12713   7495    212  -1268   -731       N  
ATOM   3647  CA  TYR D 106     -18.553 -22.805 -31.706  1.00 58.26           C  
ANISOU 3647  CA  TYR D 106     4699  11212   6227    297  -1143   -392       C  
ATOM   3648  C   TYR D 106     -18.339 -21.623 -32.649  1.00 66.58           C  
ANISOU 3648  C   TYR D 106     5633  12603   7059    623  -1095     25       C  
ATOM   3649  O   TYR D 106     -17.304 -21.503 -33.307  1.00 73.02           O  
ANISOU 3649  O   TYR D 106     6409  13571   7765    797  -1008    304       O  
ATOM   3650  CB  TYR D 106     -17.600 -23.957 -32.031  1.00 65.51           C  
ANISOU 3650  CB  TYR D 106     5690  12104   7096    292  -1140   -596       C  
ATOM   3651  CG  TYR D 106     -17.656 -25.071 -31.010  1.00 80.49           C  
ANISOU 3651  CG  TYR D 106     7740  13575   9269    -59  -1206   -930       C  
ATOM   3652  CD1 TYR D 106     -18.266 -26.283 -31.306  1.00 88.97           C  
ANISOU 3652  CD1 TYR D 106     8805  14717  10284   -154  -1401  -1403       C  
ATOM   3653  CD2 TYR D 106     -17.116 -24.903 -29.741  1.00 88.85           C  
ANISOU 3653  CD2 TYR D 106     8971  14130  10658   -301  -1128   -754       C  
ATOM   3654  CE1 TYR D 106     -18.324 -27.302 -30.371  1.00 93.29           C  
ANISOU 3654  CE1 TYR D 106     9476  14851  11121   -504  -1484  -1641       C  
ATOM   3655  CE2 TYR D 106     -17.170 -25.914 -28.800  1.00 89.80           C  
ANISOU 3655  CE2 TYR D 106     9227  13881  11011   -605  -1174  -1013       C  
ATOM   3656  CZ  TYR D 106     -17.775 -27.111 -29.121  1.00 97.40           C  
ANISOU 3656  CZ  TYR D 106    10142  14929  11937   -718  -1335  -1431       C  
ATOM   3657  OH  TYR D 106     -17.831 -28.121 -28.187  1.00109.42           O  
ANISOU 3657  OH  TYR D 106    11786  16062  13728  -1049  -1402  -1625       O  
ATOM   3658  N   PHE D 107     -19.333 -20.740 -32.707  1.00 69.75           N  
ANISOU 3658  N   PHE D 107     5954  13148   7400    730  -1140    120       N  
ATOM   3659  CA  PHE D 107     -19.256 -19.498 -33.459  1.00 79.60           C  
ANISOU 3659  CA  PHE D 107     7116  14639   8490   1014  -1128    559       C  
ATOM   3660  C   PHE D 107     -19.917 -18.397 -32.647  1.00 98.03           C  
ANISOU 3660  C   PHE D 107     9567  16686  10994   1019  -1184    739       C  
ATOM   3661  O   PHE D 107     -20.973 -18.610 -32.046  1.00108.95           O  
ANISOU 3661  O   PHE D 107    10937  18052  12407    968  -1202    461       O  
ATOM   3662  CB  PHE D 107     -19.937 -19.617 -34.828  1.00 98.40           C  
ANISOU 3662  CB  PHE D 107     9273  17668  10447   1315  -1176    422       C  
ATOM   3663  CG  PHE D 107     -18.977 -19.679 -35.981  1.00107.56           C  
ANISOU 3663  CG  PHE D 107    10354  19206  11308   1598  -1082    658       C  
ATOM   3664  CD1 PHE D 107     -18.811 -20.850 -36.701  1.00 99.20           C  
ANISOU 3664  CD1 PHE D 107     9293  18451   9948   1743  -1109    269       C  
ATOM   3665  CD2 PHE D 107     -18.237 -18.564 -36.343  1.00124.54           C  
ANISOU 3665  CD2 PHE D 107    12441  21411  13469   1755   -986   1302       C  
ATOM   3666  CE1 PHE D 107     -17.929 -20.908 -37.765  1.00101.73           C  
ANISOU 3666  CE1 PHE D 107     9553  19198   9903   2128   -975    504       C  
ATOM   3667  CE2 PHE D 107     -17.352 -18.616 -37.404  1.00126.98           C  
ANISOU 3667  CE2 PHE D 107    12615  22149  13480   2057   -833   1621       C  
ATOM   3668  CZ  PHE D 107     -17.199 -19.789 -38.117  1.00115.31           C  
ANISOU 3668  CZ  PHE D 107    11132  21061  11621   2294   -799   1217       C  
ATOM   3669  N   ASP D 108     -19.293 -17.222 -32.631  1.00105.86           N  
ANISOU 3669  N   ASP D 108    10671  17452  12097   1108  -1234   1237       N  
ATOM   3670  CA  ASP D 108     -19.829 -16.095 -31.871  1.00102.86           C  
ANISOU 3670  CA  ASP D 108    10513  16720  11849   1199  -1358   1398       C  
ATOM   3671  C   ASP D 108     -19.285 -14.810 -32.472  1.00101.16           C  
ANISOU 3671  C   ASP D 108    10324  16444  11670   1358  -1489   1982       C  
ATOM   3672  O   ASP D 108     -18.071 -14.582 -32.448  1.00108.74           O  
ANISOU 3672  O   ASP D 108    11333  17125  12857   1202  -1551   2384       O  
ATOM   3673  CB  ASP D 108     -19.455 -16.206 -30.391  1.00 91.14           C  
ANISOU 3673  CB  ASP D 108     9379  14580  10668    982  -1418   1309       C  
ATOM   3674  CG  ASP D 108     -20.313 -15.323 -29.502  1.00 98.34           C  
ANISOU 3674  CG  ASP D 108    10573  15205  11587   1195  -1523   1284       C  
ATOM   3675  OD1 ASP D 108     -20.936 -14.371 -30.018  1.00 96.51           O  
ANISOU 3675  OD1 ASP D 108    10307  15155  11209   1493  -1599   1457       O  
ATOM   3676  OD2 ASP D 108     -20.361 -15.580 -28.280  1.00102.82           O  
ANISOU 3676  OD2 ASP D 108    11417  15379  12271   1118  -1526   1096       O  
ATOM   3677  N   TYR D 109     -20.175 -13.976 -33.006  1.00 85.73           N  
ANISOU 3677  N   TYR D 109     8303  14748   9522   1653  -1549   2082       N  
ATOM   3678  CA  TYR D 109     -19.803 -12.685 -33.564  1.00 93.10           C  
ANISOU 3678  CA  TYR D 109     9283  15580  10509   1804  -1709   2660       C  
ATOM   3679  C   TYR D 109     -20.015 -11.543 -32.578  1.00107.35           C  
ANISOU 3679  C   TYR D 109    11512  16731  12544   1892  -2000   2812       C  
ATOM   3680  O   TYR D 109     -19.867 -10.376 -32.953  1.00125.14           O  
ANISOU 3680  O   TYR D 109    13932  18707  14909   1969  -2164   3173       O  
ATOM   3681  CB  TYR D 109     -20.589 -12.418 -34.850  1.00 96.27           C  
ANISOU 3681  CB  TYR D 109     9484  16510  10584   2044  -1564   2621       C  
ATOM   3682  CG  TYR D 109     -20.467 -13.518 -35.880  1.00 95.64           C  
ANISOU 3682  CG  TYR D 109     9110  17028  10199   2049  -1332   2403       C  
ATOM   3683  CD1 TYR D 109     -19.317 -13.653 -36.647  1.00 95.64           C  
ANISOU 3683  CD1 TYR D 109     8997  17179  10161   2017  -1194   2753       C  
ATOM   3684  CD2 TYR D 109     -21.502 -14.419 -36.088  1.00 90.93           C  
ANISOU 3684  CD2 TYR D 109     8370  16829   9352   2110  -1275   1859       C  
ATOM   3685  CE1 TYR D 109     -19.201 -14.657 -37.590  1.00 94.34           C  
ANISOU 3685  CE1 TYR D 109     8642  17572   9632   2148  -1008   2524       C  
ATOM   3686  CE2 TYR D 109     -21.396 -15.426 -37.029  1.00 88.46           C  
ANISOU 3686  CE2 TYR D 109     7895  16971   8744   2153  -1166   1609       C  
ATOM   3687  CZ  TYR D 109     -20.243 -15.540 -37.777  1.00 92.97           C  
ANISOU 3687  CZ  TYR D 109     8415  17712   9197   2224  -1034   1917       C  
ATOM   3688  OH  TYR D 109     -20.132 -16.541 -38.715  1.00 97.52           O  
ANISOU 3688  OH  TYR D 109     8891  18766   9397   2393   -952   1636       O  
ATOM   3689  N   ASP D 110     -20.356 -11.854 -31.329  1.00102.48           N  
ANISOU 3689  N   ASP D 110    11190  15729  12019   1847  -2018   2427       N  
ATOM   3690  CA  ASP D 110     -20.595 -10.852 -30.297  1.00 99.13           C  
ANISOU 3690  CA  ASP D 110    11279  14662  11725   2037  -2305   2466       C  
