HEADER    HYDROLASE                               28-JUL-16   5L14              
TITLE     THE CRYSTAL STRUCTURE OF NEURAMINIDASE FROM A/SHANGHAI/2/2013 (H7N9)  
TITLE    2 INFLUENZA VIRUS                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEURAMINIDASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.18;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/SHANGHAI/02/2013(H7N9));   
SOURCE   3 ORGANISM_TAXID: 1332244;                                             
SOURCE   4 STRAIN: A/SHANGHAI/02/2013(H7N9);                                    
SOURCE   5 GENE: NA;                                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    NEURAMINIDASE, H7N9, HYDROLASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.YANG,J.STEVENS                                                      
REVDAT   4   04-OCT-23 5L14    1       HETSYN LINK                              
REVDAT   3   29-JUL-20 5L14    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   04-OCT-17 5L14    1       JRNL                                     
REVDAT   1   09-AUG-17 5L14    0                                                
JRNL        AUTH   L.V.GUBAREVA,K.SLEEMAN,Z.GUO,H.YANG,E.HODGES,C.T.DAVIS,      
JRNL        AUTH 2 T.BARANOVICH,J.STEVENS                                       
JRNL        TITL   DRUG SUSCEPTIBILITY EVALUATION OF AN INFLUENZA A(H7N9) VIRUS 
JRNL        TITL 2 BY ANALYZING RECOMBINANT NEURAMINIDASE PROTEINS.             
JRNL        REF    J. INFECT. DIS.               V. 216  S566 2017              
JRNL        REFN                   ESSN 1537-6613                               
JRNL        PMID   28934455                                                     
JRNL        DOI    10.1093/INFDIS/JIW625                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 40105                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2016                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 35.6729 -  4.5763    0.99     2947   155  0.1438 0.1381        
REMARK   3     2  4.5763 -  3.6335    0.99     2778   155  0.1255 0.1344        
REMARK   3     3  3.6335 -  3.1745    0.99     2770   131  0.1491 0.1669        
REMARK   3     4  3.1745 -  2.8844    0.99     2737   150  0.1680 0.1842        
REMARK   3     5  2.8844 -  2.6777    0.99     2718   133  0.1822 0.1942        
REMARK   3     6  2.6777 -  2.5199    0.99     2732   142  0.1901 0.2202        
REMARK   3     7  2.5199 -  2.3937    0.99     2691   137  0.1883 0.2470        
REMARK   3     8  2.3937 -  2.2895    0.99     2698   148  0.1954 0.2417        
REMARK   3     9  2.2895 -  2.2014    0.99     2674   161  0.2008 0.2384        
REMARK   3    10  2.2014 -  2.1255    0.99     2704   121  0.2055 0.2116        
REMARK   3    11  2.1255 -  2.0590    0.99     2675   157  0.2043 0.2361        
REMARK   3    12  2.0590 -  2.0002    0.99     2667   133  0.2093 0.2481        
REMARK   3    13  2.0002 -  1.9475    0.98     2662   135  0.2406 0.2373        
REMARK   3    14  1.9475 -  1.9000    0.98     2636   158  0.2412 0.2616        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.650           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           3289                                  
REMARK   3   ANGLE     :  0.878           4488                                  
REMARK   3   CHIRALITY :  0.035            502                                  
REMARK   3   PLANARITY :  0.004            568                                  
REMARK   3   DIHEDRAL  : 11.937           1221                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 83 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3375 -21.7244 -49.5646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2264 T22:   0.2012                                     
REMARK   3      T33:   0.2348 T12:  -0.0086                                     
REMARK   3      T13:   0.0048 T23:   0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3348 L22:   0.0637                                     
REMARK   3      L33:   0.0613 L12:  -0.0895                                     
REMARK   3      L13:  -0.0733 L23:   0.0487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0107 S12:  -0.0169 S13:  -0.0526                       
REMARK   3      S21:   0.0140 S22:   0.0731 S23:  -0.0005                       
REMARK   3      S31:  -0.0668 S32:  -0.0188 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 136 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.0465 -12.0738 -55.1195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2178 T22:   0.1986                                     
REMARK   3      T33:   0.2475 T12:  -0.0002                                     
REMARK   3      T13:  -0.0011 T23:  -0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1496 L22:   0.1217                                     
REMARK   3      L33:   0.1196 L12:   0.0082                                     
REMARK   3      L13:   0.0786 L23:  -0.0953                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0325 S12:   0.0494 S13:  -0.0451                       
REMARK   3      S21:   0.0017 S22:   0.0014 S23:  -0.0130                       
REMARK   3      S31:   0.0752 S32:  -0.0993 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 157 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1767  -6.6279 -69.4291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2593 T22:   0.2454                                     
REMARK   3      T33:   0.2705 T12:  -0.0004                                     
REMARK   3      T13:   0.0215 T23:  -0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0374 L22:   0.0514                                     
REMARK   3      L33:   0.0420 L12:   0.0444                                     
REMARK   3      L13:   0.0253 L23:   0.0305                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1164 S12:   0.2423 S13:   0.0028                       
REMARK   3      S21:  -0.1191 S22:   0.1014 S23:  -0.1717                       
REMARK   3      S31:  -0.0046 S32:   0.1383 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 158 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7850  -8.3369 -53.0256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1975 T22:   0.2102                                     
REMARK   3      T33:   0.2505 T12:   0.0011                                     
REMARK   3      T13:  -0.0048 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0147 L22:   0.0776                                     
REMARK   3      L33:   0.1052 L12:   0.0342                                     
REMARK   3      L13:  -0.0326 L23:  -0.0469                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0083 S12:  -0.0215 S13:   0.1176                       
REMARK   3      S21:   0.0222 S22:  -0.0394 S23:   0.0324                       
REMARK   3      S31:   0.0012 S32:   0.0371 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 218 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9694  -5.1633 -49.5225              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2241 T22:   0.2007                                     
REMARK   3      T33:   0.2736 T12:   0.0091                                     
REMARK   3      T13:   0.0098 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0693 L22:   0.0689                                     
REMARK   3      L33:   0.1029 L12:   0.0538                                     
REMARK   3      L13:   0.0791 L23:   0.0404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0451 S12:  -0.0353 S13:   0.1222                       
REMARK   3      S21:  -0.0164 S22:   0.0624 S23:  -0.0989                       
REMARK   3      S31:  -0.0286 S32:   0.0078 S33:   0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 246 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  28.2211 -15.4076 -49.3392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2414 T22:   0.1995                                     
REMARK   3      T33:   0.2659 T12:   0.0127                                     
REMARK   3      T13:  -0.0001 T23:  -0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0539 L22:   0.0889                                     
REMARK   3      L33:   0.0576 L12:  -0.0376                                     
REMARK   3      L13:   0.0380 L23:   0.0151                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0068 S12:  -0.0470 S13:   0.0480                       
REMARK   3      S21:   0.0287 S22:   0.0534 S23:  -0.0537                       
REMARK   3      S31:   0.0985 S32:   0.0644 S33:   0.0002                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 247 THROUGH 318 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8543 -23.3512 -47.4600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2339 T22:   0.1956                                     
REMARK   3      T33:   0.2852 T12:   0.0114                                     
REMARK   3      T13:  -0.0103 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4921 L22:   0.1889                                     
REMARK   3      L33:   0.3275 L12:  -0.0745                                     
REMARK   3      L13:   0.4032 L23:  -0.0906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0683 S12:  -0.0303 S13:  -0.0655                       
REMARK   3      S21:   0.0543 S22:  -0.0208 S23:  -0.1515                       
REMARK   3      S31:   0.0235 S32:   0.0269 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 411 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8300 -34.8672 -57.6680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2306 T22:   0.1984                                     
REMARK   3      T33:   0.2806 T12:   0.0246                                     
REMARK   3      T13:   0.0084 T23:  -0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2706 L22:   0.3754                                     
REMARK   3      L33:   0.0506 L12:  -0.1331                                     
REMARK   3      L13:   0.1162 L23:  -0.0793                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0060 S12:   0.0401 S13:  -0.0509                       
REMARK   3      S21:  -0.0425 S22:   0.0115 S23:  -0.1055                       
REMARK   3      S31:   0.0832 S32:   0.0234 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 440 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6577 -20.8551 -58.4992              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2045 T22:   0.1818                                     
REMARK   3      T33:   0.2327 T12:   0.0163                                     
REMARK   3      T13:  -0.0005 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4442 L22:   0.3508                                     
REMARK   3      L33:   0.1220 L12:   0.0103                                     
REMARK   3      L13:   0.1358 L23:   0.1765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0295 S12:   0.0500 S13:  -0.0211                       
REMARK   3      S21:  -0.0668 S22:   0.0025 S23:   0.0320                       
REMARK   3      S31:   0.0657 S32:  -0.0462 S33:  -0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 441 THROUGH 470 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4573 -24.5234 -63.0146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2171 T22:   0.2319                                     
REMARK   3      T33:   0.2718 T12:   0.0042                                     
REMARK   3      T13:   0.0025 T23:  -0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2195 L22:   0.2103                                     
REMARK   3      L33:   0.0358 L12:  -0.0296                                     
REMARK   3      L13:   0.0658 L23:   0.0591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0179 S12:   0.1062 S13:  -0.0832                       
REMARK   3      S21:   0.0049 S22:   0.0088 S23:  -0.0240                       
REMARK   3      S31:  -0.0127 S32:  -0.0295 S33:  -0.0001                       
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 5L14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223043.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40109                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4WMJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES:NAOH PH 7.5, 25% PEG 1000,   
REMARK 280  MICROBATCH, TEMPERATURE 293K                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 3 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   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   Y,X,-Z                                                  
REMARK 290      14555   -Y,-X,-Z                                                
REMARK 290      15555   Y,-X,Z                                                  
REMARK 290      16555   -Y,X,Z                                                  
REMARK 290      17555   X,Z,-Y                                                  
REMARK 290      18555   -X,Z,Y                                                  
REMARK 290      19555   -X,-Z,-Y                                                
REMARK 290      20555   X,-Z,Y                                                  
REMARK 290      21555   Z,Y,-X                                                  
REMARK 290      22555   Z,-Y,X                                                  
REMARK 290      23555   -Z,Y,X                                                  
REMARK 290      24555   -Z,-Y,-X                                                
REMARK 290      25555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      26555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      27555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      28555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      29555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      30555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      31555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      32555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      33555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      34555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      35555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      36555   -Y+1/2,-Z+1/2,X+1/2                                     
REMARK 290      37555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      38555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290      39555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      40555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      41555   X+1/2,Z+1/2,-Y+1/2                                      
REMARK 290      42555   -X+1/2,Z+1/2,Y+1/2                                      
REMARK 290      43555   -X+1/2,-Z+1/2,-Y+1/2                                    
REMARK 290      44555   X+1/2,-Z+1/2,Y+1/2                                      
REMARK 290      45555   Z+1/2,Y+1/2,-X+1/2                                      
REMARK 290      46555   Z+1/2,-Y+1/2,X+1/2                                      
REMARK 290      47555   -Z+1/2,Y+1/2,X+1/2                                      
REMARK 290      48555   -Z+1/2,-Y+1/2,-X+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  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  25  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000       90.93250            
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       90.93250            
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000       90.93250            
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000       90.93250            
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       90.93250            
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       90.93250            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 24850 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 70.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 938  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1008  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1020  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    74                                                      
REMARK 465     SER A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     ASP A    77                                                      
REMARK 465     SER A    78                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     PRO A    81                                                      
REMARK 465     GLY A    82                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   822     O    HOH A   975              1.91            
REMARK 500   O    HOH A   946     O    HOH A   947              2.06            
REMARK 500   O    HOH A   743     O    HOH A   884              2.11            
REMARK 500   O    HOH A   904     O    HOH A   954              2.11            
REMARK 500   O    HOH A   802     O    HOH A   881              2.13            
REMARK 500   O    HOH A   601     O    HOH A   928              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 112       53.95   -147.97                                   
REMARK 500    SER A 165       -3.37     73.78                                   
REMARK 500    SER A 165       -3.04     73.78                                   
REMARK 500    ASN A 202       34.51   -155.92                                   
REMARK 500    ILE A 224       73.00     52.96                                   
REMARK 500    THR A 227     -152.73   -132.64                                   
REMARK 500    LYS A 266      149.54   -175.27                                   
REMARK 500    ARG A 286       97.46      5.38                                   
REMARK 500    THR A 287       46.93     -0.71                                   
REMARK 500    CYS A 293     -167.93   -120.26                                   
REMARK 500    TRP A 297      -84.92    -91.04                                   
REMARK 500    ASP A 357       53.73   -149.85                                   
REMARK 500    SER A 404     -138.44   -112.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1019        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A1020        DISTANCE =  7.01 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 511  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 295   O                                                      
REMARK 620 2 GLY A 299   O    86.5                                              
REMARK 620 3 ASP A 326   OD2  86.9  92.0                                        
REMARK 620 4 ASN A 348   O    98.9 161.1 106.3                                  
REMARK 620 5 HOH A 664   O    98.0  81.8 171.8  79.6                            
REMARK 620 6 HOH A 681   O   174.8  90.7  88.8  85.1  86.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5L15   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L17   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L18   RELATED DB: PDB                                   
DBREF  5L14 A   83   470  UNP    R4NFR6   R4NFR6_9INFA    78    465             
SEQADV 5L14 GLY A   74  UNP  R4NFR6              EXPRESSION TAG                 
SEQADV 5L14 SER A   75  UNP  R4NFR6              EXPRESSION TAG                 
SEQADV 5L14 GLY A   76  UNP  R4NFR6              EXPRESSION TAG                 
SEQADV 5L14 ASP A   77  UNP  R4NFR6              EXPRESSION TAG                 
SEQADV 5L14 SER A   78  UNP  R4NFR6              EXPRESSION TAG                 
SEQADV 5L14 GLY A   79  UNP  R4NFR6              EXPRESSION TAG                 
SEQADV 5L14 SER A   80  UNP  R4NFR6              EXPRESSION TAG                 
SEQADV 5L14 PRO A   81  UNP  R4NFR6              EXPRESSION TAG                 
SEQADV 5L14 GLY A   82  UNP  R4NFR6              EXPRESSION TAG                 
SEQRES   1 A  397  GLY SER GLY ASP SER GLY SER PRO GLY ARG ASN PHE ASN          
SEQRES   2 A  397  ASN LEU THR LYS GLY LEU CYS THR ILE ASN SER TRP HIS          
SEQRES   3 A  397  ILE TYR GLY LYS ASP ASN ALA VAL ARG ILE GLY GLU SER          
SEQRES   4 A  397  SER ASP VAL LEU VAL THR ARG GLU PRO TYR VAL SER CYS          
SEQRES   5 A  397  ASP PRO ASP GLU CYS ARG PHE TYR ALA LEU SER GLN GLY          
SEQRES   6 A  397  THR THR ILE ARG GLY LYS HIS SER ASN GLY THR ILE HIS          
SEQRES   7 A  397  ASP ARG SER GLN TYR ARG ALA LEU ILE SER TRP PRO LEU          
SEQRES   8 A  397  SER SER PRO PRO THR VAL TYR ASN SER ARG VAL GLU CYS          
SEQRES   9 A  397  ILE GLY TRP SER SER THR SER CYS HIS ASP GLY LYS SER          
SEQRES  10 A  397  ARG MET SER ILE CYS ILE SER GLY PRO ASN ASN ASN ALA          
SEQRES  11 A  397  SER ALA VAL VAL TRP TYR ASN ARG ARG PRO VAL ALA GLU          
SEQRES  12 A  397  ILE ASN THR TRP ALA ARG ASN ILE LEU ARG THR GLN GLU          
SEQRES  13 A  397  SER GLU CYS VAL CYS HIS ASN GLY VAL CYS PRO VAL VAL          
SEQRES  14 A  397  PHE THR ASP GLY SER ALA THR GLY PRO ALA ASP THR ARG          
SEQRES  15 A  397  ILE TYR TYR PHE LYS GLU GLY LYS ILE LEU LYS TRP GLU          
SEQRES  16 A  397  SER LEU THR GLY THR ALA LYS HIS ILE GLU GLU CYS SER          
SEQRES  17 A  397  CYS TYR GLY GLU ARG THR GLY ILE THR CYS THR CYS ARG          
SEQRES  18 A  397  ASP ASN TRP GLN GLY SER ASN ARG PRO VAL ILE GLN ILE          
SEQRES  19 A  397  ASP PRO VAL ALA MET THR HIS THR SER GLN TYR ILE CYS          
SEQRES  20 A  397  SER PRO VAL LEU THR ASP ASN PRO ARG PRO ASN ASP PRO          
SEQRES  21 A  397  ASN ILE GLY LYS CYS ASN ASP PRO TYR PRO GLY ASN ASN          
SEQRES  22 A  397  ASN ASN GLY VAL LYS GLY PHE SER TYR LEU ASP GLY ALA          
SEQRES  23 A  397  ASN THR TRP LEU GLY ARG THR ILE SER THR ALA SER ARG          
SEQRES  24 A  397  SER GLY TYR GLU MET LEU LYS VAL PRO ASN ALA LEU THR          
SEQRES  25 A  397  ASP ASP ARG SER LYS PRO ILE GLN GLY GLN THR ILE VAL          
SEQRES  26 A  397  LEU ASN ALA ASP TRP SER GLY TYR SER GLY SER PHE MET          
SEQRES  27 A  397  ASP TYR TRP ALA GLU GLY ASP CYS TYR ARG ALA CYS PHE          
SEQRES  28 A  397  TYR VAL GLU LEU ILE ARG GLY ARG PRO LYS GLU ASP LYS          
SEQRES  29 A  397  VAL TRP TRP THR SER ASN SER ILE VAL SER MET CYS SER          
SEQRES  30 A  397  SER THR GLU PHE LEU GLY GLN TRP ASN TRP PRO ASP GLY          
SEQRES  31 A  397  ALA LYS ILE GLU TYR PHE LEU                                  
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    BMA  B   3      11                                                       
HET    MAN  B   4      11                                                       
HET    MAN  B   5      11                                                       
HET    MAN  B   6      11                                                       
HET    MAN  B   7      11                                                       
HET    MAN  B   8      11                                                       
HET    MAN  B   9      11                                                       
HET    NAG  A 501      14                                                       
HET     CA  A 511       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM      CA CALCIUM ION                                                      
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   2  BMA    C6 H12 O6                                                    
FORMUL   2  MAN    6(C6 H12 O6)                                                 
FORMUL   4   CA    CA 2+                                                        
FORMUL   5  HOH   *420(H2 O)                                                    
HELIX    1 AA1 ASN A  105  GLU A  111  1                                   7    
HELIX    2 AA2 GLY A  143  ASN A  147  5                                   5    
HELIX    3 AA3 ASP A  357  ASN A  360  5                                   4    
HELIX    4 AA4 LYS A  465  LEU A  470  5                                   6    
SHEET    1 AA1 2 GLY A  91  LEU A  92  0                                        
SHEET    2 AA1 2 CYS A 419  TYR A 420  1  O  TYR A 420   N  GLY A  91           
SHEET    1 AA2 4 SER A  97  LYS A 103  0                                        
SHEET    2 AA2 4 THR A 441  SER A 451 -1  O  CYS A 449   N  HIS A  99           
SHEET    3 AA2 4 ALA A 422  GLY A 431 -1  N  VAL A 426   O  VAL A 446           
SHEET    4 AA2 4 SER A 407  MET A 411 -1  N  GLY A 408   O  TYR A 425           
SHEET    1 AA3 4 LEU A 116  CYS A 125  0                                        
SHEET    2 AA3 4 CYS A 130  THR A 140 -1  O  TYR A 133   N  TYR A 122           
SHEET    3 AA3 4 ALA A 158  PRO A 163 -1  O  ILE A 160   N  ALA A 134           
SHEET    4 AA3 4 ARG A 174  ILE A 178 -1  O  ARG A 174   N  SER A 161           
SHEET    1 AA4 4 SER A 181  HIS A 186  0                                        
SHEET    2 AA4 4 ARG A 191  SER A 197 -1  O  MET A 192   N  CYS A 185           
SHEET    3 AA4 4 SER A 204  TYR A 209 -1  O  TRP A 208   N  SER A 193           
SHEET    4 AA4 4 ARG A 212  ASN A 218 -1  O  ALA A 215   N  VAL A 207           
SHEET    1 AA5 3 VAL A 238  GLY A 246  0                                        
SHEET    2 AA5 3 ALA A 252  LYS A 260 -1  O  ARG A 255   N  PHE A 243           
SHEET    3 AA5 3 LYS A 263  SER A 269 -1  O  LEU A 265   N  TYR A 258           
SHEET    1 AA6 4 GLU A 278  GLU A 285  0                                        
SHEET    2 AA6 4 GLY A 288  ARG A 294 -1  O  THR A 292   N  SER A 281           
SHEET    3 AA6 4 PRO A 303  ASP A 308 -1  O  ILE A 307   N  ILE A 289           
SHEET    4 AA6 4 THR A 313  TYR A 318 -1  O  GLN A 317   N  VAL A 304           
SHEET    1 AA7 4 SER A 354  TYR A 355  0                                        
SHEET    2 AA7 4 TRP A 362  ARG A 365 -1  O  TRP A 362   N  TYR A 355           
SHEET    3 AA7 4 SER A 373  LYS A 379 -1  O  LEU A 378   N  LEU A 363           
SHEET    4 AA7 4 GLN A 393  TRP A 403 -1  O  GLN A 393   N  LYS A 379           
SSBOND   1 CYS A   93    CYS A  419                          1555   1555  2.03  
SSBOND   2 CYS A  125    CYS A  130                          1555   1555  2.03  
SSBOND   3 CYS A  177    CYS A  195                          1555   1555  2.03  
SSBOND   4 CYS A  185    CYS A  232                          1555   1555  2.04  
SSBOND   5 CYS A  234    CYS A  239                          1555   1555  2.03  
SSBOND   6 CYS A  280    CYS A  293                          1555   1555  2.04  
SSBOND   7 CYS A  282    CYS A  291                          1555   1555  2.03  
SSBOND   8 CYS A  320    CYS A  338                          1555   1555  2.03  
SSBOND   9 CYS A  423    CYS A  449                          1555   1555  2.03  
LINK         ND2 ASN A 147                 C1  NAG A 501     1555   1555  1.44  
LINK         ND2 ASN A 202                 C1  NAG B   1     1555   1555  1.44  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.45  
LINK         O4  NAG B   2                 C1  BMA B   3     1555   1555  1.44  
LINK         O3  BMA B   3                 C1  MAN B   4     1555   1555  1.44  
LINK         O6  BMA B   3                 C1  MAN B   7     1555   1555  1.44  
LINK         O2  MAN B   4                 C1  MAN B   5     1555   1555  1.44  
LINK         O2  MAN B   5                 C1  MAN B   6     1555   1555  1.44  
LINK         O3  MAN B   7                 C1  MAN B   8     1555   1555  1.44  
LINK         O6  MAN B   7                 C1  MAN B   9     1555   1555  1.44  
LINK         O   ASP A 295                CA    CA A 511     1555   1555  2.31  
LINK         O   GLY A 299                CA    CA A 511     1555   1555  2.34  
LINK         OD2 ASP A 326                CA    CA A 511     1555   1555  2.45  
LINK         O   ASN A 348                CA    CA A 511     1555   1555  2.44  
LINK        CA    CA A 511                 O   HOH A 664     1555   1555  2.50  
LINK        CA    CA A 511                 O   HOH A 681     1555   1555  2.46  
CISPEP   1 ASN A  327    PRO A  328          0         0.47                     
CISPEP   2 ARG A  432    PRO A  433          0         5.03                     
CRYST1  181.865  181.865  181.865  90.00  90.00  90.00 I 4 3 2      48          
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      0.005499  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005499  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005499        0.00000                         
ATOM      1  N   ARG A  83      10.387  -7.921 -30.818  1.00 50.18           N  
ATOM      2  CA  ARG A  83      10.388  -9.367 -31.011  1.00 50.23           C  
ATOM      3  C   ARG A  83      11.765  -9.968 -30.745  1.00 47.46           C  
ATOM      4  O   ARG A  83      12.667  -9.283 -30.264  1.00 46.84           O  
ATOM      5  CB  ARG A  83       9.919  -9.714 -32.425  1.00 52.16           C  
ATOM      6  CG  ARG A  83      10.282  -8.680 -33.478  1.00 55.29           C  
ATOM      7  CD  ARG A  83       9.247  -8.674 -34.593  1.00 58.38           C  
ATOM      8  NE  ARG A  83       9.778  -8.189 -35.864  1.00 61.07           N  
ATOM      9  CZ  ARG A  83       9.124  -8.264 -37.020  1.00 62.05           C  
ATOM     10  NH1 ARG A  83       7.913  -8.804 -37.064  1.00 62.17           N  
ATOM     11  NH2 ARG A  83       9.678  -7.796 -38.131  1.00 61.62           N  
ATOM     12  N   ASN A  84      11.924 -11.249 -31.061  1.00 44.03           N  
ATOM     13  CA  ASN A  84      13.154 -11.964 -30.733  1.00 40.18           C  
ATOM     14  C   ASN A  84      13.841 -12.579 -31.943  1.00 32.91           C  
ATOM     15  O   ASN A  84      13.211 -12.813 -32.976  1.00 27.64           O  
ATOM     16  CB  ASN A  84      12.866 -13.067 -29.712  1.00 43.44           C  
ATOM     17  CG  ASN A  84      12.254 -12.535 -28.434  1.00 50.16           C  
ATOM     18  OD1 ASN A  84      12.911 -11.839 -27.659  1.00 52.51           O  
ATOM     19  ND2 ASN A  84      10.988 -12.862 -28.205  1.00 52.11           N  
ATOM     20  N   PHE A  85      15.139 -12.839 -31.801  1.00 27.58           N  
ATOM     21  CA  PHE A  85      15.878 -13.620 -32.783  1.00 25.96           C  
ATOM     22  C   PHE A  85      15.261 -15.005 -32.894  1.00 25.44           C  
ATOM     23  O   PHE A  85      14.945 -15.628 -31.881  1.00 26.11           O  
ATOM     24  CB  PHE A  85      17.354 -13.750 -32.393  1.00 26.89           C  
ATOM     25  CG  PHE A  85      18.145 -12.486 -32.552  1.00 26.97           C  
ATOM     26  CD1 PHE A  85      18.013 -11.705 -33.686  1.00 27.07           C  
ATOM     27  CD2 PHE A  85      19.032 -12.085 -31.566  1.00 26.55           C  
ATOM     28  CE1 PHE A  85      18.748 -10.542 -33.832  1.00 28.29           C  
ATOM     29  CE2 PHE A  85      19.770 -10.923 -31.708  1.00 26.97           C  
ATOM     30  CZ  PHE A  85      19.626 -10.151 -32.842  1.00 26.61           C  
ATOM     31  N   ASN A  86      15.091 -15.491 -34.117  1.00 23.31           N  
ATOM     32  CA  ASN A  86      14.626 -16.858 -34.301  1.00 26.26           C  
ATOM     33  C   ASN A  86      15.682 -17.863 -33.860  1.00 26.94           C  
ATOM     34  O   ASN A  86      16.872 -17.678 -34.116  1.00 26.36           O  
ATOM     35  CB  ASN A  86      14.239 -17.116 -35.759  1.00 26.02           C  
ATOM     36  CG  ASN A  86      13.693 -18.515 -35.973  1.00 30.40           C  
ATOM     37  OD1 ASN A  86      14.160 -19.252 -36.840  1.00 32.28           O  
ATOM     38  ND2 ASN A  86      12.709 -18.894 -35.166  1.00 30.84           N  
ATOM     39  N   ASN A  87      15.237 -18.918 -33.185  1.00 24.60           N  
ATOM     40  CA  ASN A  87      16.111 -20.017 -32.801  1.00 25.92           C  
ATOM     41  C   ASN A  87      15.722 -21.279 -33.562  1.00 24.75           C  
ATOM     42  O   ASN A  87      14.546 -21.632 -33.628  1.00 28.58           O  
ATOM     43  CB  ASN A  87      16.047 -20.257 -31.288  1.00 33.11           C  
ATOM     44  CG  ASN A  87      16.690 -19.133 -30.485  1.00 40.30           C  
ATOM     45  OD1 ASN A  87      17.910 -18.945 -30.509  1.00 38.03           O  
ATOM     46  ND2 ASN A  87      15.867 -18.382 -29.765  1.00 46.82           N  
ATOM     47  N   LEU A  88      16.710 -21.951 -34.141  1.00 22.77           N  
ATOM     48  CA  LEU A  88      16.459 -23.166 -34.909  1.00 24.60           C  
ATOM     49  C   LEU A  88      16.231 -24.358 -33.983  1.00 26.17           C  
ATOM     50  O   LEU A  88      17.111 -25.199 -33.819  1.00 30.36           O  
ATOM     51  CB  LEU A  88      17.625 -23.448 -35.857  1.00 25.52           C  
ATOM     52  CG  LEU A  88      17.881 -22.410 -36.956  1.00 21.66           C  
ATOM     53  CD1 LEU A  88      19.174 -22.732 -37.704  1.00 19.12           C  
ATOM     54  CD2 LEU A  88      16.691 -22.327 -37.917  1.00 21.85           C  
ATOM     55  N   THR A  89      15.042 -24.433 -33.393  1.00 25.07           N  
ATOM     56  CA  THR A  89      14.766 -25.422 -32.353  1.00 27.74           C  
ATOM     57  C   THR A  89      13.998 -26.648 -32.840  1.00 29.53           C  
ATOM     58  O   THR A  89      13.816 -27.604 -32.089  1.00 32.37           O  
ATOM     59  CB  THR A  89      13.960 -24.798 -31.199  1.00 29.41           C  
ATOM     60  OG1 THR A  89      12.666 -24.408 -31.674  1.00 33.93           O  
ATOM     61  CG2 THR A  89      14.677 -23.586 -30.637  1.00 29.30           C  
ATOM     62  N   LYS A  90      13.542 -26.624 -34.088  1.00 22.56           N  
ATOM     63  CA  LYS A  90      12.718 -27.713 -34.600  1.00 22.96           C  
ATOM     64  C   LYS A  90      13.438 -28.571 -35.636  1.00 26.34           C  
ATOM     65  O   LYS A  90      14.407 -28.135 -36.261  1.00 26.57           O  
ATOM     66  CB  LYS A  90      11.428 -27.154 -35.204  1.00 22.77           C  
ATOM     67  CG  LYS A  90      10.673 -26.216 -34.280  1.00 25.64           C  
ATOM     68  CD  LYS A  90       9.463 -25.610 -34.974  1.00 30.56           C  
ATOM     69  CE  LYS A  90       8.716 -24.671 -34.045  1.00 35.30           C  
ATOM     70  NZ  LYS A  90       7.562 -24.027 -34.728  1.00 39.17           N  
ATOM     71  N   GLY A  91      12.953 -29.796 -35.810  1.00 24.92           N  
ATOM     72  CA  GLY A  91      13.429 -30.661 -36.871  1.00 23.11           C  
ATOM     73  C   GLY A  91      12.521 -30.511 -38.076  1.00 22.81           C  
ATOM     74  O   GLY A  91      11.510 -29.810 -38.011  1.00 25.87           O  
ATOM     75  N   LEU A  92      12.878 -31.157 -39.181  1.00 23.36           N  
ATOM     76  CA  LEU A  92      12.034 -31.134 -40.370  1.00 24.52           C  
ATOM     77  C   LEU A  92      10.776 -31.966 -40.160  1.00 25.73           C  
ATOM     78  O   LEU A  92      10.812 -33.003 -39.496  1.00 24.27           O  
ATOM     79  CB  LEU A  92      12.795 -31.659 -41.591  1.00 23.35           C  
ATOM     80  CG  LEU A  92      14.062 -30.934 -42.052  1.00 26.52           C  
ATOM     81  CD1 LEU A  92      14.559 -31.559 -43.345  1.00 27.40           C  
ATOM     82  CD2 LEU A  92      13.798 -29.454 -42.244  1.00 21.82           C  
ATOM     83  N   CYS A  93       9.663 -31.509 -40.724  1.00 24.45           N  
ATOM     84  CA  CYS A  93       8.464 -32.329 -40.780  1.00 22.45           C  
ATOM     85  C   CYS A  93       8.734 -33.540 -41.665  1.00 25.32           C  
ATOM     86  O   CYS A  93       9.587 -33.489 -42.550  1.00 25.34           O  
ATOM     87  CB  CYS A  93       7.271 -31.532 -41.320  1.00 28.13           C  
ATOM     88  SG  CYS A  93       6.857 -30.040 -40.387  1.00 36.67           S  
ATOM     89  N   THR A  94       8.015 -34.630 -41.425  1.00 25.93           N  
ATOM     90  CA  THR A  94       8.127 -35.797 -42.290  1.00 25.97           C  
ATOM     91  C   THR A  94       7.619 -35.449 -43.680  1.00 25.18           C  
ATOM     92  O   THR A  94       6.521 -34.918 -43.830  1.00 24.33           O  
ATOM     93  CB  THR A  94       7.342 -36.987 -41.729  1.00 25.86           C  
ATOM     94  OG1 THR A  94       7.847 -37.312 -40.429  1.00 27.91           O  
ATOM     95  CG2 THR A  94       7.466 -38.207 -42.644  1.00 23.00           C  
ATOM     96  N   ILE A  95       8.432 -35.732 -44.692  1.00 24.20           N  
ATOM     97  CA  ILE A  95       8.082 -35.398 -46.065  1.00 21.08           C  
ATOM     98  C   ILE A  95       7.547 -36.614 -46.819  1.00 21.80           C  
ATOM     99  O   ILE A  95       8.305 -37.517 -47.178  1.00 22.02           O  
ATOM    100  CB  ILE A  95       9.295 -34.832 -46.826  1.00 20.89           C  
ATOM    101  CG1 ILE A  95       9.888 -33.632 -46.079  1.00 20.37           C  