ATOM   3691  C   ASP D 110     -19.494 -10.788 -29.253  1.00 98.36           C  
ANISOU 3691  C   ASP D 110    11594  13789  11987   1760  -2559   2574       C  
ATOM   3692  O   ASP D 110     -19.087  -9.692 -28.860  1.00101.68           O  
ANISOU 3692  O   ASP D 110    12435  13569  12628   1822  -2980   2884       O  
ATOM   3693  CB  ASP D 110     -21.934 -11.124 -29.600  1.00107.24           C  
ANISOU 3693  CB  ASP D 110    12363  15881  12500   2336  -2134   1988       C  
ATOM   3694  CG  ASP D 110     -22.222 -10.136 -28.487  1.00119.41           C  
ANISOU 3694  CG  ASP D 110    14502  16803  14064   2681  -2402   1970       C  
ATOM   3695  OD1 ASP D 110     -22.451  -8.947 -28.791  1.00125.81           O  
ANISOU 3695  OD1 ASP D 110    15525  17432  14847   2997  -2666   2226       O  
ATOM   3696  OD2 ASP D 110     -22.220 -10.550 -27.308  1.00122.22           O  
ANISOU 3696  OD2 ASP D 110    15155  16845  14438   2678  -2368   1698       O  
ATOM   3697  N   SER D 111     -18.998 -11.937 -28.791  1.00 95.86           N  
ANISOU 3697  N   SER D 111    11193  13476  11753   1453  -2374   2327       N  
ATOM   3698  CA  SER D 111     -17.940 -11.960 -27.792  1.00109.49           C  
ANISOU 3698  CA  SER D 111    13288  14495  13819   1180  -2626   2420       C  
ATOM   3699  C   SER D 111     -16.928 -13.077 -28.002  1.00109.11           C  
ANISOU 3699  C   SER D 111    12932  14597  13928    783  -2438   2452       C  
ATOM   3700  O   SER D 111     -15.995 -13.192 -27.200  1.00110.51           O  
ANISOU 3700  O   SER D 111    13358  14225  14407    528  -2643   2547       O  
ATOM   3701  CB  SER D 111     -18.539 -12.081 -26.380  1.00117.53           C  
ANISOU 3701  CB  SER D 111    14778  15136  14743   1362  -2662   1984       C  
ATOM   3702  OG  SER D 111     -19.385 -10.983 -26.088  1.00127.09           O  
ANISOU 3702  OG  SER D 111    16354  16153  15782   1831  -2864   1965       O  
ATOM   3703  N   ASP D 112     -17.079 -13.900 -29.043  1.00 99.57           N  
ANISOU 3703  N   ASP D 112    11230  14096  12506    765  -2093   2362       N  
ATOM   3704  CA  ASP D 112     -16.171 -15.013 -29.329  1.00 95.38           C  
ANISOU 3704  CA  ASP D 112    10432  13762  12048    502  -1899   2349       C  
ATOM   3705  C   ASP D 112     -16.081 -15.984 -28.153  1.00 92.59           C  
ANISOU 3705  C   ASP D 112    10299  13083  11798    299  -1846   1923       C  
ATOM   3706  O   ASP D 112     -15.048 -16.625 -27.940  1.00100.45           O  
ANISOU 3706  O   ASP D 112    11256  13913  12996     51  -1833   2002       O  
ATOM   3707  CB  ASP D 112     -14.777 -14.507 -29.719  1.00 93.67           C  
ANISOU 3707  CB  ASP D 112    10098  13352  12141    324  -2064   3016       C  
ATOM   3708  CG  ASP D 112     -13.966 -15.544 -30.475  1.00103.18           C  
ANISOU 3708  CG  ASP D 112    10897  15037  13271    247  -1772   3089       C  
ATOM   3709  OD1 ASP D 112     -14.517 -16.621 -30.786  1.00105.98           O  
ANISOU 3709  OD1 ASP D 112    11119  15830  13317    341  -1502   2576       O  
ATOM   3710  OD2 ASP D 112     -12.778 -15.282 -30.755  1.00110.67           O  
ANISOU 3710  OD2 ASP D 112    11658  15917  14473    113  -1839   3682       O  
ATOM   3711  N   ASN D 113     -17.164 -16.094 -27.380  1.00 76.34           N  
ANISOU 3711  N   ASN D 113     8446  10965   9594    432  -1799   1519       N  
ATOM   3712  CA  ASN D 113     -17.233 -16.938 -26.188  1.00 67.71           C  
ANISOU 3712  CA  ASN D 113     7575   9588   8565    285  -1734   1163       C  
ATOM   3713  C   ASN D 113     -16.126 -16.620 -25.187  1.00 76.27           C  
ANISOU 3713  C   ASN D 113     9070   9945   9965    104  -2024   1359       C  
ATOM   3714  O   ASN D 113     -15.775 -17.464 -24.356  1.00 72.36           O  
ANISOU 3714  O   ASN D 113     8708   9217   9567    -88  -1975   1149       O  
ATOM   3715  CB  ASN D 113     -17.199 -18.427 -26.555  1.00 50.79           C  
ANISOU 3715  CB  ASN D 113     5105   7828   6365     77  -1471    859       C  
ATOM   3716  CG  ASN D 113     -18.282 -18.809 -27.544  1.00 73.99           C  
ANISOU 3716  CG  ASN D 113     7666  11429   9015    221  -1296    641       C  
ATOM   3717  OD1 ASN D 113     -19.434 -19.027 -27.167  1.00 79.04           O  
ANISOU 3717  OD1 ASN D 113     8258  12239   9535    302  -1208    392       O  
ATOM   3718  ND2 ASN D 113     -17.916 -18.896 -28.818  1.00 81.29           N  
ANISOU 3718  ND2 ASN D 113     8307  12760   9821    277  -1258    768       N  
ATOM   3719  N   PHE D 114     -15.572 -15.412 -25.250  1.00 74.79           N  
ANISOU 3719  N   PHE D 114     9935   8994   9489   -210  -2053    -75       N  
ATOM   3720  CA  PHE D 114     -14.456 -15.000 -24.411  1.00 70.53           C  
ANISOU 3720  CA  PHE D 114     9472   8521   8804   -296  -1901    -16       C  
ATOM   3721  C   PHE D 114     -14.897 -13.833 -23.541  1.00 78.79           C  
ANISOU 3721  C   PHE D 114    10573   9174  10188     23  -2311   -221       C  
ATOM   3722  O   PHE D 114     -15.518 -12.886 -24.036  1.00 87.71           O  
ANISOU 3722  O   PHE D 114    11908   9866  11552     67  -2969   -213       O  
ATOM   3723  CB  PHE D 114     -13.250 -14.605 -25.269  1.00 68.48           C  
ANISOU 3723  CB  PHE D 114     9571   8315   8135   -883  -2024    345       C  
ATOM   3724  CG  PHE D 114     -11.936 -14.684 -24.547  1.00 58.28           C  
ANISOU 3724  CG  PHE D 114     8228   7252   6664  -1018  -1665    371       C  
ATOM   3725  CD1 PHE D 114     -11.500 -13.636 -23.754  1.00 63.21           C  
ANISOU 3725  CD1 PHE D 114     9028   7642   7346   -944  -1913    385       C  
ATOM   3726  CD2 PHE D 114     -11.132 -15.805 -24.671  1.00 55.83           C  
ANISOU 3726  CD2 PHE D 114     7672   7359   6183  -1211  -1125    347       C  
ATOM   3727  CE1 PHE D 114     -10.289 -13.708 -23.093  1.00 59.94           C  
ANISOU 3727  CE1 PHE D 114     8568   7416   6791  -1067  -1620    404       C  
ATOM   3728  CE2 PHE D 114      -9.920 -15.882 -24.012  1.00 66.66           C  
ANISOU 3728  CE2 PHE D 114     8966   8883   7481  -1314   -878    326       C  
ATOM   3729  CZ  PHE D 114      -9.498 -14.832 -23.223  1.00 61.06           C  
ANISOU 3729  CZ  PHE D 114     8457   7946   6798  -1247  -1123    371       C  
ATOM   3730  N   TYR D 115     -14.578 -13.901 -22.251  1.00 69.33           N  
ANISOU 3730  N   TYR D 115     9200   8104   9036    220  -1970   -421       N  
ATOM   3731  CA  TYR D 115     -14.998 -12.891 -21.291  1.00 67.52           C  
ANISOU 3731  CA  TYR D 115     8946   7573   9137    511  -2244   -719       C  
ATOM   3732  C   TYR D 115     -13.827 -12.512 -20.397  1.00 68.69           C  
ANISOU 3732  C   TYR D 115     9222   7800   9075    388  -2081   -609       C  
ATOM   3733  O   TYR D 115     -13.033 -13.370 -20.002  1.00 68.94           O  
ANISOU 3733  O   TYR D 115     9180   8177   8838    253  -1596   -503       O  
ATOM   3734  CB  TYR D 115     -16.175 -13.392 -20.444  1.00 67.66           C  
ANISOU 3734  CB  TYR D 115     8552   7681   9474    885  -1946  -1253       C  
ATOM   3735  CG  TYR D 115     -17.357 -13.849 -21.271  1.00 78.70           C  
ANISOU 3735  CG  TYR D 115     9766   9020  11117   1035  -2070  -1415       C  
ATOM   3736  CD1 TYR D 115     -17.487 -15.177 -21.659  1.00 70.20           C  
ANISOU 3736  CD1 TYR D 115     8535   8312   9825    956  -1602  -1332       C  
ATOM   3737  CD2 TYR D 115     -18.337 -12.950 -21.672  1.00 74.26           C  
ANISOU 3737  CD2 TYR D 115     9175   7992  11049   1264  -2712  -1667       C  
ATOM   3738  CE1 TYR D 115     -18.562 -15.598 -22.419  1.00 73.33           C  
ANISOU 3738  CE1 TYR D 115     8765   8658  10438   1088  -1712  -1476       C  
ATOM   3739  CE2 TYR D 115     -19.417 -13.362 -22.432  1.00 72.70           C  
ANISOU 3739  CE2 TYR D 115     8802   7705  11116   1409  -2878  -1828       C  
ATOM   3740  CZ  TYR D 115     -19.524 -14.687 -22.802  1.00 74.47           C  
ANISOU 3740  CZ  TYR D 115     8887   8344  11064   1313  -2347  -1721       C  
ATOM   3741  OH  TYR D 115     -20.596 -15.102 -23.558  1.00 78.76           O  
ANISOU 3741  OH  TYR D 115     9257   8804  11864   1454  -2506  -1879       O  
ATOM   3742  N   TRP D 116     -13.727 -11.224 -20.086  1.00 75.74           N  
ANISOU 3742  N   TRP D 116    10304   8334  10139    444  -2545   -646       N  
ATOM   3743  CA  TRP D 116     -12.658 -10.675 -19.266  1.00 80.75           C  
ANISOU 3743  CA  TRP D 116    11091   8984  10607    335  -2478   -544       C  
ATOM   3744  C   TRP D 116     -13.204 -10.249 -17.907  1.00 85.30           C  
ANISOU 3744  C   TRP D 116    11461   9475  11476    651  -2395  -1010       C  
ATOM   3745  O   TRP D 116     -14.395 -10.385 -17.612  1.00 94.40           O  
ANISOU 3745  O   TRP D 116    12319  10582  12966    928  -2355  -1464       O  
ATOM   3746  CB  TRP D 116     -11.988  -9.494 -19.972  1.00 88.33           C  
ANISOU 3746  CB  TRP D 116    12477   9617  11468     60  -3065   -206       C  
ATOM   3747  CG  TRP D 116     -11.197  -9.870 -21.185  1.00 89.81           C  
ANISOU 3747  CG  TRP D 116    12905   9978  11242   -426  -3039    211       C  
ATOM   3748  CD1 TRP D 116     -11.646  -9.928 -22.472  1.00 71.76           C  
ANISOU 3748  CD1 TRP D 116    10795   7583   8886   -652  -3353    391       C  
ATOM   3749  CD2 TRP D 116      -9.812 -10.231 -21.227  1.00 87.79           C  
ANISOU 3749  CD2 TRP D 116    12720  10042  10595   -802  -2675    434       C  
ATOM   3750  NE1 TRP D 116     -10.628 -10.307 -23.313  1.00 66.22           N  
ANISOU 3750  NE1 TRP D 116    10276   7162   7721  -1200  -3145    692       N  
ATOM   3751  CE2 TRP D 116      -9.490 -10.499 -22.573  1.00 80.14           C  
ANISOU 3751  CE2 TRP D 116    11936   9192   9322  -1280  -2722    683       C  
ATOM   3752  CE3 TRP D 116      -8.812 -10.357 -20.257  1.00 82.36           C  
ANISOU 3752  CE3 TRP D 116    11943   9540   9809   -804  -2336    406       C  
ATOM   3753  CZ2 TRP D 116      -8.213 -10.885 -22.973  1.00 84.05           C  
ANISOU 3753  CZ2 TRP D 116    12458  10020   9458  -1757  -2385    816       C  
ATOM   3754  CZ3 TRP D 116      -7.545 -10.739 -20.656  1.00 85.96           C  
ANISOU 3754  CZ3 TRP D 116    12429  10271   9962  -1216  -2076    572       C  
ATOM   3755  CH2 TRP D 116      -7.256 -10.999 -22.002  1.00 89.29           C  
ANISOU 3755  CH2 TRP D 116    12965  10840  10121  -1687  -2074    732       C  
ATOM   3756  N   GLY D 117     -12.307  -9.722 -17.073  1.00 71.29           N  
ANISOU 3756  N   GLY D 117     9825   7698   9563    566  -2345   -942       N  
ATOM   3757  CA  GLY D 117     -12.662  -9.176 -15.785  1.00 69.83           C  
ANISOU 3757  CA  GLY D 117     9502   7436   9592    764  -2277  -1374       C  
ATOM   3758  C   GLY D 117     -12.238  -7.721 -15.664  1.00 80.18           C  
ANISOU 3758  C   GLY D 117    11049   8359  11059    776  -2809  -1325       C  
ATOM   3759  O   GLY D 117     -11.674  -7.129 -16.588  1.00 84.54           O  
ANISOU 3759  O   GLY D 117    11918   8689  11515    593  -3256   -925       O  
ATOM   3760  N   GLN D 118     -12.527  -7.154 -14.491  1.00 86.51           N  
ANISOU 3760  N   GLN D 118    11706   9091  12074    936  -2747  -1765       N  
ATOM   3761  CA  GLN D 118     -12.182  -5.757 -14.244  1.00101.33           C  
ANISOU 3761  CA  GLN D 118    13766  10583  14153    982  -3250  -1788       C  
ATOM   3762  C   GLN D 118     -10.674  -5.579 -14.113  1.00 99.16           C  
ANISOU 3762  C   GLN D 118    13843  10406  13424    683  -3188  -1272       C  
ATOM   3763  O   GLN D 118     -10.074  -4.746 -14.802  1.00 91.39           O  
ANISOU 3763  O   GLN D 118    13184   9146  12394    536  -3680   -923       O  
ATOM   3764  CB  GLN D 118     -12.899  -5.254 -12.991  1.00115.79           C  
ANISOU 3764  CB  GLN D 118    15288  12362  16344   1201  -3128  -2489       C  
ATOM   3765  N   GLY D 119     -10.048  -6.349 -13.238  1.00 99.64           N  
ANISOU 3765  N   GLY D 119    13865  10836  13155    551  -2630  -1231       N  
ATOM   3766  CA  GLY D 119      -8.611  -6.267 -13.037  1.00 96.47           C  
ANISOU 3766  CA  GLY D 119    13729  10529  12397    292  -2564   -819       C  
ATOM   3767  C   GLY D 119      -8.280  -5.755 -11.647  1.00 96.73           C  
ANISOU 3767  C   GLY D 119    13786  10555  12411    306  -2441  -1033       C  
ATOM   3768  O   GLY D 119      -8.946  -4.857 -11.116  1.00 94.92           O  
ANISOU 3768  O   GLY D 119    13468  10101  12495    490  -2640  -1436       O  
ATOM   3769  N   THR D 120      -7.240  -6.332 -11.048  1.00 99.92           N  
ANISOU 3769  N   THR D 120    14296  11187  12481    100  -2142   -800       N  
ATOM   3770  CA  THR D 120      -6.775  -5.940  -9.726  1.00 99.23           C  
ANISOU 3770  CA  THR D 120    14302  11108  12293     33  -2031   -925       C  
ATOM   3771  C   THR D 120      -5.299  -5.579  -9.792  1.00 85.56           C  
ANISOU 3771  C   THR D 120    12822   9327  10359   -156  -2181   -507       C  
ATOM   3772  O   THR D 120      -4.519  -6.238 -10.488  1.00 71.37           O  
ANISOU 3772  O   THR D 120    11050   7658   8408   -310  -2125   -186       O  
ATOM   3773  CB  THR D 120      -6.991  -7.058  -8.696  1.00102.90           C  
ANISOU 3773  CB  THR D 120    14690  11864  12542    -92  -1564  -1093       C  
ATOM   3774  OG1 THR D 120      -6.355  -8.260  -9.148  1.00107.83           O  
ANISOU 3774  OG1 THR D 120    15331  12673  12966   -225  -1414   -742       O  
ATOM   3775  CG2 THR D 120      -8.476  -7.318  -8.493  1.00 99.68           C  
ANISOU 3775  CG2 THR D 120    14016  11542  12316     30  -1355  -1615       C  
ATOM   3776  N   GLN D 121      -4.921  -4.533  -9.063  1.00 94.63           N  
ANISOU 3776  N   GLN D 121    14116  10301  11537   -158  -2356   -575       N  
ATOM   3777  CA  GLN D 121      -3.543  -4.065  -9.062  1.00 99.26           C  
ANISOU 3777  CA  GLN D 121    14933  10827  11954   -340  -2511   -231       C  
ATOM   3778  C   GLN D 121      -2.687  -4.913  -8.129  1.00 94.28           C  
ANISOU 3778  C   GLN D 121    14337  10393  11090   -505  -2230   -125       C  
ATOM   3779  O   GLN D 121      -3.107  -5.264  -7.022  1.00 97.06           O  