ATOM    102  CG2 ILE A  95       8.896 -34.443 -48.240  1.00 22.23           C  
ATOM    103  CD1 ILE A  95      11.311 -33.304 -46.491  1.00 19.34           C  
ATOM    104  N   ASN A  96       6.241 -36.634 -47.063  1.00 20.69           N  
ATOM    105  CA  ASN A  96       5.625 -37.756 -47.763  1.00 25.28           C  
ATOM    106  C   ASN A  96       5.181 -37.378 -49.171  1.00 25.16           C  
ATOM    107  O   ASN A  96       4.944 -38.248 -50.011  1.00 26.90           O  
ATOM    108  CB  ASN A  96       4.443 -38.298 -46.960  1.00 24.54           C  
ATOM    109  CG  ASN A  96       4.888 -39.098 -45.752  1.00 25.78           C  
ATOM    110  OD1 ASN A  96       5.925 -39.765 -45.785  1.00 26.27           O  
ATOM    111  ND2 ASN A  96       4.113 -39.030 -44.679  1.00 25.07           N  
ATOM    112  N   SER A  97       5.066 -36.076 -49.412  1.00 22.67           N  
ATOM    113  CA  SER A  97       4.784 -35.543 -50.740  1.00 20.89           C  
ATOM    114  C   SER A  97       4.981 -34.030 -50.728  1.00 23.35           C  
ATOM    115  O   SER A  97       5.372 -33.457 -49.712  1.00 20.42           O  
ATOM    116  CB  SER A  97       3.363 -35.893 -51.194  1.00 22.31           C  
ATOM    117  OG  SER A  97       2.391 -35.326 -50.338  1.00 23.52           O  
ATOM    118  N   TRP A  98       4.711 -33.384 -51.855  1.00 21.76           N  
ATOM    119  CA  TRP A  98       4.851 -31.938 -51.939  1.00 23.00           C  
ATOM    120  C   TRP A  98       3.569 -31.320 -52.470  1.00 24.76           C  
ATOM    121  O   TRP A  98       2.955 -31.854 -53.393  1.00 23.15           O  
ATOM    122  CB  TRP A  98       6.038 -31.560 -52.829  1.00 22.56           C  
ATOM    123  CG  TRP A  98       7.323 -32.195 -52.404  1.00 22.91           C  
ATOM    124  CD1 TRP A  98       7.790 -33.424 -52.772  1.00 20.80           C  
ATOM    125  CD2 TRP A  98       8.307 -31.641 -51.521  1.00 20.33           C  
ATOM    126  NE1 TRP A  98       9.005 -33.667 -52.178  1.00 21.39           N  
ATOM    127  CE2 TRP A  98       9.344 -32.589 -51.403  1.00 20.27           C  
ATOM    128  CE3 TRP A  98       8.410 -30.437 -50.817  1.00 20.83           C  
ATOM    129  CZ2 TRP A  98      10.469 -32.371 -50.612  1.00 20.94           C  
ATOM    130  CZ3 TRP A  98       9.532 -30.220 -50.034  1.00 22.16           C  
ATOM    131  CH2 TRP A  98      10.547 -31.183 -49.938  1.00 19.02           C  
ATOM    132  N   HIS A  99       3.158 -30.205 -51.872  1.00 22.71           N  
ATOM    133  CA  HIS A  99       1.960 -29.500 -52.314  1.00 21.96           C  
ATOM    134  C   HIS A  99       2.344 -28.145 -52.889  1.00 21.26           C  
ATOM    135  O   HIS A  99       3.376 -27.578 -52.527  1.00 17.53           O  
ATOM    136  CB  HIS A  99       0.963 -29.335 -51.159  1.00 21.84           C  
ATOM    137  CG  HIS A  99       1.386 -28.338 -50.125  1.00 23.39           C  
ATOM    138  ND1 HIS A  99       1.287 -26.976 -50.317  1.00 25.49           N  
ATOM    139  CD2 HIS A  99       1.911 -28.504 -48.887  1.00 25.28           C  
ATOM    140  CE1 HIS A  99       1.731 -26.347 -49.244  1.00 25.12           C  
ATOM    141  NE2 HIS A  99       2.115 -27.252 -48.360  1.00 26.91           N  
ATOM    142  N   ILE A 100       1.508 -27.624 -53.780  1.00 20.65           N  
ATOM    143  CA  ILE A 100       1.770 -26.326 -54.386  1.00 21.16           C  
ATOM    144  C   ILE A 100       1.743 -25.239 -53.310  1.00 22.15           C  
ATOM    145  O   ILE A 100       0.877 -25.237 -52.430  1.00 23.60           O  
ATOM    146  CB  ILE A 100       0.752 -26.012 -55.513  1.00 22.97           C  
ATOM    147  CG1 ILE A 100       1.137 -24.727 -56.250  1.00 22.51           C  
ATOM    148  CG2 ILE A 100      -0.677 -25.946 -54.971  1.00 20.64           C  
ATOM    149  CD1 ILE A 100       2.461 -24.816 -56.981  1.00 23.86           C  
ATOM    150  N   TYR A 101       2.719 -24.338 -53.363  1.00 21.33           N  
ATOM    151  CA  TYR A 101       2.833 -23.267 -52.378  1.00 20.61           C  
ATOM    152  C   TYR A 101       2.616 -21.916 -53.047  1.00 25.24           C  
ATOM    153  O   TYR A 101       1.787 -21.111 -52.611  1.00 24.45           O  
ATOM    154  CB  TYR A 101       4.202 -23.320 -51.693  1.00 18.20           C  
ATOM    155  CG  TYR A 101       4.443 -22.221 -50.686  1.00 19.91           C  
ATOM    156  CD1 TYR A 101       3.839 -22.254 -49.436  1.00 23.51           C  
ATOM    157  CD2 TYR A 101       5.276 -21.149 -50.983  1.00 25.23           C  
ATOM    158  CE1 TYR A 101       4.059 -21.254 -48.508  1.00 25.76           C  
ATOM    159  CE2 TYR A 101       5.502 -20.142 -50.061  1.00 24.89           C  
ATOM    160  CZ  TYR A 101       4.889 -20.201 -48.827  1.00 28.16           C  
ATOM    161  OH  TYR A 101       5.111 -19.204 -47.906  1.00 25.61           O  
ATOM    162  N   GLY A 102       3.367 -21.678 -54.117  1.00 22.17           N  
ATOM    163  CA  GLY A 102       3.265 -20.435 -54.856  1.00 24.37           C  
ATOM    164  C   GLY A 102       3.617 -20.584 -56.320  1.00 25.04           C  
ATOM    165  O   GLY A 102       4.345 -21.499 -56.709  1.00 23.13           O  
ATOM    166  N   LYS A 103       3.081 -19.676 -57.129  1.00 21.02           N  
ATOM    167  CA  LYS A 103       3.332 -19.637 -58.564  1.00 21.81           C  
ATOM    168  C   LYS A 103       2.908 -18.269 -59.071  1.00 23.93           C  
ATOM    169  O   LYS A 103       1.782 -17.846 -58.819  1.00 23.91           O  
ATOM    170  CB  LYS A 103       2.565 -20.743 -59.292  1.00 22.80           C  
ATOM    171  CG  LYS A 103       2.941 -20.894 -60.756  1.00 25.23           C  
ATOM    172  CD  LYS A 103       2.055 -21.899 -61.458  1.00 24.33           C  
ATOM    173  CE  LYS A 103       2.695 -22.387 -62.749  1.00 23.53           C  
ATOM    174  NZ  LYS A 103       2.989 -21.259 -63.670  1.00 22.40           N  
ATOM    175  N   ASP A 104       3.790 -17.567 -59.777  1.00 22.83           N  
ATOM    176  CA  ASP A 104       3.474 -16.188 -60.139  1.00 26.52           C  
ATOM    177  C   ASP A 104       3.072 -15.981 -61.599  1.00 24.23           C  
ATOM    178  O   ASP A 104       2.553 -14.918 -61.939  1.00 22.31           O  
ATOM    179  CB  ASP A 104       4.646 -15.259 -59.782  1.00 26.79           C  
ATOM    180  CG  ASP A 104       5.931 -15.595 -60.521  1.00 28.41           C  
ATOM    181  OD1 ASP A 104       5.946 -16.538 -61.339  1.00 26.64           O  
ATOM    182  OD2 ASP A 104       6.940 -14.895 -60.277  1.00 30.49           O  
ATOM    183  N   ASN A 105       3.289 -16.989 -62.446  1.00 21.53           N  
ATOM    184  CA  ASN A 105       2.929 -16.902 -63.865  1.00 21.21           C  
ATOM    185  C   ASN A 105       3.424 -15.610 -64.513  1.00 24.37           C  
ATOM    186  O   ASN A 105       2.705 -14.974 -65.283  1.00 21.67           O  
ATOM    187  CB  ASN A 105       1.410 -17.015 -64.037  1.00 24.08           C  
ATOM    188  CG  ASN A 105       0.857 -18.328 -63.510  1.00 25.38           C  
ATOM    189  OD1 ASN A 105       1.120 -19.393 -64.068  1.00 26.32           O  
ATOM    190  ND2 ASN A 105       0.089 -18.258 -62.430  1.00 23.28           N  
ATOM    191  N   ALA A 106       4.656 -15.230 -64.194  1.00 23.62           N  
ATOM    192  CA  ALA A 106       5.165 -13.906 -64.533  1.00 22.99           C  
ATOM    193  C   ALA A 106       5.277 -13.658 -66.037  1.00 24.25           C  
ATOM    194  O   ALA A 106       4.966 -12.565 -66.513  1.00 22.57           O  
ATOM    195  CB  ALA A 106       6.515 -13.690 -63.870  1.00 21.89           C  
ATOM    196  N   VAL A 107       5.725 -14.662 -66.782  1.00 22.22           N  
ATOM    197  CA  VAL A 107       5.938 -14.486 -68.212  1.00 21.36           C  
ATOM    198  C   VAL A 107       4.597 -14.403 -68.944  1.00 22.46           C  
ATOM    199  O   VAL A 107       4.434 -13.597 -69.864  1.00 23.70           O  
ATOM    200  CB  VAL A 107       6.795 -15.625 -68.803  1.00 24.75           C  
ATOM    201  CG1 VAL A 107       7.087 -15.360 -70.270  1.00 24.37           C  
ATOM    202  CG2 VAL A 107       8.095 -15.776 -68.016  1.00 26.55           C  
ATOM    203  N   ARG A 108       3.643 -15.233 -68.525  1.00 21.31           N  
ATOM    204  CA  ARG A 108       2.277 -15.178 -69.044  1.00 21.56           C  
ATOM    205  C   ARG A 108       1.701 -13.782 -68.882  1.00 24.00           C  
ATOM    206  O   ARG A 108       1.253 -13.162 -69.844  1.00 25.96           O  
ATOM    207  CB  ARG A 108       1.370 -16.184 -68.324  1.00 19.51           C  
ATOM    208  CG  ARG A 108       1.455 -17.612 -68.823  1.00 22.96           C  
ATOM    209  CD  ARG A 108       0.599 -18.534 -67.965  1.00 24.17           C  
ATOM    210  NE  ARG A 108      -0.821 -18.191 -68.005  1.00 22.66           N  
ATOM    211  CZ  ARG A 108      -1.678 -18.626 -68.924  1.00 26.01           C  
ATOM    212  NH1 ARG A 108      -1.263 -19.430 -69.896  1.00 24.62           N  
ATOM    213  NH2 ARG A 108      -2.955 -18.258 -68.871  1.00 23.33           N  
ATOM    214  N   ILE A 109       1.717 -13.298 -67.646  1.00 20.35           N  
ATOM    215  CA  ILE A 109       1.150 -11.998 -67.313  1.00 21.42           C  
ATOM    216  C   ILE A 109       1.969 -10.876 -67.951  1.00 22.70           C  
ATOM    217  O   ILE A 109       1.420  -9.880 -68.425  1.00 26.06           O  
ATOM    218  CB  ILE A 109       1.077 -11.815 -65.780  1.00 20.65           C  
ATOM    219  CG1 ILE A 109       0.034 -12.767 -65.191  1.00 21.41           C  
ATOM    220  CG2 ILE A 109       0.748 -10.373 -65.410  1.00 21.43           C  
ATOM    221  CD1 ILE A 109       0.176 -12.994 -63.702  1.00 21.52           C  
ATOM    222  N   GLY A 110       3.282 -11.068 -67.995  1.00 21.97           N  
ATOM    223  CA  GLY A 110       4.188 -10.071 -68.533  1.00 21.43           C  
ATOM    224  C   GLY A 110       4.057  -9.835 -70.024  1.00 23.70           C  
ATOM    225  O   GLY A 110       4.592  -8.856 -70.547  1.00 26.13           O  
ATOM    226  N   GLU A 111       3.353 -10.731 -70.710  1.00 21.71           N  
ATOM    227  CA  GLU A 111       3.098 -10.573 -72.141  1.00 23.70           C  
ATOM    228  C   GLU A 111       2.337  -9.276 -72.416  1.00 23.81           C  
ATOM    229  O   GLU A 111       2.499  -8.657 -73.471  1.00 25.76           O  
ATOM    230  CB  GLU A 111       2.322 -11.781 -72.680  1.00 25.12           C  
ATOM    231  CG  GLU A 111       2.150 -11.819 -74.196  1.00 25.73           C  
ATOM    232  CD  GLU A 111       0.991 -10.968 -74.684  1.00 28.53           C  
ATOM    233  OE1 GLU A 111      -0.001 -10.827 -73.936  1.00 28.30           O  
ATOM    234  OE2 GLU A 111       1.077 -10.429 -75.809  1.00 29.13           O  
ATOM    235  N   SER A 112       1.509  -8.865 -71.461  1.00 23.63           N  
ATOM    236  CA  SER A 112       0.755  -7.624 -71.591  1.00 30.85           C  
ATOM    237  C   SER A 112       0.536  -6.968 -70.232  1.00 35.33           C  
ATOM    238  O   SER A 112      -0.596  -6.683 -69.840  1.00 42.93           O  
ATOM    239  CB  SER A 112      -0.587  -7.880 -72.265  1.00 39.62           C  
ATOM    240  OG  SER A 112      -1.474  -8.490 -71.349  1.00 48.79           O  
ATOM    241  N   SER A 113       1.631  -6.755 -69.514  1.00 25.72           N  
ATOM    242  CA  SER A 113       1.625  -6.017 -68.255  1.00 23.17           C  
ATOM    243  C   SER A 113       3.050  -5.583 -67.988  1.00 23.20           C  
ATOM    244  O   SER A 113       3.979  -6.118 -68.591  1.00 25.71           O  
ATOM    245  CB  SER A 113       1.090  -6.868 -67.103  1.00 23.15           C  
ATOM    246  OG  SER A 113      -0.313  -7.035 -67.208  1.00 30.77           O  
ATOM    247  N   ASP A 114       3.238  -4.628 -67.087  1.00 22.76           N  
ATOM    248  CA  ASP A 114       4.578  -4.107 -66.845  1.00 19.20           C  
ATOM    249  C   ASP A 114       5.327  -4.973 -65.839  1.00 23.21           C  
ATOM    250  O   ASP A 114       5.521  -4.593 -64.686  1.00 22.80           O  
ATOM    251  CB  ASP A 114       4.505  -2.654 -66.380  1.00 20.60           C  
ATOM    252  CG  ASP A 114       3.940  -1.735 -67.453  1.00 26.80           C  
ATOM    253  OD1 ASP A 114       4.208  -1.992 -68.646  1.00 27.91           O  
ATOM    254  OD2 ASP A 114       3.229  -0.766 -67.109  1.00 29.96           O  
ATOM    255  N   VAL A 115       5.738  -6.148 -66.300  1.00 23.39           N  
ATOM    256  CA  VAL A 115       6.437  -7.121 -65.473  1.00 20.20           C  
ATOM    257  C   VAL A 115       7.932  -7.058 -65.742  1.00 19.78           C  
ATOM    258  O   VAL A 115       8.365  -7.129 -66.889  1.00 21.37           O  
ATOM    259  CB  VAL A 115       5.925  -8.550 -65.739  1.00 22.88           C  
ATOM    260  CG1 VAL A 115       6.842  -9.587 -65.096  1.00 25.87           C  
ATOM    261  CG2 VAL A 115       4.500  -8.702 -65.239  1.00 22.63           C  
ATOM    262  N   LEU A 116       8.713  -6.913 -64.678  1.00 17.95           N  
ATOM    263  CA  LEU A 116      10.161  -6.803 -64.789  1.00 20.07           C  
ATOM    264  C   LEU A 116      10.818  -8.094 -65.266  1.00 22.17           C  
ATOM    265  O   LEU A 116      10.435  -9.193 -64.855  1.00 22.54           O  
ATOM    266  CB  LEU A 116      10.758  -6.395 -63.441  1.00 18.03           C  
ATOM    267  CG  LEU A 116      10.434  -4.980 -62.957  1.00 20.90           C  
ATOM    268  CD1 LEU A 116      10.736  -4.847 -61.464  1.00 20.94           C  
ATOM    269  CD2 LEU A 116      11.215  -3.958 -63.761  1.00 22.22           C  
ATOM    270  N   VAL A 117      11.817  -7.954 -66.131  1.00 21.41           N  
ATOM    271  CA  VAL A 117      12.655  -9.080 -66.511  1.00 22.55           C  
ATOM    272  C   VAL A 117      13.509  -9.474 -65.319  1.00 22.97           C  
ATOM    273  O   VAL A 117      14.153  -8.623 -64.704  1.00 22.69           O  
ATOM    274  CB  VAL A 117      13.566  -8.747 -67.706  1.00 21.65           C  
ATOM    275  CG1 VAL A 117      14.532  -9.883 -67.964  1.00 18.59           C  
ATOM    276  CG2 VAL A 117      12.733  -8.464 -68.943  1.00 21.91           C  
ATOM    277  N   THR A 118      13.504 -10.758 -64.979  1.00 20.77           N  
ATOM    278  CA  THR A 118      14.297 -11.239 -63.857  1.00 23.00           C  
ATOM    279  C   THR A 118      15.044 -12.514 -64.201  1.00 22.40           C  
ATOM    280  O   THR A 118      14.875 -13.077 -65.280  1.00 22.30           O  
ATOM    281  CB  THR A 118      13.426 -11.530 -62.612  1.00 24.41           C  
ATOM    282  OG1 THR A 118      12.514 -12.598 -62.903  1.00 24.78           O  
ATOM    283  CG2 THR A 118      12.641 -10.300 -62.191  1.00 23.68           C  
ATOM    284  N   ARG A 119      15.883 -12.940 -63.264  1.00 20.09           N  
ATOM    285  CA  ARG A 119      16.403 -14.296 -63.205  1.00 19.24           C  
ATOM    286  C   ARG A 119      16.940 -14.513 -61.797  1.00 20.59           C  
ATOM    287  O   ARG A 119      16.940 -13.585 -60.985  1.00 20.44           O  
ATOM    288  CB  ARG A 119      17.488 -14.551 -64.253  1.00 19.54           C  
ATOM    289  CG  ARG A 119      16.987 -15.336 -65.462  1.00 20.14           C  
ATOM    290  CD  ARG A 119      18.018 -16.347 -65.946  1.00 22.30           C  
ATOM    291  NE  ARG A 119      18.247 -17.406 -64.962  1.00 24.98           N  
ATOM    292  CZ  ARG A 119      19.389 -18.073 -64.829  1.00 25.78           C  
ATOM    293  NH1 ARG A 119      20.414 -17.794 -65.621  1.00 22.94           N  
ATOM    294  NH2 ARG A 119      19.502 -19.018 -63.905  1.00 23.80           N  
ATOM    295  N   GLU A 120      17.392 -15.732 -61.518  1.00 19.19           N  
ATOM    296  CA  GLU A 120      17.896 -16.099 -60.195  1.00 21.89           C  
ATOM    297  C   GLU A 120      16.905 -15.756 -59.082  1.00 19.67           C  
ATOM    298  O   GLU A 120      17.237 -15.016 -58.158  1.00 20.69           O  
ATOM    299  CB  GLU A 120      19.240 -15.409 -59.922  1.00 20.97           C  
ATOM    300  CG  GLU A 120      20.369 -15.832 -60.855  1.00 24.68           C  
ATOM    301  CD  GLU A 120      20.382 -15.044 -62.153  1.00 27.43           C  
ATOM    302  OE1 GLU A 120      19.929 -13.879 -62.150  1.00 27.96           O  
ATOM    303  OE2 GLU A 120      20.842 -15.591 -63.178  1.00 27.91           O  
ATOM    304  N   PRO A 121      15.683 -16.300 -59.158  1.00 20.89           N  
ATOM    305  CA  PRO A 121      14.694 -15.963 -58.138  1.00 18.98           C  
ATOM    306  C   PRO A 121      14.876 -16.794 -56.878  1.00 20.00           C  
ATOM    307  O   PRO A 121      15.613 -17.775 -56.899  1.00 19.90           O  
ATOM    308  CB  PRO A 121      13.373 -16.306 -58.823  1.00 21.07           C  
ATOM    309  CG  PRO A 121      13.720 -17.508 -59.636  1.00 23.24           C  
ATOM    310  CD  PRO A 121      15.159 -17.304 -60.100  1.00 22.23           C  
ATOM    311  N   TYR A 122      14.220 -16.394 -55.795  1.00 17.80           N  
ATOM    312  CA  TYR A 122      14.058 -17.276 -54.646  1.00 19.70           C  
ATOM    313  C   TYR A 122      12.903 -16.831 -53.766  1.00 20.74           C  
ATOM    314  O   TYR A 122      12.162 -15.914 -54.112  1.00 22.04           O  
ATOM    315  CB  TYR A 122      15.349 -17.382 -53.818  1.00 22.50           C  
ATOM    316  CG  TYR A 122      16.036 -16.098 -53.387  1.00 21.33           C  
ATOM    317  CD1 TYR A 122      16.802 -15.362 -54.281  1.00 21.23           C  
ATOM    318  CD2 TYR A 122      15.967 -15.659 -52.069  1.00 21.45           C  
ATOM    319  CE1 TYR A 122      17.457 -14.207 -53.885  1.00 20.84           C  
ATOM    320  CE2 TYR A 122      16.621 -14.504 -51.662  1.00 20.45           C  
ATOM    321  CZ  TYR A 122      17.366 -13.784 -52.576  1.00 22.21           C  
ATOM    322  OH  TYR A 122      18.031 -12.639 -52.191  1.00 23.30           O  
ATOM    323  N   VAL A 123      12.736 -17.509 -52.637  1.00 20.49           N  
ATOM    324  CA  VAL A 123      11.658 -17.196 -51.712  1.00 19.24           C  
ATOM    325  C   VAL A 123      12.240 -17.061 -50.309  1.00 20.46           C  
ATOM    326  O   VAL A 123      13.147 -17.803 -49.935  1.00 21.31           O  
ATOM    327  CB  VAL A 123      10.550 -18.284 -51.716  1.00 24.43           C  
ATOM    328  CG1 VAL A 123       9.318 -17.808 -50.948  1.00 22.69           C  
ATOM    329  CG2 VAL A 123      10.174 -18.674 -53.137  1.00 23.76           C  
ATOM    330  N   SER A 124      11.729 -16.110 -49.537  1.00 20.28           N  
ATOM    331  CA  SER A 124      12.204 -15.907 -48.175  1.00 21.80           C  
ATOM    332  C   SER A 124      11.091 -15.346 -47.307  1.00 23.70           C  
ATOM    333  O   SER A 124      10.317 -14.499 -47.752  1.00 22.27           O  
ATOM    334  CB  SER A 124      13.413 -14.972 -48.158  1.00 22.29           C  
ATOM    335  OG  SER A 124      13.978 -14.915 -46.861  1.00 21.88           O  
ATOM    336  N   CYS A 125      11.017 -15.815 -46.067  1.00 23.07           N  
ATOM    337  CA  CYS A 125       9.934 -15.416 -45.179  1.00 24.73           C  
ATOM    338  C   CYS A 125      10.354 -14.415 -44.116  1.00 25.09           C  
ATOM    339  O   CYS A 125      11.444 -14.507 -43.549  1.00 24.66           O  
ATOM    340  CB  CYS A 125       9.324 -16.645 -44.499  1.00 22.55           C  
ATOM    341  SG  CYS A 125       8.476 -17.761 -45.627  1.00 29.03           S  
ATOM    342  N   ASP A 126       9.471 -13.454 -43.871  1.00 20.86           N  
ATOM    343  CA  ASP A 126       9.533 -12.605 -42.693  1.00 22.09           C  
ATOM    344  C   ASP A 126       8.661 -13.263 -41.629  1.00 23.93           C  
ATOM    345  O   ASP A 126       7.949 -14.217 -41.931  1.00 24.00           O  
ATOM    346  CB  ASP A 126       9.051 -11.186 -43.015  1.00 25.47           C  
ATOM    347  CG  ASP A 126      10.032 -10.416 -43.880  1.00 28.44           C  
ATOM    348  OD1 ASP A 126      11.007 -11.025 -44.375  1.00 26.70           O  
ATOM    349  OD2 ASP A 126       9.828  -9.197 -44.062  1.00 28.03           O  
ATOM    350  N   PRO A 127       8.715 -12.776 -40.378  1.00 23.27           N  
ATOM    351  CA  PRO A 127       7.835 -13.365 -39.362  1.00 22.97           C  
ATOM    352  C   PRO A 127       6.344 -13.201 -39.670  1.00 23.99           C  
ATOM    353  O   PRO A 127       5.530 -13.941 -39.117  1.00 28.16           O  
ATOM    354  CB  PRO A 127       8.212 -12.599 -38.090  1.00 24.47           C  
ATOM    355  CG  PRO A 127       9.627 -12.204 -38.307  1.00 25.19           C  
ATOM    356  CD  PRO A 127       9.746 -11.913 -39.777  1.00 23.81           C  
ATOM    357  N   ASP A 128       5.993 -12.258 -40.540  1.00 22.94           N  
ATOM    358  CA  ASP A 128       4.587 -11.950 -40.792  1.00 29.35           C  
ATOM    359  C   ASP A 128       4.206 -12.026 -42.269  1.00 28.82           C  
ATOM    360  O   ASP A 128       3.073 -11.721 -42.635  1.00 31.59           O  
ATOM    361  CB  ASP A 128       4.252 -10.560 -40.247  1.00 34.77           C  
ATOM    362  CG  ASP A 128       5.100  -9.464 -40.875  1.00 42.62           C  
ATOM    363  OD1 ASP A 128       6.080  -9.788 -41.582  1.00 41.97           O  
ATOM    364  OD2 ASP A 128       4.789  -8.273 -40.656  1.00 46.75           O  
ATOM    365  N   GLU A 129       5.147 -12.439 -43.112  1.00 27.71           N  
ATOM    366  CA  GLU A 129       4.917 -12.468 -44.555  1.00 26.28           C  
ATOM    367  C   GLU A 129       5.995 -13.277 -45.271  1.00 28.24           C  
ATOM    368  O   GLU A 129       7.155 -13.277 -44.861  1.00 29.21           O  
ATOM    369  CB  GLU A 129       4.877 -11.040 -45.113  1.00 29.36           C  
ATOM    370  CG  GLU A 129       4.592 -10.943 -46.603  1.00 33.86           C  
ATOM    371  CD  GLU A 129       4.775  -9.531 -47.140  1.00 36.81           C  
ATOM    372  OE1 GLU A 129       5.223  -8.653 -46.369  1.00 34.49           O  
ATOM    373  OE2 GLU A 129       4.468  -9.298 -48.331  1.00 35.61           O  
ATOM    374  N   CYS A 130       5.605 -13.974 -46.334  1.00 23.79           N  
ATOM    375  CA  CYS A 130       6.566 -14.629 -47.218  1.00 25.85           C  
ATOM    376  C   CYS A 130       6.538 -13.958 -48.587  1.00 24.78           C  
ATOM    377  O   CYS A 130       5.469 -13.637 -49.102  1.00 24.03           O  
ATOM    378  CB  CYS A 130       6.270 -16.126 -47.342  1.00 28.02           C  
ATOM    379  SG  CYS A 130       6.573 -17.072 -45.829  1.00 49.38           S  
ATOM    380  N   ARG A 131       7.713 -13.738 -49.169  1.00 21.11           N  
ATOM    381  CA  ARG A 131       7.808 -12.995 -50.420  1.00 21.14           C  
ATOM    382  C   ARG A 131       8.703 -13.673 -51.454  1.00 22.59           C  
ATOM    383  O   ARG A 131       9.617 -14.426 -51.108  1.00 20.90           O  
ATOM    384  CB  ARG A 131       8.322 -11.577 -50.147  1.00 21.77           C  
ATOM    385  CG  ARG A 131       7.338 -10.699 -49.387  1.00 24.06           C  
ATOM    386  CD  ARG A 131       8.011  -9.450 -48.847  1.00 25.13           C  
ATOM    387  NE  ARG A 131       8.373  -8.503 -49.899  1.00 24.78           N  
ATOM    388  CZ  ARG A 131       7.544  -7.599 -50.416  1.00 26.73           C  
ATOM    389  NH1 ARG A 131       6.291  -7.513 -49.983  1.00 27.84           N  
ATOM    390  NH2 ARG A 131       7.971  -6.773 -51.367  1.00 25.80           N  
ATOM    391  N   PHE A 132       8.418 -13.404 -52.725  1.00 21.05           N  
ATOM    392  CA  PHE A 132       9.291 -13.808 -53.817  1.00 19.71           C  
ATOM    393  C   PHE A 132      10.451 -12.830 -53.923  1.00 20.69           C  
ATOM    394  O   PHE A 132      10.293 -11.645 -53.646  1.00 20.75           O  
ATOM    395  CB  PHE A 132       8.528 -13.860 -55.143  1.00 18.76           C  
ATOM    396  CG  PHE A 132       7.686 -15.089 -55.319  1.00 23.77           C  
ATOM    397  CD1 PHE A 132       7.725 -16.116 -54.392  1.00 24.65           C  
ATOM    398  CD2 PHE A 132       6.854 -15.216 -56.419  1.00 26.80           C  
ATOM    399  CE1 PHE A 132       6.952 -17.250 -54.565  1.00 26.93           C  
ATOM    400  CE2 PHE A 132       6.078 -16.345 -56.594  1.00 23.77           C  
ATOM    401  CZ  PHE A 132       6.127 -17.363 -55.665  1.00 24.06           C  
ATOM    402  N   TYR A 133      11.612 -13.332 -54.324  1.00 19.52           N  
ATOM    403  CA  TYR A 133      12.789 -12.498 -54.531  1.00 20.23           C  
ATOM    404  C   TYR A 133      13.395 -12.839 -55.881  1.00 21.53           C  
ATOM    405  O   TYR A 133      13.220 -13.954 -56.360  1.00 22.44           O  
ATOM    406  CB  TYR A 133      13.824 -12.714 -53.423  1.00 22.10           C  
ATOM    407  CG  TYR A 133      13.431 -12.165 -52.072  1.00 23.54           C  
ATOM    408  CD1 TYR A 133      12.449 -12.782 -51.307  1.00 19.00           C  
ATOM    409  CD2 TYR A 133      14.054 -11.038 -51.553  1.00 24.82           C  
ATOM    410  CE1 TYR A 133      12.091 -12.283 -50.064  1.00 20.31           C  
ATOM    411  CE2 TYR A 133      13.706 -10.532 -50.311  1.00 23.46           C  
ATOM    412  CZ  TYR A 133      12.720 -11.159 -49.572  1.00 23.65           C  
ATOM    413  OH  TYR A 133      12.368 -10.658 -48.338  1.00 22.27           O  
ATOM    414  N   ALA A 134      14.100 -11.885 -56.484  1.00 18.89           N  
ATOM    415  CA  ALA A 134      14.820 -12.126 -57.732  1.00 20.09           C  
ATOM    416  C   ALA A 134      15.747 -10.971 -58.077  1.00 21.55           C  
ATOM    417  O   ALA A 134      15.679  -9.898 -57.472  1.00 19.72           O  
ATOM    418  CB  ALA A 134      13.843 -12.365 -58.879  1.00 17.63           C  
ATOM    419  N   LEU A 135      16.612 -11.203 -59.059  1.00 19.86           N  
ATOM    420  CA  LEU A 135      17.450 -10.150 -59.615  1.00 21.87           C  
ATOM    421  C   LEU A 135      16.806  -9.566 -60.866  1.00 21.23           C  
ATOM    422  O   LEU A 135      16.733 -10.225 -61.904  1.00 22.53           O  
ATOM    423  CB  LEU A 135      18.846 -10.684 -59.941  1.00 19.76           C  
ATOM    424  CG  LEU A 135      19.693 -11.119 -58.744  1.00 22.43           C  
ATOM    425  CD1 LEU A 135      20.983 -11.783 -59.224  1.00 20.35           C  
ATOM    426  CD2 LEU A 135      19.995  -9.932 -57.857  1.00 20.54           C  
ATOM    427  N   SER A 136      16.328  -8.331 -60.753  1.00 21.37           N  
ATOM    428  CA  SER A 136      15.747  -7.626 -61.884  1.00 19.60           C  
ATOM    429  C   SER A 136      16.829  -7.317 -62.909  1.00 21.23           C  
ATOM    430  O   SER A 136      18.016  -7.338 -62.589  1.00 22.44           O  
ATOM    431  CB  SER A 136      15.065  -6.333 -61.422  1.00 23.15           C  
ATOM    432  OG  SER A 136      14.653  -5.547 -62.527  1.00 25.66           O  
ATOM    433  N   GLN A 137      16.419  -7.037 -64.142  1.00 20.09           N  
ATOM    434  CA  GLN A 137      17.349  -6.621 -65.183  1.00 20.38           C  
ATOM    435  C   GLN A 137      17.123  -5.153 -65.535  1.00 21.40           C  
ATOM    436  O   GLN A 137      17.707  -4.634 -66.485  1.00 24.92           O  
ATOM    437  CB  GLN A 137      17.205  -7.502 -66.427  1.00 19.29           C  
ATOM    438  CG  GLN A 137      17.696  -8.938 -66.245  1.00 20.85           C  
ATOM    439  CD  GLN A 137      19.189  -9.097 -66.477  1.00 23.21           C  
ATOM    440  OE1 GLN A 137      19.941  -8.123 -66.478  1.00 21.95           O  
ATOM    441  NE2 GLN A 137      19.625 -10.336 -66.679  1.00 21.91           N  
ATOM    442  N   GLY A 138      16.272  -4.488 -64.761  1.00 19.52           N  
ATOM    443  CA  GLY A 138      16.029  -3.069 -64.942  1.00 18.35           C  
ATOM    444  C   GLY A 138      15.298  -2.749 -66.231  1.00 21.67           C  
ATOM    445  O   GLY A 138      15.615  -1.772 -66.910  1.00 21.00           O  
ATOM    446  N   THR A 139      14.317  -3.582 -66.561  1.00 23.14           N  
ATOM    447  CA  THR A 139      13.518  -3.429 -67.770  1.00 23.02           C  
ATOM    448  C   THR A 139      12.329  -4.371 -67.677  1.00 23.18           C  
ATOM    449  O   THR A 139      12.379  -5.359 -66.944  1.00 22.77           O  
ATOM    450  CB  THR A 139      14.331  -3.738 -69.049  1.00 23.78           C  
ATOM    451  OG1 THR A 139      13.495  -3.590 -70.204  1.00 25.75           O  
ATOM    452  CG2 THR A 139      14.886  -5.162 -69.008  1.00 24.73           C  
ATOM    453  N   THR A 140      11.258  -4.068 -68.403  1.00 23.60           N  
ATOM    454  CA  THR A 140      10.130  -4.988 -68.474  1.00 24.33           C  
ATOM    455  C   THR A 140      10.338  -5.941 -69.645  1.00 25.57           C  
ATOM    456  O   THR A 140      11.208  -5.710 -70.485  1.00 24.91           O  
ATOM    457  CB  THR A 140       8.787  -4.251 -68.625  1.00 25.99           C  
ATOM    458  OG1 THR A 140       8.736  -3.592 -69.896  1.00 25.80           O  
ATOM    459  CG2 THR A 140       8.622  -3.225 -67.522  1.00 24.96           C  
ATOM    460  N   ILE A 141       9.556  -7.017 -69.694  1.00 21.71           N  
ATOM    461  CA  ILE A 141       9.711  -8.011 -70.751  1.00 24.17           C  
ATOM    462  C   ILE A 141       9.369  -7.425 -72.113  1.00 21.70           C  
ATOM    463  O   ILE A 141      10.091  -7.631 -73.086  1.00 23.59           O  
ATOM    464  CB  ILE A 141       8.829  -9.253 -70.518  1.00 27.63           C  
ATOM    465  CG1 ILE A 141       9.058  -9.826 -69.122  1.00 33.77           C  
ATOM    466  CG2 ILE A 141       9.124 -10.310 -71.573  1.00 27.99           C  
ATOM    467  CD1 ILE A 141       8.159 -10.999 -68.799  1.00 34.94           C  
ATOM    468  N   ARG A 142       8.269  -6.683 -72.174  1.00 24.25           N  
ATOM    469  CA  ARG A 142       7.833  -6.070 -73.425  1.00 24.46           C  
ATOM    470  C   ARG A 142       8.676  -4.851 -73.786  1.00 26.24           C  
ATOM    471  O   ARG A 142       8.640  -4.379 -74.920  1.00 24.55           O  
ATOM    472  CB  ARG A 142       6.354  -5.687 -73.340  1.00 27.21           C  
ATOM    473  CG  ARG A 142       5.405  -6.850 -73.588  1.00 26.78           C  
ATOM    474  CD  ARG A 142       5.668  -7.480 -74.947  1.00 29.46           C  
ATOM    475  NE  ARG A 142       4.549  -8.307 -75.393  1.00 30.53           N  
ATOM    476  CZ  ARG A 142       4.497  -8.917 -76.572  1.00 31.75           C  
ATOM    477  NH1 ARG A 142       5.509  -8.800 -77.422  1.00 30.12           N  
ATOM    478  NH2 ARG A 142       3.437  -9.647 -76.899  1.00 30.43           N  
ATOM    479  N   GLY A 143       9.436  -4.347 -72.820  1.00 24.33           N  
ATOM    480  CA  GLY A 143      10.318  -3.221 -73.068  1.00 22.97           C  
ATOM    481  C   GLY A 143      11.434  -3.597 -74.022  1.00 24.93           C  
ATOM    482  O   GLY A 143      11.891  -4.739 -74.031  1.00 24.22           O  
ATOM    483  N   LYS A 144      11.871  -2.639 -74.831  1.00 24.23           N  
ATOM    484  CA  LYS A 144      12.925  -2.894 -75.805  1.00 23.52           C  
ATOM    485  C   LYS A 144      14.274  -3.168 -75.145  1.00 23.46           C  
ATOM    486  O   LYS A 144      15.155  -3.774 -75.755  1.00 24.60           O  
ATOM    487  CB  LYS A 144      13.047  -1.720 -76.778  1.00 24.73           C  
ATOM    488  CG  LYS A 144      11.822  -1.537 -77.670  1.00 25.99           C  
ATOM    489  CD  LYS A 144      12.108  -0.559 -78.804  1.00 29.85           C  
ATOM    490  CE  LYS A 144      10.823  -0.025 -79.420  1.00 31.88           C  
ATOM    491  NZ  LYS A 144      11.079   1.122 -80.343  1.00 34.04           N  
ATOM    492  N   HIS A 145      14.435  -2.723 -73.901  1.00 22.06           N  
ATOM    493  CA  HIS A 145      15.670  -2.974 -73.160  1.00 22.60           C  
ATOM    494  C   HIS A 145      15.756  -4.413 -72.659  1.00 24.28           C  
ATOM    495  O   HIS A 145      16.729  -4.785 -72.004  1.00 26.28           O  
ATOM    496  CB  HIS A 145      15.809  -2.009 -71.978  1.00 21.16           C  
ATOM    497  CG  HIS A 145      16.050  -0.588 -72.382  1.00 22.38           C  
ATOM    498  ND1 HIS A 145      15.055   0.365 -72.396  1.00 23.39           N  
ATOM    499  CD2 HIS A 145      17.176   0.040 -72.801  1.00 23.49           C  
ATOM    500  CE1 HIS A 145      15.555   1.519 -72.800  1.00 21.98           C  
ATOM    501  NE2 HIS A 145      16.842   1.349 -73.050  1.00 22.46           N  
ATOM    502  N   SER A 146      14.742  -5.219 -72.965  1.00 22.76           N  
ATOM    503  CA  SER A 146      14.782  -6.638 -72.628  1.00 23.53           C  
ATOM    504  C   SER A 146      15.764  -7.358 -73.546  1.00 21.58           C  
ATOM    505  O   SER A 146      16.237  -8.455 -73.240  1.00 22.11           O  
ATOM    506  CB  SER A 146      13.391  -7.268 -72.736  1.00 24.95           C  
ATOM    507  OG  SER A 146      12.961  -7.335 -74.083  1.00 25.74           O  
ATOM    508  N   ASN A 147      16.058  -6.728 -74.678  1.00 22.60           N  
ATOM    509  CA  ASN A 147      17.005  -7.262 -75.647  1.00 25.70           C  
ATOM    510  C   ASN A 147      18.402  -7.369 -75.043  1.00 26.21           C  
ATOM    511  O   ASN A 147      19.008  -6.364 -74.680  1.00 25.84           O  
ATOM    512  CB  ASN A 147      17.027  -6.375 -76.898  1.00 28.87           C  
ATOM    513  CG  ASN A 147      17.768  -7.009 -78.067  1.00 35.20           C  
ATOM    514  OD1 ASN A 147      18.554  -7.942 -77.895  1.00 31.18           O  
ATOM    515  ND2 ASN A 147      17.519  -6.493 -79.270  1.00 46.60           N  
ATOM    516  N   GLY A 148      18.903  -8.595 -74.928  1.00 25.62           N  
ATOM    517  CA  GLY A 148      20.245  -8.826 -74.424  1.00 26.67           C  
ATOM    518  C   GLY A 148      20.315  -9.262 -72.971  1.00 29.79           C  
ATOM    519  O   GLY A 148      21.403  -9.367 -72.403  1.00 29.68           O  
ATOM    520  N   THR A 149      19.161  -9.538 -72.370  1.00 24.98           N  
ATOM    521  CA  THR A 149      19.104  -9.852 -70.942  1.00 23.89           C  
ATOM    522  C   THR A 149      19.533 -11.280 -70.598  1.00 26.94           C  
ATOM    523  O   THR A 149      19.342 -11.729 -69.469  1.00 26.74           O  
ATOM    524  CB  THR A 149      17.687  -9.621 -70.372  1.00 22.22           C  
ATOM    525  OG1 THR A 149      16.709 -10.169 -71.265  1.00 23.87           O  
ATOM    526  CG2 THR A 149      17.421  -8.129 -70.196  1.00 21.70           C  
ATOM    527  N   ILE A 150      20.119 -11.994 -71.556  1.00 29.17           N  
ATOM    528  CA  ILE A 150      20.727 -13.285 -71.247  1.00 27.01           C  
ATOM    529  C   ILE A 150      21.958 -13.063 -70.369  1.00 30.17           C  
ATOM    530  O   ILE A 150      22.368 -13.943 -69.608  1.00 31.67           O  
ATOM    531  CB  ILE A 150      21.125 -14.063 -72.521  1.00 27.81           C  
ATOM    532  CG1 ILE A 150      21.528 -15.502 -72.169  1.00 28.35           C  
ATOM    533  CG2 ILE A 150      22.241 -13.342 -73.269  1.00 26.71           C  
ATOM    534  CD1 ILE A 150      21.988 -16.326 -73.356  1.00 32.35           C  
ATOM    535  N   HIS A 151      22.531 -11.867 -70.467  1.00 29.26           N  
ATOM    536  CA  HIS A 151      23.750 -11.537 -69.745  1.00 34.18           C  
ATOM    537  C   HIS A 151      23.487 -11.380 -68.249  1.00 31.03           C  
ATOM    538  O   HIS A 151      22.491 -10.785 -67.835  1.00 28.49           O  
ATOM    539  CB  HIS A 151      24.380 -10.274 -70.332  1.00 42.41           C  
ATOM    540  CG  HIS A 151      24.936 -10.473 -71.708  1.00 54.33           C  
ATOM    541  ND1 HIS A 151      24.541  -9.718 -72.792  1.00 60.60           N  
ATOM    542  CD2 HIS A 151      25.849 -11.356 -72.180  1.00 57.54           C  
ATOM    543  CE1 HIS A 151      25.192 -10.121 -73.868  1.00 62.13           C  
ATOM    544  NE2 HIS A 151      25.992 -11.114 -73.525  1.00 60.51           N  
ATOM    545  N   ASP A 152      24.398 -11.924 -67.450  1.00 30.17           N  
ATOM    546  CA  ASP A 152      24.187 -12.090 -66.016  1.00 27.95           C  
ATOM    547  C   ASP A 152      24.489 -10.849 -65.176  1.00 26.30           C  
ATOM    548  O   ASP A 152      23.851 -10.624 -64.151  1.00 28.65           O  
ATOM    549  CB  ASP A 152      25.038 -13.257 -65.511  1.00 30.80           C  
ATOM    550  CG  ASP A 152      24.661 -14.574 -66.158  1.00 36.04           C  
ATOM    551  OD1 ASP A 152      23.478 -14.738 -66.526  1.00 34.20           O  
ATOM    552  OD2 ASP A 152      25.547 -15.441 -66.307  1.00 41.52           O  