ANISOU 3779  O   GLN D 121    14679  10830  11369   -523  -2015   -350       O  
ATOM   3780  CB  GLN D 121      -3.480  -2.597  -8.636  1.00107.84           C  
ANISOU 3780  CB  GLN D 121    16173  11620  13180   -272  -2847   -340       C  
ATOM   3781  CG  GLN D 121      -2.091  -1.984  -8.708  1.00112.52           C  
ANISOU 3781  CG  GLN D 121    17017  12135  13600   -478  -3034      3       C  
ATOM   3782  CD  GLN D 121      -1.641  -1.725 -10.132  1.00113.38           C  
ANISOU 3782  CD  GLN D 121    17263  12173  13645   -660  -3299    319       C  
ATOM   3783  OE1 GLN D 121      -2.292  -0.992 -10.876  1.00116.71           O  
ANISOU 3783  OE1 GLN D 121    17781  12338  14225   -606  -3684    308       O  
ATOM   3784  NE2 GLN D 121      -0.523  -2.329 -10.519  1.00111.60           N  
ANISOU 3784  NE2 GLN D 121    17048  12156  13197   -925  -3126    563       N  
ATOM   3785  N   VAL D 122      -1.482  -5.244  -8.587  1.00 80.67           N  
ANISOU 3785  N   VAL D 122    12662   8728   9260   -676  -2263    182       N  
ATOM   3786  CA  VAL D 122      -0.502  -5.985  -7.800  1.00 60.76           C  
ANISOU 3786  CA  VAL D 122    10171   6295   6622   -819  -2153    294       C  
ATOM   3787  C   VAL D 122       0.822  -5.243  -7.914  1.00 81.71           C  
ANISOU 3787  C   VAL D 122    12946   8848   9253   -961  -2356    481       C  
ATOM   3788  O   VAL D 122       1.428  -5.209  -8.993  1.00 93.14           O  
ANISOU 3788  O   VAL D 122    14329  10345  10717  -1090  -2409    604       O  
ATOM   3789  CB  VAL D 122      -0.355  -7.441  -8.265  1.00 60.87           C  
ANISOU 3789  CB  VAL D 122     9989   6486   6652   -869  -1983    363       C  
ATOM   3790  CG1 VAL D 122       0.815  -8.107  -7.558  1.00 63.79           C  
ANISOU 3790  CG1 VAL D 122    10387   6836   7015  -1008  -2042    476       C  
ATOM   3791  CG2 VAL D 122      -1.640  -8.213  -8.008  1.00 73.02           C  
ANISOU 3791  CG2 VAL D 122    11442   8134   8169   -772  -1767    179       C  
ATOM   3792  N   THR D 123       1.271  -4.649  -6.812  1.00 79.83           N  
ANISOU 3792  N   THR D 123    12888   8493   8951   -992  -2445    470       N  
ATOM   3793  CA  THR D 123       2.498  -3.868  -6.778  1.00 76.29           C  
ANISOU 3793  CA  THR D 123    12563   7940   8483  -1123  -2636    618       C  
ATOM   3794  C   THR D 123       3.505  -4.538  -5.854  1.00 73.12           C  
ANISOU 3794  C   THR D 123    12182   7534   8065  -1232  -2649    684       C  
ATOM   3795  O   THR D 123       3.144  -5.039  -4.785  1.00 66.24           O  
ANISOU 3795  O   THR D 123    11411   6648   7109  -1238  -2596    628       O  
ATOM   3796  CB  THR D 123       2.227  -2.432  -6.310  1.00 81.22           C  
ANISOU 3796  CB  THR D 123    13398   8369   9094  -1059  -2822    551       C  
ATOM   3797  OG1 THR D 123       1.139  -1.881  -7.061  1.00 90.04           O  
ANISOU 3797  OG1 THR D 123    14489   9401  10320   -919  -2922    442       O  
ATOM   3798  CG2 THR D 123       3.460  -1.561  -6.508  1.00 79.12           C  
ANISOU 3798  CG2 THR D 123    13275   8001   8787  -1224  -3031    726       C  
ATOM   3799  N   VAL D 124       4.768  -4.552  -6.276  1.00 81.28           N  
ANISOU 3799  N   VAL D 124    13129   8568   9185  -1369  -2747    774       N  
ATOM   3800  CA  VAL D 124       5.856  -5.155  -5.514  1.00 76.91           C  
ANISOU 3800  CA  VAL D 124    12549   7939   8735  -1453  -2874    805       C  
ATOM   3801  C   VAL D 124       7.004  -4.158  -5.457  1.00 91.14           C  
ANISOU 3801  C   VAL D 124    14425   9649  10553  -1576  -3034    847       C  
ATOM   3802  O   VAL D 124       7.580  -3.810  -6.495  1.00 98.69           O  
ANISOU 3802  O   VAL D 124    15242  10701  11555  -1716  -3001    815       O  
ATOM   3803  CB  VAL D 124       6.326  -6.484  -6.128  1.00 81.08           C  
ANISOU 3803  CB  VAL D 124    12742   8558   9505  -1484  -2841    737       C  
ATOM   3804  CG1 VAL D 124       7.563  -6.993  -5.406  1.00 78.21           C  
ANISOU 3804  CG1 VAL D 124    12316   8025   9375  -1552  -3108    721       C  
ATOM   3805  CG2 VAL D 124       5.212  -7.520  -6.078  1.00 83.92           C  
ANISOU 3805  CG2 VAL D 124    13065   8990   9829  -1380  -2706    719       C  
ATOM   3806  N   SER D 125       7.336  -3.701  -4.252  1.00107.44           N  
ANISOU 3806  N   SER D 125    16731  11548  12545  -1585  -3194    902       N  
ATOM   3807  CA  SER D 125       8.453  -2.790  -4.053  1.00115.28           C  
ANISOU 3807  CA  SER D 125    17804  12438  13558  -1695  -3360    941       C  
ATOM   3808  C   SER D 125       9.734  -3.581  -3.824  1.00122.99           C  
ANISOU 3808  C   SER D 125    18578  13343  14811  -1779  -3535    889       C  
ATOM   3809  O   SER D 125       9.731  -4.608  -3.139  1.00140.72           O  
ANISOU 3809  O   SER D 125    20819  15480  17168  -1743  -3674    903       O  
ATOM   3810  CB  SER D 125       8.190  -1.859  -2.868  1.00119.04           C  
ANISOU 3810  CB  SER D 125    18627  12762  13842  -1670  -3459    995       C  
ATOM   3811  OG  SER D 125       8.007  -2.593  -1.670  1.00124.07           O  
ANISOU 3811  OG  SER D 125    19415  13315  14410  -1699  -3524   1014       O  
ATOM   3812  N   SER D 126      10.833  -3.093  -4.404  1.00121.36           N  
ANISOU 3812  N   SER D 126    18204  13172  14733  -1925  -3568    798       N  
ATOM   3813  CA  SER D 126      12.098  -3.815  -4.319  1.00123.77           C  
ANISOU 3813  CA  SER D 126    18195  13404  15428  -1992  -3747    618       C  
ATOM   3814  C   SER D 126      12.667  -3.806  -2.905  1.00139.78           C  
ANISOU 3814  C   SER D 126    20447  15134  17529  -1951  -4107    722       C  
ATOM   3815  O   SER D 126      13.348  -4.758  -2.508  1.00141.44           O  
ANISOU 3815  O   SER D 126    20473  15159  18110  -1928  -4402    622       O  
ATOM   3816  CB  SER D 126      13.106  -3.223  -5.304  1.00113.82           C  
ANISOU 3816  CB  SER D 126    16678  12308  14261  -2238  -3628    403       C  
ATOM   3817  OG  SER D 126      13.201  -1.818  -5.154  1.00112.38           O  
ANISOU 3817  OG  SER D 126    16826  12100  13774  -2345  -3638    555       O  
ATOM   3818  N   LEU D 127      12.407  -2.753  -2.136  1.00144.95           N  
ANISOU 3818  N   LEU D 127    21500  15706  17868  -1960  -4140    903       N  
ATOM   3819  CA  LEU D 127      12.888  -2.680  -0.761  1.00143.77           C  
ANISOU 3819  CA  LEU D 127    21633  15286  17707  -1989  -4472   1020       C  
ATOM   3820  C   LEU D 127      11.781  -2.222   0.183  1.00140.26           C  
ANISOU 3820  C   LEU D 127    21637  14818  16839  -1992  -4393   1184       C  
ATOM   3821  O   LEU D 127      11.753  -2.605   1.353  1.00141.78           O  
ANISOU 3821  O   LEU D 127    22121  14828  16920  -2094  -4618   1290       O  
ATOM   3822  CB  LEU D 127      14.092  -1.738  -0.653  1.00147.41           C  
ANISOU 3822  CB  LEU D 127    22072  15668  18268  -2081  -4611    970       C  
ATOM   3823  CG  LEU D 127      15.365  -2.123  -1.412  1.00150.01           C  
ANISOU 3823  CG  LEU D 127    21912  16025  19061  -2153  -4688    680       C  
ATOM   3824  CD1 LEU D 127      15.384  -1.508  -2.804  1.00148.06           C  
ANISOU 3824  CD1 LEU D 127    21448  16096  18713  -2301  -4314    527       C  
ATOM   3825  CD2 LEU D 127      16.606  -1.724  -0.628  1.00152.24           C  
ANISOU 3825  CD2 LEU D 127    22220  16070  19556  -2215  -5034    633       C  
TER    3826      LEU D 127                                                      
HETATM 3827  N   SAR B   1      -7.486 -16.447 -82.735  1.00102.93           N  
HETATM 3828  CA  SAR B   1      -7.637 -17.526 -81.773  1.00100.92           C  
HETATM 3829  C   SAR B   1      -9.055 -17.749 -81.190  1.00 94.05           C  
HETATM 3830  O   SAR B   1     -10.071 -17.355 -81.835  1.00 91.90           O  
HETATM 3831  CN  SAR B   1      -7.061 -16.899 -84.037  1.00100.79           C  
ATOM   3832  N   ARG B   2      -9.129 -18.355 -80.009  1.00118.47           N  
ANISOU 3832  N   ARG B   2    15861  15234  13919  -1475  -1729   -395       N  
ATOM   3833  CA  ARG B   2     -10.409 -18.599 -79.355  1.00105.65           C  
ANISOU 3833  CA  ARG B   2    14194  13803  12146  -1483  -1857   -144       C  
ATOM   3834  C   ARG B   2     -10.882 -17.338 -78.639  1.00 80.33           C  
ANISOU 3834  C   ARG B   2    11210  10785   8528  -1087  -1938    -75       C  
ATOM   3835  O   ARG B   2     -10.097 -16.419 -78.403  1.00 71.68           O  
ANISOU 3835  O   ARG B   2    10233   9630   7373   -831  -1865   -243       O  
ATOM   3836  CB  ARG B   2     -10.301 -19.769 -78.372  1.00113.18           C  
ANISOU 3836  CB  ARG B   2    14912  14740  13353  -1345  -1629    151       C  
ATOM   3837  CG  ARG B   2     -11.606 -20.524 -78.166  1.00114.27           C  
ANISOU 3837  CG  ARG B   2    14690  14970  13757  -1284  -1454    504       C  
ATOM   3838  CD  ARG B   2     -11.398 -21.810 -77.384  1.00112.62           C  
ANISOU 3838  CD  ARG B   2    14163  14712  13914  -1234  -1262    811       C  
ATOM   3839  NE  ARG B   2     -11.291 -21.579 -75.947  1.00101.47           N  
ANISOU 3839  NE  ARG B   2    12807  13541  12207   -813  -1167   1108       N  
ATOM   3840  CZ  ARG B   2     -12.321 -21.627 -75.108  1.00103.13           C  
ANISOU 3840  CZ  ARG B   2    12845  14012  12327   -469   -989   1520       C  
ATOM   3841  NH1 ARG B   2     -13.536 -21.897 -75.564  1.00 94.73           N  
ANISOU 3841  NH1 ARG B   2    11481  12976  11537   -502   -918   1747       N  
ATOM   3842  NH2 ARG B   2     -12.137 -21.407 -73.814  1.00112.23           N  
ANISOU 3842  NH2 ARG B   2    14131  15401  13109   -102   -888   1746       N  
ATOM   3843  N   VAL B   3     -12.167 -17.296 -78.298  1.00 76.14           N  
ANISOU 3843  N   VAL B   3    10512  10407   8013   -868  -1782    206       N  
ATOM   3844  CA  VAL B   3     -12.789 -16.134 -77.673  1.00 86.46           C  
ANISOU 3844  CA  VAL B   3    12015  11852   8982   -450  -1755    277       C  
ATOM   3845  C   VAL B   3     -13.435 -16.594 -76.373  1.00101.41           C  
ANISOU 3845  C   VAL B   3    13808  13926  10798     -7  -1419    661       C  
ATOM   3846  O   VAL B   3     -14.472 -17.270 -76.392  1.00125.09           O  
ANISOU 3846  O   VAL B   3    16415  17007  14108     19  -1207   1041       O  
ATOM   3847  CB  VAL B   3     -13.818 -15.470 -78.599  1.00 86.66           C  
ANISOU 3847  CB  VAL B   3    11892  11894   9143   -576  -1828    336       C  
ATOM   3848  CG1 VAL B   3     -14.535 -14.341 -77.879  1.00 90.90           C  
ANISOU 3848  CG1 VAL B   3    12585  12521   9432    -78  -1699    454       C  
ATOM   3849  CG2 VAL B   3     -13.141 -14.955 -79.860  1.00 88.29           C  
ANISOU 3849  CG2 VAL B   3    12133  11951   9463   -939  -2034    -26       C  
ATOM   3850  N   TYR B   4     -12.825 -16.231 -75.242  1.00 83.83           N  
ANISOU 3850  N   TYR B   4    11937  11768   8147    324  -1394    603       N  
ATOM   3851  CA  TYR B   4     -13.357 -16.575 -73.923  1.00 80.28           C  
ANISOU 3851  CA  TYR B   4    11468  11546   7488    772  -1058    958       C  
ATOM   3852  C   TYR B   4     -14.269 -15.441 -73.463  1.00 83.84           C  
ANISOU 3852  C   TYR B   4    12164  12097   7593   1259   -853    984       C  
ATOM   3853  O   TYR B   4     -13.903 -14.585 -72.656  1.00102.36           O  
ANISOU 3853  O   TYR B   4    15035  14457   9398   1582   -874    770       O  
ATOM   3854  CB  TYR B   4     -12.227 -16.832 -72.934  1.00 77.46           C  
ANISOU 3854  CB  TYR B   4    11399  11220   6814    821  -1156    915       C  
ATOM   3855  CG  TYR B   4     -12.699 -17.300 -71.574  1.00 84.66           C  
ANISOU 3855  CG  TYR B   4    12282  12422   7462   1227   -820   1317       C  
ATOM   3856  CD1 TYR B   4     -13.016 -18.632 -71.350  1.00 98.21           C  
ANISOU 3856  CD1 TYR B   4    13455  14260   9599   1148   -613   1769       C  
ATOM   3857  CD2 TYR B   4     -12.824 -16.409 -70.514  1.00 78.06           C  
ANISOU 3857  CD2 TYR B   4    11962  11721   5975   1671   -705   1238       C  
ATOM   3858  CE1 TYR B   4     -13.449 -19.065 -70.111  1.00105.90           C  
ANISOU 3858  CE1 TYR B   4    14352  15551  10335   1515   -304   2206       C  
ATOM   3859  CE2 TYR B   4     -13.257 -16.833 -69.273  1.00 95.51           C  
ANISOU 3859  CE2 TYR B   4    14140  14201   7949   1999   -356   1582       C  
ATOM   3860  CZ  TYR B   4     -13.567 -18.162 -69.077  1.00107.05           C  
ANISOU 3860  CZ  TYR B   4    15048  15895   9733   1977   -161   2136       C  
ATOM   3861  OH  TYR B   4     -13.997 -18.591 -67.842  1.00110.89           O  
ANISOU 3861  OH  TYR B   4    15453  16675  10005   2289    179   2515       O  
ATOM   3862  N   LYS B   5     -15.488 -15.443 -73.999  1.00 68.79           N  
ANISOU 3862  N   LYS B   5     9874  10224   6039   1300   -657   1273       N  
ATOM   3863  CA  LYS B   5     -16.456 -14.384 -73.754  1.00 78.15           C  
ANISOU 3863  CA  LYS B   5    11176  11445   7073   1744   -407   1367       C  
ATOM   3864  C   LYS B   5     -17.300 -14.624 -72.506  1.00 76.77           C  
ANISOU 3864  C   LYS B   5    10949  11522   6698   2342    137   1811       C  
ATOM   3865  O   LYS B   5     -18.407 -14.083 -72.405  1.00 89.18           O  
ANISOU 3865  O   LYS B   5    12389  13129   8367   2717    486   2100       O  
ATOM   3866  CB  LYS B   5     -17.352 -14.208 -74.982  1.00 88.03           C  
ANISOU 3866  CB  LYS B   5    11994  12592   8860   1459   -489   1561       C  
ATOM   3867  CG  LYS B   5     -17.624 -15.496 -75.739  1.00 84.90           C  
ANISOU 3867  CG  LYS B   5    11063  12189   9006    976   -594   1860       C  
ATOM   3868  CD  LYS B   5     -18.192 -15.212 -77.119  1.00 82.61           C  
ANISOU 3868  CD  LYS B   5    10501  11763   9125    523   -859   1918       C  
ATOM   3869  CE  LYS B   5     -18.286 -16.482 -77.949  1.00 88.20           C  
ANISOU 3869  CE  LYS B   5    10832  12398  10281    -39  -1056   2074       C  
ATOM   3870  NZ  LYS B   5     -18.774 -16.207 -79.328  1.00 88.61           N  
ANISOU 3870  NZ  LYS B   5    10705  12333  10631   -562  -1381   2106       N  