ATOM    553  N   ARG A 153      25.468 -10.056 -65.595  1.00 24.89           N  
ATOM    554  CA  ARG A 153      25.937  -8.952 -64.764  1.00 25.43           C  
ATOM    555  C   ARG A 153      25.896  -7.611 -65.481  1.00 27.94           C  
ATOM    556  O   ARG A 153      26.442  -7.461 -66.576  1.00 33.11           O  
ATOM    557  CB  ARG A 153      27.357  -9.235 -64.273  1.00 26.58           C  
ATOM    558  CG  ARG A 153      27.440 -10.416 -63.318  1.00 26.95           C  
ATOM    559  CD  ARG A 153      28.878 -10.748 -62.956  1.00 25.08           C  
ATOM    560  NE  ARG A 153      29.664 -11.077 -64.139  1.00 27.81           N  
ATOM    561  CZ  ARG A 153      29.646 -12.260 -64.743  1.00 28.57           C  
ATOM    562  NH1 ARG A 153      28.881 -13.237 -64.276  1.00 27.21           N  
ATOM    563  NH2 ARG A 153      30.392 -12.466 -65.818  1.00 27.22           N  
ATOM    564  N   SER A 154      25.245  -6.639 -64.849  1.00 21.24           N  
ATOM    565  CA  SER A 154      25.164  -5.283 -65.379  1.00 24.61           C  
ATOM    566  C   SER A 154      24.825  -4.301 -64.261  1.00 26.20           C  
ATOM    567  O   SER A 154      24.446  -4.706 -63.163  1.00 24.53           O  
ATOM    568  CB  SER A 154      24.121  -5.193 -66.495  1.00 22.97           C  
ATOM    569  OG  SER A 154      22.824  -5.026 -65.954  1.00 23.16           O  
ATOM    570  N   GLN A 155      24.952  -3.009 -64.550  1.00 23.41           N  
ATOM    571  CA  GLN A 155      24.686  -1.969 -63.560  1.00 22.61           C  
ATOM    572  C   GLN A 155      23.194  -1.757 -63.331  1.00 24.38           C  
ATOM    573  O   GLN A 155      22.796  -0.941 -62.498  1.00 23.58           O  
ATOM    574  CB  GLN A 155      25.325  -0.645 -63.991  1.00 23.18           C  
ATOM    575  CG  GLN A 155      26.843  -0.671 -64.046  1.00 22.01           C  
ATOM    576  CD  GLN A 155      27.377  -1.005 -65.421  1.00 26.29           C  
ATOM    577  OE1 GLN A 155      26.784  -1.799 -66.159  1.00 25.00           O  
ATOM    578  NE2 GLN A 155      28.506  -0.397 -65.777  1.00 27.49           N  
ATOM    579  N   TYR A 156      22.372  -2.491 -64.076  1.00 21.84           N  
ATOM    580  CA  TYR A 156      20.938  -2.245 -64.093  1.00 22.13           C  
ATOM    581  C   TYR A 156      20.189  -3.340 -63.360  1.00 23.10           C  
ATOM    582  O   TYR A 156      18.961  -3.382 -63.377  1.00 25.37           O  
ATOM    583  CB  TYR A 156      20.453  -2.121 -65.538  1.00 22.74           C  
ATOM    584  CG  TYR A 156      21.437  -1.333 -66.362  1.00 25.16           C  
ATOM    585  CD1 TYR A 156      21.741  -0.021 -66.029  1.00 27.45           C  
ATOM    586  CD2 TYR A 156      22.096  -1.907 -67.441  1.00 25.65           C  
ATOM    587  CE1 TYR A 156      22.662   0.704 -66.754  1.00 24.94           C  
ATOM    588  CE2 TYR A 156      23.017  -1.184 -68.181  1.00 26.48           C  
ATOM    589  CZ  TYR A 156      23.297   0.119 -67.831  1.00 26.64           C  
ATOM    590  OH  TYR A 156      24.212   0.844 -68.562  1.00 28.69           O  
ATOM    591  N   ARG A 157      20.937  -4.224 -62.711  1.00 22.00           N  
ATOM    592  CA  ARG A 157      20.332  -5.289 -61.929  1.00 21.22           C  
ATOM    593  C   ARG A 157      20.195  -4.885 -60.468  1.00 22.79           C  
ATOM    594  O   ARG A 157      20.959  -4.065 -59.957  1.00 21.56           O  
ATOM    595  CB  ARG A 157      21.147  -6.580 -62.049  1.00 18.83           C  
ATOM    596  CG  ARG A 157      21.334  -7.051 -63.482  1.00 20.80           C  
ATOM    597  CD  ARG A 157      21.516  -8.556 -63.555  1.00 24.26           C  
ATOM    598  NE  ARG A 157      20.259  -9.276 -63.363  1.00 23.73           N  
ATOM    599  CZ  ARG A 157      20.135 -10.596 -63.464  1.00 24.72           C  
ATOM    600  NH1 ARG A 157      18.955 -11.172 -63.277  1.00 22.92           N  
ATOM    601  NH2 ARG A 157      21.193 -11.338 -63.756  1.00 25.21           N  
ATOM    602  N   ALA A 158      19.207  -5.469 -59.804  1.00 23.85           N  
ATOM    603  CA  ALA A 158      18.955  -5.198 -58.400  1.00 25.06           C  
ATOM    604  C   ALA A 158      18.163  -6.343 -57.797  1.00 22.92           C  
ATOM    605  O   ALA A 158      17.351  -6.971 -58.480  1.00 19.65           O  
ATOM    606  CB  ALA A 158      18.206  -3.880 -58.234  1.00 26.90           C  
ATOM    607  N   LEU A 159      18.416  -6.633 -56.527  1.00 20.26           N  
ATOM    608  CA  LEU A 159      17.590  -7.589 -55.810  1.00 20.34           C  
ATOM    609  C   LEU A 159      16.255  -6.941 -55.491  1.00 21.09           C  
ATOM    610  O   LEU A 159      16.204  -5.892 -54.847  1.00 20.90           O  
ATOM    611  CB  LEU A 159      18.269  -8.062 -54.525  1.00 20.31           C  
ATOM    612  CG  LEU A 159      17.400  -8.923 -53.606  1.00 18.12           C  
ATOM    613  CD1 LEU A 159      17.040 -10.242 -54.277  1.00 18.96           C  
ATOM    614  CD2 LEU A 159      18.093  -9.154 -52.260  1.00 18.02           C  
ATOM    615  N   ILE A 160      15.177  -7.555 -55.964  1.00 19.26           N  
ATOM    616  CA  ILE A 160      13.841  -7.062 -55.670  1.00 20.31           C  
ATOM    617  C   ILE A 160      13.037  -8.123 -54.939  1.00 21.01           C  
ATOM    618  O   ILE A 160      13.337  -9.314 -55.026  1.00 18.77           O  
ATOM    619  CB  ILE A 160      13.086  -6.652 -56.948  1.00 20.82           C  
ATOM    620  CG1 ILE A 160      13.064  -7.810 -57.950  1.00 21.12           C  
ATOM    621  CG2 ILE A 160      13.732  -5.420 -57.565  1.00 19.21           C  
ATOM    622  CD1 ILE A 160      12.083  -7.618 -59.090  1.00 17.36           C  
ATOM    623  N   SER A 161      12.015  -7.683 -54.216  1.00 19.71           N  
ATOM    624  CA  SER A 161      11.072  -8.604 -53.599  1.00 17.79           C  
ATOM    625  C   SER A 161       9.655  -8.134 -53.882  1.00 19.41           C  
ATOM    626  O   SER A 161       9.423  -6.945 -54.107  1.00 21.73           O  
ATOM    627  CB  SER A 161      11.309  -8.718 -52.092  1.00 20.28           C  
ATOM    628  OG  SER A 161      10.856  -7.561 -51.416  1.00 24.62           O  
ATOM    629  N   TRP A 162       8.712  -9.069 -53.875  1.00 18.84           N  
ATOM    630  CA  TRP A 162       7.322  -8.744 -54.154  1.00 23.04           C  
ATOM    631  C   TRP A 162       6.411  -9.811 -53.535  1.00 24.07           C  
ATOM    632  O   TRP A 162       6.872 -10.910 -53.223  1.00 22.39           O  
ATOM    633  CB  TRP A 162       7.109  -8.599 -55.671  1.00 21.94           C  
ATOM    634  CG  TRP A 162       7.265  -9.855 -56.469  1.00 21.74           C  
ATOM    635  CD1 TRP A 162       6.264 -10.668 -56.913  1.00 21.78           C  
ATOM    636  CD2 TRP A 162       8.489 -10.431 -56.944  1.00 20.10           C  
ATOM    637  NE1 TRP A 162       6.787 -11.724 -57.621  1.00 20.84           N  
ATOM    638  CE2 TRP A 162       8.151 -11.602 -57.653  1.00 19.79           C  
ATOM    639  CE3 TRP A 162       9.839 -10.079 -56.825  1.00 20.53           C  
ATOM    640  CZ2 TRP A 162       9.110 -12.416 -58.249  1.00 22.20           C  
ATOM    641  CZ3 TRP A 162      10.791 -10.892 -57.417  1.00 19.38           C  
ATOM    642  CH2 TRP A 162      10.420 -12.046 -58.120  1.00 19.39           C  
ATOM    643  N   PRO A 163       5.125  -9.478 -53.321  1.00 23.79           N  
ATOM    644  CA  PRO A 163       4.221 -10.382 -52.598  1.00 25.23           C  
ATOM    645  C   PRO A 163       4.131 -11.775 -53.206  1.00 25.21           C  
ATOM    646  O   PRO A 163       4.198 -11.917 -54.428  1.00 24.96           O  
ATOM    647  CB  PRO A 163       2.870  -9.668 -52.690  1.00 25.02           C  
ATOM    648  CG  PRO A 163       3.222  -8.234 -52.803  1.00 24.94           C  
ATOM    649  CD  PRO A 163       4.471  -8.193 -53.631  1.00 22.54           C  
ATOM    650  N   LEU A 164       3.985 -12.776 -52.339  1.00 24.38           N  
ATOM    651  CA  LEU A 164       3.881 -14.180 -52.727  1.00 21.98           C  
ATOM    652  C   LEU A 164       2.884 -14.406 -53.861  1.00 21.66           C  
ATOM    653  O   LEU A 164       1.717 -14.017 -53.756  1.00 22.92           O  
ATOM    654  CB  LEU A 164       3.479 -15.030 -51.515  1.00 21.51           C  
ATOM    655  CG  LEU A 164       3.545 -16.552 -51.657  1.00 25.57           C  
ATOM    656  CD1 LEU A 164       4.982 -17.017 -51.772  1.00 29.25           C  
ATOM    657  CD2 LEU A 164       2.859 -17.221 -50.476  1.00 26.82           C  
ATOM    658  N   SER A 165       3.381 -15.010 -54.941  1.00 20.50           N  
ATOM    659  CA  SER A 165       2.594 -15.465 -56.090  1.00 22.01           C  
ATOM    660  C   SER A 165       2.089 -14.354 -57.017  1.00 24.43           C  
ATOM    661  O   SER A 165       1.461 -14.638 -58.033  1.00 25.54           O  
ATOM    662  CB  SER A 165       1.417 -16.317 -55.622  1.00 22.78           C  
ATOM    663  OG  SER A 165       1.870 -17.578 -55.162  1.00 24.44           O  
ATOM    664  N  ASER A 166       2.350 -13.101 -56.657  0.54 24.35           N  
ATOM    665  N  BSER A 166       2.352 -13.100 -56.667  0.46 24.40           N  
ATOM    666  CA ASER A 166       2.169 -11.992 -57.588  0.54 24.67           C  
ATOM    667  CA BSER A 166       2.134 -12.009 -57.609  0.46 24.53           C  
ATOM    668  C  ASER A 166       3.361 -11.973 -58.538  0.54 23.67           C  
ATOM    669  C  BSER A 166       3.349 -11.960 -58.530  0.46 23.74           C  
ATOM    670  O  ASER A 166       4.400 -12.546 -58.226  0.54 23.30           O  
ATOM    671  O  BSER A 166       4.394 -12.508 -58.192  0.46 23.53           O  
ATOM    672  CB ASER A 166       2.044 -10.658 -56.847  0.54 25.80           C  
ATOM    673  CB BSER A 166       1.934 -10.677 -56.881  0.46 25.55           C  
ATOM    674  OG ASER A 166       0.742 -10.478 -56.320  0.54 25.32           O  
ATOM    675  OG BSER A 166       3.135 -10.238 -56.274  0.46 25.48           O  
ATOM    676  N   PRO A 167       3.218 -11.335 -59.711  1.00 23.48           N  
ATOM    677  CA  PRO A 167       4.396 -11.222 -60.577  1.00 22.69           C  
ATOM    678  C   PRO A 167       5.270 -10.042 -60.166  1.00 21.53           C  
ATOM    679  O   PRO A 167       4.776  -9.136 -59.494  1.00 22.56           O  
ATOM    680  CB  PRO A 167       3.789 -11.007 -61.963  1.00 26.29           C  
ATOM    681  CG  PRO A 167       2.508 -10.307 -61.694  1.00 25.93           C  
ATOM    682  CD  PRO A 167       1.997 -10.839 -60.372  1.00 23.97           C  
ATOM    683  N   PRO A 168       6.558 -10.055 -60.549  1.00 19.89           N  
ATOM    684  CA  PRO A 168       7.411  -8.906 -60.232  1.00 20.03           C  
ATOM    685  C   PRO A 168       7.134  -7.745 -61.177  1.00 26.17           C  
ATOM    686  O   PRO A 168       7.672  -7.712 -62.283  1.00 26.27           O  
ATOM    687  CB  PRO A 168       8.828  -9.456 -60.419  1.00 21.16           C  
ATOM    688  CG  PRO A 168       8.672 -10.545 -61.426  1.00 18.73           C  
ATOM    689  CD  PRO A 168       7.309 -11.147 -61.195  1.00 19.74           C  
ATOM    690  N   THR A 169       6.291  -6.811 -60.750  1.00 23.32           N  
ATOM    691  CA  THR A 169       5.934  -5.684 -61.600  1.00 22.14           C  
ATOM    692  C   THR A 169       6.707  -4.433 -61.207  1.00 22.22           C  
ATOM    693  O   THR A 169       7.268  -4.351 -60.117  1.00 19.13           O  
ATOM    694  CB  THR A 169       4.427  -5.376 -61.538  1.00 22.84           C  
ATOM    695  OG1 THR A 169       4.131  -4.686 -60.319  1.00 27.73           O  
ATOM    696  CG2 THR A 169       3.615  -6.664 -61.594  1.00 22.40           C  
ATOM    697  N   VAL A 170       6.725  -3.459 -62.108  1.00 22.62           N  
ATOM    698  CA  VAL A 170       7.370  -2.178 -61.857  1.00 21.40           C  
ATOM    699  C   VAL A 170       6.747  -1.493 -60.646  1.00 24.22           C  
ATOM    700  O   VAL A 170       7.423  -0.784 -59.899  1.00 27.93           O  
ATOM    701  CB  VAL A 170       7.262  -1.262 -63.093  1.00 21.71           C  
ATOM    702  CG1 VAL A 170       7.802   0.138 -62.797  1.00 21.52           C  
ATOM    703  CG2 VAL A 170       7.990  -1.889 -64.271  1.00 20.22           C  
ATOM    704  N   TYR A 171       5.459  -1.739 -60.439  1.00 23.01           N  
ATOM    705  CA  TYR A 171       4.690  -0.990 -59.454  1.00 26.96           C  
ATOM    706  C   TYR A 171       4.544  -1.699 -58.104  1.00 30.93           C  
ATOM    707  O   TYR A 171       4.161  -1.071 -57.119  1.00 35.73           O  
ATOM    708  CB  TYR A 171       3.306  -0.664 -60.026  1.00 22.62           C  
ATOM    709  CG  TYR A 171       3.356  -0.229 -61.475  1.00 24.79           C  
ATOM    710  CD1 TYR A 171       4.070   0.898 -61.855  1.00 23.14           C  
ATOM    711  CD2 TYR A 171       2.704  -0.955 -62.465  1.00 24.25           C  
ATOM    712  CE1 TYR A 171       4.128   1.299 -63.179  1.00 23.77           C  
ATOM    713  CE2 TYR A 171       2.757  -0.563 -63.794  1.00 22.78           C  
ATOM    714  CZ  TYR A 171       3.473   0.568 -64.142  1.00 23.90           C  
ATOM    715  OH  TYR A 171       3.538   0.969 -65.457  1.00 25.67           O  
ATOM    716  N   ASN A 172       4.845  -2.994 -58.047  1.00 31.26           N  
ATOM    717  CA  ASN A 172       4.693  -3.726 -56.790  1.00 33.45           C  
ATOM    718  C   ASN A 172       6.000  -4.318 -56.266  1.00 33.25           C  
ATOM    719  O   ASN A 172       6.008  -4.994 -55.239  1.00 38.25           O  
ATOM    720  CB  ASN A 172       3.650  -4.843 -56.938  1.00 37.83           C  
ATOM    721  CG  ASN A 172       4.198  -6.071 -57.641  1.00 42.28           C  
ATOM    722  OD1 ASN A 172       5.074  -5.972 -58.500  1.00 45.26           O  
ATOM    723  ND2 ASN A 172       3.680  -7.240 -57.277  1.00 38.15           N  
ATOM    724  N   SER A 173       7.100  -4.068 -56.969  1.00 24.86           N  
ATOM    725  CA  SER A 173       8.388  -4.624 -56.568  1.00 23.31           C  
ATOM    726  C   SER A 173       9.162  -3.671 -55.665  1.00 27.17           C  
ATOM    727  O   SER A 173       9.276  -2.479 -55.947  1.00 30.00           O  
ATOM    728  CB  SER A 173       9.233  -4.979 -57.794  1.00 24.01           C  
ATOM    729  OG  SER A 173       8.639  -6.038 -58.527  1.00 26.76           O  
ATOM    730  N   ARG A 174       9.692  -4.215 -54.576  1.00 24.25           N  
ATOM    731  CA  ARG A 174      10.493  -3.455 -53.631  1.00 23.80           C  
ATOM    732  C   ARG A 174      11.967  -3.799 -53.803  1.00 23.35           C  
ATOM    733  O   ARG A 174      12.346  -4.968 -53.740  1.00 22.96           O  
ATOM    734  CB  ARG A 174      10.037  -3.748 -52.198  1.00 26.23           C  
ATOM    735  CG  ARG A 174      10.807  -3.011 -51.116  1.00 30.73           C  
ATOM    736  CD  ARG A 174      10.132  -3.199 -49.762  1.00 32.02           C  
ATOM    737  NE  ARG A 174      10.253  -4.572 -49.274  1.00 31.66           N  
ATOM    738  CZ  ARG A 174       9.376  -5.166 -48.469  1.00 32.98           C  
ATOM    739  NH1 ARG A 174       8.298  -4.513 -48.057  1.00 31.41           N  
ATOM    740  NH2 ARG A 174       9.582  -6.416 -48.074  1.00 31.10           N  
ATOM    741  N   VAL A 175      12.799  -2.789 -54.032  1.00 22.49           N  
ATOM    742  CA  VAL A 175      14.230  -3.019 -54.195  1.00 22.93           C  
ATOM    743  C   VAL A 175      14.896  -3.188 -52.837  1.00 23.92           C  
ATOM    744  O   VAL A 175      14.724  -2.354 -51.949  1.00 26.01           O  
ATOM    745  CB  VAL A 175      14.915  -1.866 -54.953  1.00 25.22           C  
ATOM    746  CG1 VAL A 175      16.424  -2.090 -55.015  1.00 26.07           C  
ATOM    747  CG2 VAL A 175      14.331  -1.723 -56.348  1.00 23.42           C  
ATOM    748  N   GLU A 176      15.647  -4.273 -52.677  1.00 22.16           N  
ATOM    749  CA  GLU A 176      16.351  -4.542 -51.430  1.00 24.77           C  
ATOM    750  C   GLU A 176      17.756  -3.943 -51.467  1.00 25.91           C  
ATOM    751  O   GLU A 176      18.208  -3.332 -50.497  1.00 26.50           O  
ATOM    752  CB  GLU A 176      16.416  -6.049 -51.168  1.00 28.78           C  
ATOM    753  CG  GLU A 176      15.058  -6.742 -51.194  1.00 31.72           C  
ATOM    754  CD  GLU A 176      14.132  -6.281 -50.080  1.00 39.81           C  
ATOM    755  OE1 GLU A 176      14.638  -5.870 -49.016  1.00 43.04           O  
ATOM    756  OE2 GLU A 176      12.896  -6.332 -50.270  1.00 40.48           O  
ATOM    757  N   CYS A 177      18.437  -4.122 -52.596  1.00 22.23           N  
ATOM    758  CA  CYS A 177      19.747  -3.511 -52.830  1.00 21.11           C  
ATOM    759  C   CYS A 177      20.172  -3.671 -54.287  1.00 21.63           C  
ATOM    760  O   CYS A 177      19.543  -4.407 -55.050  1.00 22.58           O  
ATOM    761  CB  CYS A 177      20.811  -4.106 -51.901  1.00 22.06           C  
ATOM    762  SG  CYS A 177      20.727  -5.896 -51.661  1.00 31.40           S  
ATOM    763  N   ILE A 178      21.240  -2.976 -54.667  1.00 20.19           N  
ATOM    764  CA  ILE A 178      21.708  -2.961 -56.052  1.00 21.13           C  
ATOM    765  C   ILE A 178      22.861  -3.942 -56.274  1.00 23.06           C  
ATOM    766  O   ILE A 178      23.845  -3.934 -55.531  1.00 21.09           O  
ATOM    767  CB  ILE A 178      22.167  -1.545 -56.463  1.00 22.03           C  
ATOM    768  CG1 ILE A 178      21.085  -0.519 -56.124  1.00 21.60           C  
ATOM    769  CG2 ILE A 178      22.520  -1.497 -57.946  1.00 21.22           C  
ATOM    770  CD1 ILE A 178      19.797  -0.714 -56.887  1.00 22.17           C  
ATOM    771  N   GLY A 179      22.741  -4.777 -57.305  1.00 23.21           N  
ATOM    772  CA  GLY A 179      23.777  -5.743 -57.628  1.00 23.38           C  
ATOM    773  C   GLY A 179      23.319  -6.890 -58.512  1.00 24.78           C  
ATOM    774  O   GLY A 179      22.160  -6.937 -58.935  1.00 21.84           O  
ATOM    775  N   TRP A 180      24.230  -7.818 -58.797  1.00 22.71           N  
ATOM    776  CA  TRP A 180      23.926  -8.927 -59.699  1.00 18.37           C  
ATOM    777  C   TRP A 180      24.174 -10.296 -59.070  1.00 21.64           C  
ATOM    778  O   TRP A 180      24.185 -11.310 -59.764  1.00 23.04           O  
ATOM    779  CB  TRP A 180      24.728  -8.798 -60.999  1.00 18.78           C  
ATOM    780  CG  TRP A 180      26.125  -8.263 -60.823  1.00 21.32           C  
ATOM    781  CD1 TRP A 180      26.577  -7.025 -61.186  1.00 21.64           C  
ATOM    782  CD2 TRP A 180      27.250  -8.946 -60.251  1.00 24.38           C  
ATOM    783  NE1 TRP A 180      27.908  -6.895 -60.873  1.00 20.41           N  
ATOM    784  CE2 TRP A 180      28.346  -8.059 -60.300  1.00 20.46           C  
ATOM    785  CE3 TRP A 180      27.439 -10.221 -59.704  1.00 24.64           C  
ATOM    786  CZ2 TRP A 180      29.608  -8.401 -59.817  1.00 23.01           C  
ATOM    787  CZ3 TRP A 180      28.695 -10.560 -59.229  1.00 21.96           C  
ATOM    788  CH2 TRP A 180      29.763  -9.654 -59.289  1.00 21.11           C  
ATOM    789  N   SER A 181      24.375 -10.318 -57.757  1.00 19.31           N  
ATOM    790  CA  SER A 181      24.432 -11.566 -56.999  1.00 21.93           C  
ATOM    791  C   SER A 181      23.973 -11.260 -55.587  1.00 23.21           C  
ATOM    792  O   SER A 181      24.379 -10.250 -55.016  1.00 24.43           O  
ATOM    793  CB  SER A 181      25.839 -12.167 -56.995  1.00 21.86           C  
ATOM    794  OG  SER A 181      25.853 -13.421 -56.323  1.00 20.83           O  
ATOM    795  N   SER A 182      23.124 -12.112 -55.019  1.00 21.09           N  
ATOM    796  CA  SER A 182      22.500 -11.755 -53.753  1.00 18.37           C  
ATOM    797  C   SER A 182      22.138 -12.918 -52.843  1.00 21.86           C  
ATOM    798  O   SER A 182      22.123 -14.078 -53.248  1.00 23.37           O  
ATOM    799  CB  SER A 182      21.233 -10.939 -54.017  1.00 21.58           C  
ATOM    800  OG  SER A 182      20.135 -11.790 -54.291  1.00 24.03           O  
ATOM    801  N   THR A 183      21.855 -12.561 -51.597  1.00 20.96           N  
ATOM    802  CA  THR A 183      21.195 -13.435 -50.644  1.00 20.48           C  
ATOM    803  C   THR A 183      20.404 -12.546 -49.697  1.00 22.07           C  
ATOM    804  O   THR A 183      20.618 -11.332 -49.646  1.00 20.99           O  
ATOM    805  CB  THR A 183      22.187 -14.314 -49.854  1.00 22.84           C  
ATOM    806  OG1 THR A 183      21.463 -15.300 -49.107  1.00 23.81           O  
ATOM    807  CG2 THR A 183      23.020 -13.464 -48.894  1.00 19.68           C  
ATOM    808  N   SER A 184      19.482 -13.146 -48.958  1.00 21.94           N  
ATOM    809  CA  SER A 184      18.662 -12.390 -48.024  1.00 20.58           C  
ATOM    810  C   SER A 184      18.015 -13.327 -47.020  1.00 23.15           C  
ATOM    811  O   SER A 184      17.660 -14.453 -47.366  1.00 22.89           O  
ATOM    812  CB  SER A 184      17.597 -11.585 -48.774  1.00 21.71           C  
ATOM    813  OG  SER A 184      16.821 -10.813 -47.874  1.00 21.86           O  
ATOM    814  N   CYS A 185      17.868 -12.867 -45.782  1.00 23.99           N  
ATOM    815  CA  CYS A 185      17.199 -13.656 -44.760  1.00 23.33           C  
ATOM    816  C   CYS A 185      16.783 -12.796 -43.570  1.00 22.75           C  
ATOM    817  O   CYS A 185      17.396 -11.767 -43.282  1.00 24.66           O  
ATOM    818  CB  CYS A 185      18.091 -14.803 -44.285  1.00 20.96           C  
ATOM    819  SG  CYS A 185      19.787 -14.348 -43.859  1.00 27.67           S  
ATOM    820  N   HIS A 186      15.726 -13.224 -42.890  1.00 23.71           N  
ATOM    821  CA  HIS A 186      15.229 -12.532 -41.711  1.00 22.37           C  
ATOM    822  C   HIS A 186      15.728 -13.266 -40.475  1.00 21.60           C  
ATOM    823  O   HIS A 186      15.658 -14.491 -40.421  1.00 22.06           O  
ATOM    824  CB  HIS A 186      13.701 -12.472 -41.734  1.00 22.29           C  
ATOM    825  CG  HIS A 186      13.128 -11.327 -40.961  1.00 22.46           C  
ATOM    826  ND1 HIS A 186      13.087 -11.301 -39.584  1.00 23.36           N  
ATOM    827  CD2 HIS A 186      12.575 -10.160 -41.374  1.00 20.53           C  
ATOM    828  CE1 HIS A 186      12.533 -10.172 -39.181  1.00 19.93           C  
ATOM    829  NE2 HIS A 186      12.209  -9.464 -40.249  1.00 19.80           N  
ATOM    830  N   ASP A 187      16.238 -12.531 -39.489  1.00 21.73           N  
ATOM    831  CA  ASP A 187      16.778 -13.171 -38.288  1.00 21.30           C  
ATOM    832  C   ASP A 187      15.750 -13.248 -37.163  1.00 22.93           C  
ATOM    833  O   ASP A 187      16.054 -13.716 -36.065  1.00 23.76           O  
ATOM    834  CB  ASP A 187      18.049 -12.449 -37.796  1.00 21.57           C  
ATOM    835  CG  ASP A 187      17.801 -10.998 -37.373  1.00 23.20           C  
ATOM    836  OD1 ASP A 187      16.641 -10.595 -37.142  1.00 23.73           O  
ATOM    837  OD2 ASP A 187      18.794 -10.249 -37.262  1.00 24.86           O  
ATOM    838  N   GLY A 188      14.537 -12.782 -37.442  1.00 21.98           N  
ATOM    839  CA  GLY A 188      13.486 -12.751 -36.443  1.00 19.92           C  
ATOM    840  C   GLY A 188      13.145 -11.335 -36.022  1.00 24.32           C  
ATOM    841  O   GLY A 188      11.997 -11.036 -35.689  1.00 24.17           O  
ATOM    842  N   LYS A 189      14.147 -10.462 -36.033  1.00 23.54           N  
ATOM    843  CA  LYS A 189      13.940  -9.053 -35.718  1.00 24.18           C  
ATOM    844  C   LYS A 189      13.904  -8.214 -36.990  1.00 23.59           C  
ATOM    845  O   LYS A 189      12.948  -7.478 -37.232  1.00 24.43           O  
ATOM    846  CB  LYS A 189      15.035  -8.538 -34.781  1.00 23.05           C  
ATOM    847  CG  LYS A 189      15.063  -9.199 -33.414  1.00 25.15           C  
ATOM    848  CD  LYS A 189      16.067  -8.503 -32.502  1.00 28.55           C  
ATOM    849  CE  LYS A 189      16.247  -9.252 -31.195  1.00 31.88           C  
ATOM    850  NZ  LYS A 189      17.176  -8.528 -30.279  1.00 31.58           N  
ATOM    851  N   SER A 190      14.949  -8.335 -37.802  1.00 21.91           N  
ATOM    852  CA  SER A 190      15.028  -7.605 -39.063  1.00 21.02           C  
ATOM    853  C   SER A 190      15.624  -8.460 -40.172  1.00 23.51           C  
ATOM    854  O   SER A 190      16.180  -9.528 -39.921  1.00 22.36           O  
ATOM    855  CB  SER A 190      15.853  -6.328 -38.895  1.00 21.42           C  
ATOM    856  OG  SER A 190      15.175  -5.388 -38.082  1.00 24.06           O  
ATOM    857  N   ARG A 191      15.514  -7.972 -41.401  1.00 22.71           N  
ATOM    858  CA  ARG A 191      16.025  -8.689 -42.558  1.00 21.58           C  
ATOM    859  C   ARG A 191      17.424  -8.223 -42.941  1.00 20.86           C  
ATOM    860  O   ARG A 191      17.708  -7.025 -42.969  1.00 19.19           O  
ATOM    861  CB  ARG A 191      15.077  -8.518 -43.751  1.00 22.24           C  
ATOM    862  CG  ARG A 191      15.627  -9.046 -45.074  1.00 21.64           C  
ATOM    863  CD  ARG A 191      14.512  -9.305 -46.074  1.00 21.09           C  
ATOM    864  NE  ARG A 191      13.611 -10.348 -45.596  1.00 18.82           N  
ATOM    865  CZ  ARG A 191      13.796 -11.646 -45.816  1.00 23.27           C  
ATOM    866  NH1 ARG A 191      14.842 -12.055 -46.520  1.00 20.98           N  
ATOM    867  NH2 ARG A 191      12.930 -12.533 -45.344  1.00 22.57           N  
ATOM    868  N   MET A 192      18.298  -9.179 -43.230  1.00 20.25           N  
ATOM    869  CA  MET A 192      19.589  -8.865 -43.822  1.00 22.42           C  
ATOM    870  C   MET A 192      19.554  -9.184 -45.312  1.00 22.54           C  
ATOM    871  O   MET A 192      19.149 -10.276 -45.709  1.00 22.46           O  
ATOM    872  CB  MET A 192      20.715  -9.646 -43.142  1.00 20.57           C  
ATOM    873  CG  MET A 192      22.066  -9.472 -43.827  1.00 26.05           C  
ATOM    874  SD  MET A 192      23.363 -10.526 -43.152  1.00 24.61           S  
ATOM    875  CE  MET A 192      22.853 -12.128 -43.771  1.00 25.33           C  
ATOM    876  N   SER A 193      19.969  -8.227 -46.135  1.00 21.87           N  
ATOM    877  CA  SER A 193      20.098  -8.461 -47.568  1.00 22.67           C  
ATOM    878  C   SER A 193      21.503  -8.109 -48.029  1.00 25.32           C  
ATOM    879  O   SER A 193      22.068  -7.100 -47.610  1.00 25.30           O  
ATOM    880  CB  SER A 193      19.063  -7.652 -48.352  1.00 22.60           C  
ATOM    881  OG  SER A 193      17.746  -8.120 -48.100  1.00 24.18           O  
ATOM    882  N   ILE A 194      22.068  -8.946 -48.888  1.00 21.58           N  
ATOM    883  CA  ILE A 194      23.410  -8.713 -49.394  1.00 17.66           C  
ATOM    884  C   ILE A 194      23.386  -8.704 -50.911  1.00 21.46           C  
ATOM    885  O   ILE A 194      22.879  -9.634 -51.531  1.00 24.05           O  
ATOM    886  CB  ILE A 194      24.406  -9.784 -48.898  1.00 22.88           C  
ATOM    887  CG1 ILE A 194      24.380  -9.873 -47.369  1.00 22.10           C  
ATOM    888  CG2 ILE A 194      25.816  -9.474 -49.402  1.00 20.70           C  
ATOM    889  CD1 ILE A 194      25.387 -10.848 -46.793  1.00 18.30           C  
ATOM    890  N   CYS A 195      23.922  -7.641 -51.500  1.00 19.25           N  
ATOM    891  CA  CYS A 195      24.037  -7.534 -52.948  1.00 19.12           C  
ATOM    892  C   CYS A 195      25.477  -7.269 -53.354  1.00 22.33           C  
ATOM    893  O   CYS A 195      26.154  -6.432 -52.755  1.00 23.66           O  
ATOM    894  CB  CYS A 195      23.134  -6.421 -53.484  1.00 22.66           C  
ATOM    895  SG  CYS A 195      21.375  -6.768 -53.377  1.00 40.23           S  
ATOM    896  N   ILE A 196      25.938  -7.981 -54.377  1.00 21.10           N  
ATOM    897  CA  ILE A 196      27.272  -7.764 -54.918  1.00 18.99           C  
ATOM    898  C   ILE A 196      27.182  -7.046 -56.258  1.00 21.05           C  
ATOM    899  O   ILE A 196      26.400  -7.436 -57.126  1.00 21.58           O  
ATOM    900  CB  ILE A 196      28.037  -9.089 -55.098  1.00 18.90           C  
ATOM    901  CG1 ILE A 196      28.210  -9.782 -53.748  1.00 22.53           C  
ATOM    902  CG2 ILE A 196      29.399  -8.838 -55.731  1.00 22.57           C  
ATOM    903  CD1 ILE A 196      28.530 -11.252 -53.851  1.00 25.23           C  
ATOM    904  N   SER A 197      27.977  -5.991 -56.415  1.00 18.74           N  
ATOM    905  CA  SER A 197      28.039  -5.255 -57.672  1.00 21.34           C  
ATOM    906  C   SER A 197      29.487  -4.972 -58.032  1.00 24.62           C  
ATOM    907  O   SER A 197      30.384  -5.169 -57.215  1.00 24.83           O  
ATOM    908  CB  SER A 197      27.250  -3.945 -57.581  1.00 22.72           C  
ATOM    909  OG  SER A 197      27.985  -2.951 -56.889  1.00 22.83           O  
ATOM    910  N   GLY A 198      29.711  -4.507 -59.256  1.00 23.73           N  
ATOM    911  CA  GLY A 198      31.045  -4.148 -59.697  1.00 22.54           C  
ATOM    912  C   GLY A 198      31.465  -4.876 -60.957  1.00 23.36           C  
ATOM    913  O   GLY A 198      30.762  -5.770 -61.429  1.00 22.15           O  
ATOM    914  N   PRO A 199      32.621  -4.493 -61.517  1.00 23.20           N  
ATOM    915  CA  PRO A 199      33.203  -5.241 -62.631  1.00 22.36           C  
ATOM    916  C   PRO A 199      33.747  -6.570 -62.128  1.00 22.39           C  
ATOM    917  O   PRO A 199      33.907  -6.731 -60.915  1.00 20.69           O  
ATOM    918  CB  PRO A 199      34.323  -4.323 -63.125  1.00 24.19           C  
ATOM    919  CG  PRO A 199      34.743  -3.586 -61.906  1.00 24.08           C  
ATOM    920  CD  PRO A 199      33.490  -3.388 -61.080  1.00 21.73           C  
ATOM    921  N   ASN A 200      34.024  -7.504 -63.032  1.00 24.70           N  
ATOM    922  CA  ASN A 200      34.451  -8.840 -62.629  1.00 24.82           C  
ATOM    923  C   ASN A 200      35.713  -8.845 -61.763  1.00 25.98           C  
ATOM    924  O   ASN A 200      35.884  -9.725 -60.919  1.00 26.10           O  
ATOM    925  CB  ASN A 200      34.671  -9.720 -63.861  1.00 27.18           C  
ATOM    926  CG  ASN A 200      33.390  -9.965 -64.638  1.00 31.55           C  
ATOM    927  OD1 ASN A 200      32.289  -9.724 -64.139  1.00 31.07           O  
ATOM    928  ND2 ASN A 200      33.527 -10.455 -65.865  1.00 34.22           N  
ATOM    929  N   ASN A 201      36.588  -7.862 -61.961  1.00 24.88           N  
ATOM    930  CA  ASN A 201      37.857  -7.833 -61.236  1.00 25.69           C  
ATOM    931  C   ASN A 201      37.888  -6.857 -60.058  1.00 25.71           C  
ATOM    932  O   ASN A 201      38.945  -6.607 -59.483  1.00 26.65           O  
ATOM    933  CB  ASN A 201      39.012  -7.510 -62.194  1.00 29.11           C  
ATOM    934  CG  ASN A 201      38.937  -6.099 -62.766  1.00 32.72           C  
ATOM    935  OD1 ASN A 201      38.016  -5.331 -62.474  1.00 28.56           O  
ATOM    936  ND2 ASN A 201      39.923  -5.751 -63.587  1.00 31.62           N  
ATOM    937  N   ASN A 202      36.734  -6.311 -59.694  1.00 23.97           N  
ATOM    938  CA  ASN A 202      36.694  -5.298 -58.644  1.00 21.94           C  
ATOM    939  C   ASN A 202      35.331  -5.217 -57.965  1.00 21.65           C  
ATOM    940  O   ASN A 202      34.896  -4.138 -57.564  1.00 23.98           O  
ATOM    941  CB  ASN A 202      37.063  -3.931 -59.224  1.00 23.25           C  
ATOM    942  CG  ASN A 202      38.163  -3.233 -58.444  1.00 28.26           C  
ATOM    943  OD1 ASN A 202      38.569  -3.679 -57.372  1.00 28.81           O  
ATOM    944  ND2 ASN A 202      38.649  -2.123 -58.990  1.00 35.25           N  
ATOM    945  N   ALA A 203      34.665  -6.360 -57.832  1.00 22.60           N  
ATOM    946  CA  ALA A 203      33.326  -6.408 -57.255  1.00 22.66           C  
ATOM    947  C   ALA A 203      33.360  -6.234 -55.740  1.00 23.99           C  
ATOM    948  O   ALA A 203      34.390  -6.448 -55.102  1.00 20.19           O  
ATOM    949  CB  ALA A 203      32.638  -7.718 -57.622  1.00 22.06           C  
ATOM    950  N   SER A 204      32.225  -5.848 -55.168  1.00 22.01           N  
ATOM    951  CA  SER A 204      32.123  -5.690 -53.723  1.00 24.19           C  
ATOM    952  C   SER A 204      30.722  -6.033 -53.236  1.00 23.38           C  
ATOM    953  O   SER A 204      29.737  -5.824 -53.946  1.00 24.11           O  
ATOM    954  CB  SER A 204      32.490  -4.263 -53.306  1.00 24.26           C  
ATOM    955  OG  SER A 204      31.600  -3.320 -53.873  1.00 26.27           O  
ATOM    956  N   ALA A 205      30.643  -6.562 -52.020  1.00 21.08           N  
ATOM    957  CA  ALA A 205      29.362  -6.859 -51.397  1.00 21.41           C  
ATOM    958  C   ALA A 205      28.984  -5.757 -50.418  1.00 24.60           C  
ATOM    959  O   ALA A 205      29.829  -5.259 -49.673  1.00 24.34           O  
ATOM    960  CB  ALA A 205      29.411  -8.207 -50.687  1.00 21.74           C  
ATOM    961  N   VAL A 206      27.717  -5.362 -50.439  1.00 24.89           N  
ATOM    962  CA  VAL A 206      27.194  -4.446 -49.438  1.00 22.89           C  
ATOM    963  C   VAL A 206      26.145  -5.170 -48.610  1.00 22.79           C  
ATOM    964  O   VAL A 206      25.207  -5.751 -49.153  1.00 21.80           O  
ATOM    965  CB  VAL A 206      26.581  -3.181 -50.067  1.00 22.21           C  
ATOM    966  CG1 VAL A 206      26.018  -2.281 -48.984  1.00 22.53           C  
ATOM    967  CG2 VAL A 206      27.624  -2.434 -50.891  1.00 23.89           C  
ATOM    968  N   VAL A 207      26.318  -5.154 -47.295  1.00 21.84           N  
ATOM    969  CA  VAL A 207      25.412  -5.865 -46.412  1.00 22.31           C  
ATOM    970  C   VAL A 207      24.398  -4.909 -45.808  1.00 20.51           C  
ATOM    971  O   VAL A 207      24.759  -3.993 -45.070  1.00 24.21           O  
ATOM    972  CB  VAL A 207      26.169  -6.585 -45.283  1.00 24.57           C  
ATOM    973  CG1 VAL A 207      25.192  -7.351 -44.403  1.00 23.80           C  
ATOM    974  CG2 VAL A 207      27.219  -7.529 -45.865  1.00 23.95           C  
ATOM    975  N   TRP A 208      23.130  -5.126 -46.137  1.00 19.75           N  
ATOM    976  CA  TRP A 208      22.043  -4.308 -45.614  1.00 20.47           C  
ATOM    977  C   TRP A 208      21.373  -5.012 -44.447  1.00 22.16           C  
ATOM    978  O   TRP A 208      21.191  -6.227 -44.471  1.00 22.74           O  
ATOM    979  CB  TRP A 208      21.007  -4.008 -46.702  1.00 20.82           C  
ATOM    980  CG  TRP A 208      21.515  -3.145 -47.814  1.00 21.77           C  
ATOM    981  CD1 TRP A 208      22.497  -3.455 -48.709  1.00 20.45           C  
ATOM    982  CD2 TRP A 208      21.051  -1.835 -48.164  1.00 21.44           C  
ATOM    983  NE1 TRP A 208      22.682  -2.413 -49.586  1.00 20.91           N  
ATOM    984  CE2 TRP A 208      21.805  -1.409 -49.274  1.00 21.12           C  
ATOM    985  CE3 TRP A 208      20.074  -0.980 -47.645  1.00 22.41           C  
ATOM    986  CZ2 TRP A 208      21.614  -0.165 -49.874  1.00 21.60           C  
ATOM    987  CZ3 TRP A 208      19.886   0.256 -48.243  1.00 22.16           C  
ATOM    988  CH2 TRP A 208      20.653   0.650 -49.346  1.00 21.98           C  
ATOM    989  N   TYR A 209      21.017  -4.245 -43.423  1.00 20.05           N  
ATOM    990  CA  TYR A 209      20.265  -4.774 -42.293  1.00 19.63           C  
ATOM    991  C   TYR A 209      19.244  -3.739 -41.856  1.00 20.43           C  
ATOM    992  O   TYR A 209      19.584  -2.569 -41.678  1.00 20.66           O  
ATOM    993  CB  TYR A 209      21.188  -5.137 -41.127  1.00 20.71           C  
ATOM    994  CG  TYR A 209      20.472  -5.840 -39.994  1.00 19.03           C  
ATOM    995  CD1 TYR A 209      20.128  -7.183 -40.093  1.00 19.88           C  
ATOM    996  CD2 TYR A 209      20.126  -5.158 -38.832  1.00 21.93           C  
ATOM    997  CE1 TYR A 209      19.468  -7.829 -39.063  1.00 20.85           C  
ATOM    998  CE2 TYR A 209      19.466  -5.796 -37.798  1.00 21.42           C  
ATOM    999  CZ  TYR A 209      19.137  -7.129 -37.919  1.00 22.54           C  
ATOM   1000  OH  TYR A 209      18.483  -7.761 -36.886  1.00 19.79           O  
ATOM   1001  N   ASN A 210      17.998  -4.177 -41.690  1.00 22.16           N  
ATOM   1002  CA  ASN A 210      16.888  -3.276 -41.393  1.00 25.15           C  
ATOM   1003  C   ASN A 210      16.825  -2.173 -42.445  1.00 24.64           C  
ATOM   1004  O   ASN A 210      16.625  -0.999 -42.128  1.00 22.63           O  