ATOM   3871  N   HIS B   6     -16.797 -15.415 -71.550  1.00 79.80           N  
ANISOU 3871  N   HIS B   6    11406  12091   6824   2443    238   1924       N  
ATOM   3872  CA  HIS B   6     -17.512 -15.649 -70.305  1.00 83.77           C  
ANISOU 3872  CA  HIS B   6    11889  12896   7044   3018    767   2361       C  
ATOM   3873  C   HIS B   6     -17.028 -14.688 -69.223  1.00 88.83           C  
ANISOU 3873  C   HIS B   6    13326  13590   6834   3458    869   1982       C  
ATOM   3874  O   HIS B   6     -15.873 -14.250 -69.244  1.00 96.51           O  
ANISOU 3874  O   HIS B   6    14742  14349   7577   3163    423   1441       O  
ATOM   3875  CB  HIS B   6     -17.307 -17.086 -69.834  1.00 89.21           C  
ANISOU 3875  CB  HIS B   6    12162  13792   7942   2865    810   2781       C  
ATOM   3876  CG  HIS B   6     -17.559 -18.112 -70.894  1.00 83.89           C  
ANISOU 3876  CG  HIS B   6    10816  12981   8078   2355    609   3039       C  
ATOM   3877  ND1 HIS B   6     -18.810 -18.348 -71.421  1.00 83.19           N  
ANISOU 3877  ND1 HIS B   6    10184  12889   8534   2382    784   3532       N  
ATOM   3878  CD2 HIS B   6     -16.719 -18.969 -71.522  1.00 72.19           C  
ANISOU 3878  CD2 HIS B   6     9148  11324   6958   1799    245   2877       C  
ATOM   3879  CE1 HIS B   6     -18.730 -19.303 -72.330  1.00 75.39           C  
ANISOU 3879  CE1 HIS B   6     8762  11727   8155   1833    480   3618       C  
ATOM   3880  NE2 HIS B   6     -17.472 -19.698 -72.410  1.00 78.42           N  
ANISOU 3880  NE2 HIS B   6     9362  11998   8434   1498    193   3195       N  
ATOM   3881  N   PRO B   7     -17.892 -14.338 -68.266  1.00 92.22           N  
ANISOU 3881  N   PRO B   7    13894  14209   6935   4084   1433   2220       N  
ATOM   3882  CA  PRO B   7     -17.447 -13.488 -67.153  1.00 86.21           C  
ANISOU 3882  CA  PRO B   7    13811  13333   5610   4335   1469   1726       C  
ATOM   3883  C   PRO B   7     -16.474 -14.210 -66.234  1.00 91.86           C  
ANISOU 3883  C   PRO B   7    14628  14141   6136   4034   1235   1657       C  
ATOM   3884  O   PRO B   7     -16.890 -14.850 -65.263  1.00114.94           O  
ANISOU 3884  O   PRO B   7    17390  17358   8925   4289   1592   2037       O  
ATOM   3885  CB  PRO B   7     -18.754 -13.140 -66.431  1.00 87.12           C  
ANISOU 3885  CB  PRO B   7    13905  13618   5578   5066   2201   2087       C  
ATOM   3886  CG  PRO B   7     -19.691 -14.243 -66.792  1.00 85.99           C  
ANISOU 3886  CG  PRO B   7    12924  13766   5983   5108   2526   2903       C  
ATOM   3887  CD  PRO B   7     -19.332 -14.639 -68.194  1.00 94.81           C  
ANISOU 3887  CD  PRO B   7    13668  14733   7624   4491   2020   2915       C  
ATOM   3888  N   ALA B   8     -15.182 -14.107 -66.546  1.00 95.95           N  
ANISOU 3888  N   ALA B   8    15355  14412   6691   3477    642   1245       N  
ATOM   3889  CA  ALA B   8     -14.094 -14.745 -65.795  1.00107.77           C  
ANISOU 3889  CA  ALA B   8    16923  15958   8068   3094    353   1240       C  
ATOM   3890  C   ALA B   8     -14.162 -16.272 -65.837  1.00108.61           C  
ANISOU 3890  C   ALA B   8    16423  16341   8502   2938    439   1804       C  
ATOM   3891  O   ALA B   8     -13.137 -16.933 -66.004  1.00106.82           O  
ANISOU 3891  O   ALA B   8    16075  16041   8472   2464     64   1828       O  
ATOM   3892  CB  ALA B   8     -14.081 -14.256 -64.346  1.00124.59           C  
ANISOU 3892  CB  ALA B   8    19548  18179   9612   3363    526   1128       C  
ATOM   3893  OXT ALA B   8     -15.218 -16.893 -65.715  1.00113.67           O  
ANISOU 3893  OXT ALA B   8    16623  17262   9305   3272    880   2304       O  
TER    3894      ALA B   8                                                      
HETATM 3895  C24 OLC A1401      -5.406 -13.723 -38.031  1.00112.65           C  
HETATM 3896  C3  OLC A1401      -1.805 -16.888 -43.463  1.00 97.02           C  
HETATM 3897  C2  OLC A1401      -2.081 -16.855 -41.961  1.00 92.50           C  
HETATM 3898  C21 OLC A1401      -4.457 -14.538 -40.191  1.00108.78           C  
HETATM 3899  C1  OLC A1401      -2.998 -15.677 -41.638  1.00106.72           C  
HETATM 3900  C22 OLC A1401      -5.526 -14.779 -39.128  1.00111.08           C  
HETATM 3901  O19 OLC A1401      -2.960 -14.697 -42.302  1.00121.30           O  
HETATM 3902  O25 OLC A1401      -6.524 -13.795 -37.190  1.00108.86           O  
HETATM 3903  O23 OLC A1401      -6.795 -14.700 -39.715  1.00106.87           O  
HETATM 3904  O20 OLC A1401      -3.886 -15.761 -40.559  1.00108.41           O  
HETATM 3905  C8  OLC A1402     -23.933 -27.232 -54.505  1.00 96.99           C  
HETATM 3906  C24 OLC A1402     -25.421 -33.669 -43.875  1.00 98.76           C  
HETATM 3907  C7  OLC A1402     -23.078 -27.755 -53.354  1.00 92.35           C  
HETATM 3908  C6  OLC A1402     -23.970 -28.035 -52.146  1.00 97.80           C  
HETATM 3909  C5  OLC A1402     -23.178 -28.814 -51.099  1.00104.61           C  
HETATM 3910  C4  OLC A1402     -24.068 -29.096 -49.891  1.00106.88           C  
HETATM 3911  C3  OLC A1402     -23.311 -29.980 -48.902  1.00102.83           C  
HETATM 3912  C2  OLC A1402     -24.241 -30.400 -47.767  1.00102.01           C  
HETATM 3913  C21 OLC A1402     -23.369 -32.800 -44.995  1.00103.12           C  
HETATM 3914  C1  OLC A1402     -23.521 -31.414 -46.880  1.00116.38           C  
HETATM 3915  C22 OLC A1402     -24.024 -33.097 -43.648  1.00 99.05           C  
HETATM 3916  O19 OLC A1402     -22.522 -31.924 -47.261  1.00127.97           O  
HETATM 3917  O25 OLC A1402     -25.738 -34.551 -42.834  1.00 98.72           O  
HETATM 3918  O23 OLC A1402     -23.247 -34.028 -42.949  1.00102.34           O  
HETATM 3919  O20 OLC A1402     -24.038 -31.743 -45.622  1.00113.22           O  
HETATM 3920  C24 OLC A1403     -28.039 -24.793 -35.586  1.00130.13           C  
HETATM 3921  C3  OLC A1403     -26.344 -22.829 -42.376  1.00104.98           C  
HETATM 3922  C2  OLC A1403     -26.726 -23.932 -41.392  1.00106.67           C  
HETATM 3923  C21 OLC A1403     -27.292 -24.165 -37.884  1.00117.55           C  
HETATM 3924  C1  OLC A1403     -27.105 -23.304 -40.053  1.00115.95           C  
HETATM 3925  C22 OLC A1403     -28.328 -23.903 -36.793  1.00120.72           C  
HETATM 3926  O19 OLC A1403     -26.733 -22.211 -39.787  1.00127.74           O  
HETATM 3927  O25 OLC A1403     -28.333 -24.090 -34.410  1.00139.66           O  
HETATM 3928  O23 OLC A1403     -28.261 -22.559 -36.406  1.00109.39           O  
HETATM 3929  O20 OLC A1403     -27.891 -24.012 -39.138  1.00113.58           O  
HETATM 3930  C24 OLC A1404     -10.116 -38.091 -37.403  1.00124.28           C  
HETATM 3931  C21 OLC A1404     -11.247 -36.965 -39.320  1.00119.56           C  
HETATM 3932  C1  OLC A1404     -12.240 -35.783 -41.087  1.00116.19           C  
HETATM 3933  C22 OLC A1404      -9.907 -37.202 -38.628  1.00124.02           C  
HETATM 3934  O19 OLC A1404     -12.367 -34.688 -41.523  1.00109.08           O  
HETATM 3935  O25 OLC A1404      -8.878 -38.357 -36.803  1.00123.62           O  
HETATM 3936  O23 OLC A1404      -9.026 -37.832 -39.516  1.00127.84           O  