ATOM   1005  CB  ASN A 210      17.021  -2.685 -39.986  1.00 26.90           C  
ATOM   1006  CG  ASN A 210      15.752  -1.997 -39.518  1.00 29.87           C  
ATOM   1007  OD1 ASN A 210      14.649  -2.327 -39.960  1.00 28.12           O  
ATOM   1008  ND2 ASN A 210      15.902  -1.035 -38.613  1.00 30.02           N  
ATOM   1009  N   ARG A 211      17.031  -2.577 -43.698  1.00 23.81           N  
ATOM   1010  CA  ARG A 211      16.917  -1.706 -44.869  1.00 24.39           C  
ATOM   1011  C   ARG A 211      17.912  -0.545 -44.856  1.00 23.72           C  
ATOM   1012  O   ARG A 211      17.663   0.503 -45.453  1.00 22.93           O  
ATOM   1013  CB  ARG A 211      15.482  -1.184 -44.991  1.00 27.58           C  
ATOM   1014  CG  ARG A 211      14.436  -2.283 -44.814  1.00 33.68           C  
ATOM   1015  CD  ARG A 211      13.096  -1.916 -45.427  1.00 37.67           C  
ATOM   1016  NE  ARG A 211      13.222  -1.590 -46.845  1.00 41.54           N  
ATOM   1017  CZ  ARG A 211      13.245  -2.492 -47.820  1.00 42.46           C  
ATOM   1018  NH1 ARG A 211      13.149  -3.785 -47.536  1.00 40.45           N  
ATOM   1019  NH2 ARG A 211      13.365  -2.100 -49.081  1.00 43.92           N  
ATOM   1020  N   ARG A 212      19.044  -0.751 -44.187  1.00 21.53           N  
ATOM   1021  CA  ARG A 212      20.145   0.212 -44.182  1.00 21.68           C  
ATOM   1022  C   ARG A 212      21.473  -0.488 -44.446  1.00 22.76           C  
ATOM   1023  O   ARG A 212      21.681  -1.611 -43.993  1.00 21.75           O  
ATOM   1024  CB  ARG A 212      20.222   0.952 -42.846  1.00 21.84           C  
ATOM   1025  CG  ARG A 212      18.991   1.763 -42.490  1.00 24.36           C  
ATOM   1026  CD  ARG A 212      19.222   2.548 -41.213  1.00 24.65           C  
ATOM   1027  NE  ARG A 212      18.121   3.466 -40.925  1.00 26.39           N  
ATOM   1028  CZ  ARG A 212      17.175   3.234 -40.022  1.00 29.21           C  
ATOM   1029  NH1 ARG A 212      17.196   2.110 -39.318  1.00 30.20           N  
ATOM   1030  NH2 ARG A 212      16.209   4.122 -39.825  1.00 28.07           N  
ATOM   1031  N   PRO A 213      22.382   0.177 -45.174  1.00 23.33           N  
ATOM   1032  CA  PRO A 213      23.703  -0.413 -45.404  1.00 23.29           C  
ATOM   1033  C   PRO A 213      24.539  -0.386 -44.129  1.00 23.91           C  
ATOM   1034  O   PRO A 213      24.588   0.644 -43.453  1.00 24.03           O  
ATOM   1035  CB  PRO A 213      24.303   0.482 -46.490  1.00 24.34           C  
ATOM   1036  CG  PRO A 213      23.644   1.809 -46.279  1.00 23.73           C  
ATOM   1037  CD  PRO A 213      22.246   1.505 -45.801  1.00 24.05           C  
ATOM   1038  N   VAL A 214      25.182  -1.504 -43.806  1.00 21.02           N  
ATOM   1039  CA  VAL A 214      25.871  -1.635 -42.528  1.00 24.81           C  
ATOM   1040  C   VAL A 214      27.337  -2.044 -42.688  1.00 27.45           C  
ATOM   1041  O   VAL A 214      28.210  -1.518 -41.997  1.00 28.51           O  
ATOM   1042  CB  VAL A 214      25.144  -2.655 -41.619  1.00 24.95           C  
ATOM   1043  CG1 VAL A 214      26.014  -3.057 -40.442  1.00 30.61           C  
ATOM   1044  CG2 VAL A 214      23.815  -2.079 -41.143  1.00 24.94           C  
ATOM   1045  N   ALA A 215      27.608  -2.973 -43.600  1.00 27.99           N  
ATOM   1046  CA  ALA A 215      28.973  -3.453 -43.810  1.00 25.52           C  
ATOM   1047  C   ALA A 215      29.263  -3.701 -45.285  1.00 23.52           C  
ATOM   1048  O   ALA A 215      28.349  -3.927 -46.078  1.00 23.69           O  
ATOM   1049  CB  ALA A 215      29.218  -4.721 -43.009  1.00 24.82           C  
ATOM   1050  N   GLU A 216      30.544  -3.654 -45.645  1.00 20.02           N  
ATOM   1051  CA  GLU A 216      30.968  -3.838 -47.030  1.00 22.81           C  
ATOM   1052  C   GLU A 216      32.148  -4.796 -47.114  1.00 24.05           C  
ATOM   1053  O   GLU A 216      33.032  -4.778 -46.257  1.00 26.47           O  
ATOM   1054  CB  GLU A 216      31.346  -2.500 -47.677  1.00 23.03           C  
ATOM   1055  CG  GLU A 216      30.310  -1.392 -47.527  1.00 27.03           C  
ATOM   1056  CD  GLU A 216      30.364  -0.726 -46.164  1.00 31.30           C  
ATOM   1057  OE1 GLU A 216      31.479  -0.380 -45.713  1.00 30.27           O  
ATOM   1058  OE2 GLU A 216      29.294  -0.563 -45.540  1.00 30.28           O  
ATOM   1059  N   ILE A 217      32.158  -5.624 -48.154  1.00 23.37           N  
ATOM   1060  CA  ILE A 217      33.228  -6.594 -48.360  1.00 24.03           C  
ATOM   1061  C   ILE A 217      33.796  -6.484 -49.770  1.00 25.05           C  
ATOM   1062  O   ILE A 217      33.077  -6.670 -50.753  1.00 24.01           O  
ATOM   1063  CB  ILE A 217      32.738  -8.039 -48.131  1.00 22.80           C  
ATOM   1064  CG1 ILE A 217      32.058  -8.171 -46.766  1.00 24.10           C  
ATOM   1065  CG2 ILE A 217      33.894  -9.021 -48.242  1.00 23.38           C  
ATOM   1066  CD1 ILE A 217      31.247  -9.438 -46.619  1.00 25.75           C  
ATOM   1067  N   ASN A 218      35.086  -6.183 -49.873  1.00 24.92           N  
ATOM   1068  CA  ASN A 218      35.722  -6.105 -51.180  1.00 24.86           C  
ATOM   1069  C   ASN A 218      36.122  -7.485 -51.685  1.00 24.27           C  
ATOM   1070  O   ASN A 218      36.334  -8.409 -50.898  1.00 24.40           O  
ATOM   1071  CB  ASN A 218      36.944  -5.188 -51.141  1.00 26.58           C  
ATOM   1072  CG  ASN A 218      37.322  -4.670 -52.514  1.00 30.33           C  
ATOM   1073  OD1 ASN A 218      36.453  -4.356 -53.330  1.00 28.44           O  
ATOM   1074  ND2 ASN A 218      38.622  -4.583 -52.781  1.00 30.65           N  
ATOM   1075  N   THR A 219      36.208  -7.619 -53.004  1.00 20.57           N  
ATOM   1076  CA  THR A 219      36.650  -8.857 -53.631  1.00 22.97           C  
ATOM   1077  C   THR A 219      38.029  -9.273 -53.114  1.00 26.28           C  
ATOM   1078  O   THR A 219      38.916  -8.434 -52.941  1.00 28.38           O  
ATOM   1079  CB  THR A 219      36.694  -8.714 -55.167  1.00 22.83           C  
ATOM   1080  OG1 THR A 219      37.267  -9.890 -55.745  1.00 23.68           O  
ATOM   1081  CG2 THR A 219      37.517  -7.502 -55.572  1.00 21.35           C  
ATOM   1082  N   TRP A 220      38.205 -10.562 -52.847  1.00 24.77           N  
ATOM   1083  CA  TRP A 220      39.489 -11.039 -52.350  1.00 27.54           C  
ATOM   1084  C   TRP A 220      40.264 -11.836 -53.394  1.00 29.12           C  
ATOM   1085  O   TRP A 220      41.451 -12.104 -53.215  1.00 29.98           O  
ATOM   1086  CB  TRP A 220      39.306 -11.882 -51.081  1.00 27.10           C  
ATOM   1087  CG  TRP A 220      38.306 -13.004 -51.185  1.00 24.87           C  
ATOM   1088  CD1 TRP A 220      38.527 -14.259 -51.677  1.00 26.53           C  
ATOM   1089  CD2 TRP A 220      36.945 -12.984 -50.738  1.00 24.21           C  
ATOM   1090  NE1 TRP A 220      37.382 -15.014 -51.584  1.00 25.77           N  
ATOM   1091  CE2 TRP A 220      36.395 -14.253 -51.014  1.00 23.76           C  
ATOM   1092  CE3 TRP A 220      36.135 -12.016 -50.137  1.00 24.52           C  
ATOM   1093  CZ2 TRP A 220      35.075 -14.578 -50.710  1.00 23.31           C  
ATOM   1094  CZ3 TRP A 220      34.821 -12.341 -49.839  1.00 24.93           C  
ATOM   1095  CH2 TRP A 220      34.308 -13.611 -50.123  1.00 22.05           C  
ATOM   1096  N   ALA A 221      39.601 -12.204 -54.486  1.00 25.80           N  
ATOM   1097  CA  ALA A 221      40.260 -12.965 -55.543  1.00 24.72           C  
ATOM   1098  C   ALA A 221      40.127 -12.276 -56.900  1.00 26.38           C  
ATOM   1099  O   ALA A 221      40.669 -12.750 -57.899  1.00 27.71           O  
ATOM   1100  CB  ALA A 221      39.697 -14.379 -55.609  1.00 24.17           C  
ATOM   1101  N   ARG A 222      39.398 -11.162 -56.922  1.00 27.13           N  
ATOM   1102  CA  ARG A 222      39.261 -10.324 -58.114  1.00 30.24           C  
ATOM   1103  C   ARG A 222      38.748 -11.097 -59.327  1.00 29.37           C  
ATOM   1104  O   ARG A 222      39.203 -10.888 -60.452  1.00 29.70           O  
ATOM   1105  CB  ARG A 222      40.598  -9.651 -58.433  1.00 33.67           C  
ATOM   1106  CG  ARG A 222      41.022  -8.672 -57.349  1.00 38.20           C  
ATOM   1107  CD  ARG A 222      42.301  -7.942 -57.691  1.00 46.67           C  
ATOM   1108  NE  ARG A 222      42.657  -7.016 -56.622  1.00 58.16           N  
ATOM   1109  CZ  ARG A 222      42.140  -5.797 -56.493  1.00 64.72           C  
ATOM   1110  NH1 ARG A 222      42.512  -5.017 -55.486  1.00 66.58           N  
ATOM   1111  NH2 ARG A 222      41.247  -5.360 -57.372  1.00 64.12           N  
ATOM   1112  N   ASN A 223      37.791 -11.987 -59.089  1.00 25.95           N  
ATOM   1113  CA  ASN A 223      37.204 -12.774 -60.163  1.00 26.73           C  
ATOM   1114  C   ASN A 223      35.751 -13.120 -59.852  1.00 26.95           C  
ATOM   1115  O   ASN A 223      35.442 -14.240 -59.446  1.00 26.36           O  
ATOM   1116  CB  ASN A 223      38.027 -14.044 -60.406  1.00 28.28           C  
ATOM   1117  CG  ASN A 223      37.608 -14.783 -61.664  1.00 31.79           C  
ATOM   1118  OD1 ASN A 223      36.666 -14.387 -62.349  1.00 30.18           O  
ATOM   1119  ND2 ASN A 223      38.316 -15.864 -61.977  1.00 35.08           N  
ATOM   1120  N   ILE A 224      34.876 -12.137 -60.047  1.00 23.96           N  
ATOM   1121  CA  ILE A 224      33.438 -12.277 -59.834  1.00 23.12           C  
ATOM   1122  C   ILE A 224      33.103 -12.817 -58.446  1.00 23.66           C  
ATOM   1123  O   ILE A 224      32.716 -13.978 -58.288  1.00 24.32           O  
ATOM   1124  CB  ILE A 224      32.791 -13.184 -60.903  1.00 22.35           C  
ATOM   1125  CG1 ILE A 224      33.329 -12.830 -62.292  1.00 26.17           C  
ATOM   1126  CG2 ILE A 224      31.272 -13.045 -60.872  1.00 20.92           C  
ATOM   1127  CD1 ILE A 224      32.659 -13.582 -63.424  1.00 25.88           C  
ATOM   1128  N   LEU A 225      33.275 -11.963 -57.443  1.00 24.51           N  
ATOM   1129  CA  LEU A 225      32.752 -12.224 -56.110  1.00 24.16           C  
ATOM   1130  C   LEU A 225      31.262 -12.523 -56.227  1.00 23.18           C  
ATOM   1131  O   LEU A 225      30.523 -11.767 -56.852  1.00 21.00           O  
ATOM   1132  CB  LEU A 225      33.006 -11.026 -55.195  1.00 21.98           C  
ATOM   1133  CG  LEU A 225      32.355 -11.016 -53.812  1.00 23.35           C  
ATOM   1134  CD1 LEU A 225      32.923 -12.112 -52.934  1.00 22.07           C  
ATOM   1135  CD2 LEU A 225      32.541  -9.658 -53.155  1.00 22.51           C  
ATOM   1136  N   ARG A 226      30.828 -13.639 -55.654  1.00 22.12           N  
ATOM   1137  CA  ARG A 226      29.455 -14.090 -55.839  1.00 24.67           C  
ATOM   1138  C   ARG A 226      28.968 -14.908 -54.651  1.00 25.54           C  
ATOM   1139  O   ARG A 226      29.769 -15.492 -53.919  1.00 24.63           O  
ATOM   1140  CB  ARG A 226      29.342 -14.899 -57.133  1.00 24.46           C  
ATOM   1141  CG  ARG A 226      30.323 -16.060 -57.232  1.00 24.79           C  
ATOM   1142  CD  ARG A 226      30.524 -16.475 -58.681  1.00 22.55           C  
ATOM   1143  NE  ARG A 226      31.360 -17.666 -58.813  1.00 23.54           N  
ATOM   1144  CZ  ARG A 226      32.689 -17.649 -58.879  1.00 25.92           C  
ATOM   1145  NH1 ARG A 226      33.344 -16.497 -58.816  1.00 23.45           N  
ATOM   1146  NH2 ARG A 226      33.363 -18.787 -59.005  1.00 24.75           N  
ATOM   1147  N   THR A 227      27.652 -14.949 -54.466  1.00 23.07           N  
ATOM   1148  CA  THR A 227      27.074 -15.627 -53.314  1.00 20.60           C  
ATOM   1149  C   THR A 227      25.910 -16.552 -53.704  1.00 22.66           C  
ATOM   1150  O   THR A 227      25.857 -17.053 -54.829  1.00 25.89           O  
ATOM   1151  CB  THR A 227      26.627 -14.599 -52.236  1.00 22.87           C  
ATOM   1152  OG1 THR A 227      26.168 -15.286 -51.064  1.00 26.57           O  
ATOM   1153  CG2 THR A 227      25.544 -13.658 -52.766  1.00 22.01           C  
ATOM   1154  N   GLN A 228      24.984 -16.769 -52.774  1.00 19.42           N  
ATOM   1155  CA  GLN A 228      24.080 -17.921 -52.825  1.00 19.78           C  
ATOM   1156  C   GLN A 228      22.958 -17.894 -53.871  1.00 22.27           C  
ATOM   1157  O   GLN A 228      22.635 -18.936 -54.445  1.00 22.84           O  
ATOM   1158  CB  GLN A 228      23.466 -18.121 -51.439  1.00 19.77           C  
ATOM   1159  CG  GLN A 228      24.506 -18.401 -50.369  1.00 22.43           C  
ATOM   1160  CD  GLN A 228      23.902 -18.630 -48.999  1.00 27.62           C  
ATOM   1161  OE1 GLN A 228      24.619 -18.729 -48.004  1.00 30.22           O  
ATOM   1162  NE2 GLN A 228      22.579 -18.714 -48.940  1.00 29.52           N  
ATOM   1163  N   GLU A 229      22.380 -16.718 -54.116  1.00 18.32           N  
ATOM   1164  CA  GLU A 229      21.209 -16.548 -54.995  1.00 19.92           C  
ATOM   1165  C   GLU A 229      19.962 -17.262 -54.457  1.00 20.63           C  
ATOM   1166  O   GLU A 229      19.032 -17.560 -55.208  1.00 22.00           O  
ATOM   1167  CB  GLU A 229      21.498 -17.026 -56.430  1.00 25.55           C  
ATOM   1168  CG  GLU A 229      22.911 -16.770 -56.955  1.00 26.86           C  
ATOM   1169  CD  GLU A 229      23.248 -15.296 -57.126  1.00 32.33           C  
ATOM   1170  OE1 GLU A 229      22.403 -14.429 -56.808  1.00 27.78           O  
ATOM   1171  OE2 GLU A 229      24.371 -15.002 -57.592  1.00 33.14           O  
ATOM   1172  N   SER A 230      19.961 -17.541 -53.158  1.00 21.42           N  
ATOM   1173  CA  SER A 230      18.755 -17.933 -52.435  1.00 21.43           C  
ATOM   1174  C   SER A 230      18.938 -17.520 -50.983  1.00 25.96           C  
ATOM   1175  O   SER A 230      19.979 -16.966 -50.625  1.00 25.44           O  
ATOM   1176  CB  SER A 230      18.464 -19.433 -52.556  1.00 19.74           C  
ATOM   1177  OG  SER A 230      19.505 -20.230 -52.020  1.00 20.47           O  
ATOM   1178  N   GLU A 231      17.940 -17.781 -50.146  1.00 24.91           N  
ATOM   1179  CA  GLU A 231      17.940 -17.208 -48.804  1.00 22.52           C  
ATOM   1180  C   GLU A 231      19.005 -17.812 -47.893  1.00 24.01           C  
ATOM   1181  O   GLU A 231      19.336 -18.994 -47.992  1.00 22.41           O  
ATOM   1182  CB  GLU A 231      16.563 -17.356 -48.147  1.00 22.23           C  
ATOM   1183  CG  GLU A 231      16.276 -18.723 -47.537  1.00 23.30           C  
ATOM   1184  CD  GLU A 231      15.082 -18.691 -46.592  1.00 26.54           C  
ATOM   1185  OE1 GLU A 231      14.413 -17.637 -46.521  1.00 26.99           O  
ATOM   1186  OE2 GLU A 231      14.816 -19.709 -45.913  1.00 23.69           O  
ATOM   1187  N   CYS A 232      19.548 -16.983 -47.009  1.00 24.51           N  
ATOM   1188  CA  CYS A 232      20.409 -17.483 -45.947  1.00 24.86           C  
ATOM   1189  C   CYS A 232      19.534 -17.913 -44.780  1.00 22.67           C  
ATOM   1190  O   CYS A 232      18.313 -17.814 -44.853  1.00 22.79           O  
ATOM   1191  CB  CYS A 232      21.441 -16.426 -45.524  1.00 23.48           C  
ATOM   1192  SG  CYS A 232      20.856 -14.707 -45.563  1.00 26.24           S  
ATOM   1193  N   VAL A 233      20.155 -18.415 -43.720  1.00 20.00           N  
ATOM   1194  CA  VAL A 233      19.418 -18.865 -42.544  1.00 21.02           C  
ATOM   1195  C   VAL A 233      20.063 -18.293 -41.291  1.00 23.47           C  
ATOM   1196  O   VAL A 233      21.285 -18.211 -41.211  1.00 21.34           O  
ATOM   1197  CB  VAL A 233      19.381 -20.401 -42.450  1.00 24.67           C  
ATOM   1198  CG1 VAL A 233      18.528 -20.853 -41.271  1.00 22.86           C  
ATOM   1199  CG2 VAL A 233      18.846 -20.991 -43.742  1.00 27.23           C  
ATOM   1200  N   CYS A 234      19.245 -17.895 -40.322  1.00 21.17           N  
ATOM   1201  CA  CYS A 234      19.755 -17.303 -39.093  1.00 21.10           C  
ATOM   1202  C   CYS A 234      19.436 -18.155 -37.871  1.00 25.01           C  
ATOM   1203  O   CYS A 234      18.394 -18.809 -37.807  1.00 27.53           O  
ATOM   1204  CB  CYS A 234      19.183 -15.895 -38.907  1.00 23.51           C  
ATOM   1205  SG  CYS A 234      19.532 -14.771 -40.275  1.00 28.30           S  
ATOM   1206  N   HIS A 235      20.350 -18.146 -36.907  1.00 23.32           N  
ATOM   1207  CA  HIS A 235      20.102 -18.745 -35.603  1.00 23.75           C  
ATOM   1208  C   HIS A 235      20.621 -17.829 -34.504  1.00 25.16           C  
ATOM   1209  O   HIS A 235      21.810 -17.506 -34.469  1.00 24.49           O  
ATOM   1210  CB  HIS A 235      20.759 -20.119 -35.487  1.00 25.12           C  
ATOM   1211  CG  HIS A 235      20.662 -20.712 -34.117  1.00 28.02           C  
ATOM   1212  ND1 HIS A 235      19.491 -21.236 -33.614  1.00 29.10           N  
ATOM   1213  CD2 HIS A 235      21.586 -20.852 -33.136  1.00 28.77           C  
ATOM   1214  CE1 HIS A 235      19.697 -21.677 -32.386  1.00 33.70           C  
ATOM   1215  NE2 HIS A 235      20.963 -21.457 -32.074  1.00 33.26           N  
ATOM   1216  N   ASN A 236      19.720 -17.416 -33.617  1.00 25.58           N  
ATOM   1217  CA  ASN A 236      20.050 -16.519 -32.512  1.00 26.82           C  
ATOM   1218  C   ASN A 236      20.773 -15.260 -32.992  1.00 28.02           C  
ATOM   1219  O   ASN A 236      21.700 -14.774 -32.345  1.00 27.08           O  
ATOM   1220  CB  ASN A 236      20.897 -17.250 -31.465  1.00 28.44           C  
ATOM   1221  CG  ASN A 236      20.920 -16.534 -30.130  1.00 30.29           C  
ATOM   1222  OD1 ASN A 236      19.982 -15.814 -29.787  1.00 29.79           O  
ATOM   1223  ND2 ASN A 236      21.994 -16.724 -29.370  1.00 33.43           N  
ATOM   1224  N   GLY A 237      20.348 -14.742 -34.139  1.00 26.09           N  
ATOM   1225  CA  GLY A 237      20.909 -13.514 -34.673  1.00 26.26           C  
ATOM   1226  C   GLY A 237      22.093 -13.705 -35.603  1.00 27.35           C  
ATOM   1227  O   GLY A 237      22.481 -12.778 -36.312  1.00 27.37           O  
ATOM   1228  N   VAL A 238      22.671 -14.902 -35.606  1.00 23.79           N  
ATOM   1229  CA  VAL A 238      23.829 -15.179 -36.450  1.00 21.88           C  
ATOM   1230  C   VAL A 238      23.403 -15.769 -37.788  1.00 23.94           C  
ATOM   1231  O   VAL A 238      22.792 -16.835 -37.836  1.00 22.62           O  
ATOM   1232  CB  VAL A 238      24.813 -16.144 -35.766  1.00 22.75           C  
ATOM   1233  CG1 VAL A 238      25.972 -16.459 -36.701  1.00 22.64           C  
ATOM   1234  CG2 VAL A 238      25.319 -15.550 -34.459  1.00 24.21           C  
ATOM   1235  N   CYS A 239      23.737 -15.072 -38.869  1.00 24.28           N  
ATOM   1236  CA  CYS A 239      23.346 -15.494 -40.209  1.00 22.65           C  
ATOM   1237  C   CYS A 239      24.560 -15.810 -41.066  1.00 24.53           C  
ATOM   1238  O   CYS A 239      25.217 -14.895 -41.561  1.00 22.72           O  
ATOM   1239  CB  CYS A 239      22.508 -14.408 -40.892  1.00 22.86           C  
ATOM   1240  SG  CYS A 239      21.210 -13.701 -39.858  1.00 27.09           S  
ATOM   1241  N   PRO A 240      24.873 -17.106 -41.231  1.00 25.12           N  
ATOM   1242  CA  PRO A 240      25.968 -17.536 -42.111  1.00 23.70           C  
ATOM   1243  C   PRO A 240      25.644 -17.342 -43.592  1.00 21.85           C  
ATOM   1244  O   PRO A 240      24.512 -17.576 -44.018  1.00 20.35           O  
ATOM   1245  CB  PRO A 240      26.127 -19.029 -41.782  1.00 21.36           C  
ATOM   1246  CG  PRO A 240      25.441 -19.218 -40.470  1.00 25.18           C  
ATOM   1247  CD  PRO A 240      24.322 -18.228 -40.455  1.00 24.74           C  
ATOM   1248  N   VAL A 241      26.634 -16.908 -44.363  1.00 22.36           N  
ATOM   1249  CA  VAL A 241      26.484 -16.762 -45.807  1.00 22.40           C  
ATOM   1250  C   VAL A 241      27.719 -17.316 -46.516  1.00 23.03           C  
ATOM   1251  O   VAL A 241      28.848 -17.067 -46.090  1.00 25.33           O  
ATOM   1252  CB  VAL A 241      26.276 -15.286 -46.223  1.00 20.67           C  
ATOM   1253  CG1 VAL A 241      26.174 -15.173 -47.739  1.00 20.79           C  
ATOM   1254  CG2 VAL A 241      25.033 -14.700 -45.555  1.00 18.52           C  
ATOM   1255  N   VAL A 242      27.508 -18.064 -47.596  1.00 20.80           N  
ATOM   1256  CA  VAL A 242      28.614 -18.629 -48.359  1.00 20.47           C  
ATOM   1257  C   VAL A 242      28.950 -17.767 -49.572  1.00 23.98           C  
ATOM   1258  O   VAL A 242      28.088 -17.492 -50.407  1.00 23.53           O  
ATOM   1259  CB  VAL A 242      28.295 -20.062 -48.825  1.00 22.70           C  
ATOM   1260  CG1 VAL A 242      29.517 -20.695 -49.491  1.00 24.41           C  
ATOM   1261  CG2 VAL A 242      27.828 -20.900 -47.640  1.00 19.04           C  
ATOM   1262  N   PHE A 243      30.212 -17.351 -49.663  1.00 21.23           N  
ATOM   1263  CA  PHE A 243      30.710 -16.580 -50.800  1.00 22.14           C  
ATOM   1264  C   PHE A 243      31.749 -17.367 -51.585  1.00 23.55           C  
ATOM   1265  O   PHE A 243      32.485 -18.171 -51.015  1.00 25.62           O  
ATOM   1266  CB  PHE A 243      31.345 -15.263 -50.343  1.00 20.41           C  
ATOM   1267  CG  PHE A 243      30.380 -14.275 -49.757  1.00 22.75           C  
ATOM   1268  CD1 PHE A 243      30.025 -14.339 -48.421  1.00 26.96           C  
ATOM   1269  CD2 PHE A 243      29.855 -13.256 -50.537  1.00 24.34           C  
ATOM   1270  CE1 PHE A 243      29.150 -13.419 -47.877  1.00 27.34           C  
ATOM   1271  CE2 PHE A 243      28.978 -12.332 -49.999  1.00 27.16           C  
ATOM   1272  CZ  PHE A 243      28.626 -12.413 -48.667  1.00 29.62           C  
ATOM   1273  N   THR A 244      31.830 -17.110 -52.886  1.00 21.85           N  
ATOM   1274  CA  THR A 244      32.942 -17.607 -53.685  1.00 23.09           C  
ATOM   1275  C   THR A 244      33.553 -16.474 -54.501  1.00 24.50           C  
ATOM   1276  O   THR A 244      32.842 -15.632 -55.047  1.00 26.09           O  
ATOM   1277  CB  THR A 244      32.509 -18.750 -54.629  1.00 22.61           C  
ATOM   1278  OG1 THR A 244      31.996 -19.836 -53.851  1.00 24.39           O  
ATOM   1279  CG2 THR A 244      33.693 -19.247 -55.458  1.00 22.48           C  
ATOM   1280  N   ASP A 245      34.879 -16.449 -54.560  1.00 22.79           N  
ATOM   1281  CA  ASP A 245      35.593 -15.505 -55.402  1.00 25.41           C  
ATOM   1282  C   ASP A 245      36.727 -16.264 -56.082  1.00 28.29           C  
ATOM   1283  O   ASP A 245      37.497 -16.961 -55.421  1.00 27.72           O  
ATOM   1284  CB  ASP A 245      36.120 -14.329 -54.574  1.00 22.88           C  
ATOM   1285  CG  ASP A 245      36.448 -13.110 -55.421  1.00 26.36           C  
ATOM   1286  OD1 ASP A 245      36.503 -13.235 -56.662  1.00 24.69           O  
ATOM   1287  OD2 ASP A 245      36.657 -12.022 -54.840  1.00 24.51           O  
ATOM   1288  N   GLY A 246      36.811 -16.155 -57.403  1.00 26.24           N  
ATOM   1289  CA  GLY A 246      37.801 -16.901 -58.154  1.00 26.79           C  
ATOM   1290  C   GLY A 246      37.200 -17.688 -59.301  1.00 26.49           C  
ATOM   1291  O   GLY A 246      36.043 -17.482 -59.668  1.00 26.80           O  
ATOM   1292  N   SER A 247      37.990 -18.601 -59.858  1.00 24.80           N  
ATOM   1293  CA  SER A 247      37.626 -19.317 -61.078  1.00 24.20           C  
ATOM   1294  C   SER A 247      36.324 -20.109 -60.978  1.00 26.40           C  
ATOM   1295  O   SER A 247      35.981 -20.648 -59.923  1.00 27.49           O  
ATOM   1296  CB  SER A 247      38.756 -20.265 -61.480  1.00 26.42           C  
ATOM   1297  OG  SER A 247      38.384 -21.041 -62.605  1.00 27.84           O  
ATOM   1298  N   ALA A 248      35.611 -20.181 -62.097  1.00 28.96           N  
ATOM   1299  CA  ALA A 248      34.398 -20.982 -62.193  1.00 30.95           C  
ATOM   1300  C   ALA A 248      34.710 -22.362 -62.761  1.00 33.81           C  
ATOM   1301  O   ALA A 248      33.840 -23.231 -62.829  1.00 36.02           O  
ATOM   1302  CB  ALA A 248      33.371 -20.277 -63.054  1.00 29.26           C  
ATOM   1303  N   THR A 249      35.962 -22.552 -63.166  1.00 32.85           N  
ATOM   1304  CA  THR A 249      36.387 -23.775 -63.840  1.00 34.13           C  
ATOM   1305  C   THR A 249      37.691 -24.327 -63.264  1.00 35.61           C  
ATOM   1306  O   THR A 249      38.491 -24.930 -63.979  1.00 34.91           O  
ATOM   1307  CB  THR A 249      36.575 -23.535 -65.346  1.00 33.40           C  
ATOM   1308  OG1 THR A 249      37.511 -22.469 -65.541  1.00 34.92           O  
ATOM   1309  CG2 THR A 249      35.252 -23.160 -65.998  1.00 30.37           C  
ATOM   1310  N   GLY A 250      37.899 -24.112 -61.970  1.00 32.93           N  
ATOM   1311  CA  GLY A 250      39.099 -24.558 -61.285  1.00 33.21           C  
ATOM   1312  C   GLY A 250      39.011 -24.130 -59.834  1.00 31.77           C  
ATOM   1313  O   GLY A 250      37.999 -23.559 -59.427  1.00 31.18           O  
ATOM   1314  N   PRO A 251      40.067 -24.394 -59.047  1.00 29.63           N  
ATOM   1315  CA  PRO A 251      40.074 -24.048 -57.620  1.00 29.67           C  
ATOM   1316  C   PRO A 251      39.770 -22.573 -57.367  1.00 29.75           C  
ATOM   1317  O   PRO A 251      40.395 -21.702 -57.971  1.00 29.24           O  
ATOM   1318  CB  PRO A 251      41.500 -24.390 -57.186  1.00 30.00           C  
ATOM   1319  CG  PRO A 251      41.930 -25.449 -58.142  1.00 30.50           C  
ATOM   1320  CD  PRO A 251      41.305 -25.080 -59.453  1.00 30.33           C  
ATOM   1321  N   ALA A 252      38.809 -22.304 -56.490  1.00 27.84           N  
ATOM   1322  CA  ALA A 252      38.416 -20.936 -56.177  1.00 27.42           C  
ATOM   1323  C   ALA A 252      38.520 -20.664 -54.679  1.00 28.25           C  
ATOM   1324  O   ALA A 252      38.777 -21.575 -53.892  1.00 28.83           O  
ATOM   1325  CB  ALA A 252      37.004 -20.666 -56.671  1.00 26.75           C  
ATOM   1326  N   ASP A 253      38.322 -19.406 -54.294  1.00 27.97           N  
ATOM   1327  CA  ASP A 253      38.420 -19.006 -52.894  1.00 28.11           C  
ATOM   1328  C   ASP A 253      37.043 -18.834 -52.268  1.00 25.12           C  
ATOM   1329  O   ASP A 253      36.436 -17.769 -52.374  1.00 24.15           O  
ATOM   1330  CB  ASP A 253      39.216 -17.705 -52.759  1.00 31.57           C  
ATOM   1331  CG  ASP A 253      40.664 -17.864 -53.169  1.00 44.07           C  
ATOM   1332  OD1 ASP A 253      41.177 -19.003 -53.115  1.00 44.56           O  
ATOM   1333  OD2 ASP A 253      41.292 -16.851 -53.540  1.00 52.57           O  
ATOM   1334  N   THR A 254      36.558 -19.883 -51.611  1.00 22.49           N  
ATOM   1335  CA  THR A 254      35.252 -19.846 -50.968  1.00 22.99           C  
ATOM   1336  C   THR A 254      35.391 -19.467 -49.498  1.00 22.38           C  
ATOM   1337  O   THR A 254      36.265 -19.979 -48.795  1.00 22.32           O  
ATOM   1338  CB  THR A 254      34.527 -21.205 -51.088  1.00 24.21           C  
ATOM   1339  OG1 THR A 254      34.210 -21.453 -52.462  1.00 26.21           O  
ATOM   1340  CG2 THR A 254      33.241 -21.212 -50.274  1.00 23.24           C  
ATOM   1341  N   ARG A 255      34.535 -18.555 -49.045  1.00 21.87           N  
ATOM   1342  CA  ARG A 255      34.526 -18.133 -47.650  1.00 24.27           C  
ATOM   1343  C   ARG A 255      33.133 -18.245 -47.055  1.00 23.90           C  
ATOM   1344  O   ARG A 255      32.138 -18.026 -47.745  1.00 22.55           O  
ATOM   1345  CB  ARG A 255      35.016 -16.691 -47.506  1.00 21.03           C  
ATOM   1346  CG  ARG A 255      36.455 -16.455 -47.910  1.00 24.46           C  
ATOM   1347  CD  ARG A 255      36.842 -15.002 -47.660  1.00 21.56           C  
ATOM   1348  NE  ARG A 255      38.239 -14.733 -47.989  1.00 25.13           N  
ATOM   1349  CZ  ARG A 255      38.827 -13.553 -47.822  1.00 25.57           C  
ATOM   1350  NH1 ARG A 255      38.137 -12.535 -47.326  1.00 26.94           N  
ATOM   1351  NH2 ARG A 255      40.104 -13.391 -48.146  1.00 26.86           N  
ATOM   1352  N   ILE A 256      33.064 -18.578 -45.771  1.00 25.56           N  
ATOM   1353  CA  ILE A 256      31.799 -18.543 -45.050  1.00 26.32           C  
ATOM   1354  C   ILE A 256      31.821 -17.382 -44.072  1.00 28.34           C  
ATOM   1355  O   ILE A 256      32.624 -17.365 -43.139  1.00 28.91           O  
ATOM   1356  CB  ILE A 256      31.512 -19.845 -44.274  1.00 28.93           C  
ATOM   1357  CG1 ILE A 256      31.288 -21.020 -45.231  1.00 32.20           C  
ATOM   1358  CG2 ILE A 256      30.287 -19.670 -43.386  1.00 28.73           C  
ATOM   1359  CD1 ILE A 256      32.552 -21.751 -45.639  1.00 35.47           C  
ATOM   1360  N   TYR A 257      30.948 -16.407 -44.300  1.00 24.36           N  
ATOM   1361  CA  TYR A 257      30.847 -15.252 -43.420  1.00 23.69           C  
ATOM   1362  C   TYR A 257      29.739 -15.449 -42.401  1.00 25.01           C  
ATOM   1363  O   TYR A 257      28.717 -16.063 -42.695  1.00 27.39           O  
ATOM   1364  CB  TYR A 257      30.594 -13.976 -44.222  1.00 23.41           C  
ATOM   1365  CG  TYR A 257      31.847 -13.336 -44.764  1.00 23.73           C  
ATOM   1366  CD1 TYR A 257      32.511 -13.878 -45.858  1.00 24.56           C  
ATOM   1367  CD2 TYR A 257      32.369 -12.188 -44.182  1.00 23.47           C  
ATOM   1368  CE1 TYR A 257      33.661 -13.291 -46.357  1.00 26.68           C  
ATOM   1369  CE2 TYR A 257      33.519 -11.594 -44.672  1.00 25.38           C  
ATOM   1370  CZ  TYR A 257      34.160 -12.150 -45.759  1.00 27.28           C  
ATOM   1371  OH  TYR A 257      35.304 -11.565 -46.248  1.00 28.39           O  
ATOM   1372  N   TYR A 258      29.950 -14.926 -41.200  1.00 26.05           N  
ATOM   1373  CA  TYR A 258      28.944 -14.993 -40.152  1.00 21.58           C  
ATOM   1374  C   TYR A 258      28.557 -13.577 -39.761  1.00 23.58           C  
ATOM   1375  O   TYR A 258      29.376 -12.829 -39.227  1.00 25.12           O  
ATOM   1376  CB  TYR A 258      29.463 -15.769 -38.936  1.00 25.01           C  
ATOM   1377  CG  TYR A 258      29.876 -17.191 -39.248  1.00 24.17           C  
ATOM   1378  CD1 TYR A 258      31.148 -17.476 -39.728  1.00 24.59           C  
ATOM   1379  CD2 TYR A 258      28.990 -18.247 -39.075  1.00 23.02           C  
ATOM   1380  CE1 TYR A 258      31.531 -18.774 -40.021  1.00 23.18           C  
ATOM   1381  CE2 TYR A 258      29.365 -19.552 -39.363  1.00 22.63           C  
ATOM   1382  CZ  TYR A 258      30.635 -19.808 -39.835  1.00 23.18           C  
ATOM   1383  OH  TYR A 258      31.017 -21.098 -40.126  1.00 23.17           O  
ATOM   1384  N   PHE A 259      27.311 -13.209 -40.043  1.00 24.88           N  
ATOM   1385  CA  PHE A 259      26.830 -11.862 -39.758  1.00 21.02           C  
ATOM   1386  C   PHE A 259      25.893 -11.819 -38.558  1.00 23.94           C  
ATOM   1387  O   PHE A 259      25.199 -12.789 -38.259  1.00 22.13           O  
ATOM   1388  CB  PHE A 259      26.097 -11.280 -40.967  1.00 19.17           C  
ATOM   1389  CG  PHE A 259      26.926 -11.217 -42.214  1.00 22.36           C  
ATOM   1390  CD1 PHE A 259      27.762 -10.139 -42.451  1.00 22.36           C  
ATOM   1391  CD2 PHE A 259      26.851 -12.222 -43.162  1.00 23.54           C  
ATOM   1392  CE1 PHE A 259      28.518 -10.072 -43.605  1.00 21.47           C  
ATOM   1393  CE2 PHE A 259      27.602 -12.160 -44.321  1.00 21.82           C  
ATOM   1394  CZ  PHE A 259      28.436 -11.083 -44.541  1.00 22.48           C  
ATOM   1395  N   LYS A 260      25.875 -10.678 -37.880  1.00 21.47           N  
ATOM   1396  CA  LYS A 260      24.841 -10.396 -36.893  1.00 22.67           C  
ATOM   1397  C   LYS A 260      24.480  -8.921 -36.972  1.00 25.06           C  
ATOM   1398  O   LYS A 260      25.344  -8.053 -36.811  1.00 24.44           O  
ATOM   1399  CB  LYS A 260      25.292 -10.768 -35.481  1.00 25.82           C  
ATOM   1400  CG  LYS A 260      24.263 -10.418 -34.420  1.00 26.11           C  
ATOM   1401  CD  LYS A 260      24.450 -11.251 -33.163  1.00 33.59           C  
ATOM   1402  CE  LYS A 260      23.506 -10.797 -32.066  1.00 37.33           C  
ATOM   1403  NZ  LYS A 260      23.602 -11.672 -30.865  1.00 45.54           N  
ATOM   1404  N   GLU A 261      23.204  -8.653 -37.239  1.00 25.26           N  
ATOM   1405  CA  GLU A 261      22.712  -7.303 -37.484  1.00 25.96           C  
ATOM   1406  C   GLU A 261      23.536  -6.615 -38.573  1.00 24.99           C  
ATOM   1407  O   GLU A 261      23.760  -5.406 -38.533  1.00 28.50           O  
ATOM   1408  CB  GLU A 261      22.712  -6.488 -36.187  1.00 27.72           C  
ATOM   1409  CG  GLU A 261      21.666  -6.967 -35.183  1.00 31.30           C  
ATOM   1410  CD  GLU A 261      21.763  -6.271 -33.838  1.00 43.36           C  
ATOM   1411  OE1 GLU A 261      22.695  -5.460 -33.650  1.00 47.27           O  
ATOM   1412  OE2 GLU A 261      20.904  -6.536 -32.968  1.00 44.43           O  
ATOM   1413  N   GLY A 262      23.976  -7.401 -39.552  1.00 25.10           N  
ATOM   1414  CA  GLY A 262      24.707  -6.874 -40.689  1.00 25.86           C  
ATOM   1415  C   GLY A 262      26.201  -6.738 -40.464  1.00 27.26           C  
ATOM   1416  O   GLY A 262      26.954  -6.498 -41.407  1.00 28.10           O  
ATOM   1417  N   LYS A 263      26.635  -6.896 -39.217  1.00 25.65           N  
ATOM   1418  CA  LYS A 263      28.050  -6.770 -38.886  1.00 27.86           C  
ATOM   1419  C   LYS A 263      28.772  -8.103 -39.037  1.00 26.72           C  
ATOM   1420  O   LYS A 263      28.212  -9.157 -38.738  1.00 24.63           O  
ATOM   1421  CB  LYS A 263      28.225  -6.236 -37.463  1.00 34.90           C  
ATOM   1422  CG  LYS A 263      27.855  -4.768 -37.303  1.00 43.63           C  
ATOM   1423  CD  LYS A 263      28.380  -4.211 -35.987  1.00 53.32           C  
ATOM   1424  CE  LYS A 263      28.762  -2.744 -36.112  1.00 60.47           C  
ATOM   1425  NZ  LYS A 263      28.860  -2.304 -37.532  1.00 63.29           N  
ATOM   1426  N   ILE A 264      30.016  -8.049 -39.504  1.00 26.38           N  
ATOM   1427  CA  ILE A 264      30.818  -9.256 -39.662  1.00 25.20           C  
ATOM   1428  C   ILE A 264      31.372  -9.716 -38.320  1.00 25.52           C  
ATOM   1429  O   ILE A 264      32.177  -9.024 -37.698  1.00 25.54           O  
ATOM   1430  CB  ILE A 264      31.992  -9.045 -40.639  1.00 24.19           C  
ATOM   1431  CG1 ILE A 264      31.471  -8.728 -42.043  1.00 28.13           C  
ATOM   1432  CG2 ILE A 264      32.883 -10.274 -40.676  1.00 22.97           C  
ATOM   1433  CD1 ILE A 264      32.485  -8.024 -42.916  1.00 29.27           C  
ATOM   1434  N   LEU A 265      30.931 -10.885 -37.874  1.00 24.35           N  
ATOM   1435  CA  LEU A 265      31.451 -11.469 -36.648  1.00 25.98           C  
ATOM   1436  C   LEU A 265      32.751 -12.195 -36.936  1.00 26.22           C  
ATOM   1437  O   LEU A 265      33.686 -12.162 -36.137  1.00 27.05           O  
ATOM   1438  CB  LEU A 265      30.441 -12.440 -36.034  1.00 26.74           C  
ATOM   1439  CG  LEU A 265      29.087 -11.860 -35.625  1.00 28.04           C  
ATOM   1440  CD1 LEU A 265      28.223 -12.934 -34.966  1.00 25.43           C  
ATOM   1441  CD2 LEU A 265      29.280 -10.668 -34.701  1.00 30.06           C  
ATOM   1442  N   LYS A 266      32.797 -12.839 -38.097  1.00 22.81           N  
ATOM   1443  CA  LYS A 266      33.853 -13.784 -38.428  1.00 25.61           C  
ATOM   1444  C   LYS A 266      33.692 -14.264 -39.867  1.00 23.72           C  
ATOM   1445  O   LYS A 266      32.577 -14.317 -40.387  1.00 24.04           O  
ATOM   1446  CB  LYS A 266      33.809 -14.972 -37.454  1.00 29.61           C  
ATOM   1447  CG  LYS A 266      34.681 -16.167 -37.810  1.00 32.61           C  
ATOM   1448  CD  LYS A 266      34.499 -17.281 -36.791  1.00 32.39           C  
ATOM   1449  CE  LYS A 266      35.403 -18.470 -37.094  1.00 31.49           C  
ATOM   1450  NZ  LYS A 266      35.135 -19.604 -36.169  1.00 31.73           N  
ATOM   1451  N   TRP A 267      34.802 -14.589 -40.520  1.00 21.64           N  
ATOM   1452  CA  TRP A 267      34.738 -15.373 -41.746  1.00 25.03           C  
ATOM   1453  C   TRP A 267      35.802 -16.456 -41.696  1.00 26.71           C  
ATOM   1454  O   TRP A 267      36.773 -16.347 -40.955  1.00 25.53           O  
ATOM   1455  CB  TRP A 267      34.912 -14.499 -42.992  1.00 23.88           C  
ATOM   1456  CG  TRP A 267      36.250 -13.828 -43.136  1.00 26.53           C  
ATOM   1457  CD1 TRP A 267      36.577 -12.560 -42.753  1.00 27.40           C  
ATOM   1458  CD2 TRP A 267      37.428 -14.381 -43.736  1.00 26.52           C  
ATOM   1459  NE1 TRP A 267      37.888 -12.292 -43.069  1.00 29.22           N  
ATOM   1460  CE2 TRP A 267      38.433 -13.394 -43.672  1.00 27.37           C  
ATOM   1461  CE3 TRP A 267      37.731 -15.614 -44.319  1.00 23.31           C  
ATOM   1462  CZ2 TRP A 267      39.720 -13.605 -44.166  1.00 25.08           C  
ATOM   1463  CZ3 TRP A 267      39.009 -15.821 -44.808  1.00 26.23           C  
ATOM   1464  CH2 TRP A 267      39.987 -14.823 -44.727  1.00 25.03           C  
ATOM   1465  N   GLU A 268      35.602 -17.512 -42.473  1.00 25.10           N  
ATOM   1466  CA  GLU A 268      36.576 -18.591 -42.548  1.00 28.12           C  
ATOM   1467  C   GLU A 268      36.663 -19.130 -43.964  1.00 27.33           C  
ATOM   1468  O   GLU A 268      35.665 -19.163 -44.689  1.00 23.29           O  
ATOM   1469  CB  GLU A 268      36.220 -19.731 -41.592  1.00 32.91           C  
ATOM   1470  CG  GLU A 268      34.736 -19.899 -41.339  1.00 38.52           C  
ATOM   1471  CD  GLU A 268      34.416 -21.188 -40.606  1.00 41.56           C  
ATOM   1472  OE1 GLU A 268      35.302 -21.703 -39.891  1.00 45.77           O  
ATOM   1473  OE2 GLU A 268      33.282 -21.690 -40.754  1.00 38.30           O  
ATOM   1474  N  ASER A 269      37.861 -19.543 -44.361  0.54 24.92           N  
ATOM   1475  N  BSER A 269      37.861 -19.538 -44.366  0.46 24.98           N  
ATOM   1476  CA ASER A 269      38.045 -20.189 -45.650  0.54 24.93           C  
ATOM   1477  CA BSER A 269      38.040 -20.181 -45.658  0.46 24.86           C  
ATOM   1478  C  ASER A 269      37.366 -21.551 -45.636  0.54 24.37           C  
ATOM   1479  C  BSER A 269      37.388 -21.556 -45.643  0.46 24.35           C  
ATOM   1480  O  ASER A 269      37.264 -22.191 -44.588  0.54 23.49           O  
ATOM   1481  O  BSER A 269      37.328 -22.211 -44.600  0.46 23.41           O  
ATOM   1482  CB ASER A 269      39.530 -20.334 -45.978  0.54 24.34           C  
ATOM   1483  CB BSER A 269      39.524 -20.297 -46.005  0.46 24.42           C  
ATOM   1484  OG ASER A 269      40.246 -20.848 -44.870  0.54 25.10           O  
ATOM   1485  OG BSER A 269      40.128 -19.017 -46.079  0.46 22.93           O  
ATOM   1486  N   LEU A 270      36.900 -21.989 -46.801  1.00 23.40           N  
ATOM   1487  CA  LEU A 270      36.240 -23.283 -46.921  1.00 23.07           C  
ATOM   1488  C   LEU A 270      37.176 -24.420 -46.521  1.00 26.60           C  
ATOM   1489  O   LEU A 270      38.328 -24.472 -46.951  1.00 24.73           O  
ATOM   1490  CB  LEU A 270      35.740 -23.497 -48.351  1.00 23.03           C  
ATOM   1491  CG  LEU A 270      35.220 -24.902 -48.677  1.00 24.36           C  
ATOM   1492  CD1 LEU A 270      33.821 -25.124 -48.107  1.00 21.87           C  
ATOM   1493  CD2 LEU A 270      35.233 -25.141 -50.180  1.00 22.20           C  
ATOM   1494  N   THR A 271      36.676 -25.313 -45.677  1.00 26.03           N  
ATOM   1495  CA  THR A 271      37.410 -26.513 -45.300  1.00 27.58           C  
ATOM   1496  C   THR A 271      36.584 -27.738 -45.686  1.00 28.06           C  
ATOM   1497  O   THR A 271      35.445 -27.607 -46.138  1.00 28.33           O  
ATOM   1498  CB  THR A 271      37.727 -26.536 -43.792  1.00 31.69           C  
ATOM   1499  OG1 THR A 271      38.686 -27.563 -43.514  1.00 41.25           O  
ATOM   1500  CG2 THR A 271      36.467 -26.790 -42.985  1.00 26.40           C  
ATOM   1501  N   GLY A 272      37.153 -28.926 -45.515  1.00 27.44           N  
ATOM   1502  CA  GLY A 272      36.460 -30.144 -45.886  1.00 28.10           C  
ATOM   1503  C   GLY A 272      36.884 -30.640 -47.254  1.00 29.52           C  
ATOM   1504  O   GLY A 272      37.912 -30.211 -47.783  1.00 26.42           O  
ATOM   1505  N   THR A 273      36.081 -31.527 -47.836  1.00 27.25           N  
ATOM   1506  CA  THR A 273      36.478 -32.224 -49.057  1.00 26.64           C  
ATOM   1507  C   THR A 273      35.749 -31.743 -50.312  1.00 26.35           C  
ATOM   1508  O   THR A 273      35.971 -32.276 -51.399  1.00 28.06           O  
ATOM   1509  CB  THR A 273      36.260 -33.740 -48.914  1.00 28.08           C  
ATOM   1510  OG1 THR A 273      34.872 -34.003 -48.678  1.00 28.91           O  
ATOM   1511  CG2 THR A 273      37.082 -34.288 -47.753  1.00 24.70           C  
ATOM   1512  N   ALA A 274      34.874 -30.752 -50.168  1.00 23.71           N  
ATOM   1513  CA  ALA A 274      34.253 -30.137 -51.335  1.00 25.13           C  
ATOM   1514  C   ALA A 274      35.325 -29.396 -52.129  1.00 25.90           C  
ATOM   1515  O   ALA A 274      36.092 -28.616 -51.567  1.00 27.40           O  
ATOM   1516  CB  ALA A 274      33.134 -29.194 -50.924  1.00 23.65           C  
ATOM   1517  N   LYS A 275      35.382 -29.642 -53.433  1.00 23.34           N  
ATOM   1518  CA  LYS A 275      36.472 -29.120 -54.252  1.00 26.48           C  
ATOM   1519  C   LYS A 275      36.109 -27.832 -54.991  1.00 26.02           C  
ATOM   1520  O   LYS A 275      36.993 -27.103 -55.442  1.00 26.82           O  
ATOM   1521  CB  LYS A 275      36.927 -30.185 -55.253  1.00 23.85           C  
ATOM   1522  CG  LYS A 275      37.473 -31.447 -54.601  1.00 24.51           C  
ATOM   1523  CD  LYS A 275      38.540 -31.122 -53.558  1.00 25.40           C  
ATOM   1524  CE  LYS A 275      39.217 -32.388 -53.045  1.00 25.11           C  
ATOM   1525  NZ  LYS A 275      38.248 -33.315 -52.392  1.00 24.70           N  
ATOM   1526  N   HIS A 276      34.816 -27.549 -55.108  1.00 22.51           N  
ATOM   1527  CA  HIS A 276      34.362 -26.321 -55.755  1.00 20.61           C  
ATOM   1528  C   HIS A 276      32.950 -25.967 -55.298  1.00 23.89           C  
ATOM   1529  O   HIS A 276      32.075 -26.831 -55.246  1.00 25.23           O  
ATOM   1530  CB  HIS A 276      34.413 -26.462 -57.277  1.00 22.32           C  
ATOM   1531  CG  HIS A 276      34.296 -25.160 -58.007  1.00 23.76           C  
ATOM   1532  ND1 HIS A 276      33.129 -24.741 -58.603  1.00 25.35           N  
ATOM   1533  CD2 HIS A 276      35.207 -24.181 -58.230  1.00 24.79           C  
ATOM   1534  CE1 HIS A 276      33.323 -23.559 -59.166  1.00 28.31           C  
ATOM   1535  NE2 HIS A 276      34.575 -23.200 -58.955  1.00 26.85           N  
ATOM   1536  N   ILE A 277      32.735 -24.695 -54.970  1.00 21.71           N  
ATOM   1537  CA  ILE A 277      31.478 -24.256 -54.366  1.00 22.30           C  
ATOM   1538  C   ILE A 277      30.842 -23.061 -55.074  1.00 25.37           C  
ATOM   1539  O   ILE A 277      31.465 -22.009 -55.221  1.00 24.87           O  
ATOM   1540  CB  ILE A 277      31.685 -23.880 -52.883  1.00 23.62           C  
ATOM   1541  CG1 ILE A 277      32.048 -25.114 -52.060  1.00 26.02           C  
ATOM   1542  CG2 ILE A 277      30.432 -23.227 -52.315  1.00 23.13           C  
ATOM   1543  CD1 ILE A 277      30.900 -26.066 -51.862  1.00 27.64           C  
ATOM   1544  N   GLU A 278      29.595 -23.234 -55.504  1.00 24.58           N  
ATOM   1545  CA  GLU A 278      28.814 -22.151 -56.094  1.00 26.54           C  
ATOM   1546  C   GLU A 278      27.361 -22.209 -55.635  1.00 24.72           C  
ATOM   1547  O   GLU A 278      26.814 -23.295 -55.429  1.00 25.86           O  
ATOM   1548  CB  GLU A 278      28.854 -22.205 -57.628  1.00 30.75           C  
ATOM   1549  CG  GLU A 278      30.235 -22.202 -58.257  1.00 35.64           C  
ATOM   1550  CD  GLU A 278      30.543 -20.902 -58.975  1.00 41.18           C  
ATOM   1551  OE1 GLU A 278      29.932 -19.870 -58.627  1.00 46.47           O  
ATOM   1552  OE2 GLU A 278      31.391 -20.913 -59.894  1.00 39.48           O  
ATOM   1553  N   GLU A 279      26.756 -21.032 -55.472  1.00 22.28           N  
ATOM   1554  CA  GLU A 279      25.305 -20.883 -55.340  1.00 22.78           C  
ATOM   1555  C   GLU A 279      24.657 -21.837 -54.338  1.00 24.22           C  
ATOM   1556  O   GLU A 279      23.794 -22.637 -54.700  1.00 24.22           O  
ATOM   1557  CB  GLU A 279      24.659 -21.062 -56.714  1.00 20.25           C  
ATOM   1558  CG  GLU A 279      25.193 -20.089 -57.759  1.00 25.68           C  
ATOM   1559  CD  GLU A 279      24.759 -20.435 -59.171  1.00 29.41           C  
ATOM   1560  OE1 GLU A 279      24.348 -21.591 -59.407  1.00 29.94           O  
ATOM   1561  OE2 GLU A 279      24.829 -19.546 -60.046  1.00 31.81           O  
ATOM   1562  N   CYS A 280      25.067 -21.743 -53.078  1.00 21.69           N  
ATOM   1563  CA  CYS A 280      24.567 -22.644 -52.045  1.00 19.50           C  
ATOM   1564  C   CYS A 280      23.104 -22.396 -51.704  1.00 22.81           C  
ATOM   1565  O   CYS A 280      22.677 -21.252 -51.566  1.00 20.43           O  
ATOM   1566  CB  CYS A 280      25.423 -22.520 -50.783  1.00 20.81           C  
ATOM   1567  SG  CYS A 280      27.102 -23.134 -50.990  1.00 27.96           S  
ATOM   1568  N   SER A 281      22.349 -23.484 -51.574  1.00 22.10           N  
ATOM   1569  CA  SER A 281      20.973 -23.429 -51.100  1.00 21.86           C  
ATOM   1570  C   SER A 281      20.913 -23.990 -49.685  1.00 24.37           C  
ATOM   1571  O   SER A 281      21.298 -25.136 -49.453  1.00 23.69           O  
ATOM   1572  CB  SER A 281      20.043 -24.214 -52.026  1.00 20.90           C  
ATOM   1573  OG  SER A 281      20.103 -23.707 -53.344  1.00 20.97           O  
ATOM   1574  N   CYS A 282      20.423 -23.193 -48.741  1.00 23.70           N  
ATOM   1575  CA  CYS A 282      20.531 -23.564 -47.334  1.00 26.04           C  
ATOM   1576  C   CYS A 282      19.192 -23.644 -46.605  1.00 23.84           C  
ATOM   1577  O   CYS A 282      18.200 -23.049 -47.023  1.00 22.00           O  
ATOM   1578  CB  CYS A 282      21.452 -22.575 -46.606  1.00 27.47           C  
ATOM   1579  SG  CYS A 282      23.053 -22.302 -47.416  1.00 29.58           S  
ATOM   1580  N   TYR A 283      19.187 -24.397 -45.509  1.00 21.16           N  
ATOM   1581  CA  TYR A 283      18.053 -24.451 -44.597  1.00 22.32           C  
ATOM   1582  C   TYR A 283      18.580 -24.789 -43.209  1.00 22.30           C  
ATOM   1583  O   TYR A 283      19.695 -25.297 -43.072  1.00 24.39           O  
ATOM   1584  CB  TYR A 283      17.018 -25.484 -45.047  1.00 20.32           C  
ATOM   1585  CG  TYR A 283      17.497 -26.914 -44.950  1.00 20.34           C  
ATOM   1586  CD1 TYR A 283      18.189 -27.509 -45.997  1.00 23.45           C  
ATOM   1587  CD2 TYR A 283      17.258 -27.671 -43.809  1.00 21.63           C  
ATOM   1588  CE1 TYR A 283      18.635 -28.817 -45.910  1.00 20.22           C  
ATOM   1589  CE2 TYR A 283      17.701 -28.978 -43.712  1.00 24.89           C  
ATOM   1590  CZ  TYR A 283      18.386 -29.546 -44.766  1.00 24.27           C  
ATOM   1591  OH  TYR A 283      18.826 -30.846 -44.672  1.00 27.10           O  
ATOM   1592  N   GLY A 284      17.782 -24.509 -42.183  1.00 22.12           N  
ATOM   1593  CA  GLY A 284      18.189 -24.773 -40.815  1.00 23.28           C  
ATOM   1594  C   GLY A 284      17.203 -25.626 -40.040  1.00 22.41           C  
ATOM   1595  O   GLY A 284      15.999 -25.551 -40.254  1.00 24.59           O  
ATOM   1596  N   GLU A 285      17.725 -26.443 -39.135  1.00 23.58           N  
ATOM   1597  CA  GLU A 285      16.905 -27.280 -38.265  1.00 24.82           C  
ATOM   1598  C   GLU A 285      17.795 -27.743 -37.124  1.00 31.24           C  
ATOM   1599  O   GLU A 285      19.011 -27.714 -37.277  1.00 36.10           O  
ATOM   1600  CB  GLU A 285      16.316 -28.467 -39.028  1.00 33.11           C  
ATOM   1601  CG  GLU A 285      17.345 -29.262 -39.811  1.00 40.87           C  
ATOM   1602  CD  GLU A 285      17.710 -30.569 -39.132  1.00 50.81           C  
ATOM   1603  OE1 GLU A 285      17.141 -30.869 -38.061  1.00 50.64           O  
ATOM   1604  OE2 GLU A 285      18.566 -31.299 -39.673  1.00 57.81           O  
ATOM   1605  N   ARG A 286      17.183 -28.191 -36.023  1.00 28.97           N  
ATOM   1606  CA  ARG A 286      17.838 -28.389 -34.715  1.00 34.54           C  
ATOM   1607  C   ARG A 286      19.300 -27.909 -34.664  1.00 38.00           C  
ATOM   1608  O   ARG A 286      20.242 -28.608 -35.056  1.00 38.64           O  
ATOM   1609  CB  ARG A 286      17.707 -29.852 -34.259  1.00 35.31           C  
ATOM   1610  CG  ARG A 286      16.395 -30.534 -34.682  1.00 36.47           C  
ATOM   1611  CD  ARG A 286      16.240 -31.902 -34.017  1.00 37.96           C  
ATOM   1612  NE  ARG A 286      14.900 -32.489 -34.148  1.00 39.56           N  
ATOM   1613  CZ  ARG A 286      13.938 -32.400 -33.231  1.00 44.89           C  
ATOM   1614  NH1 ARG A 286      14.142 -31.726 -32.105  1.00 47.04           N  
ATOM   1615  NH2 ARG A 286      12.760 -32.971 -33.449  1.00 47.84           N  
ATOM   1616  N   THR A 287      19.419 -26.690 -34.139  1.00 45.25           N  
ATOM   1617  CA  THR A 287      20.482 -25.698 -34.382  1.00 45.66           C  
ATOM   1618  C   THR A 287      21.638 -26.043 -35.334  1.00 42.72           C  
ATOM   1619  O   THR A 287      22.798 -25.783 -35.012  1.00 43.59           O  
ATOM   1620  CB  THR A 287      21.125 -25.263 -33.043  1.00 51.87           C  
ATOM   1621  OG1 THR A 287      22.022 -26.279 -32.580  1.00 55.77           O  
ATOM   1622  CG2 THR A 287      20.051 -25.021 -31.984  1.00 53.37           C  
ATOM   1623  N   GLY A 288      21.326 -26.587 -36.507  1.00 37.80           N  
ATOM   1624  CA  GLY A 288      22.323 -26.770 -37.549  1.00 34.08           C  
ATOM   1625  C   GLY A 288      21.842 -26.232 -38.887  1.00 32.68           C  
ATOM   1626  O   GLY A 288      20.649 -26.280 -39.181  1.00 32.05           O  
ATOM   1627  N   ILE A 289      22.759 -25.712 -39.699  1.00 27.63           N  
ATOM   1628  CA  ILE A 289      22.402 -25.207 -41.025  1.00 23.12           C  
ATOM   1629  C   ILE A 289      23.055 -26.046 -42.126  1.00 24.75           C  
ATOM   1630  O   ILE A 289      24.270 -26.256 -42.124  1.00 22.72           O  
ATOM   1631  CB  ILE A 289      22.808 -23.730 -41.199  1.00 22.10           C  
ATOM   1632  CG1 ILE A 289      21.983 -22.838 -40.266  1.00 23.29           C  
ATOM   1633  CG2 ILE A 289      22.624 -23.287 -42.643  1.00 19.65           C  
ATOM   1634  CD1 ILE A 289      22.549 -21.446 -40.106  1.00 23.00           C  
ATOM   1635  N   THR A 290      22.243 -26.525 -43.062  1.00 24.91           N  
ATOM   1636  CA  THR A 290      22.725 -27.379 -44.140  1.00 23.95           C  
ATOM   1637  C   THR A 290      22.617 -26.674 -45.485  1.00 23.51           C  
ATOM   1638  O   THR A 290      21.555 -26.174 -45.846  1.00 22.26           O  
ATOM   1639  CB  THR A 290      21.936 -28.702 -44.206  1.00 24.15           C  
ATOM   1640  OG1 THR A 290      22.057 -29.399 -42.961  1.00 26.08           O  
ATOM   1641  CG2 THR A 290      22.467 -29.583 -45.323  1.00 26.77           C  
ATOM   1642  N   CYS A 291      23.721 -26.636 -46.222  1.00 22.74           N  
ATOM   1643  CA  CYS A 291      23.741 -26.003 -47.536  1.00 24.23           C  
ATOM   1644  C   CYS A 291      24.081 -27.000 -48.634  1.00 25.81           C  
ATOM   1645  O   CYS A 291      25.058 -27.737 -48.529  1.00 28.08           O  
ATOM   1646  CB  CYS A 291      24.743 -24.847 -47.560  1.00 25.40           C  
ATOM   1647  SG  CYS A 291      24.352 -23.511 -46.421  1.00 28.95           S  
ATOM   1648  N   THR A 292      23.266 -27.020 -49.683  1.00 19.39           N  
ATOM   1649  CA  THR A 292      23.553 -27.835 -50.855  1.00 22.73           C  
ATOM   1650  C   THR A 292      23.966 -26.907 -51.981  1.00 19.59           C  
ATOM   1651  O   THR A 292      23.236 -25.976 -52.320  1.00 22.92           O  
ATOM   1652  CB  THR A 292      22.344 -28.680 -51.287  1.00 24.00           C  
ATOM   1653  OG1 THR A 292      21.857 -29.424 -50.165  1.00 25.12           O  
ATOM   1654  CG2 THR A 292      22.731 -29.639 -52.404  1.00 26.52           C  
ATOM   1655  N   CYS A 293      25.137 -27.157 -52.556  1.00 21.39           N  
ATOM   1656  CA  CYS A 293      25.726 -26.216 -53.497  1.00 21.63           C  
ATOM   1657  C   CYS A 293      25.959 -26.807 -54.880  1.00 22.58           C  
ATOM   1658  O   CYS A 293      25.479 -27.890 -55.206  1.00 23.21           O  
ATOM   1659  CB  CYS A 293      27.047 -25.684 -52.934  1.00 23.16           C  
ATOM   1660  SG  CYS A 293      26.953 -25.157 -51.202  1.00 28.05           S  
ATOM   1661  N   ARG A 294      26.715 -26.072 -55.684  1.00 21.32           N  
ATOM   1662  CA  ARG A 294      26.993 -26.449 -57.057  1.00 21.63           C  
ATOM   1663  C   ARG A 294      28.497 -26.522 -57.288  1.00 20.95           C  
ATOM   1664  O   ARG A 294      29.219 -25.549 -57.054  1.00 25.56           O  
ATOM   1665  CB  ARG A 294      26.340 -25.446 -58.014  1.00 21.66           C  
ATOM   1666  CG  ARG A 294      26.921 -25.387 -59.425  1.00 21.11           C  
ATOM   1667  CD  ARG A 294      26.229 -24.261 -60.192  1.00 25.53           C  
ATOM   1668  NE  ARG A 294      26.792 -24.019 -61.517  1.00 28.03           N  
ATOM   1669  CZ  ARG A 294      26.304 -23.137 -62.385  1.00 28.30           C  
ATOM   1670  NH1 ARG A 294      25.247 -22.405 -62.063  1.00 25.27           N  
ATOM   1671  NH2 ARG A 294      26.877 -22.981 -63.573  1.00 28.36           N  
ATOM   1672  N   ASP A 295      28.967 -27.690 -57.711  1.00 21.63           N  
ATOM   1673  CA  ASP A 295      30.347 -27.848 -58.152  1.00 20.05           C  
ATOM   1674  C   ASP A 295      30.366 -27.545 -59.643  1.00 21.90           C  
ATOM   1675  O   ASP A 295      29.838 -28.311 -60.447  1.00 22.05           O  
ATOM   1676  CB  ASP A 295      30.867 -29.265 -57.853  1.00 23.34           C  
ATOM   1677  CG  ASP A 295      32.325 -29.476 -58.272  1.00 25.02           C  
ATOM   1678  OD1 ASP A 295      32.753 -28.940 -59.313  1.00 25.05           O  
ATOM   1679  OD2 ASP A 295      33.051 -30.201 -57.555  1.00 26.96           O  
ATOM   1680  N   ASN A 296      30.963 -26.420 -60.010  1.00 23.57           N  
ATOM   1681  CA  ASN A 296      30.986 -26.019 -61.409  1.00 25.49           C  
ATOM   1682  C   ASN A 296      32.263 -26.465 -62.107  1.00 31.15           C  
ATOM   1683  O   ASN A 296      32.448 -26.211 -63.291  1.00 33.37           O  
ATOM   1684  CB  ASN A 296      30.828 -24.505 -61.535  1.00 25.57           C  
ATOM   1685  CG  ASN A 296      30.292 -24.092 -62.886  1.00 28.15           C  
ATOM   1686  OD1 ASN A 296      29.130 -24.336 -63.201  1.00 27.00           O  
ATOM   1687  ND2 ASN A 296      31.140 -23.474 -63.698  1.00 28.62           N  
ATOM   1688  N   TRP A 297      33.141 -27.134 -61.369  1.00 27.68           N  
ATOM   1689  CA  TRP A 297      34.430 -27.543 -61.915  1.00 26.37           C  
ATOM   1690  C   TRP A 297      34.358 -28.939 -62.534  1.00 27.91           C  
ATOM   1691  O   TRP A 297      34.156 -29.070 -63.740  1.00 30.37           O  
ATOM   1692  CB  TRP A 297      35.503 -27.481 -60.826  1.00 26.06           C  
ATOM   1693  CG  TRP A 297      36.901 -27.825 -61.277  1.00 28.65           C  
ATOM   1694  CD1 TRP A 297      37.351 -27.964 -62.562  1.00 28.36           C  
ATOM   1695  CD2 TRP A 297      38.035 -28.048 -60.431  1.00 27.37           C  
ATOM   1696  NE1 TRP A 297      38.691 -28.276 -62.564  1.00 31.10           N  
ATOM   1697  CE2 TRP A 297      39.134 -28.332 -61.268  1.00 29.69           C  
ATOM   1698  CE3 TRP A 297      38.225 -28.044 -59.044  1.00 28.26           C  
ATOM   1699  CZ2 TRP A 297      40.403 -28.606 -60.763  1.00 32.19           C  
ATOM   1700  CZ3 TRP A 297      39.483 -28.315 -58.547  1.00 31.15           C  
ATOM   1701  CH2 TRP A 297      40.557 -28.592 -59.403  1.00 31.98           C  
ATOM   1702  N   GLN A 298      34.517 -29.978 -61.717  1.00 27.09           N  
ATOM   1703  CA  GLN A 298      34.553 -31.345 -62.235  1.00 25.50           C  
ATOM   1704  C   GLN A 298      33.376 -32.221 -61.798  1.00 28.04           C  
ATOM   1705  O   GLN A 298      33.195 -33.321 -62.322  1.00 30.99           O  
ATOM   1706  CB  GLN A 298      35.856 -32.037 -61.818  1.00 28.58           C  
ATOM   1707  CG  GLN A 298      37.126 -31.383 -62.324  1.00 31.20           C  
ATOM   1708  CD  GLN A 298      38.349 -32.238 -62.068  1.00 39.04           C  
ATOM   1709  OE1 GLN A 298      38.993 -32.714 -63.003  1.00 46.15           O  
ATOM   1710  NE2 GLN A 298      38.674 -32.445 -60.796  1.00 37.28           N  
ATOM   1711  N   GLY A 299      32.580 -31.745 -60.846  1.00 26.62           N  
ATOM   1712  CA  GLY A 299      31.581 -32.596 -60.220  1.00 25.99           C  
ATOM   1713  C   GLY A 299      30.162 -32.499 -60.732  1.00 26.26           C  
ATOM   1714  O   GLY A 299      29.695 -31.425 -61.099  1.00 25.83           O  
ATOM   1715  N   SER A 300      29.472 -33.636 -60.746  1.00 22.00           N  
ATOM   1716  CA  SER A 300      28.049 -33.661 -61.064  1.00 25.73           C  
ATOM   1717  C   SER A 300      27.251 -34.166 -59.871  1.00 26.70           C  
ATOM   1718  O   SER A 300      26.018 -34.186 -59.893  1.00 27.47           O  
ATOM   1719  CB  SER A 300      27.781 -34.524 -62.288  1.00 27.96           C  
ATOM   1720  OG  SER A 300      28.292 -33.901 -63.452  1.00 30.95           O  
ATOM   1721  N   ASN A 301      27.967 -34.593 -58.836  1.00 26.46           N  
ATOM   1722  CA  ASN A 301      27.367 -34.736 -57.518  1.00 25.35           C  
ATOM   1723  C   ASN A 301      27.455 -33.374 -56.841  1.00 24.00           C  
ATOM   1724  O   ASN A 301      28.292 -32.551 -57.212  1.00 24.72           O  
ATOM   1725  CB  ASN A 301      28.066 -35.818 -56.690  1.00 25.11           C  
ATOM   1726  CG  ASN A 301      29.572 -35.637 -56.639  1.00 24.40           C  
ATOM   1727  OD1 ASN A 301      30.148 -34.888 -57.430  1.00 24.00           O  
ATOM   1728  ND2 ASN A 301      30.220 -36.333 -55.710  1.00 25.85           N  
ATOM   1729  N   ARG A 302      26.593 -33.116 -55.866  1.00 22.28           N  
ATOM   1730  CA  ARG A 302      26.563 -31.794 -55.253  1.00 20.60           C  
ATOM   1731  C   ARG A 302      27.358 -31.726 -53.962  1.00 23.39           C  
ATOM   1732  O   ARG A 302      27.264 -32.619 -53.119  1.00 22.19           O  
ATOM   1733  CB  ARG A 302      25.122 -31.357 -54.988  1.00 19.62           C  
ATOM   1734  CG  ARG A 302      24.337 -31.088 -56.253  1.00 20.31           C  
ATOM   1735  CD  ARG A 302      23.079 -30.293 -55.967  1.00 20.43           C  
ATOM   1736  NE  ARG A 302      22.376 -29.956 -57.201  1.00 22.36           N  
ATOM   1737  CZ  ARG A 302      22.654 -28.897 -57.955  1.00 22.49           C  
ATOM   1738  NH1 ARG A 302      23.622 -28.064 -57.601  1.00 20.49           N  
ATOM   1739  NH2 ARG A 302      21.964 -28.674 -59.063  1.00 19.69           N  
ATOM   1740  N   PRO A 303      28.138 -30.649 -53.800  1.00 24.42           N  
ATOM   1741  CA  PRO A 303      28.836 -30.413 -52.536  1.00 24.98           C  
ATOM   1742  C   PRO A 303      27.853 -30.020 -51.441  1.00 25.80           C  
ATOM   1743  O   PRO A 303      26.834 -29.392 -51.725  1.00 27.19           O  
ATOM   1744  CB  PRO A 303      29.795 -29.258 -52.860  1.00 28.13           C  
ATOM   1745  CG  PRO A 303      29.712 -29.052 -54.348  1.00 27.50           C  
ATOM   1746  CD  PRO A 303      28.383 -29.575 -54.774  1.00 25.11           C  
ATOM   1747  N   VAL A 304      28.150 -30.405 -50.207  1.00 23.48           N  
ATOM   1748  CA  VAL A 304      27.328 -30.016 -49.072  1.00 22.40           C  
ATOM   1749  C   VAL A 304      28.184 -29.329 -48.030  1.00 25.06           C  
ATOM   1750  O   VAL A 304      29.254 -29.820 -47.681  1.00 26.17           O  
ATOM   1751  CB  VAL A 304      26.624 -31.225 -48.431  1.00 23.98           C  
ATOM   1752  CG1 VAL A 304      25.837 -30.798 -47.193  1.00 24.04           C  
ATOM   1753  CG2 VAL A 304      25.705 -31.882 -49.430  1.00 28.33           C  
ATOM   1754  N   ILE A 305      27.718 -28.183 -47.548  1.00 22.80           N  
ATOM   1755  CA  ILE A 305      28.369 -27.504 -46.440  1.00 22.95           C  
ATOM   1756  C   ILE A 305      27.457 -27.556 -45.226  1.00 25.67           C  
ATOM   1757  O   ILE A 305      26.305 -27.130 -45.292  1.00 24.04           O  
ATOM   1758  CB  ILE A 305      28.697 -26.039 -46.772  1.00 23.27           C  
ATOM   1759  CG1 ILE A 305      29.683 -25.966 -47.938  1.00 23.18           C  
ATOM   1760  CG2 ILE A 305      29.279 -25.339 -45.553  1.00 26.57           C  
ATOM   1761  CD1 ILE A 305      29.905 -24.560 -48.455  1.00 24.84           C  
ATOM   1762  N   GLN A 306      27.965 -28.087 -44.121  1.00 22.75           N  
ATOM   1763  CA  GLN A 306      27.186 -28.141 -42.893  1.00 24.22           C  
ATOM   1764  C   GLN A 306      27.747 -27.155 -41.880  1.00 23.78           C  
ATOM   1765  O   GLN A 306      28.894 -27.264 -41.460  1.00 25.53           O  
ATOM   1766  CB  GLN A 306      27.164 -29.565 -42.334  1.00 30.03           C  
ATOM   1767  CG  GLN A 306      26.241 -30.489 -43.122  1.00 39.26           C  
ATOM   1768  CD  GLN A 306      26.424 -31.952 -42.773  1.00 46.06           C  
ATOM   1769  OE1 GLN A 306      27.537 -32.481 -42.809  1.00 46.52           O  
ATOM   1770  NE2 GLN A 306      25.325 -32.617 -42.436  1.00 49.15           N  
ATOM   1771  N   ILE A 307      26.923 -26.184 -41.502  1.00 23.92           N  
ATOM   1772  CA  ILE A 307      27.372 -25.051 -40.704  1.00 25.22           C  
ATOM   1773  C   ILE A 307      26.812 -25.072 -39.286  1.00 27.19           C  
ATOM   1774  O   ILE A 307      25.608 -25.222 -39.085  1.00 27.73           O  
ATOM   1775  CB  ILE A 307      26.968 -23.716 -41.364  1.00 24.50           C  
ATOM   1776  CG1 ILE A 307      27.413 -23.680 -42.828  1.00 23.48           C  
ATOM   1777  CG2 ILE A 307      27.543 -22.535 -40.588  1.00 21.91           C  
ATOM   1778  CD1 ILE A 307      26.988 -22.428 -43.564  1.00 24.38           C  
ATOM   1779  N   ASP A 308      27.700 -24.921 -38.308  1.00 26.15           N  
ATOM   1780  CA  ASP A 308      27.308 -24.742 -36.915  1.00 26.54           C  
ATOM   1781  C   ASP A 308      27.273 -23.246 -36.627  1.00 26.23           C  
ATOM   1782  O   ASP A 308      28.320 -22.626 -36.492  1.00 25.22           O  
ATOM   1783  CB  ASP A 308      28.293 -25.461 -35.985  1.00 28.53           C  
ATOM   1784  CG  ASP A 308      27.893 -25.390 -34.514  1.00 35.33           C  
ATOM   1785  OD1 ASP A 308      27.052 -24.546 -34.132  1.00 33.99           O  
ATOM   1786  OD2 ASP A 308      28.436 -26.194 -33.727  1.00 38.63           O  
ATOM   1787  N   PRO A 309      26.069 -22.659 -36.536  1.00 27.25           N  
ATOM   1788  CA  PRO A 309      25.972 -21.202 -36.391  1.00 27.94           C  
ATOM   1789  C   PRO A 309      26.308 -20.715 -34.983  1.00 27.20           C  
ATOM   1790  O   PRO A 309      26.485 -19.515 -34.782  1.00 24.80           O  
ATOM   1791  CB  PRO A 309      24.508 -20.920 -36.730  1.00 27.35           C  
ATOM   1792  CG  PRO A 309      23.797 -22.146 -36.290  1.00 25.98           C  
ATOM   1793  CD  PRO A 309      24.743 -23.300 -36.550  1.00 26.44           C  
ATOM   1794  N   VAL A 310      26.390 -21.631 -34.024  1.00 27.49           N  
ATOM   1795  CA  VAL A 310      26.762 -21.266 -32.662  1.00 29.68           C  
ATOM   1796  C   VAL A 310      28.279 -21.217 -32.516  1.00 28.84           C  
ATOM   1797  O   VAL A 310      28.835 -20.223 -32.049  1.00 28.34           O  
ATOM   1798  CB  VAL A 310      26.184 -22.249 -31.631  1.00 27.15           C  
ATOM   1799  CG1 VAL A 310      26.580 -21.828 -30.218  1.00 30.76           C  
ATOM   1800  CG2 VAL A 310      24.670 -22.328 -31.770  1.00 27.90           C  
ATOM   1801  N   ALA A 311      28.944 -22.294 -32.919  1.00 26.23           N  
ATOM   1802  CA  ALA A 311      30.400 -22.350 -32.890  1.00 26.86           C  
ATOM   1803  C   ALA A 311      30.993 -21.539 -34.040  1.00 28.44           C  
ATOM   1804  O   ALA A 311      32.171 -21.174 -34.016  1.00 30.01           O  
ATOM   1805  CB  ALA A 311      30.876 -23.794 -32.953  1.00 29.50           C  
ATOM   1806  N   MET A 312      30.154 -21.252 -35.033  1.00 25.66           N  
ATOM   1807  CA  MET A 312      30.566 -20.565 -36.254  1.00 22.23           C  
ATOM   1808  C   MET A 312      31.700 -21.322 -36.932  1.00 27.50           C  
ATOM   1809  O   MET A 312      32.744 -20.758 -37.266  1.00 27.03           O  
ATOM   1810  CB  MET A 312      30.951 -19.113 -35.962  1.00 26.74           C  
ATOM   1811  CG  MET A 312      29.811 -18.329 -35.330  1.00 26.81           C  
ATOM   1812  SD  MET A 312      30.036 -16.544 -35.342  1.00 29.38           S  
ATOM   1813  CE  MET A 312      31.451 -16.378 -34.269  1.00 27.81           C  
ATOM   1814  N   THR A 313      31.472 -22.619 -37.116  1.00 24.90           N  
ATOM   1815  CA  THR A 313      32.383 -23.487 -37.850  1.00 25.28           C  
ATOM   1816  C   THR A 313      31.599 -24.297 -38.878  1.00 24.92           C  
ATOM   1817  O   THR A 313      30.367 -24.294 -38.874  1.00 25.35           O  
ATOM   1818  CB  THR A 313      33.135 -24.447 -36.915  1.00 28.65           C  
ATOM   1819  OG1 THR A 313      32.187 -25.213 -36.160  1.00 28.25           O  
ATOM   1820  CG2 THR A 313      34.042 -23.674 -35.959  1.00 30.22           C  
ATOM   1821  N   HIS A 314      32.308 -24.997 -39.756  1.00 26.70           N  
ATOM   1822  CA  HIS A 314      31.647 -25.768 -40.801  1.00 22.78           C  
ATOM   1823  C   HIS A 314      32.480 -26.962 -41.248  1.00 24.87           C  
ATOM   1824  O   HIS A 314      33.678 -27.035 -40.987  1.00 24.69           O  
ATOM   1825  CB  HIS A 314      31.356 -24.885 -42.014  1.00 24.19           C  
ATOM   1826  CG  HIS A 314      32.566 -24.598 -42.846  1.00 27.08           C  
ATOM   1827  ND1 HIS A 314      33.479 -23.617 -42.519  1.00 26.08           N  
ATOM   1828  CD2 HIS A 314      33.028 -25.181 -43.976  1.00 28.19           C  
ATOM   1829  CE1 HIS A 314      34.444 -23.601 -43.421  1.00 30.68           C  
ATOM   1830  NE2 HIS A 314      34.195 -24.539 -44.316  1.00 29.19           N  
ATOM   1831  N   THR A 315      31.823 -27.893 -41.927  1.00 25.51           N  
ATOM   1832  CA  THR A 315      32.497 -28.975 -42.628  1.00 29.03           C  
ATOM   1833  C   THR A 315      31.933 -29.030 -44.040  1.00 29.43           C  
ATOM   1834  O   THR A 315      30.920 -28.386 -44.330  1.00 26.54           O  
ATOM   1835  CB  THR A 315      32.302 -30.333 -41.934  1.00 34.81           C  
ATOM   1836  OG1 THR A 315      30.902 -30.576 -41.745  1.00 39.23           O  
ATOM   1837  CG2 THR A 315      32.995 -30.343 -40.585  1.00 37.13           C  
ATOM   1838  N   SER A 316      32.578 -29.784 -44.922  1.00 25.97           N  
ATOM   1839  CA  SER A 316      32.033 -29.966 -46.261  1.00 25.11           C  
ATOM   1840  C   SER A 316      32.397 -31.317 -46.855  1.00 25.97           C  
ATOM   1841  O   SER A 316      33.436 -31.895 -46.538  1.00 24.91           O  
ATOM   1842  CB  SER A 316      32.501 -28.850 -47.197  1.00 22.75           C  
ATOM   1843  OG  SER A 316      33.853 -29.023 -47.576  1.00 24.70           O  
ATOM   1844  N   GLN A 317      31.512 -31.806 -47.715  1.00 24.59           N  
ATOM   1845  CA  GLN A 317      31.727 -33.030 -48.471  1.00 25.20           C  
ATOM   1846  C   GLN A 317      30.834 -32.985 -49.701  1.00 24.04           C  
ATOM   1847  O   GLN A 317      30.385 -31.916 -50.106  1.00 23.04           O  
ATOM   1848  CB  GLN A 317      31.427 -34.269 -47.622  1.00 25.15           C  
ATOM   1849  CG  GLN A 317      29.984 -34.374 -47.146  1.00 28.13           C  
ATOM   1850  CD  GLN A 317      29.702 -35.678 -46.425  1.00 31.82           C  
ATOM   1851  OE1 GLN A 317      29.840 -35.768 -45.206  1.00 33.51           O  
ATOM   1852  NE2 GLN A 317      29.312 -36.700 -47.180  1.00 30.05           N  
ATOM   1853  N   TYR A 318      30.583 -34.144 -50.296  1.00 20.45           N  
ATOM   1854  CA  TYR A 318      29.608 -34.255 -51.371  1.00 21.92           C  
ATOM   1855  C   TYR A 318      28.461 -35.142 -50.915  1.00 23.56           C  
ATOM   1856  O   TYR A 318      28.608 -35.906 -49.965  1.00 23.73           O  
ATOM   1857  CB  TYR A 318      30.243 -34.831 -52.641  1.00 24.04           C  
ATOM   1858  CG  TYR A 318      31.162 -33.882 -53.375  1.00 24.81           C  
ATOM   1859  CD1 TYR A 318      32.489 -33.735 -52.997  1.00 24.20           C  
ATOM   1860  CD2 TYR A 318      30.701 -33.139 -54.455  1.00 25.01           C  
ATOM   1861  CE1 TYR A 318      33.334 -32.868 -53.671  1.00 25.02           C  
ATOM   1862  CE2 TYR A 318      31.537 -32.266 -55.135  1.00 24.79           C  
ATOM   1863  CZ  TYR A 318      32.856 -32.139 -54.738  1.00 26.34           C  
ATOM   1864  OH  TYR A 318      33.697 -31.277 -55.406  1.00 27.69           O  
ATOM   1865  N   ILE A 319      27.318 -35.035 -51.582  1.00 21.78           N  
ATOM   1866  CA  ILE A 319      26.258 -36.018 -51.393  1.00 23.53           C  
ATOM   1867  C   ILE A 319      26.773 -37.357 -51.908  1.00 23.69           C  
ATOM   1868  O   ILE A 319      27.126 -37.475 -53.081  1.00 25.00           O  
ATOM   1869  CB  ILE A 319      24.963 -35.634 -52.130  1.00 26.00           C  
ATOM   1870  CG1 ILE A 319      24.409 -34.317 -51.583  1.00 26.38           C  
ATOM   1871  CG2 ILE A 319      23.922 -36.733 -51.987  1.00 25.72           C  
ATOM   1872  CD1 ILE A 319      23.181 -33.822 -52.307  1.00 27.10           C  
ATOM   1873  N   CYS A 320      26.829 -38.353 -51.028  1.00 24.47           N  
ATOM   1874  CA  CYS A 320      27.430 -39.643 -51.358  1.00 24.36           C  
ATOM   1875  C   CYS A 320      26.630 -40.435 -52.389  1.00 23.91           C  
ATOM   1876  O   CYS A 320      27.187 -41.258 -53.113  1.00 25.47           O  
ATOM   1877  CB  CYS A 320      27.601 -40.490 -50.089  1.00 20.65           C  
ATOM   1878  SG  CYS A 320      28.944 -39.958 -49.001  1.00 50.10           S  
ATOM   1879  N   SER A 321      25.326 -40.186 -52.449  1.00 22.71           N  
ATOM   1880  CA  SER A 321      24.425 -40.974 -53.286  1.00 23.27           C  
ATOM   1881  C   SER A 321      24.814 -40.968 -54.765  1.00 24.00           C  
ATOM   1882  O   SER A 321      25.243 -39.942 -55.292  1.00 21.51           O  
ATOM   1883  CB  SER A 321      22.993 -40.459 -53.133  1.00 22.43           C  
ATOM   1884  OG  SER A 321      22.100 -41.208 -53.937  1.00 24.06           O  
ATOM   1885  N   PRO A 322      24.664 -42.123 -55.438  1.00 22.08           N  
ATOM   1886  CA  PRO A 322      24.865 -42.214 -56.887  1.00 23.49           C  
ATOM   1887  C   PRO A 322      23.719 -41.573 -57.666  1.00 25.33           C  
ATOM   1888  O   PRO A 322      23.763 -41.515 -58.895  1.00 24.00           O  
ATOM   1889  CB  PRO A 322      24.928 -43.722 -57.140  1.00 24.36           C  
ATOM   1890  CG  PRO A 322      24.121 -44.315 -56.045  1.00 25.03           C  
ATOM   1891  CD  PRO A 322      24.354 -43.435 -54.844  1.00 23.56           C  
ATOM   1892  N   VAL A 323      22.695 -41.115 -56.953  1.00 22.72           N  
ATOM   1893  CA  VAL A 323      21.654 -40.297 -57.558  1.00 24.47           C  
ATOM   1894  C   VAL A 323      22.207 -38.889 -57.741  1.00 27.56           C  
ATOM   1895  O   VAL A 323      22.124 -38.058 -56.836  1.00 26.10           O  
ATOM   1896  CB  VAL A 323      20.375 -40.263 -56.697  1.00 25.41           C  
ATOM   1897  CG1 VAL A 323      19.291 -39.434 -57.374  1.00 26.25           C  
ATOM   1898  CG2 VAL A 323      19.881 -41.678 -56.432  1.00 20.64           C  
ATOM   1899  N   LEU A 324      22.795 -38.641 -58.909  1.00 24.11           N  
ATOM   1900  CA  LEU A 324      23.452 -37.370 -59.202  1.00 24.50           C  
ATOM   1901  C   LEU A 324      22.422 -36.281 -59.493  1.00 24.67           C  
ATOM   1902  O   LEU A 324      21.439 -36.527 -60.195  1.00 24.06           O  
ATOM   1903  CB  LEU A 324      24.402 -37.527 -60.389  1.00 21.39           C  
ATOM   1904  CG  LEU A 324      25.435 -38.651 -60.295  1.00 25.97           C  
ATOM   1905  CD1 LEU A 324      26.275 -38.703 -61.568  1.00 27.18           C  
ATOM   1906  CD2 LEU A 324      26.318 -38.493 -59.062  1.00 27.56           C  
ATOM   1907  N   THR A 325      22.647 -35.076 -58.968  1.00 22.40           N  