HETATM 3937  O20 OLC A1404     -11.055 -36.144 -40.437  1.00121.43           O  
HETATM 3938  C24 OLC A1405     -27.473 -35.087 -47.779  1.00111.67           C  
HETATM 3939  C6  OLC A1405     -28.895 -30.230 -54.760  1.00 91.07           C  
HETATM 3940  C5  OLC A1405     -29.046 -31.748 -54.682  1.00 90.78           C  
HETATM 3941  C4  OLC A1405     -28.187 -32.291 -53.542  1.00100.45           C  
HETATM 3942  C3  OLC A1405     -28.894 -32.062 -52.208  1.00108.92           C  
HETATM 3943  C2  OLC A1405     -28.043 -31.147 -51.330  1.00112.64           C  
HETATM 3944  C21 OLC A1405     -28.980 -33.217 -48.464  1.00110.36           C  
HETATM 3945  C1  OLC A1405     -28.308 -31.455 -49.858  1.00118.55           C  
HETATM 3946  C22 OLC A1405     -28.296 -33.901 -47.283  1.00110.43           C  
HETATM 3947  O19 OLC A1405     -28.761 -30.620 -49.151  1.00119.06           O  
HETATM 3948  O25 OLC A1405     -26.599 -35.502 -46.765  1.00113.08           O  
HETATM 3949  O23 OLC A1405     -27.451 -32.985 -46.644  1.00113.53           O  
HETATM 3950  O20 OLC A1405     -28.009 -32.720 -49.341  1.00112.77           O  
HETATM 3951  C10 OLC A1406      -4.485 -17.388 -48.856  1.00 97.77           C  
HETATM 3952  C9  OLC A1406      -5.138 -16.845 -47.850  1.00 95.66           C  
HETATM 3953  C11 OLC A1406      -4.570 -18.894 -49.097  1.00 91.94           C  
HETATM 3954  C8  OLC A1406      -5.052 -15.339 -47.608  1.00 88.36           C  
HETATM 3955  C12 OLC A1406      -3.626 -19.282 -50.232  1.00 86.70           C  
HETATM 3956  C7  OLC A1406      -3.591 -14.900 -47.663  1.00 80.68           C  
HETATM 3957  C6  OLC A1406      -3.485 -13.427 -47.278  1.00 79.55           C  
HETATM 3958  C5  OLC A1406      -3.229 -13.312 -45.777  1.00 81.68           C  
HETATM 3959  C4  OLC A1406      -3.171 -11.839 -45.381  1.00 84.41           C  
HETATM 3960  C3  OLC A1406      -2.729 -11.720 -43.924  1.00 91.93           C  
HETATM 3961  C1  CLR A1407     -36.468  -6.342 -45.616  1.00108.53           C  
HETATM 3962  C2  CLR A1407     -37.630  -6.502 -44.634  1.00109.74           C  
HETATM 3963  C3  CLR A1407     -37.263  -5.944 -43.275  1.00104.99           C  
HETATM 3964  C4  CLR A1407     -36.887  -4.479 -43.395  1.00 99.10           C  
HETATM 3965  C5  CLR A1407     -35.822  -4.246 -44.440  1.00103.66           C  
HETATM 3966  C6  CLR A1407     -34.743  -3.531 -44.153  1.00108.27           C  
HETATM 3967  C7  CLR A1407     -33.632  -3.231 -45.109  1.00116.15           C  
HETATM 3968  C8  CLR A1407     -34.052  -3.461 -46.553  1.00112.67           C  
HETATM 3969  C9  CLR A1407     -34.775  -4.809 -46.672  1.00101.64           C  
HETATM 3970  C10 CLR A1407     -36.070  -4.870 -45.810  1.00107.62           C  
HETATM 3971  C11 CLR A1407     -35.010  -5.218 -48.140  1.00 97.79           C  
HETATM 3972  C12 CLR A1407     -33.803  -5.029 -49.069  1.00102.55           C  
HETATM 3973  C13 CLR A1407     -33.223  -3.612 -48.971  1.00115.48           C  
HETATM 3974  C14 CLR A1407     -32.843  -3.476 -47.484  1.00117.11           C  
HETATM 3975  C15 CLR A1407     -31.815  -2.356 -47.466  1.00121.33           C  
HETATM 3976  C16 CLR A1407     -30.879  -2.912 -48.529  1.00124.04           C  
HETATM 3977  C17 CLR A1407     -31.828  -3.378 -49.659  1.00122.38           C  
HETATM 3978  C18 CLR A1407     -34.321  -2.593 -49.328  1.00115.04           C  
HETATM 3979  C19 CLR A1407     -37.234  -4.114 -46.480  1.00112.16           C  
HETATM 3980  C20 CLR A1407     -31.636  -2.540 -50.949  1.00116.40           C  
HETATM 3981  C21 CLR A1407     -32.129  -1.092 -50.884  1.00112.78           C  
HETATM 3982  C22 CLR A1407     -32.182  -3.263 -52.195  1.00117.36           C  
HETATM 3983  C23 CLR A1407     -32.320  -2.392 -53.443  1.00122.39           C  
HETATM 3984  C24 CLR A1407     -30.996  -1.937 -54.052  1.00121.31           C  
HETATM 3985  C25 CLR A1407     -30.352  -2.882 -55.049  1.00119.62           C  
HETATM 3986  C26 CLR A1407     -29.017  -2.340 -55.530  1.00118.16           C  
HETATM 3987  C27 CLR A1407     -31.278  -3.135 -56.227  1.00114.46           C  
HETATM 3988  O1  CLR A1407     -38.362  -6.084 -42.371  1.00103.42           O  
HETATM 3989  O   HOH A1501     -13.957 -18.806 -79.530  1.00 61.66           O  
HETATM 3990  O   HOH A1502     -18.618  -9.133 -74.290  1.00 79.20           O  
HETATM 3991  O   HOH A1503     -22.214 -32.976 -22.091  1.00 68.87           O  
HETATM 3992  O   HOH A1504      -4.963 -21.885 -25.051  1.00 40.58           O  
HETATM 3993  O   HOH A1505     -23.472 -14.503 -32.990  1.00 57.24           O  
HETATM 3994  O   HOH A1506      -6.809 -14.774 -63.217  1.00 74.23           O  
HETATM 3995  O   HOH A1507     -16.270 -65.640 -14.189  1.00 67.42           O  
HETATM 3996  O   HOH A1508     -17.538 -38.612 -36.098  1.00 65.18           O  
HETATM 3997  O   HOH A1509     -16.411   3.638 -72.624  1.00 86.48           O  
HETATM 3998  O   HOH A1510      -0.863 -22.811 -79.755  1.00 62.02           O  
HETATM 3999  O   HOH A1511      -7.900  -8.852 -27.080  1.00 78.45           O  
HETATM 4000  O   HOH A1512      -5.629 -37.134 -41.903  1.00 69.32           O  
HETATM 4001  O   HOH A1513       0.163  -8.807 -67.112  1.00 76.80           O  
HETATM 4002  O   HOH A1514      -0.832 -19.817 -31.364  1.00 57.38           O  
HETATM 4003  O   HOH A1515     -26.881  -4.138 -79.312  1.00 67.73           O  
HETATM 4004  O   HOH D 201      -1.484  -5.111 -24.599  1.00 70.69           O  
HETATM 4005  O   HOH D 202     -24.268 -18.650 -21.861  1.00 64.14           O  
CONECT   57 2546                                                                
CONECT  730 1342                                                                
CONECT 1342  730                                                                
CONECT 2546   57                                                                
CONECT 3030 3574                                                                
CONECT 3574 3030                                                                
CONECT 3827 3828 3831                                                           
CONECT 3828 3827 3829                                                           
CONECT 3829 3828 3830 3832                                                      
CONECT 3830 3829                                                                
CONECT 3831 3827                                                                
CONECT 3832 3829                                                                
CONECT 3895 3900 3902                                                           
CONECT 3896 3897                                                                
CONECT 3897 3896 3899                                                           
CONECT 3898 3900 3904                                                           
CONECT 3899 3897 3901 3904                                                      
CONECT 3900 3895 3898 3903                                                      
CONECT 3901 3899                                                                