ATOM   1908  CA  THR A 325      21.624 -34.033 -59.032  1.00 21.51           C  
ATOM   1909  C   THR A 325      22.088 -32.680 -59.571  1.00 22.66           C  
ATOM   1910  O   THR A 325      21.364 -31.690 -59.455  1.00 21.89           O  
ATOM   1911  CB  THR A 325      21.001 -33.792 -57.645  1.00 22.18           C  
ATOM   1912  OG1 THR A 325      22.009 -33.322 -56.741  1.00 21.59           O  
ATOM   1913  CG2 THR A 325      20.388 -35.080 -57.102  1.00 22.25           C  
ATOM   1914  N   ASP A 326      23.281 -32.621 -60.152  1.00 23.19           N  
ATOM   1915  CA  ASP A 326      23.680 -31.415 -60.869  1.00 21.37           C  
ATOM   1916  C   ASP A 326      23.125 -31.498 -62.287  1.00 23.70           C  
ATOM   1917  O   ASP A 326      22.486 -32.485 -62.651  1.00 25.17           O  
ATOM   1918  CB  ASP A 326      25.204 -31.243 -60.893  1.00 21.93           C  
ATOM   1919  CG  ASP A 326      25.626 -29.790 -61.093  1.00 28.12           C  
ATOM   1920  OD1 ASP A 326      24.745 -28.938 -61.341  1.00 24.65           O  
ATOM   1921  OD2 ASP A 326      26.838 -29.501 -61.014  1.00 30.56           O  
ATOM   1922  N   ASN A 327      23.360 -30.461 -63.083  1.00 21.75           N  
ATOM   1923  CA  ASN A 327      22.975 -30.475 -64.492  1.00 23.49           C  
ATOM   1924  C   ASN A 327      23.859 -29.536 -65.301  1.00 24.15           C  
ATOM   1925  O   ASN A 327      23.994 -28.370 -64.949  1.00 25.74           O  
ATOM   1926  CB  ASN A 327      21.505 -30.084 -64.666  1.00 20.63           C  
ATOM   1927  CG  ASN A 327      21.080 -30.049 -66.124  1.00 24.81           C  
ATOM   1928  OD1 ASN A 327      21.255 -29.042 -66.810  1.00 26.82           O  
ATOM   1929  ND2 ASN A 327      20.520 -31.155 -66.606  1.00 23.41           N  
ATOM   1930  N   PRO A 328      24.458 -30.034 -66.398  1.00 25.67           N  
ATOM   1931  CA  PRO A 328      24.348 -31.402 -66.920  1.00 26.26           C  
ATOM   1932  C   PRO A 328      25.073 -32.425 -66.051  1.00 25.92           C  
ATOM   1933  O   PRO A 328      25.826 -32.043 -65.153  1.00 27.17           O  
ATOM   1934  CB  PRO A 328      25.005 -31.303 -68.300  1.00 27.43           C  
ATOM   1935  CG  PRO A 328      25.975 -30.191 -68.166  1.00 28.15           C  
ATOM   1936  CD  PRO A 328      25.327 -29.196 -67.242  1.00 28.46           C  
ATOM   1937  N   ARG A 329      24.844 -33.705 -66.316  1.00 25.24           N  
ATOM   1938  CA  ARG A 329      25.404 -34.757 -65.479  1.00 23.63           C  
ATOM   1939  C   ARG A 329      25.470 -36.078 -66.230  1.00 26.17           C  
ATOM   1940  O   ARG A 329      24.741 -36.279 -67.202  1.00 24.66           O  
ATOM   1941  CB  ARG A 329      24.566 -34.924 -64.209  1.00 20.09           C  
ATOM   1942  CG  ARG A 329      23.132 -35.356 -64.488  1.00 20.96           C  
ATOM   1943  CD  ARG A 329      22.371 -35.651 -63.209  1.00 23.14           C  
ATOM   1944  NE  ARG A 329      21.037 -36.177 -63.490  1.00 22.13           N  
ATOM   1945  CZ  ARG A 329      19.947 -35.426 -63.613  1.00 22.51           C  
ATOM   1946  NH1 ARG A 329      20.027 -34.109 -63.476  1.00 21.59           N  
ATOM   1947  NH2 ARG A 329      18.777 -35.992 -63.875  1.00 20.19           N  
ATOM   1948  N   PRO A 330      26.352 -36.987 -65.784  1.00 25.25           N  
ATOM   1949  CA  PRO A 330      26.339 -38.352 -66.315  1.00 25.59           C  
ATOM   1950  C   PRO A 330      25.108 -39.111 -65.841  1.00 27.49           C  
ATOM   1951  O   PRO A 330      24.359 -38.606 -65.002  1.00 26.37           O  
ATOM   1952  CB  PRO A 330      27.615 -38.977 -65.732  1.00 28.66           C  
ATOM   1953  CG  PRO A 330      28.444 -37.827 -65.266  1.00 29.54           C  
ATOM   1954  CD  PRO A 330      27.473 -36.774 -64.858  1.00 24.83           C  
ATOM   1955  N   ASN A 331      24.901 -40.310 -66.371  1.00 25.36           N  
ATOM   1956  CA  ASN A 331      23.837 -41.161 -65.871  1.00 29.23           C  
ATOM   1957  C   ASN A 331      24.169 -41.662 -64.472  1.00 27.90           C  
ATOM   1958  O   ASN A 331      25.336 -41.706 -64.088  1.00 27.83           O  
ATOM   1959  CB  ASN A 331      23.586 -42.335 -66.821  1.00 31.83           C  
ATOM   1960  CG  ASN A 331      22.949 -41.897 -68.126  1.00 35.02           C  
ATOM   1961  OD1 ASN A 331      22.034 -41.072 -68.137  1.00 35.14           O  
ATOM   1962  ND2 ASN A 331      23.426 -42.450 -69.233  1.00 36.87           N  
ATOM   1963  N   ASP A 332      23.142 -42.022 -63.708  1.00 23.84           N  
ATOM   1964  CA  ASP A 332      23.345 -42.504 -62.345  1.00 24.65           C  
ATOM   1965  C   ASP A 332      24.088 -43.834 -62.326  1.00 26.55           C  
ATOM   1966  O   ASP A 332      23.621 -44.817 -62.899  1.00 26.68           O  
ATOM   1967  CB  ASP A 332      22.009 -42.654 -61.618  1.00 26.72           C  
ATOM   1968  CG  ASP A 332      21.336 -41.318 -61.345  1.00 30.35           C  
ATOM   1969  OD1 ASP A 332      22.034 -40.282 -61.354  1.00 29.76           O  
ATOM   1970  OD2 ASP A 332      20.108 -41.314 -61.115  1.00 28.89           O  
ATOM   1971  N   PRO A 333      25.250 -43.868 -61.659  1.00 26.27           N  
ATOM   1972  CA  PRO A 333      25.972 -45.122 -61.433  1.00 26.33           C  
ATOM   1973  C   PRO A 333      25.372 -45.889 -60.257  1.00 27.24           C  
ATOM   1974  O   PRO A 333      24.250 -45.595 -59.850  1.00 26.85           O  
ATOM   1975  CB  PRO A 333      27.390 -44.650 -61.120  1.00 24.66           C  
ATOM   1976  CG  PRO A 333      27.174 -43.341 -60.427  1.00 23.20           C  
ATOM   1977  CD  PRO A 333      25.972 -42.710 -61.101  1.00 23.91           C  
ATOM   1978  N   ASN A 334      26.107 -46.852 -59.714  1.00 27.40           N  
ATOM   1979  CA  ASN A 334      25.637 -47.575 -58.541  1.00 28.53           C  
ATOM   1980  C   ASN A 334      26.471 -47.240 -57.315  1.00 28.50           C  
ATOM   1981  O   ASN A 334      26.116 -47.598 -56.192  1.00 27.28           O  
ATOM   1982  CB  ASN A 334      25.644 -49.083 -58.794  1.00 29.15           C  
ATOM   1983  CG  ASN A 334      24.539 -49.516 -59.735  1.00 29.87           C  
ATOM   1984  OD1 ASN A 334      23.572 -48.782 -59.956  1.00 28.27           O  
ATOM   1985  ND2 ASN A 334      24.670 -50.715 -60.290  1.00 28.00           N  
ATOM   1986  N   ILE A 335      27.583 -46.549 -57.540  1.00 27.48           N  
ATOM   1987  CA  ILE A 335      28.398 -46.028 -56.446  1.00 26.44           C  
ATOM   1988  C   ILE A 335      28.658 -44.538 -56.645  1.00 25.11           C  
ATOM   1989  O   ILE A 335      29.144 -44.123 -57.696  1.00 24.00           O  
ATOM   1990  CB  ILE A 335      29.749 -46.760 -56.324  1.00 27.44           C  
ATOM   1991  CG1 ILE A 335      29.550 -48.279 -56.305  1.00 28.02           C  
ATOM   1992  CG2 ILE A 335      30.490 -46.298 -55.074  1.00 28.67           C  
ATOM   1993  CD1 ILE A 335      30.844 -49.052 -56.167  1.00 29.76           C  
ATOM   1994  N   GLY A 336      28.331 -43.737 -55.638  1.00 23.96           N  
ATOM   1995  CA  GLY A 336      28.565 -42.308 -55.710  1.00 24.54           C  
ATOM   1996  C   GLY A 336      29.910 -41.938 -55.121  1.00 25.46           C  
ATOM   1997  O   GLY A 336      30.757 -42.804 -54.903  1.00 24.49           O  
ATOM   1998  N   LYS A 337      30.107 -40.650 -54.855  1.00 26.15           N  
ATOM   1999  CA  LYS A 337      31.369 -40.172 -54.297  1.00 29.32           C  
ATOM   2000  C   LYS A 337      31.121 -39.197 -53.156  1.00 25.79           C  
ATOM   2001  O   LYS A 337      30.418 -38.204 -53.324  1.00 24.85           O  
ATOM   2002  CB  LYS A 337      32.219 -39.508 -55.381  1.00 29.17           C  
ATOM   2003  CG  LYS A 337      32.724 -40.463 -56.451  1.00 34.11           C  
ATOM   2004  CD  LYS A 337      34.009 -41.148 -56.018  1.00 35.52           C  
ATOM   2005  CE  LYS A 337      35.222 -40.287 -56.338  1.00 36.73           C  
ATOM   2006  NZ  LYS A 337      36.482 -40.877 -55.804  1.00 35.76           N  
ATOM   2007  N   CYS A 338      31.713 -39.483 -52.000  1.00 28.35           N  
ATOM   2008  CA  CYS A 338      31.481 -38.696 -50.793  1.00 24.68           C  
ATOM   2009  C   CYS A 338      32.442 -37.516 -50.658  1.00 25.15           C  
ATOM   2010  O   CYS A 338      32.081 -36.469 -50.123  1.00 28.92           O  
ATOM   2011  CB  CYS A 338      31.600 -39.588 -49.550  1.00 27.97           C  
ATOM   2012  SG  CYS A 338      30.553 -41.065 -49.556  1.00 52.51           S  
ATOM   2013  N   ASN A 339      33.667 -37.688 -51.141  1.00 25.81           N  
ATOM   2014  CA  ASN A 339      34.729 -36.735 -50.845  1.00 27.46           C  
ATOM   2015  C   ASN A 339      35.487 -36.256 -52.074  1.00 28.09           C  
ATOM   2016  O   ASN A 339      36.614 -35.771 -51.968  1.00 29.49           O  
ATOM   2017  CB  ASN A 339      35.707 -37.357 -49.851  1.00 30.20           C  
ATOM   2018  CG  ASN A 339      35.059 -37.663 -48.517  1.00 34.33           C  
ATOM   2019  OD1 ASN A 339      34.494 -36.780 -47.871  1.00 35.16           O  
ATOM   2020  ND2 ASN A 339      35.120 -38.924 -48.106  1.00 36.31           N  
ATOM   2021  N   ASP A 340      34.863 -36.395 -53.238  1.00 28.76           N  
ATOM   2022  CA  ASP A 340      35.451 -35.946 -54.494  1.00 28.09           C  
ATOM   2023  C   ASP A 340      34.361 -35.810 -55.553  1.00 28.49           C  
ATOM   2024  O   ASP A 340      33.302 -36.425 -55.435  1.00 25.85           O  
ATOM   2025  CB  ASP A 340      36.542 -36.917 -54.961  1.00 27.16           C  
ATOM   2026  CG  ASP A 340      37.945 -36.403 -54.668  1.00 31.98           C  
ATOM   2027  OD1 ASP A 340      38.159 -35.171 -54.728  1.00 32.38           O  
ATOM   2028  OD2 ASP A 340      38.832 -37.231 -54.376  1.00 32.30           O  
ATOM   2029  N   PRO A 341      34.610 -34.990 -56.584  1.00 27.97           N  
ATOM   2030  CA  PRO A 341      33.627 -34.822 -57.656  1.00 27.12           C  
ATOM   2031  C   PRO A 341      33.375 -36.115 -58.422  1.00 28.00           C  
ATOM   2032  O   PRO A 341      34.324 -36.856 -58.689  1.00 29.96           O  
ATOM   2033  CB  PRO A 341      34.281 -33.773 -58.567  1.00 28.33           C  
ATOM   2034  CG  PRO A 341      35.734 -33.853 -58.261  1.00 28.97           C  
ATOM   2035  CD  PRO A 341      35.789 -34.132 -56.791  1.00 28.57           C  
ATOM   2036  N   TYR A 342      32.119 -36.391 -58.761  1.00 27.93           N  
ATOM   2037  CA  TYR A 342      31.844 -37.469 -59.701  1.00 27.49           C  
ATOM   2038  C   TYR A 342      32.023 -36.929 -61.115  1.00 24.96           C  
ATOM   2039  O   TYR A 342      31.368 -35.961 -61.503  1.00 23.10           O  
ATOM   2040  CB  TYR A 342      30.443 -38.055 -59.520  1.00 26.07           C  
ATOM   2041  CG  TYR A 342      30.265 -39.335 -60.305  1.00 27.30           C  
ATOM   2042  CD1 TYR A 342      29.739 -39.317 -61.589  1.00 28.57           C  
ATOM   2043  CD2 TYR A 342      30.650 -40.558 -59.772  1.00 27.65           C  
ATOM   2044  CE1 TYR A 342      29.592 -40.483 -62.321  1.00 31.22           C  
ATOM   2045  CE2 TYR A 342      30.506 -41.731 -60.495  1.00 31.29           C  
ATOM   2046  CZ  TYR A 342      29.976 -41.688 -61.768  1.00 33.90           C  
ATOM   2047  OH  TYR A 342      29.827 -42.854 -62.488  1.00 38.86           O  
ATOM   2048  N   PRO A 343      32.918 -37.561 -61.888  1.00 23.97           N  
ATOM   2049  CA  PRO A 343      33.365 -37.082 -63.200  1.00 25.80           C  
ATOM   2050  C   PRO A 343      32.392 -37.380 -64.340  1.00 29.13           C  
ATOM   2051  O   PRO A 343      31.532 -38.257 -64.226  1.00 28.68           O  
ATOM   2052  CB  PRO A 343      34.679 -37.839 -63.405  1.00 27.55           C  
ATOM   2053  CG  PRO A 343      34.447 -39.134 -62.708  1.00 28.68           C  
ATOM   2054  CD  PRO A 343      33.593 -38.814 -61.505  1.00 25.54           C  
ATOM   2055  N   GLY A 344      32.551 -36.651 -65.440  1.00 29.38           N  
ATOM   2056  CA  GLY A 344      31.722 -36.837 -66.614  1.00 29.39           C  
ATOM   2057  C   GLY A 344      31.394 -35.519 -67.285  1.00 30.94           C  
ATOM   2058  O   GLY A 344      31.362 -35.423 -68.512  1.00 30.79           O  
ATOM   2059  N   ASN A 345      31.157 -34.494 -66.473  1.00 27.12           N  
ATOM   2060  CA  ASN A 345      30.790 -33.181 -66.986  1.00 26.68           C  
ATOM   2061  C   ASN A 345      31.601 -32.076 -66.324  1.00 29.95           C  
ATOM   2062  O   ASN A 345      31.560 -31.910 -65.105  1.00 28.25           O  
ATOM   2063  CB  ASN A 345      29.292 -32.931 -66.787  1.00 26.11           C  
ATOM   2064  CG  ASN A 345      28.434 -33.789 -67.695  1.00 30.61           C  
ATOM   2065  OD1 ASN A 345      28.158 -34.949 -67.394  1.00 34.28           O  
ATOM   2066  ND2 ASN A 345      28.002 -33.219 -68.811  1.00 32.07           N  
ATOM   2067  N   ASN A 346      32.334 -31.322 -67.137  1.00 29.15           N  
ATOM   2068  CA  ASN A 346      33.202 -30.267 -66.632  1.00 30.86           C  
ATOM   2069  C   ASN A 346      32.652 -28.873 -66.906  1.00 28.57           C  
ATOM   2070  O   ASN A 346      31.900 -28.669 -67.860  1.00 27.36           O  
ATOM   2071  CB  ASN A 346      34.601 -30.388 -67.247  1.00 30.51           C  
ATOM   2072  CG  ASN A 346      35.297 -31.687 -66.877  1.00 38.21           C  
ATOM   2073  OD1 ASN A 346      35.147 -32.196 -65.767  1.00 36.99           O  
ATOM   2074  ND2 ASN A 346      36.070 -32.226 -67.812  1.00 42.66           N  
ATOM   2075  N   ASN A 347      33.032 -27.927 -66.053  1.00 23.47           N  
ATOM   2076  CA  ASN A 347      32.821 -26.503 -66.302  1.00 24.70           C  
ATOM   2077  C   ASN A 347      31.366 -26.102 -66.521  1.00 25.49           C  
ATOM   2078  O   ASN A 347      31.071 -25.217 -67.323  1.00 27.60           O  
ATOM   2079  CB  ASN A 347      33.662 -26.066 -67.502  1.00 28.00           C  
ATOM   2080  CG  ASN A 347      35.134 -26.378 -67.318  1.00 31.95           C  
ATOM   2081  OD1 ASN A 347      35.607 -26.532 -66.193  1.00 30.84           O  
ATOM   2082  ND2 ASN A 347      35.865 -26.477 -68.421  1.00 36.40           N  
ATOM   2083  N   ASN A 348      30.460 -26.751 -65.801  1.00 24.10           N  
ATOM   2084  CA  ASN A 348      29.052 -26.391 -65.859  1.00 26.76           C  
ATOM   2085  C   ASN A 348      28.301 -26.929 -64.652  1.00 26.38           C  
ATOM   2086  O   ASN A 348      28.838 -27.707 -63.863  1.00 21.41           O  
ATOM   2087  CB  ASN A 348      28.408 -26.903 -67.150  1.00 30.08           C  
ATOM   2088  CG  ASN A 348      27.280 -26.005 -67.632  1.00 41.91           C  
ATOM   2089  OD1 ASN A 348      26.773 -25.166 -66.882  1.00 41.25           O  
ATOM   2090  ND2 ASN A 348      26.889 -26.170 -68.893  1.00 46.16           N  
ATOM   2091  N   GLY A 349      27.054 -26.503 -64.514  1.00 26.52           N  
ATOM   2092  CA  GLY A 349      26.232 -26.905 -63.395  1.00 23.74           C  
ATOM   2093  C   GLY A 349      24.974 -26.065 -63.342  1.00 24.47           C  
ATOM   2094  O   GLY A 349      24.704 -25.274 -64.244  1.00 25.37           O  
ATOM   2095  N   VAL A 350      24.196 -26.251 -62.286  1.00 22.91           N  
ATOM   2096  CA  VAL A 350      23.007 -25.447 -62.060  1.00 20.98           C  
ATOM   2097  C   VAL A 350      22.786 -25.368 -60.558  1.00 21.55           C  
ATOM   2098  O   VAL A 350      23.126 -26.301 -59.826  1.00 23.90           O  
ATOM   2099  CB  VAL A 350      21.759 -26.034 -62.780  1.00 20.27           C  
ATOM   2100  CG1 VAL A 350      21.306 -27.331 -62.126  1.00 20.32           C  
ATOM   2101  CG2 VAL A 350      20.622 -25.028 -62.794  1.00 18.90           C  
ATOM   2102  N   LYS A 351      22.258 -24.243 -60.091  1.00 22.55           N  
ATOM   2103  CA  LYS A 351      21.926 -24.118 -58.681  1.00 21.43           C  
ATOM   2104  C   LYS A 351      20.831 -25.116 -58.345  1.00 20.92           C  
ATOM   2105  O   LYS A 351      19.841 -25.228 -59.069  1.00 21.81           O  
ATOM   2106  CB  LYS A 351      21.479 -22.701 -58.335  1.00 18.11           C  
ATOM   2107  CG  LYS A 351      21.094 -22.528 -56.877  1.00 20.93           C  
ATOM   2108  CD  LYS A 351      20.596 -21.119 -56.610  1.00 22.57           C  
ATOM   2109  CE  LYS A 351      20.013 -21.009 -55.215  1.00 22.80           C  
ATOM   2110  NZ  LYS A 351      21.032 -21.246 -54.141  1.00 20.74           N  
ATOM   2111  N   GLY A 352      21.024 -25.849 -57.255  1.00 21.81           N  
ATOM   2112  CA  GLY A 352      20.071 -26.855 -56.832  1.00 21.81           C  
ATOM   2113  C   GLY A 352      20.003 -26.941 -55.322  1.00 24.38           C  
ATOM   2114  O   GLY A 352      20.589 -26.121 -54.615  1.00 25.75           O  
ATOM   2115  N   PHE A 353      19.294 -27.944 -54.822  1.00 22.38           N  
ATOM   2116  CA  PHE A 353      19.099 -28.073 -53.387  1.00 21.37           C  
ATOM   2117  C   PHE A 353      18.797 -29.512 -52.999  1.00 23.12           C  
ATOM   2118  O   PHE A 353      18.526 -30.365 -53.849  1.00 21.46           O  
ATOM   2119  CB  PHE A 353      17.950 -27.174 -52.919  1.00 20.35           C  
ATOM   2120  CG  PHE A 353      16.601 -27.764 -53.185  1.00 23.15           C  
ATOM   2121  CD1 PHE A 353      16.042 -27.682 -54.446  1.00 25.48           C  
ATOM   2122  CD2 PHE A 353      15.913 -28.443 -52.192  1.00 23.28           C  
ATOM   2123  CE1 PHE A 353      14.808 -28.242 -54.706  1.00 24.20           C  
ATOM   2124  CE2 PHE A 353      14.686 -29.012 -52.449  1.00 20.59           C  
ATOM   2125  CZ  PHE A 353      14.137 -28.917 -53.708  1.00 22.20           C  
ATOM   2126  N   SER A 354      18.814 -29.760 -51.698  1.00 18.99           N  
ATOM   2127  CA  SER A 354      18.367 -31.030 -51.155  1.00 22.31           C  
ATOM   2128  C   SER A 354      17.939 -30.837 -49.709  1.00 24.61           C  
ATOM   2129  O   SER A 354      18.287 -29.840 -49.076  1.00 27.11           O  
ATOM   2130  CB  SER A 354      19.474 -32.079 -51.246  1.00 23.67           C  
ATOM   2131  OG  SER A 354      20.576 -31.710 -50.434  1.00 27.97           O  
ATOM   2132  N   TYR A 355      17.163 -31.783 -49.195  1.00 21.63           N  
ATOM   2133  CA  TYR A 355      16.908 -31.851 -47.765  1.00 21.60           C  
ATOM   2134  C   TYR A 355      17.484 -33.152 -47.232  1.00 23.98           C  
ATOM   2135  O   TYR A 355      16.988 -34.234 -47.535  1.00 24.11           O  
ATOM   2136  CB  TYR A 355      15.415 -31.736 -47.460  1.00 21.82           C  
ATOM   2137  CG  TYR A 355      14.910 -30.313 -47.531  1.00 20.81           C  
ATOM   2138  CD1 TYR A 355      14.970 -29.479 -46.422  1.00 19.31           C  
ATOM   2139  CD2 TYR A 355      14.382 -29.799 -48.708  1.00 19.99           C  
ATOM   2140  CE1 TYR A 355      14.514 -28.172 -46.481  1.00 18.25           C  
ATOM   2141  CE2 TYR A 355      13.924 -28.493 -48.779  1.00 21.31           C  
ATOM   2142  CZ  TYR A 355      13.995 -27.684 -47.661  1.00 19.13           C  
ATOM   2143  OH  TYR A 355      13.542 -26.383 -47.720  1.00 20.20           O  
ATOM   2144  N   LEU A 356      18.553 -33.032 -46.453  1.00 22.67           N  
ATOM   2145  CA  LEU A 356      19.295 -34.188 -45.967  1.00 22.95           C  
ATOM   2146  C   LEU A 356      18.904 -34.486 -44.527  1.00 26.52           C  
ATOM   2147  O   LEU A 356      19.296 -33.770 -43.605  1.00 27.04           O  
ATOM   2148  CB  LEU A 356      20.797 -33.933 -46.088  1.00 25.48           C  
ATOM   2149  CG  LEU A 356      21.217 -33.513 -47.500  1.00 25.33           C  
ATOM   2150  CD1 LEU A 356      22.676 -33.084 -47.542  1.00 27.79           C  
ATOM   2151  CD2 LEU A 356      20.962 -34.648 -48.495  1.00 25.51           C  
ATOM   2152  N   ASP A 357      18.123 -35.545 -44.343  1.00 24.02           N  
ATOM   2153  CA  ASP A 357      17.487 -35.805 -43.058  1.00 26.65           C  
ATOM   2154  C   ASP A 357      17.289 -37.299 -42.819  1.00 26.29           C  
ATOM   2155  O   ASP A 357      16.178 -37.752 -42.541  1.00 26.27           O  
ATOM   2156  CB  ASP A 357      16.141 -35.072 -42.989  1.00 28.09           C  
ATOM   2157  CG  ASP A 357      15.557 -35.043 -41.589  1.00 30.70           C  
ATOM   2158  OD1 ASP A 357      16.343 -34.999 -40.620  1.00 32.07           O  
ATOM   2159  OD2 ASP A 357      14.315 -35.073 -41.458  1.00 29.77           O  
ATOM   2160  N   GLY A 358      18.372 -38.063 -42.934  1.00 26.40           N  
ATOM   2161  CA  GLY A 358      18.315 -39.501 -42.743  1.00 25.36           C  
ATOM   2162  C   GLY A 358      17.347 -40.169 -43.704  1.00 25.74           C  
ATOM   2163  O   GLY A 358      17.472 -40.026 -44.917  1.00 25.43           O  
ATOM   2164  N   ALA A 359      16.375 -40.892 -43.157  1.00 25.90           N  
ATOM   2165  CA  ALA A 359      15.379 -41.583 -43.968  1.00 26.95           C  
ATOM   2166  C   ALA A 359      14.363 -40.607 -44.558  1.00 25.13           C  
ATOM   2167  O   ALA A 359      13.577 -40.968 -45.437  1.00 25.59           O  
ATOM   2168  CB  ALA A 359      14.671 -42.650 -43.139  1.00 27.54           C  
ATOM   2169  N   ASN A 360      14.386 -39.372 -44.072  1.00 22.63           N  
ATOM   2170  CA  ASN A 360      13.478 -38.335 -44.548  1.00 23.79           C  
ATOM   2171  C   ASN A 360      14.154 -37.459 -45.606  1.00 26.39           C  
ATOM   2172  O   ASN A 360      13.788 -36.302 -45.803  1.00 27.39           O  
ATOM   2173  CB  ASN A 360      12.992 -37.484 -43.368  1.00 23.42           C  
ATOM   2174  CG  ASN A 360      11.824 -36.580 -43.730  1.00 26.82           C  
ATOM   2175  OD1 ASN A 360      10.932 -36.965 -44.494  1.00 24.13           O  
ATOM   2176  ND2 ASN A 360      11.829 -35.365 -43.184  1.00 26.06           N  
ATOM   2177  N   THR A 361      15.138 -38.026 -46.295  1.00 22.65           N  
ATOM   2178  CA  THR A 361      15.931 -37.270 -47.257  1.00 22.30           C  
ATOM   2179  C   THR A 361      15.269 -37.186 -48.633  1.00 23.89           C  
ATOM   2180  O   THR A 361      14.871 -38.202 -49.204  1.00 23.76           O  
ATOM   2181  CB  THR A 361      17.335 -37.884 -47.417  1.00 23.20           C  
ATOM   2182  OG1 THR A 361      18.069 -37.718 -46.199  1.00 23.60           O  
ATOM   2183  CG2 THR A 361      18.092 -37.210 -48.551  1.00 21.11           C  
ATOM   2184  N   TRP A 362      15.151 -35.967 -49.157  1.00 23.73           N  
ATOM   2185  CA  TRP A 362      14.640 -35.748 -50.510  1.00 19.84           C  
ATOM   2186  C   TRP A 362      15.619 -34.923 -51.340  1.00 23.51           C  
ATOM   2187  O   TRP A 362      16.121 -33.894 -50.881  1.00 21.79           O  
ATOM   2188  CB  TRP A 362      13.278 -35.052 -50.473  1.00 20.06           C  
ATOM   2189  CG  TRP A 362      12.144 -35.936 -50.066  1.00 20.34           C  
ATOM   2190  CD1 TRP A 362      11.853 -36.374 -48.804  1.00 21.42           C  
ATOM   2191  CD2 TRP A 362      11.134 -36.480 -50.922  1.00 21.17           C  
ATOM   2192  NE1 TRP A 362      10.730 -37.166 -48.827  1.00 21.15           N  
ATOM   2193  CE2 TRP A 362      10.267 -37.242 -50.114  1.00 21.95           C  
ATOM   2194  CE3 TRP A 362      10.877 -36.395 -52.295  1.00 24.97           C  
ATOM   2195  CZ2 TRP A 362       9.164 -37.917 -50.632  1.00 23.18           C  
ATOM   2196  CZ3 TRP A 362       9.782 -37.068 -52.808  1.00 24.27           C  
ATOM   2197  CH2 TRP A 362       8.939 -37.818 -51.978  1.00 23.08           C  
ATOM   2198  N   LEU A 363      15.885 -35.379 -52.560  1.00 22.74           N  
ATOM   2199  CA  LEU A 363      16.770 -34.662 -53.471  1.00 21.85           C  
ATOM   2200  C   LEU A 363      15.974 -34.077 -54.629  1.00 21.94           C  
ATOM   2201  O   LEU A 363      15.051 -34.709 -55.138  1.00 21.96           O  
ATOM   2202  CB  LEU A 363      17.868 -35.579 -54.019  1.00 21.91           C  
ATOM   2203  CG  LEU A 363      18.663 -36.465 -53.058  1.00 23.54           C  
ATOM   2204  CD1 LEU A 363      19.712 -37.246 -53.831  1.00 21.52           C  
ATOM   2205  CD2 LEU A 363      19.311 -35.644 -51.951  1.00 22.17           C  
ATOM   2206  N   GLY A 364      16.338 -32.870 -55.046  1.00 21.58           N  
ATOM   2207  CA  GLY A 364      15.759 -32.279 -56.237  1.00 23.05           C  
ATOM   2208  C   GLY A 364      16.740 -32.327 -57.393  1.00 25.48           C  
ATOM   2209  O   GLY A 364      17.952 -32.241 -57.189  1.00 24.20           O  
ATOM   2210  N   ARG A 365      16.224 -32.486 -58.606  1.00 20.78           N  
ATOM   2211  CA  ARG A 365      17.066 -32.404 -59.791  1.00 21.01           C  
ATOM   2212  C   ARG A 365      16.246 -32.193 -61.050  1.00 20.44           C  
ATOM   2213  O   ARG A 365      15.046 -32.475 -61.078  1.00 20.80           O  
ATOM   2214  CB  ARG A 365      17.926 -33.666 -59.945  1.00 19.65           C  
ATOM   2215  CG  ARG A 365      17.171 -34.947 -60.294  1.00 18.92           C  
ATOM   2216  CD  ARG A 365      18.169 -36.091 -60.486  1.00 19.63           C  
ATOM   2217  NE  ARG A 365      17.553 -37.377 -60.808  1.00 21.47           N  
ATOM   2218  CZ  ARG A 365      18.240 -38.498 -61.015  1.00 23.23           C  
ATOM   2219  NH1 ARG A 365      19.563 -38.493 -60.929  1.00 21.64           N  
ATOM   2220  NH2 ARG A 365      17.607 -39.627 -61.300  1.00 23.61           N  
ATOM   2221  N   THR A 366      16.902 -31.686 -62.087  1.00 18.74           N  
ATOM   2222  CA  THR A 366      16.301 -31.629 -63.409  1.00 21.15           C  
ATOM   2223  C   THR A 366      16.086 -33.056 -63.898  1.00 22.81           C  
ATOM   2224  O   THR A 366      16.819 -33.967 -63.509  1.00 24.12           O  
ATOM   2225  CB  THR A 366      17.186 -30.868 -64.416  1.00 22.00           C  
ATOM   2226  OG1 THR A 366      18.404 -31.595 -64.628  1.00 27.19           O  
ATOM   2227  CG2 THR A 366      17.518 -29.477 -63.899  1.00 20.19           C  
ATOM   2228  N   ILE A 367      15.086 -33.262 -64.746  1.00 21.64           N  
ATOM   2229  CA  ILE A 367      14.834 -34.600 -65.267  1.00 21.74           C  
ATOM   2230  C   ILE A 367      15.865 -34.940 -66.344  1.00 25.74           C  
ATOM   2231  O   ILE A 367      16.430 -36.035 -66.354  1.00 27.23           O  
ATOM   2232  CB  ILE A 367      13.404 -34.728 -65.822  1.00 24.23           C  
ATOM   2233  CG1 ILE A 367      12.395 -34.618 -64.676  1.00 27.07           C  
ATOM   2234  CG2 ILE A 367      13.227 -36.054 -66.549  1.00 22.11           C  
ATOM   2235  CD1 ILE A 367      10.952 -34.663 -65.124  1.00 29.41           C  
ATOM   2236  N   SER A 368      16.125 -33.988 -67.234  1.00 24.86           N  
ATOM   2237  CA  SER A 368      17.136 -34.167 -68.268  1.00 27.62           C  
ATOM   2238  C   SER A 368      18.543 -34.161 -67.678  1.00 30.00           C  
ATOM   2239  O   SER A 368      18.831 -33.405 -66.746  1.00 27.74           O  
ATOM   2240  CB  SER A 368      17.013 -33.073 -69.329  1.00 29.68           C  
ATOM   2241  OG  SER A 368      18.150 -33.056 -70.175  1.00 30.48           O  
ATOM   2242  N   THR A 369      19.416 -35.003 -68.225  1.00 28.26           N  
ATOM   2243  CA  THR A 369      20.817 -35.026 -67.814  1.00 27.54           C  
ATOM   2244  C   THR A 369      21.644 -34.063 -68.657  1.00 27.24           C  
ATOM   2245  O   THR A 369      22.819 -33.830 -68.374  1.00 25.94           O  
ATOM   2246  CB  THR A 369      21.429 -36.436 -67.935  1.00 25.77           C  
ATOM   2247  OG1 THR A 369      21.335 -36.882 -69.294  1.00 26.48           O  
ATOM   2248  CG2 THR A 369      20.700 -37.423 -67.030  1.00 24.40           C  
ATOM   2249  N   ALA A 370      21.025 -33.507 -69.693  1.00 25.17           N  
ATOM   2250  CA  ALA A 370      21.752 -32.703 -70.671  1.00 24.75           C  
ATOM   2251  C   ALA A 370      21.470 -31.209 -70.542  1.00 25.94           C  
ATOM   2252  O   ALA A 370      22.344 -30.382 -70.809  1.00 30.48           O  
ATOM   2253  CB  ALA A 370      21.421 -33.178 -72.081  1.00 28.36           C  
ATOM   2254  N   SER A 371      20.255 -30.860 -70.134  1.00 26.96           N  
ATOM   2255  CA  SER A 371      19.867 -29.455 -70.075  1.00 25.98           C  
ATOM   2256  C   SER A 371      18.891 -29.150 -68.943  1.00 23.03           C  
ATOM   2257  O   SER A 371      18.371 -30.054 -68.287  1.00 24.55           O  
ATOM   2258  CB  SER A 371      19.255 -29.025 -71.409  1.00 32.23           C  
ATOM   2259  OG  SER A 371      18.064 -29.746 -71.671  1.00 37.12           O  
ATOM   2260  N   ARG A 372      18.649 -27.861 -68.727  1.00 24.12           N  
ATOM   2261  CA  ARG A 372      17.778 -27.405 -67.652  1.00 23.73           C  
ATOM   2262  C   ARG A 372      16.308 -27.535 -68.030  1.00 24.34           C  
ATOM   2263  O   ARG A 372      15.616 -26.537 -68.226  1.00 24.93           O  
ATOM   2264  CB  ARG A 372      18.107 -25.958 -67.287  1.00 20.58           C  
ATOM   2265  CG  ARG A 372      19.521 -25.787 -66.758  1.00 24.03           C  
ATOM   2266  CD  ARG A 372      19.918 -24.324 -66.651  1.00 23.78           C  
ATOM   2267  NE  ARG A 372      21.264 -24.189 -66.098  1.00 24.61           N  
ATOM   2268  CZ  ARG A 372      21.878 -23.032 -65.878  1.00 25.47           C  
ATOM   2269  NH1 ARG A 372      21.269 -21.890 -66.160  1.00 26.71           N  
ATOM   2270  NH2 ARG A 372      23.100 -23.022 -65.365  1.00 24.26           N  
ATOM   2271  N   SER A 373      15.840 -28.774 -68.137  1.00 25.64           N  
ATOM   2272  CA  SER A 373      14.443 -29.039 -68.443  1.00 26.16           C  
ATOM   2273  C   SER A 373      13.899 -30.111 -67.509  1.00 25.75           C  
ATOM   2274  O   SER A 373      14.599 -31.065 -67.165  1.00 24.98           O  
ATOM   2275  CB  SER A 373      14.273 -29.465 -69.904  1.00 28.53           C  
ATOM   2276  OG  SER A 373      14.899 -30.713 -70.151  1.00 32.90           O  
ATOM   2277  N   GLY A 374      12.650 -29.937 -67.092  1.00 25.31           N  
ATOM   2278  CA  GLY A 374      12.021 -30.846 -66.154  1.00 22.66           C  
ATOM   2279  C   GLY A 374      12.523 -30.637 -64.738  1.00 22.81           C  
ATOM   2280  O   GLY A 374      13.587 -30.053 -64.520  1.00 21.19           O  
ATOM   2281  N   TYR A 375      11.749 -31.104 -63.765  1.00 22.58           N  
ATOM   2282  CA  TYR A 375      12.211 -31.112 -62.384  1.00 19.76           C  
ATOM   2283  C   TYR A 375      11.473 -32.172 -61.586  1.00 21.79           C  
ATOM   2284  O   TYR A 375      10.256 -32.304 -61.692  1.00 23.14           O  
ATOM   2285  CB  TYR A 375      12.030 -29.745 -61.726  1.00 20.39           C  
ATOM   2286  CG  TYR A 375      13.005 -29.528 -60.594  1.00 19.20           C  
ATOM   2287  CD1 TYR A 375      14.265 -28.997 -60.837  1.00 19.72           C  
ATOM   2288  CD2 TYR A 375      12.686 -29.893 -59.292  1.00 20.14           C  
ATOM   2289  CE1 TYR A 375      15.172 -28.812 -59.813  1.00 21.73           C  
ATOM   2290  CE2 TYR A 375      13.587 -29.707 -58.257  1.00 23.34           C  
ATOM   2291  CZ  TYR A 375      14.828 -29.163 -58.524  1.00 23.47           C  
ATOM   2292  OH  TYR A 375      15.736 -28.978 -57.507  1.00 25.04           O  
ATOM   2293  N   GLU A 376      12.218 -32.924 -60.786  1.00 22.75           N  
ATOM   2294  CA  GLU A 376      11.629 -33.973 -59.970  1.00 20.74           C  
ATOM   2295  C   GLU A 376      12.227 -33.980 -58.571  1.00 21.62           C  
ATOM   2296  O   GLU A 376      13.379 -33.584 -58.375  1.00 22.63           O  
ATOM   2297  CB  GLU A 376      11.827 -35.341 -60.628  1.00 22.75           C  
ATOM   2298  CG  GLU A 376      13.281 -35.760 -60.754  1.00 23.37           C  
ATOM   2299  CD  GLU A 376      13.445 -37.082 -61.480  1.00 28.13           C  
ATOM   2300  OE1 GLU A 376      12.415 -37.714 -61.798  1.00 27.51           O  
ATOM   2301  OE2 GLU A 376      14.600 -37.488 -61.732  1.00 28.14           O  
ATOM   2302  N   MET A 377      11.427 -34.413 -57.603  1.00 21.91           N  
ATOM   2303  CA  MET A 377      11.916 -34.676 -56.257  1.00 22.94           C  
ATOM   2304  C   MET A 377      12.039 -36.179 -56.087  1.00 23.27           C  
ATOM   2305  O   MET A 377      11.169 -36.923 -56.530  1.00 23.64           O  
ATOM   2306  CB  MET A 377      10.981 -34.092 -55.197  1.00 20.49           C  
ATOM   2307  CG  MET A 377      10.821 -32.584 -55.270  1.00 19.64           C  
ATOM   2308  SD  MET A 377      12.388 -31.729 -55.020  1.00 26.19           S  
ATOM   2309  CE  MET A 377      12.808 -32.254 -53.356  1.00 24.76           C  
ATOM   2310  N   LEU A 378      13.121 -36.625 -55.461  1.00 21.43           N  
ATOM   2311  CA  LEU A 378      13.339 -38.047 -55.243  1.00 22.05           C  
ATOM   2312  C   LEU A 378      13.655 -38.313 -53.783  1.00 21.57           C  
ATOM   2313  O   LEU A 378      14.520 -37.659 -53.199  1.00 22.67           O  
ATOM   2314  CB  LEU A 378      14.474 -38.566 -56.133  1.00 22.79           C  
ATOM   2315  CG  LEU A 378      14.230 -38.487 -57.642  1.00 24.60           C  
ATOM   2316  CD1 LEU A 378      15.508 -38.797 -58.419  1.00 22.34           C  
ATOM   2317  CD2 LEU A 378      13.111 -39.440 -58.050  1.00 25.44           C  
ATOM   2318  N   LYS A 379      12.945 -39.270 -53.193  1.00 20.66           N  
ATOM   2319  CA  LYS A 379      13.203 -39.660 -51.812  1.00 21.17           C  
ATOM   2320  C   LYS A 379      14.331 -40.681 -51.770  1.00 22.52           C  
ATOM   2321  O   LYS A 379      14.171 -41.816 -52.214  1.00 21.35           O  
ATOM   2322  CB  LYS A 379      11.943 -40.225 -51.157  1.00 21.22           C  
ATOM   2323  CG  LYS A 379      12.099 -40.496 -49.674  1.00 21.98           C  
ATOM   2324  CD  LYS A 379      10.832 -41.092 -49.078  1.00 22.05           C  
ATOM   2325  CE  LYS A 379      11.015 -41.382 -47.597  1.00 26.01           C  
ATOM   2326  NZ  LYS A 379       9.819 -42.066 -47.025  1.00 30.11           N  
ATOM   2327  N   VAL A 380      15.478 -40.260 -51.250  1.00 21.13           N  
ATOM   2328  CA  VAL A 380      16.675 -41.090 -51.246  1.00 21.38           C  
ATOM   2329  C   VAL A 380      17.227 -41.199 -49.833  1.00 24.86           C  
ATOM   2330  O   VAL A 380      17.988 -40.337 -49.400  1.00 23.88           O  
ATOM   2331  CB  VAL A 380      17.772 -40.517 -52.178  1.00 19.38           C  
ATOM   2332  CG1 VAL A 380      18.939 -41.488 -52.291  1.00 19.91           C  
ATOM   2333  CG2 VAL A 380      17.203 -40.199 -53.562  1.00 21.65           C  
ATOM   2334  N   PRO A 381      16.837 -42.257 -49.107  1.00 24.06           N  
ATOM   2335  CA  PRO A 381      17.256 -42.461 -47.713  1.00 25.43           C  
ATOM   2336  C   PRO A 381      18.770 -42.383 -47.509  1.00 26.02           C  
ATOM   2337  O   PRO A 381      19.525 -43.102 -48.170  1.00 24.72           O  
ATOM   2338  CB  PRO A 381      16.740 -43.869 -47.397  1.00 26.82           C  
ATOM   2339  CG  PRO A 381      15.587 -44.060 -48.320  1.00 25.61           C  
ATOM   2340  CD  PRO A 381      15.953 -43.335 -49.583  1.00 22.78           C  
ATOM   2341  N   ASN A 382      19.189 -41.500 -46.604  1.00 20.19           N  
ATOM   2342  CA  ASN A 382      20.593 -41.333 -46.247  1.00 22.15           C  
ATOM   2343  C   ASN A 382      21.479 -41.009 -47.445  1.00 21.45           C  
ATOM   2344  O   ASN A 382      22.619 -41.471 -47.522  1.00 21.92           O  
ATOM   2345  CB  ASN A 382      21.111 -42.591 -45.547  1.00 28.38           C  
ATOM   2346  CG  ASN A 382      20.265 -42.980 -44.351  1.00 37.85           C  
ATOM   2347  OD1 ASN A 382      20.296 -42.320 -43.315  1.00 42.40           O  
ATOM   2348  ND2 ASN A 382      19.496 -44.052 -44.492  1.00 42.29           N  
ATOM   2349  N   ALA A 383      20.951 -40.206 -48.366  1.00 24.91           N  
ATOM   2350  CA  ALA A 383      21.677 -39.825 -49.577  1.00 25.66           C  
ATOM   2351  C   ALA A 383      23.034 -39.206 -49.254  1.00 27.50           C  
ATOM   2352  O   ALA A 383      24.013 -39.429 -49.963  1.00 25.72           O  
ATOM   2353  CB  ALA A 383      20.844 -38.860 -50.410  1.00 27.12           C  
ATOM   2354  N   LEU A 384      23.084 -38.438 -48.170  1.00 24.84           N  
ATOM   2355  CA  LEU A 384      24.298 -37.735 -47.775  1.00 24.85           C  
ATOM   2356  C   LEU A 384      25.459 -38.679 -47.452  1.00 26.79           C  
ATOM   2357  O   LEU A 384      26.608 -38.381 -47.770  1.00 26.85           O  
ATOM   2358  CB  LEU A 384      24.017 -36.838 -46.566  1.00 23.36           C  
ATOM   2359  CG  LEU A 384      25.224 -36.085 -45.999  1.00 25.44           C  
ATOM   2360  CD1 LEU A 384      25.834 -35.175 -47.060  1.00 23.59           C  
ATOM   2361  CD2 LEU A 384      24.838 -35.286 -44.765  1.00 24.04           C  
ATOM   2362  N   THR A 385      25.160 -39.817 -46.830  1.00 25.06           N  
ATOM   2363  CA  THR A 385      26.212 -40.676 -46.287  1.00 28.61           C  
ATOM   2364  C   THR A 385      26.327 -42.061 -46.931  1.00 26.78           C  
ATOM   2365  O   THR A 385      27.331 -42.748 -46.745  1.00 27.21           O  
ATOM   2366  CB  THR A 385      26.018 -40.876 -44.770  1.00 29.65           C  
ATOM   2367  OG1 THR A 385      24.734 -41.462 -44.527  1.00 30.42           O  
ATOM   2368  CG2 THR A 385      26.106 -39.540 -44.042  1.00 31.38           C  
ATOM   2369  N   ASP A 386      25.309 -42.469 -47.681  1.00 25.93           N  
ATOM   2370  CA  ASP A 386      25.268 -43.813 -48.263  1.00 26.62           C  
ATOM   2371  C   ASP A 386      25.567 -43.750 -49.763  1.00 28.43           C  
ATOM   2372  O   ASP A 386      24.740 -43.283 -50.543  1.00 29.04           O  
ATOM   2373  CB  ASP A 386      23.897 -44.455 -48.002  1.00 25.20           C  
ATOM   2374  CG  ASP A 386      23.776 -45.868 -48.561  1.00 30.76           C  
ATOM   2375  OD1 ASP A 386      24.764 -46.406 -49.107  1.00 30.36           O  
ATOM   2376  OD2 ASP A 386      22.675 -46.448 -48.448  1.00 34.76           O  
ATOM   2377  N   ASP A 387      26.744 -44.227 -50.167  1.00 26.07           N  
ATOM   2378  CA  ASP A 387      27.155 -44.108 -51.566  1.00 26.90           C  
ATOM   2379  C   ASP A 387      26.526 -45.169 -52.472  1.00 26.25           C  
ATOM   2380  O   ASP A 387      26.906 -45.300 -53.636  1.00 27.85           O  
ATOM   2381  CB  ASP A 387      28.689 -44.142 -51.690  1.00 26.56           C  
ATOM   2382  CG  ASP A 387      29.304 -45.484 -51.296  1.00 32.56           C  
ATOM   2383  OD1 ASP A 387      28.568 -46.458 -51.027  1.00 32.75           O  
ATOM   2384  OD2 ASP A 387      30.553 -45.564 -51.266  1.00 31.69           O  
ATOM   2385  N   ARG A 388      25.563 -45.916 -51.938  1.00 26.59           N  
ATOM   2386  CA  ARG A 388      24.820 -46.894 -52.731  1.00 28.09           C  
ATOM   2387  C   ARG A 388      23.334 -46.541 -52.819  1.00 29.18           C  
ATOM   2388  O   ARG A 388      22.561 -47.242 -53.472  1.00 27.43           O  
ATOM   2389  CB  ARG A 388      24.968 -48.301 -52.141  1.00 29.58           C  
ATOM   2390  CG  ARG A 388      26.390 -48.730 -51.824  1.00 31.70           C  
ATOM   2391  CD  ARG A 388      27.235 -48.865 -53.077  1.00 34.18           C  
ATOM   2392  NE  ARG A 388      28.641 -49.094 -52.749  1.00 36.07           N  
ATOM   2393  CZ  ARG A 388      29.217 -50.292 -52.729  1.00 35.35           C  
ATOM   2394  NH1 ARG A 388      28.510 -51.375 -53.026  1.00 34.31           N  
ATOM   2395  NH2 ARG A 388      30.502 -50.405 -52.415  1.00 35.01           N  
ATOM   2396  N   SER A 389      22.939 -45.455 -52.161  1.00 24.94           N  
ATOM   2397  CA  SER A 389      21.522 -45.144 -51.978  1.00 24.65           C  
ATOM   2398  C   SER A 389      20.782 -44.804 -53.275  1.00 25.43           C  
ATOM   2399  O   SER A 389      21.296 -44.089 -54.137  1.00 26.99           O  
ATOM   2400  CB  SER A 389      21.366 -43.998 -50.978  1.00 26.53           C  
ATOM   2401  OG  SER A 389      22.160 -42.888 -51.346  1.00 27.13           O  
ATOM   2402  N   LYS A 390      19.565 -45.330 -53.388  1.00 23.41           N  
ATOM   2403  CA  LYS A 390      18.712 -45.138 -54.559  1.00 25.81           C  
ATOM   2404  C   LYS A 390      17.333 -44.624 -54.128  1.00 24.92           C  
ATOM   2405  O   LYS A 390      16.989 -44.701 -52.949  1.00 26.19           O  
ATOM   2406  CB  LYS A 390      18.586 -46.453 -55.339  1.00 26.55           C  
ATOM   2407  CG  LYS A 390      19.876 -46.912 -56.014  1.00 30.24           C  
ATOM   2408  CD  LYS A 390      20.331 -45.916 -57.067  1.00 32.39           C  
ATOM   2409  CE  LYS A 390      21.557 -46.420 -57.815  1.00 37.68           C  
ATOM   2410  NZ  LYS A 390      21.275 -47.701 -58.518  1.00 39.44           N  
ATOM   2411  N   PRO A 391      16.541 -44.089 -55.075  1.00 25.00           N  
ATOM   2412  CA  PRO A 391      15.215 -43.582 -54.696  1.00 24.46           C  
ATOM   2413  C   PRO A 391      14.220 -44.684 -54.320  1.00 28.86           C  
ATOM   2414  O   PRO A 391      14.279 -45.787 -54.871  1.00 30.04           O  
ATOM   2415  CB  PRO A 391      14.742 -42.844 -55.958  1.00 27.31           C  
ATOM   2416  CG  PRO A 391      15.966 -42.644 -56.793  1.00 26.98           C  
ATOM   2417  CD  PRO A 391      16.855 -43.798 -56.484  1.00 26.25           C  
ATOM   2418  N   ILE A 392      13.320 -44.376 -53.388  1.00 24.73           N  
ATOM   2419  CA  ILE A 392      12.233 -45.287 -53.035  1.00 25.43           C  
ATOM   2420  C   ILE A 392      10.886 -44.602 -53.239  1.00 26.60           C  
ATOM   2421  O   ILE A 392       9.829 -45.215 -53.087  1.00 27.28           O  
ATOM   2422  CB  ILE A 392      12.337 -45.780 -51.579  1.00 25.20           C  
ATOM   2423  CG1 ILE A 392      12.255 -44.599 -50.611  1.00 24.50           C  
ATOM   2424  CG2 ILE A 392      13.619 -46.585 -51.376  1.00 27.31           C  
ATOM   2425  CD1 ILE A 392      12.157 -45.012 -49.163  1.00 26.38           C  
ATOM   2426  N   GLN A 393      10.939 -43.321 -53.583  1.00 26.81           N  
ATOM   2427  CA  GLN A 393       9.737 -42.539 -53.847  1.00 26.90           C  
ATOM   2428  C   GLN A 393      10.125 -41.280 -54.604  1.00 26.33           C  
ATOM   2429  O   GLN A 393      11.278 -40.855 -54.561  1.00 27.62           O  
ATOM   2430  CB  GLN A 393       9.012 -42.180 -52.546  1.00 27.85           C  
ATOM   2431  CG  GLN A 393       7.570 -41.724 -52.734  1.00 26.29           C  
ATOM   2432  CD  GLN A 393       6.947 -41.207 -51.454  1.00 25.57           C  
ATOM   2433  OE1 GLN A 393       7.281 -41.659 -50.358  1.00 28.07           O  
ATOM   2434  NE2 GLN A 393       6.029 -40.254 -51.587  1.00 24.02           N  
ATOM   2435  N   GLY A 394       9.167 -40.685 -55.302  1.00 28.22           N  
ATOM   2436  CA  GLY A 394       9.439 -39.472 -56.045  1.00 26.24           C  
ATOM   2437  C   GLY A 394       8.206 -38.644 -56.341  1.00 28.07           C  
ATOM   2438  O   GLY A 394       7.079 -39.062 -56.081  1.00 26.22           O  
ATOM   2439  N   GLN A 395       8.430 -37.455 -56.886  1.00 25.91           N  
ATOM   2440  CA  GLN A 395       7.342 -36.611 -57.357  1.00 25.34           C  
ATOM   2441  C   GLN A 395       7.838 -35.700 -58.466  1.00 25.94           C  
ATOM   2442  O   GLN A 395       8.808 -34.961 -58.289  1.00 26.26           O  
ATOM   2443  CB  GLN A 395       6.746 -35.776 -56.220  1.00 23.85           C  
ATOM   2444  CG  GLN A 395       5.524 -34.972 -56.648  1.00 23.18           C  
ATOM   2445  CD  GLN A 395       4.802 -34.323 -55.482  1.00 24.26           C  
ATOM   2446  OE1 GLN A 395       4.819 -34.837 -54.362  1.00 26.10           O  
ATOM   2447  NE2 GLN A 395       4.163 -33.186 -55.741  1.00 21.35           N  
ATOM   2448  N   THR A 396       7.174 -35.766 -59.614  1.00 23.13           N  
ATOM   2449  CA  THR A 396       7.500 -34.893 -60.730  1.00 25.84           C  
ATOM   2450  C   THR A 396       6.911 -33.515 -60.472  1.00 25.37           C  
ATOM   2451  O   THR A 396       5.737 -33.393 -60.128  1.00 24.73           O  
ATOM   2452  CB  THR A 396       6.966 -35.452 -62.061  1.00 29.48           C  
ATOM   2453  OG1 THR A 396       7.665 -36.661 -62.381  1.00 30.91           O  
ATOM   2454  CG2 THR A 396       7.165 -34.445 -63.190  1.00 30.84           C  
ATOM   2455  N   ILE A 397       7.733 -32.483 -60.629  1.00 20.03           N  
ATOM   2456  CA  ILE A 397       7.297 -31.110 -60.405  1.00 20.73           C  
ATOM   2457  C   ILE A 397       7.077 -30.399 -61.731  1.00 21.26           C  
ATOM   2458  O   ILE A 397       6.072 -29.718 -61.929  1.00 22.65           O  
ATOM   2459  CB  ILE A 397       8.324 -30.317 -59.575  1.00 20.48           C  
ATOM   2460  CG1 ILE A 397       8.726 -31.104 -58.327  1.00 21.38           C  
ATOM   2461  CG2 ILE A 397       7.767 -28.950 -59.197  1.00 21.75           C  
ATOM   2462  CD1 ILE A 397       7.577 -31.368 -57.376  1.00 23.78           C  
ATOM   2463  N   VAL A 398       8.038 -30.559 -62.635  1.00 19.15           N  
ATOM   2464  CA  VAL A 398       7.960 -29.979 -63.968  1.00 21.42           C  
ATOM   2465  C   VAL A 398       8.267 -31.059 -65.000  1.00 22.81           C  
ATOM   2466  O   VAL A 398       9.243 -31.794 -64.852  1.00 21.84           O  
ATOM   2467  CB  VAL A 398       8.944 -28.799 -64.131  1.00 23.64           C  
ATOM   2468  CG1 VAL A 398       8.836 -28.199 -65.524  1.00 23.40           C  
ATOM   2469  CG2 VAL A 398       8.694 -27.737 -63.061  1.00 22.29           C  
ATOM   2470  N   LEU A 399       7.428 -31.166 -66.027  1.00 22.86           N  
ATOM   2471  CA  LEU A 399       7.645 -32.147 -67.086  1.00 23.61           C  
ATOM   2472  C   LEU A 399       8.970 -31.893 -67.797  1.00 26.68           C  
ATOM   2473  O   LEU A 399       9.409 -30.750 -67.915  1.00 25.45           O  
ATOM   2474  CB  LEU A 399       6.503 -32.116 -68.107  1.00 25.65           C  
ATOM   2475  CG  LEU A 399       5.089 -32.455 -67.632  1.00 26.46           C  
ATOM   2476  CD1 LEU A 399       4.118 -32.413 -68.800  1.00 26.62           C  
ATOM   2477  CD2 LEU A 399       5.049 -33.816 -66.960  1.00 26.23           C  
ATOM   2478  N   ASN A 400       9.593 -32.961 -68.289  1.00 26.79           N  
ATOM   2479  CA  ASN A 400      10.832 -32.844 -69.053  1.00 27.94           C  
ATOM   2480  C   ASN A 400      10.645 -31.980 -70.295  1.00 28.06           C  
ATOM   2481  O   ASN A 400      11.595 -31.387 -70.803  1.00 29.99           O  
ATOM   2482  CB  ASN A 400      11.345 -34.229 -69.452  1.00 31.70           C  
ATOM   2483  CG  ASN A 400      12.793 -34.207 -69.901  1.00 36.09           C  
ATOM   2484  OD1 ASN A 400      13.578 -33.372 -69.456  1.00 33.36           O  
ATOM   2485  ND2 ASN A 400      13.153 -35.129 -70.786  1.00 42.09           N  
ATOM   2486  N   ALA A 401       9.406 -31.904 -70.771  1.00 30.02           N  
ATOM   2487  CA  ALA A 401       9.073 -31.111 -71.947  1.00 30.73           C  
ATOM   2488  C   ALA A 401       9.109 -29.612 -71.665  1.00 29.98           C  
ATOM   2489  O   ALA A 401       9.120 -28.802 -72.591  1.00 30.88           O  
ATOM   2490  CB  ALA A 401       7.705 -31.508 -72.469  1.00 29.60           C  
ATOM   2491  N   ASP A 402       9.118 -29.244 -70.388  1.00 25.33           N  
ATOM   2492  CA  ASP A 402       9.098 -27.837 -70.001  1.00 24.81           C  
ATOM   2493  C   ASP A 402      10.426 -27.392 -69.402  1.00 25.41           C  
ATOM   2494  O   ASP A 402      11.127 -28.180 -68.767  1.00 26.34           O  
ATOM   2495  CB  ASP A 402       7.967 -27.576 -69.007  1.00 28.22           C  
ATOM   2496  CG  ASP A 402       6.599 -27.750 -69.629  1.00 35.29           C  
ATOM   2497  OD1 ASP A 402       6.336 -27.121 -70.677  1.00 39.34           O  
ATOM   2498  OD2 ASP A 402       5.788 -28.520 -69.074  1.00 33.41           O  
ATOM   2499  N   TRP A 403      10.760 -26.122 -69.604  1.00 24.93           N  
ATOM   2500  CA  TRP A 403      12.022 -25.580 -69.119  1.00 25.34           C  
ATOM   2501  C   TRP A 403      11.990 -25.323 -67.621  1.00 25.97           C  
ATOM   2502  O   TRP A 403      11.005 -24.811 -67.086  1.00 25.32           O  
ATOM   2503  CB  TRP A 403      12.372 -24.284 -69.855  1.00 26.56           C  
ATOM   2504  CG  TRP A 403      12.481 -24.457 -71.332  1.00 29.51           C  
ATOM   2505  CD1 TRP A 403      11.696 -23.880 -72.288  1.00 33.45           C  
ATOM   2506  CD2 TRP A 403      13.422 -25.280 -72.027  1.00 30.07           C  
ATOM   2507  NE1 TRP A 403      12.097 -24.288 -73.537  1.00 33.46           N  
ATOM   2508  CE2 TRP A 403      13.154 -25.148 -73.404  1.00 33.78           C  
ATOM   2509  CE3 TRP A 403      14.468 -26.112 -71.620  1.00 31.56           C  
ATOM   2510  CZ2 TRP A 403      13.893 -25.819 -74.375  1.00 33.35           C  
ATOM   2511  CZ3 TRP A 403      15.200 -26.776 -72.583  1.00 33.54           C  
ATOM   2512  CH2 TRP A 403      14.909 -26.627 -73.946  1.00 34.04           C  
ATOM   2513  N   SER A 404      13.076 -25.691 -66.951  1.00 26.20           N  
ATOM   2514  CA  SER A 404      13.248 -25.365 -65.546  1.00 22.67           C  
ATOM   2515  C   SER A 404      14.387 -24.362 -65.401  1.00 23.16           C  
ATOM   2516  O   SER A 404      14.500 -23.425 -66.193  1.00 24.22           O  
ATOM   2517  CB  SER A 404      13.513 -26.626 -64.714  1.00 25.35           C  
ATOM   2518  OG  SER A 404      14.589 -27.381 -65.237  1.00 24.45           O  
ATOM   2519  N   GLY A 405      15.227 -24.553 -64.390  1.00 23.57           N  
ATOM   2520  CA  GLY A 405      16.322 -23.637 -64.127  1.00 18.32           C  
ATOM   2521  C   GLY A 405      16.854 -23.795 -62.716  1.00 20.33           C  
ATOM   2522  O   GLY A 405      16.911 -24.910 -62.195  1.00 23.95           O  
ATOM   2523  N   TYR A 406      17.253 -22.687 -62.098  1.00 20.54           N  
ATOM   2524  CA  TYR A 406      17.742 -22.726 -60.722  1.00 21.02           C  
ATOM   2525  C   TYR A 406      16.657 -23.217 -59.764  1.00 24.53           C  
ATOM   2526  O   TYR A 406      15.467 -22.999 -59.987  1.00 23.31           O  
ATOM   2527  CB  TYR A 406      18.233 -21.350 -60.269  1.00 20.20           C  
ATOM   2528  CG  TYR A 406      19.611 -20.960 -60.756  1.00 21.63           C  
ATOM   2529  CD1 TYR A 406      20.268 -21.698 -61.732  1.00 20.76           C  
ATOM   2530  CD2 TYR A 406      20.263 -19.854 -60.223  1.00 21.00           C  
ATOM   2531  CE1 TYR A 406      21.536 -21.338 -62.173  1.00 23.22           C  
ATOM   2532  CE2 TYR A 406      21.530 -19.488 -60.655  1.00 23.22           C  
ATOM   2533  CZ  TYR A 406      22.159 -20.234 -61.630  1.00 21.57           C  
ATOM   2534  OH  TYR A 406      23.413 -19.877 -62.062  1.00 22.29           O  
ATOM   2535  N   SER A 407      17.077 -23.886 -58.699  1.00 22.59           N  
ATOM   2536  CA  SER A 407      16.160 -24.292 -57.647  1.00 20.34           C  
ATOM   2537  C   SER A 407      16.852 -24.134 -56.305  1.00 21.51           C  
ATOM   2538  O   SER A 407      18.072 -24.256 -56.216  1.00 22.39           O  
ATOM   2539  CB  SER A 407      15.693 -25.733 -57.850  1.00 21.11           C  
ATOM   2540  OG  SER A 407      16.795 -26.622 -57.869  1.00 23.28           O  
ATOM   2541  N   GLY A 408      16.082 -23.849 -55.263  1.00 18.44           N  
ATOM   2542  CA  GLY A 408      16.668 -23.632 -53.955  1.00 21.57           C  
ATOM   2543  C   GLY A 408      15.685 -23.858 -52.830  1.00 21.07           C  
ATOM   2544  O   GLY A 408      14.482 -23.989 -53.053  1.00 19.04           O  
ATOM   2545  N   SER A 409      16.209 -23.893 -51.611  1.00 21.24           N  
ATOM   2546  CA  SER A 409      15.406 -24.191 -50.436  1.00 21.23           C  
ATOM   2547  C   SER A 409      15.051 -22.938 -49.646  1.00 22.53           C  
ATOM   2548  O   SER A 409      15.782 -21.947 -49.656  1.00 23.70           O  
ATOM   2549  CB  SER A 409      16.147 -25.176 -49.529  1.00 23.35           C  
ATOM   2550  OG  SER A 409      17.463 -24.723 -49.263  1.00 20.89           O  
ATOM   2551  N   PHE A 410      13.914 -23.002 -48.965  1.00 24.21           N  
ATOM   2552  CA  PHE A 410      13.525 -22.002 -47.987  1.00 21.25           C  
ATOM   2553  C   PHE A 410      12.517 -22.660 -47.063  1.00 23.25           C  
ATOM   2554  O   PHE A 410      11.936 -23.683 -47.415  1.00 22.15           O  
ATOM   2555  CB  PHE A 410      12.921 -20.760 -48.648  1.00 21.57           C  
ATOM   2556  CG  PHE A 410      11.565 -20.993 -49.258  1.00 21.55           C  
ATOM   2557  CD1 PHE A 410      11.440 -21.553 -50.519  1.00 23.80           C  
ATOM   2558  CD2 PHE A 410      10.414 -20.646 -48.568  1.00 20.46           C  
ATOM   2559  CE1 PHE A 410      10.191 -21.773 -51.076  1.00 22.06           C  
ATOM   2560  CE2 PHE A 410       9.161 -20.862 -49.121  1.00 23.05           C  
ATOM   2561  CZ  PHE A 410       9.051 -21.420 -50.378  1.00 21.76           C  
ATOM   2562  N   MET A 411      12.318 -22.091 -45.881  1.00 21.58           N  
ATOM   2563  CA  MET A 411      11.276 -22.566 -44.981  1.00 21.42           C  
ATOM   2564  C   MET A 411      10.658 -21.395 -44.235  1.00 22.43           C  
ATOM   2565  O   MET A 411      11.297 -20.358 -44.047  1.00 24.71           O  
ATOM   2566  CB  MET A 411      11.827 -23.600 -43.988  1.00 23.02           C  
ATOM   2567  CG  MET A 411      12.298 -24.904 -44.633  1.00 24.96           C  
ATOM   2568  SD  MET A 411      12.476 -26.271 -43.476  1.00 23.91           S  
ATOM   2569  CE  MET A 411      13.827 -25.672 -42.471  1.00 18.28           C  
ATOM   2570  N   ASP A 412       9.406 -21.556 -43.824  1.00 18.78           N  
ATOM   2571  CA  ASP A 412       8.770 -20.572 -42.961  1.00 20.65           C  
ATOM   2572  C   ASP A 412       9.102 -20.911 -41.515  1.00 22.28           C  
ATOM   2573  O   ASP A 412       8.417 -21.708 -40.877  1.00 21.43           O  
ATOM   2574  CB  ASP A 412       7.257 -20.542 -43.175  1.00 23.72           C  
ATOM   2575  CG  ASP A 412       6.591 -19.376 -42.465  1.00 27.08           C  
ATOM   2576  OD1 ASP A 412       7.284 -18.641 -41.727  1.00 24.65           O  
ATOM   2577  OD2 ASP A 412       5.371 -19.198 -42.642  1.00 29.64           O  
ATOM   2578  N   TYR A 413      10.156 -20.290 -41.001  1.00 20.59           N  
ATOM   2579  CA  TYR A 413      10.637 -20.578 -39.659  1.00 23.89           C  
ATOM   2580  C   TYR A 413       9.725 -20.012 -38.578  1.00 26.33           C  
ATOM   2581  O   TYR A 413       9.958 -20.228 -37.391  1.00 26.24           O  
ATOM   2582  CB  TYR A 413      12.059 -20.037 -39.496  1.00 22.86           C  
ATOM   2583  CG  TYR A 413      13.037 -20.716 -40.423  1.00 23.38           C  
ATOM   2584  CD1 TYR A 413      13.654 -21.903 -40.057  1.00 24.68           C  
ATOM   2585  CD2 TYR A 413      13.322 -20.187 -41.676  1.00 22.64           C  
ATOM   2586  CE1 TYR A 413      14.542 -22.539 -40.905  1.00 24.71           C  
ATOM   2587  CE2 TYR A 413      14.209 -20.819 -42.534  1.00 23.61           C  
ATOM   2588  CZ  TYR A 413      14.815 -21.997 -42.140  1.00 22.18           C  
ATOM   2589  OH  TYR A 413      15.696 -22.640 -42.982  1.00 24.29           O  
ATOM   2590  N   TRP A 414       8.682 -19.299 -38.993  1.00 24.06           N  
ATOM   2591  CA  TRP A 414       7.780 -18.641 -38.055  1.00 26.04           C  
ATOM   2592  C   TRP A 414       6.372 -19.222 -38.114  1.00 25.50           C  
ATOM   2593  O   TRP A 414       5.439 -18.669 -37.536  1.00 27.67           O  
ATOM   2594  CB  TRP A 414       7.757 -17.135 -38.330  1.00 24.84           C  
ATOM   2595  CG  TRP A 414       9.104 -16.521 -38.123  1.00 21.47           C  
ATOM   2596  CD1 TRP A 414       9.594 -15.996 -36.963  1.00 21.35           C  
ATOM   2597  CD2 TRP A 414      10.158 -16.412 -39.090  1.00 17.82           C  
ATOM   2598  NE1 TRP A 414      10.880 -15.551 -37.150  1.00 20.43           N  
ATOM   2599  CE2 TRP A 414      11.250 -15.795 -38.447  1.00 21.72           C  
ATOM   2600  CE3 TRP A 414      10.279 -16.766 -40.438  1.00 18.48           C  
ATOM   2601  CZ2 TRP A 414      12.450 -15.525 -39.105  1.00 20.64           C  
ATOM   2602  CZ3 TRP A 414      11.473 -16.496 -41.091  1.00 19.91           C  
ATOM   2603  CH2 TRP A 414      12.544 -15.887 -40.421  1.00 21.70           C  
ATOM   2604  N   ALA A 415       6.226 -20.344 -38.810  1.00 22.06           N  
ATOM   2605  CA  ALA A 415       4.938 -21.027 -38.892  1.00 23.46           C  
ATOM   2606  C   ALA A 415       4.607 -21.738 -37.587  1.00 25.48           C  
ATOM   2607  O   ALA A 415       5.478 -21.945 -36.746  1.00 25.63           O  
ATOM   2608  CB  ALA A 415       4.936 -22.017 -40.043  1.00 23.53           C  
ATOM   2609  N   GLU A 416       3.342 -22.112 -37.428  1.00 24.42           N  
ATOM   2610  CA  GLU A 416       2.903 -22.867 -36.261  1.00 33.42           C  
ATOM   2611  C   GLU A 416       3.325 -24.331 -36.380  1.00 30.74           C  
ATOM   2612  O   GLU A 416       3.660 -24.800 -37.467  1.00 29.90           O  
ATOM   2613  CB  GLU A 416       1.383 -22.768 -36.099  1.00 40.02           C  
ATOM   2614  CG  GLU A 416       0.868 -21.361 -35.841  1.00 48.04           C  
ATOM   2615  CD  GLU A 416       1.447 -20.749 -34.581  1.00 56.42           C  
ATOM   2616  OE1 GLU A 416       1.272 -21.345 -33.497  1.00 59.25           O  
ATOM   2617  OE2 GLU A 416       2.078 -19.674 -34.675  1.00 60.42           O  
ATOM   2618  N   GLY A 417       3.311 -25.050 -35.262  1.00 32.99           N  
ATOM   2619  CA  GLY A 417       3.639 -26.465 -35.274  1.00 32.67           C  
ATOM   2620  C   GLY A 417       4.971 -26.791 -34.626  1.00 35.30           C  
ATOM   2621  O   GLY A 417       5.730 -25.894 -34.260  1.00 35.86           O  
ATOM   2622  N   ASP A 418       5.257 -28.083 -34.494  1.00 36.10           N  
ATOM   2623  CA  ASP A 418       6.466 -28.537 -33.812  1.00 35.97           C  
ATOM   2624  C   ASP A 418       7.596 -28.915 -34.775  1.00 30.69           C  
ATOM   2625  O   ASP A 418       8.653 -29.379 -34.348  1.00 29.84           O  
ATOM   2626  CB  ASP A 418       6.138 -29.723 -32.894  1.00 41.76           C  
ATOM   2627  CG  ASP A 418       5.679 -30.955 -33.658  1.00 50.42           C  
ATOM   2628  OD1 ASP A 418       5.450 -30.867 -34.885  1.00 53.44           O  
ATOM   2629  OD2 ASP A 418       5.551 -32.024 -33.023  1.00 54.18           O  
ATOM   2630  N   CYS A 419       7.374 -28.714 -36.071  1.00 26.24           N  
ATOM   2631  CA  CYS A 419       8.399 -29.023 -37.061  1.00 24.89           C  
ATOM   2632  C   CYS A 419       8.441 -27.977 -38.171  1.00 26.09           C  
ATOM   2633  O   CYS A 419       7.453 -27.288 -38.426  1.00 24.25           O  
ATOM   2634  CB  CYS A 419       8.169 -30.413 -37.660  1.00 27.45           C  
ATOM   2635  SG  CYS A 419       6.566 -30.639 -38.465  1.00 40.35           S  
ATOM   2636  N   TYR A 420       9.597 -27.857 -38.817  1.00 24.28           N  
ATOM   2637  CA  TYR A 420       9.752 -26.975 -39.967  1.00 24.72           C  
ATOM   2638  C   TYR A 420       9.303 -27.683 -41.235  1.00 24.93           C  
ATOM   2639  O   TYR A 420       9.715 -28.811 -41.501  1.00 22.00           O  
ATOM   2640  CB  TYR A 420      11.206 -26.522 -40.118  1.00 25.97           C  
ATOM   2641  CG  TYR A 420      11.725 -25.652 -39.000  1.00 27.79           C  
ATOM   2642  CD1 TYR A 420      10.947 -24.635 -38.463  1.00 26.36           C  
ATOM   2643  CD2 TYR A 420      13.003 -25.840 -38.490  1.00 26.58           C  
ATOM   2644  CE1 TYR A 420      11.427 -23.832 -37.439  1.00 25.41           C  
ATOM   2645  CE2 TYR A 420      13.490 -25.048 -37.469  1.00 27.66           C  
ATOM   2646  CZ  TYR A 420      12.702 -24.045 -36.949  1.00 26.24           C  
ATOM   2647  OH  TYR A 420      13.195 -23.260 -35.931  1.00 26.87           O  
ATOM   2648  N   ARG A 421       8.464 -27.016 -42.020  1.00 24.08           N  
ATOM   2649  CA  ARG A 421       7.971 -27.584 -43.265  1.00 22.57           C  
ATOM   2650  C   ARG A 421       8.920 -27.250 -44.407  1.00 21.47           C  
ATOM   2651  O   ARG A 421       9.074 -26.086 -44.775  1.00 22.77           O  
ATOM   2652  CB  ARG A 421       6.563 -27.069 -43.568  1.00 26.49           C  
ATOM   2653  CG  ARG A 421       5.914 -27.677 -44.800  1.00 28.34           C  
ATOM   2654  CD  ARG A 421       4.539 -27.068 -45.028  1.00 30.57           C  
ATOM   2655  NE  ARG A 421       3.597 -27.428 -43.972  1.00 30.19           N  
ATOM   2656  CZ  ARG A 421       2.335 -27.788 -44.184  1.00 34.47           C  
ATOM   2657  NH1 ARG A 421       1.851 -27.830 -45.416  1.00 31.59           N  
ATOM   2658  NH2 ARG A 421       1.553 -28.098 -43.159  1.00 35.98           N  
ATOM   2659  N   ALA A 422       9.559 -28.276 -44.958  1.00 22.16           N  
ATOM   2660  CA  ALA A 422      10.508 -28.094 -46.045  1.00 23.06           C  
ATOM   2661  C   ALA A 422       9.834 -27.488 -47.269  1.00 23.66           C  
ATOM   2662  O   ALA A 422       8.776 -27.949 -47.698  1.00 22.73           O  
ATOM   2663  CB  ALA A 422      11.154 -29.413 -46.402  1.00 22.45           C  
ATOM   2664  N   CYS A 423      10.452 -26.453 -47.829  1.00 23.86           N  
ATOM   2665  CA  CYS A 423       9.935 -25.831 -49.042  1.00 21.66           C  
ATOM   2666  C   CYS A 423      11.027 -25.636 -50.079  1.00 21.42           C  
ATOM   2667  O   CYS A 423      12.214 -25.681 -49.766  1.00 18.62           O  
ATOM   2668  CB  CYS A 423       9.284 -24.481 -48.736  1.00 21.84           C  
ATOM   2669  SG  CYS A 423       7.946 -24.522 -47.539  1.00 26.99           S  
ATOM   2670  N   PHE A 424      10.615 -25.411 -51.318  1.00 19.67           N  
ATOM   2671  CA  PHE A 424      11.561 -25.095 -52.372  1.00 20.32           C  
ATOM   2672  C   PHE A 424      10.878 -24.384 -53.524  1.00 21.48           C  
ATOM   2673  O   PHE A 424       9.653 -24.422 -53.658  1.00 21.13           O  
ATOM   2674  CB  PHE A 424      12.258 -26.358 -52.878  1.00 16.51           C  
ATOM   2675  CG  PHE A 424      11.363 -27.287 -53.658  1.00 19.41           C  
ATOM   2676  CD1 PHE A 424      10.626 -28.262 -53.008  1.00 17.92           C  
ATOM   2677  CD2 PHE A 424      11.285 -27.209 -55.043  1.00 20.06           C  
ATOM   2678  CE1 PHE A 424       9.813 -29.126 -53.719  1.00 19.90           C  
ATOM   2679  CE2 PHE A 424      10.470 -28.069 -55.757  1.00 20.42           C  
ATOM   2680  CZ  PHE A 424       9.732 -29.026 -55.093  1.00 22.27           C  
ATOM   2681  N   TYR A 425      11.685 -23.730 -54.350  1.00 19.41           N  
ATOM   2682  CA  TYR A 425      11.198 -23.088 -55.557  1.00 17.89           C  
ATOM   2683  C   TYR A 425      11.929 -23.685 -56.752  1.00 19.95           C  
ATOM   2684  O   TYR A 425      13.028 -24.231 -56.614  1.00 18.15           O  
ATOM   2685  CB  TYR A 425      11.416 -21.570 -55.504  1.00 18.46           C  
ATOM   2686  CG  TYR A 425      12.879 -21.192 -55.510  1.00 19.63           C  
ATOM   2687  CD1 TYR A 425      13.563 -20.995 -56.704  1.00 18.79           C  
ATOM   2688  CD2 TYR A 425      13.585 -21.063 -54.323  1.00 20.65           C  
ATOM   2689  CE1 TYR A 425      14.904 -20.672 -56.715  1.00 20.97           C  
ATOM   2690  CE2 TYR A 425      14.929 -20.740 -54.323  1.00 21.49           C  
ATOM   2691  CZ  TYR A 425      15.584 -20.543 -55.522  1.00 21.75           C  
ATOM   2692  OH  TYR A 425      16.922 -20.216 -55.528  1.00 23.55           O  
ATOM   2693  N   VAL A 426      11.324 -23.573 -57.924  1.00 21.59           N  
ATOM   2694  CA  VAL A 426      12.022 -23.878 -59.159  1.00 18.76           C  
ATOM   2695  C   VAL A 426      11.897 -22.698 -60.107  1.00 22.60           C  
ATOM   2696  O   VAL A 426      10.794 -22.218 -60.375  1.00 21.97           O  
ATOM   2697  CB  VAL A 426      11.476 -25.147 -59.836  1.00 19.87           C  
ATOM   2698  CG1 VAL A 426      12.223 -25.411 -61.137  1.00 18.55           C  
ATOM   2699  CG2 VAL A 426      11.594 -26.340 -58.896  1.00 20.60           C  
ATOM   2700  N   GLU A 427      13.036 -22.212 -60.585  1.00 19.24           N  
ATOM   2701  CA  GLU A 427      13.056 -21.147 -61.574  1.00 21.99           C  
ATOM   2702  C   GLU A 427      12.684 -21.722 -62.927  1.00 22.58           C  
ATOM   2703  O   GLU A 427      13.300 -22.678 -63.383  1.00 22.76           O  
ATOM   2704  CB  GLU A 427      14.435 -20.485 -61.634  1.00 22.15           C  
ATOM   2705  CG  GLU A 427      14.598 -19.481 -62.760  1.00 21.29           C  
ATOM   2706  CD  GLU A 427      16.044 -19.051 -62.941  1.00 20.06           C  
ATOM   2707  OE1 GLU A 427      16.938 -19.912 -62.822  1.00 20.56           O  
ATOM   2708  OE2 GLU A 427      16.286 -17.851 -63.187  1.00 21.96           O  
ATOM   2709  N   LEU A 428      11.671 -21.145 -63.562  1.00 20.78           N  
ATOM   2710  CA  LEU A 428      11.252 -21.600 -64.880  1.00 19.37           C  
ATOM   2711  C   LEU A 428      11.732 -20.620 -65.942  1.00 24.39           C  
ATOM   2712  O   LEU A 428      11.049 -19.645 -66.253  1.00 20.97           O  
ATOM   2713  CB  LEU A 428       9.732 -21.762 -64.931  1.00 20.19           C  
ATOM   2714  CG  LEU A 428       9.146 -22.544 -63.754  1.00 19.64           C  
ATOM   2715  CD1 LEU A 428       7.624 -22.489 -63.768  1.00 20.40           C  
ATOM   2716  CD2 LEU A 428       9.633 -23.990 -63.786  1.00 21.77           C  
ATOM   2717  N   ILE A 429      12.921 -20.880 -66.479  1.00 20.66           N  
ATOM   2718  CA  ILE A 429      13.560 -19.958 -67.407  1.00 20.81           C  
ATOM   2719  C   ILE A 429      12.909 -19.993 -68.785  1.00 21.43           C  
ATOM   2720  O   ILE A 429      12.739 -21.058 -69.380  1.00 21.38           O  
ATOM   2721  CB  ILE A 429      15.064 -20.264 -67.561  1.00 20.66           C  
ATOM   2722  CG1 ILE A 429      15.768 -20.162 -66.209  1.00 21.44           C  
ATOM   2723  CG2 ILE A 429      15.701 -19.316 -68.561  1.00 19.53           C  
ATOM   2724  CD1 ILE A 429      17.201 -20.654 -66.229  1.00 20.93           C  
ATOM   2725  N   ARG A 430      12.544 -18.818 -69.285  1.00 22.00           N  
ATOM   2726  CA  ARG A 430      12.013 -18.698 -70.636  1.00 22.14           C  
ATOM   2727  C   ARG A 430      12.883 -17.745 -71.440  1.00 25.21           C  
ATOM   2728  O   ARG A 430      13.519 -16.848 -70.881  1.00 22.71           O  
ATOM   2729  CB  ARG A 430      10.562 -18.209 -70.621  1.00 22.61           C  
ATOM   2730  CG  ARG A 430       9.595 -19.095 -69.845  1.00 23.95           C  
ATOM   2731  CD  ARG A 430       9.559 -20.511 -70.399  1.00 22.30           C  
ATOM   2732  NE  ARG A 430       9.182 -20.553 -71.809  1.00 24.79           N  
ATOM   2733  CZ  ARG A 430       7.931 -20.653 -72.245  1.00 28.87           C  
ATOM   2734  NH1 ARG A 430       6.932 -20.711 -71.375  1.00 29.63           N  
ATOM   2735  NH2 ARG A 430       7.678 -20.694 -73.547  1.00 28.28           N  
ATOM   2736  N   GLY A 431      12.910 -17.940 -72.753  1.00 24.53           N  
ATOM   2737  CA  GLY A 431      13.733 -17.118 -73.617  1.00 26.39           C  
ATOM   2738  C   GLY A 431      15.087 -17.748 -73.882  1.00 27.10           C  
ATOM   2739  O   GLY A 431      15.220 -18.972 -73.933  1.00 25.65           O  
ATOM   2740  N   ARG A 432      16.102 -16.907 -74.045  1.00 24.75           N  
ATOM   2741  CA  ARG A 432      17.419 -17.379 -74.454  1.00 24.99           C  
ATOM   2742  C   ARG A 432      18.158 -18.057 -73.303  1.00 24.19           C  
ATOM   2743  O   ARG A 432      17.940 -17.718 -72.143  1.00 23.45           O  
ATOM   2744  CB  ARG A 432      18.227 -16.213 -75.029  1.00 25.65           C  
ATOM   2745  CG  ARG A 432      17.743 -15.855 -76.423  1.00 27.79           C  
ATOM   2746  CD  ARG A 432      18.513 -14.728 -77.077  1.00 28.42           C  
ATOM   2747  NE  ARG A 432      18.000 -14.509 -78.426  1.00 31.28           N  
ATOM   2748  CZ  ARG A 432      18.745 -14.171 -79.472  1.00 35.82           C  
ATOM   2749  NH1 ARG A 432      20.053 -14.006 -79.333  1.00 34.42           N  
ATOM   2750  NH2 ARG A 432      18.181 -14.007 -80.660  1.00 39.93           N  
ATOM   2751  N   PRO A 433      19.040 -19.020 -73.622  1.00 26.12           N  
ATOM   2752  CA  PRO A 433      19.446 -19.422 -74.975  1.00 26.66           C  
ATOM   2753  C   PRO A 433      18.520 -20.432 -75.662  1.00 29.33           C  
ATOM   2754  O   PRO A 433      18.564 -20.546 -76.886  1.00 30.15           O  
ATOM   2755  CB  PRO A 433      20.821 -20.045 -74.741  1.00 27.06           C  
ATOM   2756  CG  PRO A 433      20.707 -20.651 -73.378  1.00 25.75           C  
ATOM   2757  CD  PRO A 433      19.812 -19.732 -72.585  1.00 25.90           C  
ATOM   2758  N   LYS A 434      17.699 -21.145 -74.897  1.00 26.09           N  
ATOM   2759  CA  LYS A 434      16.932 -22.264 -75.444  1.00 27.61           C  
ATOM   2760  C   LYS A 434      15.821 -21.830 -76.400  1.00 30.18           C  
ATOM   2761  O   LYS A 434      15.457 -22.568 -77.314  1.00 28.77           O  
ATOM   2762  CB  LYS A 434      16.341 -23.100 -74.308  1.00 28.74           C  
ATOM   2763  CG  LYS A 434      17.359 -23.986 -73.610  1.00 34.05           C  
ATOM   2764  CD  LYS A 434      17.982 -24.966 -74.598  1.00 41.04           C  
ATOM   2765  CE  LYS A 434      19.013 -25.859 -73.933  1.00 44.99           C  
ATOM   2766  NZ  LYS A 434      20.264 -25.117 -73.621  1.00 47.43           N  
ATOM   2767  N   GLU A 435      15.282 -20.636 -76.186  1.00 27.83           N  
ATOM   2768  CA  GLU A 435      14.220 -20.114 -77.040  1.00 29.17           C  
ATOM   2769  C   GLU A 435      14.642 -18.777 -77.643  1.00 30.25           C  
ATOM   2770  O   GLU A 435      14.278 -17.719 -77.135  1.00 31.43           O  
ATOM   2771  CB  GLU A 435      12.921 -19.964 -76.244  1.00 29.54           C  
ATOM   2772  CG  GLU A 435      12.418 -21.268 -75.623  1.00 29.58           C  
ATOM   2773  CD  GLU A 435      11.296 -21.051 -74.620  1.00 31.72           C  
ATOM   2774  OE1 GLU A 435      11.510 -20.314 -73.634  1.00 28.54           O  
ATOM   2775  OE2 GLU A 435      10.200 -21.619 -74.816  1.00 34.12           O  
ATOM   2776  N   ASP A 436      15.409 -18.827 -78.728  1.00 33.76           N  
ATOM   2777  CA  ASP A 436      16.051 -17.621 -79.252  1.00 35.96           C  
ATOM   2778  C   ASP A 436      15.236 -16.871 -80.307  1.00 34.54           C  
ATOM   2779  O   ASP A 436      15.768 -15.996 -80.993  1.00 32.26           O  
ATOM   2780  CB  ASP A 436      17.437 -17.964 -79.816  1.00 39.17           C  
ATOM   2781  CG  ASP A 436      17.387 -18.986 -80.942  1.00 45.26           C  
ATOM   2782  OD1 ASP A 436      16.289 -19.281 -81.460  1.00 45.47           O  
ATOM   2783  OD2 ASP A 436      18.465 -19.499 -81.313  1.00 51.56           O  
ATOM   2784  N   LYS A 437      13.955 -17.204 -80.438  1.00 32.86           N  
ATOM   2785  CA  LYS A 437      13.066 -16.416 -81.288  1.00 34.78           C  
ATOM   2786  C   LYS A 437      12.804 -15.060 -80.640  1.00 33.87           C  
ATOM   2787  O   LYS A 437      12.500 -14.076 -81.319  1.00 30.76           O  
ATOM   2788  CB  LYS A 437      11.749 -17.150 -81.550  1.00 40.39           C  
ATOM   2789  CG  LYS A 437      11.857 -18.287 -82.556  1.00 44.76           C  
ATOM   2790  CD  LYS A 437      10.615 -19.170 -82.528  1.00 50.76           C  
ATOM   2791  CE  LYS A 437      10.233 -19.646 -83.923  1.00 54.62           C  
ATOM   2792  NZ  LYS A 437      11.355 -20.343 -84.612  1.00 56.84           N  
ATOM   2793  N   VAL A 438      12.914 -15.023 -79.317  1.00 29.52           N  
ATOM   2794  CA  VAL A 438      12.894 -13.767 -78.583  1.00 26.70           C  
ATOM   2795  C   VAL A 438      14.324 -13.398 -78.212  1.00 26.72           C  
ATOM   2796  O   VAL A 438      15.212 -14.252 -78.203  1.00 27.09           O  
ATOM   2797  CB  VAL A 438      12.032 -13.848 -77.312  1.00 24.91           C  
ATOM   2798  CG1 VAL A 438      10.562 -14.038 -77.671  1.00 26.64           C  
ATOM   2799  CG2 VAL A 438      12.520 -14.971 -76.415  1.00 25.10           C  
ATOM   2800  N   TRP A 439      14.545 -12.126 -77.909  1.00 24.53           N  
ATOM   2801  CA  TRP A 439      15.890 -11.653 -77.622  1.00 26.04           C  
ATOM   2802  C   TRP A 439      16.107 -11.447 -76.131  1.00 27.45           C  
ATOM   2803  O   TRP A 439      17.162 -10.974 -75.711  1.00 27.17           O  
ATOM   2804  CB  TRP A 439      16.167 -10.361 -78.386  1.00 28.74           C  
ATOM   2805  CG  TRP A 439      16.313 -10.593 -79.854  1.00 31.11           C  
ATOM   2806  CD1 TRP A 439      15.310 -10.673 -80.776  1.00 34.81           C  
ATOM   2807  CD2 TRP A 439      17.535 -10.793 -80.573  1.00 35.06           C  
ATOM   2808  NE1 TRP A 439      15.833 -10.903 -82.025  1.00 39.26           N  
ATOM   2809  CE2 TRP A 439      17.197 -10.982 -81.927  1.00 37.42           C  
ATOM   2810  CE3 TRP A 439      18.884 -10.830 -80.202  1.00 36.12           C  