CONECT 3902 3895                                                                
CONECT 3903 3900                                                                
CONECT 3904 3898 3899                                                           
CONECT 3905 3907                                                                
CONECT 3906 3915 3917                                                           
CONECT 3907 3905 3908                                                           
CONECT 3908 3907 3909                                                           
CONECT 3909 3908 3910                                                           
CONECT 3910 3909 3911                                                           
CONECT 3911 3910 3912                                                           
CONECT 3912 3911 3914                                                           
CONECT 3913 3915 3919                                                           
CONECT 3914 3912 3916 3919                                                      
CONECT 3915 3906 3913 3918                                                      
CONECT 3916 3914                                                                
CONECT 3917 3906                                                                
CONECT 3918 3915                                                                
CONECT 3919 3913 3914                                                           
CONECT 3920 3925 3927                                                           
CONECT 3921 3922                                                                
CONECT 3922 3921 3924                                                           
CONECT 3923 3925 3929                                                           
CONECT 3924 3922 3926 3929                                                      
CONECT 3925 3920 3923 3928                                                      
CONECT 3926 3924                                                                
CONECT 3927 3920                                                                
CONECT 3928 3925                                                                
CONECT 3929 3923 3924                                                           
CONECT 3930 3933 3935                                                           
CONECT 3931 3933 3937                                                           
CONECT 3932 3934 3937                                                           
CONECT 3933 3930 3931 3936                                                      
CONECT 3934 3932                                                                
CONECT 3935 3930                                                                
CONECT 3936 3933                                                                
CONECT 3937 3931 3932                                                           
CONECT 3938 3946 3948                                                           
CONECT 3939 3940                                                                
CONECT 3940 3939 3941                                                           
CONECT 3941 3940 3942                                                           
CONECT 3942 3941 3943                                                           
CONECT 3943 3942 3945                                                           
CONECT 3944 3946 3950                                                           
CONECT 3945 3943 3947 3950                                                      
CONECT 3946 3938 3944 3949                                                      
CONECT 3947 3945                                                                
CONECT 3948 3938                                                                
CONECT 3949 3946                                                                
CONECT 3950 3944 3945                                                           
CONECT 3951 3952 3953                                                           
CONECT 3952 3951 3954                                                           
CONECT 3953 3951 3955                                                           
CONECT 3954 3952 3956                                                           
CONECT 3955 3953                                                                
CONECT 3956 3954 3957                                                           
CONECT 3957 3956 3958                                                           
CONECT 3958 3957 3959                                                           
CONECT 3959 3958 3960                                                           
CONECT 3960 3959                                                                
CONECT 3961 3962 3970                                                           
CONECT 3962 3961 3963                                                           
CONECT 3963 3962 3964 3988                                                      
CONECT 3964 3963 3965                                                           
CONECT 3965 3964 3966 3970                                                      
CONECT 3966 3965 3967                                                           
CONECT 3967 3966 3968                                                           
CONECT 3968 3967 3969 3974                                                      
CONECT 3969 3968 3970 3971                                                      
CONECT 3970 3961 3965 3969 3979                                                 
CONECT 3971 3969 3972                                                           
CONECT 3972 3971 3973                                                           
CONECT 3973 3972 3974 3977 3978                                                 
CONECT 3974 3968 3973 3975                                                      
CONECT 3975 3974 3976                                                           
CONECT 3976 3975 3977                                                           
CONECT 3977 3973 3976 3980                                                      
CONECT 3978 3973                                                                
CONECT 3979 3970                                                                
CONECT 3980 3977 3981 3982                                                      
CONECT 3981 3980                                                                
CONECT 3982 3980 3983                                                           
CONECT 3983 3982 3984                                                           
CONECT 3984 3983 3985                                                           
CONECT 3985 3984 3986 3987                                                      
CONECT 3986 3985                                                                
CONECT 3987 3985                                                                
CONECT 3988 3963                                                                
MASTER      527    0    8   16   18    0    8    6 3990    3  106   44          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.