ATOM   2811  CZ2 TRP A 439      18.157 -11.201 -82.912  1.00 38.90           C  
ATOM   2812  CZ3 TRP A 439      19.835 -11.050 -81.182  1.00 39.41           C  
ATOM   2813  CH2 TRP A 439      19.467 -11.233 -82.520  1.00 39.63           C  
ATOM   2814  N   TRP A 440      15.111 -11.813 -75.331  1.00 25.35           N  
ATOM   2815  CA  TRP A 440      15.229 -11.678 -73.886  1.00 23.75           C  
ATOM   2816  C   TRP A 440      15.374 -13.015 -73.167  1.00 24.65           C  
ATOM   2817  O   TRP A 440      15.127 -14.080 -73.737  1.00 22.76           O  
ATOM   2818  CB  TRP A 440      14.024 -10.922 -73.315  1.00 25.70           C  
ATOM   2819  CG  TRP A 440      12.673 -11.418 -73.770  1.00 25.32           C  
ATOM   2820  CD1 TRP A 440      11.885 -10.861 -74.738  1.00 25.13           C  
ATOM   2821  CD2 TRP A 440      11.942 -12.545 -73.259  1.00 25.29           C  
ATOM   2822  NE1 TRP A 440      10.717 -11.573 -74.869  1.00 24.49           N  
ATOM   2823  CE2 TRP A 440      10.726 -12.611 -73.975  1.00 24.65           C  
ATOM   2824  CE3 TRP A 440      12.200 -13.507 -72.276  1.00 21.66           C  
ATOM   2825  CZ2 TRP A 440       9.771 -13.599 -73.737  1.00 24.99           C  
ATOM   2826  CZ3 TRP A 440      11.249 -14.487 -72.040  1.00 24.29           C  
ATOM   2827  CH2 TRP A 440      10.048 -14.525 -72.768  1.00 24.79           C  
ATOM   2828  N   THR A 441      15.795 -12.936 -71.909  1.00 21.41           N  
ATOM   2829  CA  THR A 441      15.777 -14.070 -70.998  1.00 23.44           C  
ATOM   2830  C   THR A 441      15.094 -13.659 -69.708  1.00 23.75           C  
ATOM   2831  O   THR A 441      15.487 -12.682 -69.078  1.00 23.50           O  
ATOM   2832  CB  THR A 441      17.190 -14.584 -70.672  1.00 25.27           C  
ATOM   2833  OG1 THR A 441      17.851 -14.968 -71.882  1.00 24.00           O  
ATOM   2834  CG2 THR A 441      17.123 -15.776 -69.720  1.00 24.35           C  
ATOM   2835  N   SER A 442      14.061 -14.393 -69.323  1.00 24.23           N  
ATOM   2836  CA  SER A 442      13.422 -14.151 -68.042  1.00 22.84           C  
ATOM   2837  C   SER A 442      12.973 -15.468 -67.427  1.00 27.74           C  
ATOM   2838  O   SER A 442      13.410 -16.539 -67.848  1.00 30.43           O  
ATOM   2839  CB  SER A 442      12.239 -13.194 -68.196  1.00 22.46           C  
ATOM   2840  OG  SER A 442      11.857 -12.662 -66.939  1.00 21.76           O  
ATOM   2841  N   ASN A 443      12.100 -15.385 -66.432  1.00 21.30           N  
ATOM   2842  CA  ASN A 443      11.633 -16.576 -65.745  1.00 19.99           C  
ATOM   2843  C   ASN A 443      10.329 -16.338 -65.013  1.00 23.72           C  
ATOM   2844  O   ASN A 443       9.927 -15.194 -64.793  1.00 22.74           O  
ATOM   2845  CB  ASN A 443      12.679 -17.053 -64.741  1.00 19.21           C  
ATOM   2846  CG  ASN A 443      12.762 -16.149 -63.526  1.00 21.67           C  
ATOM   2847  OD1 ASN A 443      13.372 -15.084 -63.577  1.00 24.99           O  
ATOM   2848  ND2 ASN A 443      12.137 -16.566 -62.429  1.00 20.72           N  
ATOM   2849  N   SER A 444       9.671 -17.428 -64.635  1.00 21.01           N  
ATOM   2850  CA  SER A 444       8.626 -17.359 -63.628  1.00 22.04           C  
ATOM   2851  C   SER A 444       9.012 -18.284 -62.489  1.00 21.85           C  
ATOM   2852  O   SER A 444      10.060 -18.932 -62.531  1.00 22.00           O  
ATOM   2853  CB  SER A 444       7.259 -17.733 -64.197  1.00 24.04           C  
ATOM   2854  OG  SER A 444       7.142 -19.132 -64.386  1.00 30.12           O  
ATOM   2855  N   ILE A 445       8.164 -18.343 -61.472  1.00 23.22           N  
ATOM   2856  CA  ILE A 445       8.469 -19.107 -60.275  1.00 24.29           C  
ATOM   2857  C   ILE A 445       7.370 -20.112 -59.974  1.00 22.78           C  
ATOM   2858  O   ILE A 445       6.188 -19.788 -60.064  1.00 21.32           O  
ATOM   2859  CB  ILE A 445       8.643 -18.176 -59.054  1.00 26.02           C  
ATOM   2860  CG1 ILE A 445       9.811 -17.211 -59.270  1.00 26.79           C  
ATOM   2861  CG2 ILE A 445       8.855 -18.982 -57.783  1.00 28.05           C  
ATOM   2862  CD1 ILE A 445       9.846 -16.081 -58.264  1.00 25.87           C  
ATOM   2863  N   VAL A 446       7.757 -21.337 -59.634  1.00 21.12           N  
ATOM   2864  CA  VAL A 446       6.832 -22.256 -58.989  1.00 20.33           C  
ATOM   2865  C   VAL A 446       7.465 -22.687 -57.667  1.00 22.82           C  
ATOM   2866  O   VAL A 446       8.684 -22.814 -57.563  1.00 21.89           O  
ATOM   2867  CB  VAL A 446       6.493 -23.475 -59.878  1.00 22.61           C  
ATOM   2868  CG1 VAL A 446       7.714 -24.357 -60.089  1.00 19.32           C  
ATOM   2869  CG2 VAL A 446       5.345 -24.269 -59.267  1.00 24.05           C  
ATOM   2870  N   SER A 447       6.639 -22.875 -56.646  1.00 19.98           N  
ATOM   2871  CA  SER A 447       7.144 -23.178 -55.315  1.00 21.47           C  
ATOM   2872  C   SER A 447       6.292 -24.236 -54.630  1.00 22.64           C  
ATOM   2873  O   SER A 447       5.065 -24.212 -54.738  1.00 21.17           O  
ATOM   2874  CB  SER A 447       7.185 -21.909 -54.462  1.00 24.30           C  
ATOM   2875  OG  SER A 447       7.766 -22.178 -53.202  1.00 33.11           O  
ATOM   2876  N   MET A 448       6.943 -25.157 -53.925  1.00 21.92           N  
ATOM   2877  CA  MET A 448       6.242 -26.237 -53.236  1.00 21.37           C  
ATOM   2878  C   MET A 448       6.663 -26.330 -51.774  1.00 24.51           C  
ATOM   2879  O   MET A 448       7.748 -25.892 -51.406  1.00 22.75           O  
ATOM   2880  CB  MET A 448       6.499 -27.583 -53.926  1.00 22.31           C  
ATOM   2881  CG  MET A 448       6.517 -27.527 -55.443  1.00 28.20           C  
ATOM   2882  SD  MET A 448       4.869 -27.674 -56.148  1.00 33.62           S  
ATOM   2883  CE  MET A 448       4.471 -29.378 -55.766  1.00 24.37           C  
ATOM   2884  N   CYS A 449       5.794 -26.903 -50.949  1.00 23.77           N  
ATOM   2885  CA  CYS A 449       6.130 -27.226 -49.568  1.00 23.69           C  
ATOM   2886  C   CYS A 449       5.740 -28.667 -49.295  1.00 23.82           C  
ATOM   2887  O   CYS A 449       4.904 -29.225 -49.999  1.00 22.80           O  
ATOM   2888  CB  CYS A 449       5.434 -26.278 -48.592  1.00 23.73           C  
ATOM   2889  SG  CYS A 449       6.180 -24.638 -48.540  1.00 32.59           S  
ATOM   2890  N   SER A 450       6.349 -29.267 -48.278  1.00 22.58           N  
ATOM   2891  CA  SER A 450       6.131 -30.681 -47.994  1.00 24.16           C  
ATOM   2892  C   SER A 450       4.798 -30.932 -47.293  1.00 24.22           C  
ATOM   2893  O   SER A 450       4.263 -30.059 -46.608  1.00 22.75           O  
ATOM   2894  CB  SER A 450       7.276 -31.241 -47.143  1.00 23.52           C  
ATOM   2895  OG  SER A 450       7.291 -30.658 -45.852  1.00 27.57           O  
ATOM   2896  N   SER A 451       4.274 -32.141 -47.471  1.00 25.04           N  
ATOM   2897  CA  SER A 451       3.054 -32.572 -46.801  1.00 23.48           C  
ATOM   2898  C   SER A 451       3.285 -33.924 -46.139  1.00 24.91           C  
ATOM   2899  O   SER A 451       4.062 -34.740 -46.639  1.00 21.61           O  
ATOM   2900  CB  SER A 451       1.891 -32.653 -47.796  1.00 23.71           C  
ATOM   2901  OG  SER A 451       0.748 -33.252 -47.208  1.00 24.22           O  
ATOM   2902  N   THR A 452       2.619 -34.160 -45.012  1.00 25.63           N  
ATOM   2903  CA  THR A 452       2.699 -35.460 -44.356  1.00 25.98           C  
ATOM   2904  C   THR A 452       1.729 -36.432 -45.014  1.00 26.48           C  
ATOM   2905  O   THR A 452       1.785 -37.639 -44.778  1.00 24.88           O  
ATOM   2906  CB  THR A 452       2.397 -35.364 -42.849  1.00 28.55           C  
ATOM   2907  OG1 THR A 452       1.078 -34.834 -42.655  1.00 28.58           O  
ATOM   2908  CG2 THR A 452       3.413 -34.460 -42.162  1.00 26.96           C  
ATOM   2909  N   GLU A 453       0.838 -35.894 -45.840  1.00 25.78           N  
ATOM   2910  CA  GLU A 453      -0.048 -36.712 -46.654  1.00 27.53           C  
ATOM   2911  C   GLU A 453       0.684 -37.198 -47.903  1.00 28.37           C  
ATOM   2912  O   GLU A 453       1.711 -36.639 -48.287  1.00 29.03           O  
ATOM   2913  CB  GLU A 453      -1.295 -35.922 -47.056  1.00 28.39           C  
ATOM   2914  CG  GLU A 453      -2.033 -35.263 -45.901  1.00 31.58           C  
ATOM   2915  CD  GLU A 453      -2.623 -36.265 -44.924  1.00 41.33           C  
ATOM   2916  OE1 GLU A 453      -3.048 -37.354 -45.366  1.00 45.22           O  
ATOM   2917  OE2 GLU A 453      -2.675 -35.955 -43.715  1.00 46.76           O  
ATOM   2918  N   PHE A 454       0.152 -38.239 -48.533  1.00 24.42           N  
ATOM   2919  CA  PHE A 454       0.662 -38.690 -49.824  1.00 26.79           C  
ATOM   2920  C   PHE A 454      -0.212 -38.123 -50.937  1.00 27.35           C  
ATOM   2921  O   PHE A 454      -1.115 -38.793 -51.442  1.00 25.59           O  
ATOM   2922  CB  PHE A 454       0.708 -40.217 -49.889  1.00 26.82           C  
ATOM   2923  CG  PHE A 454       1.722 -40.831 -48.963  1.00 30.46           C  
ATOM   2924  CD1 PHE A 454       1.439 -41.012 -47.618  1.00 29.85           C  
ATOM   2925  CD2 PHE A 454       2.962 -41.224 -49.438  1.00 30.51           C  
ATOM   2926  CE1 PHE A 454       2.375 -41.572 -46.766  1.00 28.29           C  
ATOM   2927  CE2 PHE A 454       3.900 -41.786 -48.592  1.00 29.48           C  
ATOM   2928  CZ  PHE A 454       3.606 -41.960 -47.256  1.00 28.71           C  
ATOM   2929  N   LEU A 455       0.059 -36.874 -51.302  1.00 23.44           N  
ATOM   2930  CA  LEU A 455      -0.797 -36.135 -52.221  1.00 23.54           C  
ATOM   2931  C   LEU A 455      -0.552 -36.493 -53.679  1.00 25.57           C  
ATOM   2932  O   LEU A 455       0.563 -36.844 -54.067  1.00 24.73           O  
ATOM   2933  CB  LEU A 455      -0.594 -34.631 -52.030  1.00 25.43           C  
ATOM   2934  CG  LEU A 455      -0.909 -34.065 -50.647  1.00 26.33           C  
ATOM   2935  CD1 LEU A 455      -0.557 -32.581 -50.601  1.00 26.18           C  
ATOM   2936  CD2 LEU A 455      -2.377 -34.292 -50.302  1.00 26.07           C  
ATOM   2937  N   GLY A 456      -1.605 -36.386 -54.484  1.00 24.85           N  
ATOM   2938  CA  GLY A 456      -1.485 -36.564 -55.918  1.00 22.68           C  
ATOM   2939  C   GLY A 456      -0.598 -35.481 -56.499  1.00 25.33           C  
ATOM   2940  O   GLY A 456      -0.514 -34.377 -55.957  1.00 26.53           O  
ATOM   2941  N   GLN A 457       0.070 -35.792 -57.603  1.00 24.31           N  
ATOM   2942  CA  GLN A 457       0.989 -34.842 -58.210  1.00 27.80           C  
ATOM   2943  C   GLN A 457       0.415 -34.229 -59.483  1.00 26.45           C  
ATOM   2944  O   GLN A 457      -0.311 -34.882 -60.231  1.00 26.05           O  
ATOM   2945  CB  GLN A 457       2.328 -35.517 -58.519  1.00 29.88           C  
ATOM   2946  CG  GLN A 457       2.238 -36.636 -59.543  1.00 32.30           C  
ATOM   2947  CD  GLN A 457       3.589 -37.244 -59.864  1.00 37.30           C  
ATOM   2948  OE1 GLN A 457       4.612 -36.840 -59.314  1.00 36.84           O  
ATOM   2949  NE2 GLN A 457       3.598 -38.223 -60.759  1.00 40.86           N  
ATOM   2950  N   TRP A 458       0.731 -32.959 -59.707  1.00 24.08           N  
ATOM   2951  CA  TRP A 458       0.486 -32.313 -60.987  1.00 24.57           C  
ATOM   2952  C   TRP A 458       1.845 -31.953 -61.561  1.00 28.01           C  
ATOM   2953  O   TRP A 458       2.871 -32.256 -60.955  1.00 31.24           O  
ATOM   2954  CB  TRP A 458      -0.386 -31.061 -60.835  1.00 25.23           C  
ATOM   2955  CG  TRP A 458      -1.294 -30.802 -62.009  1.00 24.22           C  
ATOM   2956  CD1 TRP A 458      -1.425 -31.568 -63.132  1.00 25.84           C  
ATOM   2957  CD2 TRP A 458      -2.192 -29.695 -62.174  1.00 23.26           C  
ATOM   2958  NE1 TRP A 458      -2.353 -31.013 -63.981  1.00 23.83           N  
ATOM   2959  CE2 TRP A 458      -2.840 -29.864 -63.415  1.00 25.11           C  
ATOM   2960  CE3 TRP A 458      -2.513 -28.580 -61.392  1.00 23.12           C  
ATOM   2961  CZ2 TRP A 458      -3.787 -28.960 -63.892  1.00 24.29           C  
ATOM   2962  CZ3 TRP A 458      -3.456 -27.687 -61.865  1.00 24.24           C  
ATOM   2963  CH2 TRP A 458      -4.081 -27.882 -63.103  1.00 25.98           C  
ATOM   2964  N   ASN A 459       1.861 -31.317 -62.725  1.00 24.58           N  
ATOM   2965  CA  ASN A 459       3.090 -30.736 -63.243  1.00 23.08           C  
ATOM   2966  C   ASN A 459       2.863 -29.249 -63.437  1.00 23.85           C  
ATOM   2967  O   ASN A 459       1.757 -28.829 -63.765  1.00 26.76           O  
ATOM   2968  CB  ASN A 459       3.519 -31.405 -64.547  1.00 25.41           C  
ATOM   2969  CG  ASN A 459       2.574 -31.114 -65.691  1.00 24.04           C  
ATOM   2970  OD1 ASN A 459       2.743 -30.132 -66.411  1.00 24.89           O  
ATOM   2971  ND2 ASN A 459       1.576 -31.969 -65.869  1.00 25.14           N  
ATOM   2972  N   TRP A 460       3.903 -28.451 -63.231  1.00 22.91           N  
ATOM   2973  CA  TRP A 460       3.727 -27.004 -63.143  1.00 23.04           C  
ATOM   2974  C   TRP A 460       4.624 -26.237 -64.109  1.00 23.06           C  
ATOM   2975  O   TRP A 460       5.713 -25.805 -63.737  1.00 25.03           O  
ATOM   2976  CB  TRP A 460       3.988 -26.541 -61.710  1.00 21.65           C  
ATOM   2977  CG  TRP A 460       3.041 -27.142 -60.718  1.00 23.48           C  
ATOM   2978  CD1 TRP A 460       3.221 -28.297 -60.011  1.00 27.11           C  
ATOM   2979  CD2 TRP A 460       1.761 -26.628 -60.329  1.00 22.05           C  
ATOM   2980  NE1 TRP A 460       2.133 -28.533 -59.205  1.00 23.84           N  
ATOM   2981  CE2 TRP A 460       1.222 -27.525 -59.381  1.00 21.63           C  
ATOM   2982  CE3 TRP A 460       1.017 -25.499 -60.690  1.00 18.89           C  
ATOM   2983  CZ2 TRP A 460      -0.021 -27.324 -58.786  1.00 22.72           C  
ATOM   2984  CZ3 TRP A 460      -0.216 -25.301 -60.101  1.00 18.87           C  
ATOM   2985  CH2 TRP A 460      -0.725 -26.208 -59.158  1.00 22.80           C  
ATOM   2986  N   PRO A 461       4.161 -26.059 -65.354  1.00 23.55           N  
ATOM   2987  CA  PRO A 461       4.938 -25.340 -66.368  1.00 25.74           C  
ATOM   2988  C   PRO A 461       4.823 -23.829 -66.204  1.00 24.12           C  
ATOM   2989  O   PRO A 461       3.924 -23.363 -65.505  1.00 22.67           O  
ATOM   2990  CB  PRO A 461       4.308 -25.797 -67.695  1.00 28.05           C  
ATOM   2991  CG  PRO A 461       3.112 -26.667 -67.322  1.00 28.97           C  
ATOM   2992  CD  PRO A 461       2.841 -26.456 -65.865  1.00 27.13           C  
ATOM   2993  N   ASP A 462       5.731 -23.082 -66.828  1.00 23.41           N  
ATOM   2994  CA  ASP A 462       5.654 -21.627 -66.837  1.00 24.47           C  
ATOM   2995  C   ASP A 462       4.346 -21.184 -67.483  1.00 23.88           C  
ATOM   2996  O   ASP A 462       3.640 -20.320 -66.958  1.00 23.66           O  
ATOM   2997  CB  ASP A 462       6.854 -21.029 -67.574  1.00 25.63           C  
ATOM   2998  CG  ASP A 462       6.648 -19.577 -67.937  1.00 28.66           C  
ATOM   2999  OD1 ASP A 462       6.788 -18.713 -67.049  1.00 29.58           O  
ATOM   3000  OD2 ASP A 462       6.344 -19.298 -69.114  1.00 31.03           O  
ATOM   3001  N   GLY A 463       4.031 -21.790 -68.623  1.00 23.55           N  
ATOM   3002  CA  GLY A 463       2.728 -21.634 -69.240  1.00 24.13           C  
ATOM   3003  C   GLY A 463       2.597 -20.538 -70.276  1.00 25.30           C  
ATOM   3004  O   GLY A 463       1.512 -20.318 -70.817  1.00 23.51           O  
ATOM   3005  N   ALA A 464       3.690 -19.841 -70.556  1.00 22.44           N  
ATOM   3006  CA  ALA A 464       3.651 -18.795 -71.567  1.00 25.10           C  
ATOM   3007  C   ALA A 464       3.944 -19.368 -72.948  1.00 26.41           C  
ATOM   3008  O   ALA A 464       4.702 -20.329 -73.086  1.00 23.58           O  
ATOM   3009  CB  ALA A 464       4.629 -17.695 -71.236  1.00 25.85           C  
ATOM   3010  N   LYS A 465       3.328 -18.775 -73.965  1.00 28.54           N  
ATOM   3011  CA  LYS A 465       3.568 -19.170 -75.346  1.00 29.67           C  
ATOM   3012  C   LYS A 465       4.481 -18.150 -76.020  1.00 27.33           C  
ATOM   3013  O   LYS A 465       4.117 -16.984 -76.176  1.00 25.16           O  
ATOM   3014  CB  LYS A 465       2.244 -19.303 -76.102  1.00 34.15           C  
ATOM   3015  CG  LYS A 465       1.308 -20.359 -75.521  1.00 41.32           C  
ATOM   3016  CD  LYS A 465      -0.040 -20.366 -76.230  1.00 48.39           C  
ATOM   3017  CE  LYS A 465       0.124 -20.476 -77.738  1.00 52.65           C  
ATOM   3018  NZ  LYS A 465      -0.908 -21.359 -78.349  1.00 56.30           N  
ATOM   3019  N   ILE A 466       5.671 -18.599 -76.409  1.00 25.15           N  
ATOM   3020  CA  ILE A 466       6.691 -17.727 -76.985  1.00 27.35           C  
ATOM   3021  C   ILE A 466       6.189 -16.989 -78.227  1.00 28.51           C  
ATOM   3022  O   ILE A 466       6.519 -15.821 -78.439  1.00 28.24           O  
ATOM   3023  CB  ILE A 466       7.964 -18.536 -77.332  1.00 34.20           C  
ATOM   3024  CG1 ILE A 466       8.801 -18.759 -76.072  1.00 35.44           C  
ATOM   3025  CG2 ILE A 466       8.802 -17.833 -78.395  1.00 38.98           C  
ATOM   3026  CD1 ILE A 466       9.524 -17.519 -75.583  1.00 35.11           C  
ATOM   3027  N   GLU A 467       5.362 -17.664 -79.022  1.00 31.59           N  
ATOM   3028  CA  GLU A 467       4.840 -17.095 -80.264  1.00 35.93           C  
ATOM   3029  C   GLU A 467       4.109 -15.769 -80.037  1.00 30.50           C  
ATOM   3030  O   GLU A 467       4.079 -14.912 -80.921  1.00 29.31           O  
ATOM   3031  CB  GLU A 467       3.906 -18.093 -80.959  1.00 46.01           C  
ATOM   3032  CG  GLU A 467       2.460 -18.046 -80.479  1.00 61.15           C  
ATOM   3033  CD  GLU A 467       1.617 -19.182 -81.030  1.00 75.60           C  
ATOM   3034  OE1 GLU A 467       1.773 -20.328 -80.555  1.00 78.06           O  
ATOM   3035  OE2 GLU A 467       0.794 -18.926 -81.936  1.00 86.29           O  
ATOM   3036  N   TYR A 468       3.540 -15.598 -78.847  1.00 29.24           N  
ATOM   3037  CA  TYR A 468       2.808 -14.382 -78.510  1.00 28.84           C  
ATOM   3038  C   TYR A 468       3.740 -13.178 -78.397  1.00 31.01           C  
ATOM   3039  O   TYR A 468       3.309 -12.032 -78.552  1.00 32.84           O  
ATOM   3040  CB  TYR A 468       2.038 -14.561 -77.199  1.00 27.75           C  
ATOM   3041  CG  TYR A 468       0.822 -15.461 -77.288  1.00 25.52           C  
ATOM   3042  CD1 TYR A 468       0.227 -15.752 -78.510  1.00 29.17           C  
ATOM   3043  CD2 TYR A 468       0.256 -16.004 -76.140  1.00 23.71           C  
ATOM   3044  CE1 TYR A 468      -0.893 -16.570 -78.584  1.00 29.37           C  
ATOM   3045  CE2 TYR A 468      -0.857 -16.820 -76.205  1.00 24.57           C  
ATOM   3046  CZ  TYR A 468      -1.429 -17.099 -77.427  1.00 26.89           C  
ATOM   3047  OH  TYR A 468      -2.538 -17.912 -77.482  1.00 24.86           O  
ATOM   3048  N   PHE A 469       5.015 -13.443 -78.120  1.00 27.60           N  
ATOM   3049  CA  PHE A 469       5.995 -12.378 -77.918  1.00 30.15           C  
ATOM   3050  C   PHE A 469       6.682 -11.967 -79.213  1.00 32.31           C  
ATOM   3051  O   PHE A 469       7.511 -11.058 -79.218  1.00 31.06           O  
ATOM   3052  CB  PHE A 469       7.055 -12.807 -76.899  1.00 27.17           C  
ATOM   3053  CG  PHE A 469       6.557 -12.850 -75.484  1.00 25.83           C  
ATOM   3054  CD1 PHE A 469       5.935 -13.984 -74.991  1.00 24.84           C  
ATOM   3055  CD2 PHE A 469       6.713 -11.759 -74.644  1.00 27.50           C  
ATOM   3056  CE1 PHE A 469       5.475 -14.031 -73.688  1.00 25.92           C  
ATOM   3057  CE2 PHE A 469       6.256 -11.800 -73.337  1.00 28.35           C  
ATOM   3058  CZ  PHE A 469       5.638 -12.937 -72.861  1.00 27.20           C  
ATOM   3059  N   LEU A 470       6.343 -12.636 -80.309  1.00 34.02           N  
ATOM   3060  CA  LEU A 470       7.012 -12.392 -81.582  1.00 38.19           C  
ATOM   3061  C   LEU A 470       6.393 -11.221 -82.341  1.00 42.53           C  
ATOM   3062  O   LEU A 470       5.243 -10.847 -82.114  1.00 43.37           O  
ATOM   3063  CB  LEU A 470       6.982 -13.657 -82.443  1.00 39.24           C  
ATOM   3064  CG  LEU A 470       7.791 -14.836 -81.896  1.00 40.96           C  
ATOM   3065  CD1 LEU A 470       7.935 -15.929 -82.944  1.00 43.18           C  
ATOM   3066  CD2 LEU A 470       9.156 -14.373 -81.401  1.00 39.71           C  
ATOM   3067  OXT LEU A 470       7.037 -10.619 -83.203  1.00 46.70           O  
TER    3068      LEU A 470                                                      
HETATM 3069  C1  NAG B   1      39.688  -1.330 -58.392  1.00 26.43           C  
HETATM 3070  C2  NAG B   1      40.644  -0.797 -59.475  1.00 29.82           C  
HETATM 3071  C3  NAG B   1      41.639   0.213 -58.889  1.00 29.05           C  
HETATM 3072  C4  NAG B   1      40.938   1.258 -58.030  1.00 28.90           C  
HETATM 3073  C5  NAG B   1      40.073   0.550 -56.996  1.00 27.59           C  
HETATM 3074  C6  NAG B   1      39.297   1.487 -56.100  1.00 28.19           C  
HETATM 3075  C7  NAG B   1      41.304  -2.171 -61.409  1.00 36.24           C  
HETATM 3076  C8  NAG B   1      42.111  -3.350 -61.864  1.00 36.55           C  
HETATM 3077  N2  NAG B   1      41.357  -1.898 -60.100  1.00 31.33           N  
HETATM 3078  O3  NAG B   1      42.323   0.853 -59.960  1.00 27.95           O  
HETATM 3079  O4  NAG B   1      41.905   2.078 -57.383  1.00 34.67           O  
HETATM 3080  O5  NAG B   1      39.109  -0.248 -57.688  1.00 26.75           O  
HETATM 3081  O6  NAG B   1      38.504   2.390 -56.857  1.00 26.85           O  
HETATM 3082  O7  NAG B   1      40.637  -1.497 -62.188  1.00 40.91           O  
HETATM 3083  C1  NAG B   2      41.666   3.476 -57.664  1.00 30.12           C  
HETATM 3084  C2  NAG B   2      42.251   4.336 -56.553  1.00 28.93           C  
HETATM 3085  C3  NAG B   2      41.908   5.802 -56.796  1.00 28.16           C  
HETATM 3086  C4  NAG B   2      42.349   6.230 -58.193  1.00 31.30           C  
HETATM 3087  C5  NAG B   2      41.792   5.262 -59.239  1.00 31.57           C  
HETATM 3088  C6  NAG B   2      42.295   5.533 -60.638  1.00 34.40           C  
HETATM 3089  C7  NAG B   2      42.431   3.051 -54.468  1.00 32.26           C  
HETATM 3090  C8  NAG B   2      41.786   2.729 -53.153  1.00 28.36           C  
HETATM 3091  N2  NAG B   2      41.770   3.911 -55.247  1.00 29.67           N  
HETATM 3092  O3  NAG B   2      42.521   6.618 -55.805  1.00 28.90           O  
HETATM 3093  O4  NAG B   2      41.849   7.536 -58.453  1.00 28.79           O  
HETATM 3094  O5  NAG B   2      42.170   3.913 -58.920  1.00 31.16           O  
HETATM 3095  O6  NAG B   2      43.704   5.368 -60.727  1.00 36.52           O  
HETATM 3096  O7  NAG B   2      43.499   2.549 -54.808  1.00 32.29           O  
HETATM 3097  C1  BMA B   3      42.886   8.489 -58.756  1.00 30.04           C  
HETATM 3098  C2  BMA B   3      42.186   9.630 -59.492  1.00 32.13           C  
HETATM 3099  C3  BMA B   3      43.101  10.834 -59.696  1.00 31.43           C  
HETATM 3100  C4  BMA B   3      43.946  11.159 -58.463  1.00 32.33           C  
HETATM 3101  C5  BMA B   3      44.596   9.902 -57.888  1.00 32.78           C  
HETATM 3102  C6  BMA B   3      45.309  10.208 -56.597  1.00 30.45           C  
HETATM 3103  O2  BMA B   3      41.082  10.102 -58.728  1.00 32.61           O  
HETATM 3104  O3  BMA B   3      42.315  11.971 -60.023  1.00 31.56           O  
HETATM 3105  O4  BMA B   3      44.973  12.086 -58.806  1.00 32.95           O  
HETATM 3106  O5  BMA B   3      43.570   8.934 -57.612  1.00 30.14           O  
HETATM 3107  O6  BMA B   3      46.078   9.077 -56.221  1.00 32.47           O  
HETATM 3108  C1  MAN B   4      42.929  12.649 -61.129  1.00 31.03           C  
HETATM 3109  C2  MAN B   4      42.251  13.978 -61.377  1.00 31.37           C  
HETATM 3110  C3  MAN B   4      40.832  13.680 -61.878  1.00 29.22           C  
HETATM 3111  C4  MAN B   4      40.904  12.868 -63.178  1.00 33.10           C  
HETATM 3112  C5  MAN B   4      41.671  11.561 -62.914  1.00 36.06           C  
HETATM 3113  C6  MAN B   4      41.930  10.754 -64.172  1.00 39.40           C  
HETATM 3114  O2  MAN B   4      42.962  14.568 -62.455  1.00 33.18           O  
HETATM 3115  O3  MAN B   4      40.006  14.841 -62.039  1.00 26.58           O  
HETATM 3116  O4  MAN B   4      39.596  12.567 -63.641  1.00 33.96           O  
HETATM 3117  O5  MAN B   4      42.963  11.858 -62.303  1.00 32.29           O  
HETATM 3118  O6  MAN B   4      42.222   9.419 -63.776  1.00 43.13           O  
HETATM 3119  C1  MAN B   5      42.724  15.967 -62.665  1.00 34.49           C  
HETATM 3120  C2  MAN B   5      43.637  16.368 -63.821  1.00 34.99           C  
HETATM 3121  C3  MAN B   5      45.060  16.525 -63.304  1.00 34.99           C  
HETATM 3122  C4  MAN B   5      45.092  17.511 -62.128  1.00 35.40           C  
HETATM 3123  C5  MAN B   5      44.180  17.001 -61.005  1.00 35.77           C  
HETATM 3124  C6  MAN B   5      44.076  17.974 -59.846  1.00 36.32           C  
HETATM 3125  O2  MAN B   5      43.260  17.634 -64.331  1.00 34.11           O  
HETATM 3126  O3  MAN B   5      45.957  16.937 -64.327  1.00 33.73           O  
HETATM 3127  O4  MAN B   5      46.416  17.634 -61.633  1.00 36.28           O  
HETATM 3128  O5  MAN B   5      42.840  16.794 -61.522  1.00 35.71           O  
HETATM 3129  O6  MAN B   5      43.668  19.235 -60.357  1.00 36.14           O  
HETATM 3130  C1  MAN B   6      42.618  17.485 -65.607  1.00 32.64           C  
HETATM 3131  C2  MAN B   6      42.393  18.895 -66.116  1.00 36.29           C  
HETATM 3132  C3  MAN B   6      41.309  19.533 -65.259  1.00 36.16           C  
HETATM 3133  C4  MAN B   6      40.023  18.709 -65.316  1.00 33.56           C  
HETATM 3134  C5  MAN B   6      40.306  17.297 -64.814  1.00 35.60           C  
HETATM 3135  C6  MAN B   6      39.109  16.366 -64.946  1.00 35.67           C  
HETATM 3136  O2  MAN B   6      41.891  18.904 -67.456  1.00 35.07           O  
HETATM 3137  O3  MAN B   6      41.039  20.843 -65.665  1.00 36.98           O  
HETATM 3138  O4  MAN B   6      39.032  19.309 -64.492  1.00 29.73           O  
HETATM 3139  O5  MAN B   6      41.422  16.721 -65.563  1.00 35.86           O  
HETATM 3140  O6  MAN B   6      38.598  16.469 -66.272  1.00 36.81           O  
HETATM 3141  C1  MAN B   7      47.434   9.249 -56.665  1.00 35.38           C  
HETATM 3142  C2  MAN B   7      48.199   7.972 -56.323  1.00 36.73           C  
HETATM 3143  C3  MAN B   7      48.437   7.903 -54.815  1.00 37.78           C  
HETATM 3144  C4  MAN B   7      49.065   9.206 -54.284  1.00 34.99           C  
HETATM 3145  C5  MAN B   7      48.192  10.401 -54.686  1.00 36.75           C  
HETATM 3146  C6  MAN B   7      48.782  11.742 -54.301  1.00 42.95           C  
HETATM 3147  O2  MAN B   7      49.494   7.963 -56.920  1.00 36.99           O  
HETATM 3148  O3  MAN B   7      49.251   6.792 -54.477  1.00 41.81           O  
HETATM 3149  O4  MAN B   7      49.160   9.144 -52.872  1.00 33.71           O  
HETATM 3150  O5  MAN B   7      48.036  10.398 -56.125  1.00 35.22           O  
HETATM 3151  O6  MAN B   7      50.131  11.742 -54.745  1.00 48.19           O  
HETATM 3152  C1  MAN B   8      48.516   5.875 -53.646  1.00 44.85           C  
HETATM 3153  C2  MAN B   8      49.522   4.902 -53.035  1.00 48.09           C  
HETATM 3154  C3  MAN B   8      50.060   3.995 -54.138  1.00 50.62           C  
HETATM 3155  C4  MAN B   8      48.905   3.298 -54.875  1.00 50.32           C  
HETATM 3156  C5  MAN B   8      47.923   4.349 -55.420  1.00 46.58           C  
HETATM 3157  C6  MAN B   8      46.684   3.738 -56.046  1.00 46.44           C  
HETATM 3158  O2  MAN B   8      48.897   4.032 -52.082  1.00 48.13           O  
HETATM 3159  O3  MAN B   8      50.976   3.035 -53.632  1.00 53.47           O  
HETATM 3160  O4  MAN B   8      49.412   2.528 -55.953  1.00 51.06           O  
HETATM 3161  O5  MAN B   8      47.488   5.208 -54.339  1.00 43.37           O  
HETATM 3162  O6  MAN B   8      46.087   4.717 -56.893  1.00 45.96           O  
HETATM 3163  C1  MAN B   9      50.743  13.028 -54.548  1.00 54.05           C  
HETATM 3164  C2  MAN B   9      52.090  12.972 -55.225  1.00 55.96           C  
HETATM 3165  C3  MAN B   9      52.878  11.860 -54.563  1.00 56.13           C  
HETATM 3166  C4  MAN B   9      53.009  12.100 -53.041  1.00 56.25           C  
HETATM 3167  C5  MAN B   9      51.642  12.436 -52.381  1.00 61.09           C  
HETATM 3168  C6  MAN B   9      51.793  13.074 -51.007  1.00 65.06           C  
HETATM 3169  O2  MAN B   9      52.842  14.170 -54.991  1.00 56.56           O  
HETATM 3170  O3  MAN B   9      54.163  11.706 -55.151  1.00 57.94           O  
HETATM 3171  O4  MAN B   9      53.537  10.936 -52.427  1.00 54.65           O  
HETATM 3172  O5  MAN B   9      50.875  13.362 -53.196  1.00 57.20           O  
HETATM 3173  O6  MAN B   9      51.437  12.110 -50.021  1.00 67.26           O  
HETATM 3174  C1  NAG A 501      18.154  -6.983 -80.469  1.00 38.03           C  
HETATM 3175  C2  NAG A 501      17.291  -6.788 -81.712  1.00 44.08           C  
HETATM 3176  C3  NAG A 501      18.003  -7.358 -82.934  1.00 50.47           C  
HETATM 3177  C4  NAG A 501      19.385  -6.736 -83.076  1.00 53.65           C  
HETATM 3178  C5  NAG A 501      20.176  -6.906 -81.780  1.00 51.51           C  
HETATM 3179  C6  NAG A 501      21.499  -6.178 -81.806  1.00 52.99           C  
HETATM 3180  C7  NAG A 501      14.848  -6.688 -81.496  1.00 45.51           C  
HETATM 3181  C8  NAG A 501      13.585  -7.480 -81.335  1.00 45.45           C  
HETATM 3182  N2  NAG A 501      15.981  -7.397 -81.553  1.00 43.03           N  
HETATM 3183  O3  NAG A 501      17.228  -7.100 -84.099  1.00 51.80           O  
HETATM 3184  O4  NAG A 501      20.090  -7.355 -84.146  1.00 57.23           O  
HETATM 3185  O5  NAG A 501      19.435  -6.373 -80.671  1.00 46.24           O  
HETATM 3186  O6  NAG A 501      22.423  -6.751 -80.891  1.00 56.38           O  
HETATM 3187  O7  NAG A 501      14.843  -5.463 -81.568  1.00 47.06           O  
HETATM 3188 CA    CA A 511      28.973 -29.508 -62.223  1.00 30.03          CA  
HETATM 3189  O   HOH A 601      22.967 -15.903 -68.475  1.00 32.44           O  
HETATM 3190  O   HOH A 602      15.845 -18.500 -38.286  1.00 41.03           O  
HETATM 3191  O   HOH A 603      24.078 -14.264 -59.801  1.00 40.96           O  
HETATM 3192  O   HOH A 604      38.039 -31.319 -58.774  1.00 29.45           O  
HETATM 3193  O   HOH A 605      25.641  -0.199 -70.235  1.00 47.86           O  
HETATM 3194  O   HOH A 606      28.284  -3.173 -54.482  1.00 22.00           O  
HETATM 3195  O   HOH A 607      16.332  -5.814 -47.261  1.00 33.68           O  
HETATM 3196  O   HOH A 608      19.391  -7.166 -31.158  1.00 42.24           O  
HETATM 3197  O   HOH A 609      10.417 -32.915 -32.672  1.00 34.22           O  
HETATM 3198  O   HOH A 610      34.533 -36.467 -45.405  1.00 38.46           O  
HETATM 3199  O   HOH A 611       9.059 -14.538 -61.532  1.00 27.20           O  
HETATM 3200  O   HOH A 612      11.762 -21.374 -35.158  1.00 34.53           O  
HETATM 3201  O   HOH A 613       9.296 -22.420 -77.007  1.00 41.70           O  
HETATM 3202  O   HOH A 614      14.130  -3.197 -61.833  1.00 25.59           O  
HETATM 3203  O   HOH A 615      19.929 -45.577 -48.159  1.00 36.07           O  
HETATM 3204  O   HOH A 616      17.011 -12.307 -67.122  1.00 24.69           O  
HETATM 3205  O   HOH A 617      20.330  -5.721 -67.087  1.00 28.74           O  
HETATM 3206  O   HOH A 618      31.739   1.147 -43.734  1.00 28.36           O  
HETATM 3207  O   HOH A 619      21.069 -39.507 -69.860  1.00 45.73           O  
HETATM 3208  O   HOH A 620      18.600 -29.800 -57.214  1.00 29.70           O  
HETATM 3209  O   HOH A 621      34.723 -34.257 -64.370  1.00 38.41           O  
HETATM 3210  O   HOH A 622      17.180  -3.360 -48.184  1.00 37.93           O  
HETATM 3211  O   HOH A 623       5.671  -9.852 -36.514  1.00 48.16           O  
HETATM 3212  O   HOH A 624      45.915  14.321 -58.064  1.00 45.19           O  
HETATM 3213  O   HOH A 625       3.812 -28.883 -70.628  1.00 39.66           O  
HETATM 3214  O   HOH A 626      14.696 -40.690 -47.705  1.00 42.95           O  
HETATM 3215  O   HOH A 627      30.465 -19.374 -61.706  1.00 56.25           O  
HETATM 3216  O   HOH A 628       9.933 -39.029 -45.629  1.00 31.95           O  
HETATM 3217  O   HOH A 629       5.496 -29.240 -66.635  1.00 22.13           O  
HETATM 3218  O   HOH A 630      11.482  -7.709 -45.333  1.00 29.73           O  
HETATM 3219  O   HOH A 631      22.799 -26.648 -66.439  1.00 23.88           O  
HETATM 3220  O   HOH A 632      19.157  -4.509 -71.200  1.00 33.68           O  
HETATM 3221  O   HOH A 633      44.987   6.831 -55.095  1.00 28.69           O  
HETATM 3222  O   HOH A 634       3.934 -19.240 -45.615  1.00 39.70           O  
HETATM 3223  O   HOH A 635       0.659 -18.621 -53.139  1.00 23.67           O  
HETATM 3224  O   HOH A 636      20.599 -28.504 -41.032  1.00 43.28           O  
HETATM 3225  O   HOH A 637      10.757 -25.727 -30.548  1.00 47.90           O  
HETATM 3226  O   HOH A 638      19.311 -14.166 -27.914  1.00 45.97           O  
HETATM 3227  O   HOH A 639       5.286 -14.525 -36.608  1.00 42.31           O  
HETATM 3228  O   HOH A 640      16.071 -21.954 -45.451  1.00 26.04           O  
HETATM 3229  O   HOH A 641      10.584 -31.055 -34.761  1.00 32.08           O  
HETATM 3230  O   HOH A 642      28.621 -48.140 -49.052  1.00 42.61           O  
HETATM 3231  O   HOH A 643       0.603 -13.894 -60.367  1.00 23.64           O  
HETATM 3232  O   HOH A 644      12.444 -17.846 -44.835  1.00 21.77           O  
HETATM 3233  O   HOH A 645      21.205 -13.962 -65.182  1.00 29.18           O  
HETATM 3234  O   HOH A 646      17.951 -18.757 -57.513  1.00 17.46           O  
HETATM 3235  O   HOH A 647      34.559 -18.933 -33.711  1.00 50.13           O  
HETATM 3236  O   HOH A 648      38.815  10.356 -60.008  1.00 45.96           O  
HETATM 3237  O   HOH A 649      16.178 -36.271 -38.340  1.00 35.09           O  
HETATM 3238  O   HOH A 650       1.670 -29.667 -68.770  1.00 30.89           O  
HETATM 3239  O   HOH A 651      12.443 -35.370 -39.628  1.00 36.06           O  
HETATM 3240  O   HOH A 652       3.775  -9.540 -83.874  1.00 49.20           O  
HETATM 3241  O   HOH A 653      24.164 -37.356 -55.317  1.00 26.97           O  
HETATM 3242  O   HOH A 654      39.543 -23.039 -48.806  1.00 35.66           O  
HETATM 3243  O   HOH A 655      23.457   2.634 -42.137  1.00 32.61           O  
HETATM 3244  O   HOH A 656      23.675 -48.527 -55.796  1.00 34.73           O  
HETATM 3245  O   HOH A 657      45.075   1.141 -53.222  1.00 44.79           O  
HETATM 3246  O   HOH A 658      21.773 -44.640 -64.781  1.00 45.05           O  
HETATM 3247  O   HOH A 659       7.605 -40.756 -47.640  1.00 24.23           O  
HETATM 3248  O   HOH A 660      11.747  -7.936 -48.105  1.00 27.66           O  
HETATM 3249  O   HOH A 661      11.396 -36.927 -71.614  1.00 56.46           O  
HETATM 3250  O   HOH A 662       7.955 -23.767 -44.150  1.00 24.61           O  
HETATM 3251  O   HOH A 663      24.580 -12.552 -62.073  1.00 35.63           O  
HETATM 3252  O   HOH A 664      31.109 -29.871 -63.471  1.00 23.28           O  
HETATM 3253  O   HOH A 665      40.277 -34.269 -56.045  1.00 35.55           O  
HETATM 3254  O   HOH A 666      19.545 -31.203 -42.136  1.00 54.00           O  
HETATM 3255  O   HOH A 667      17.963 -26.598 -60.351  1.00 21.64           O  
HETATM 3256  O   HOH A 668       4.426 -17.523 -66.811  1.00 23.37           O  
HETATM 3257  O   HOH A 669       6.063 -16.284 -41.821  1.00 29.13           O  
HETATM 3258  O   HOH A 670      21.394 -10.750 -37.650  1.00 25.41           O  
HETATM 3259  O   HOH A 671       5.065 -19.620 -62.794  1.00 22.16           O  
HETATM 3260  O   HOH A 672      16.834   3.019 -45.719  1.00 46.34           O  
HETATM 3261  O   HOH A 673      10.242 -11.726 -47.139  1.00 23.37           O  
HETATM 3262  O   HOH A 674      15.380 -48.207 -55.093  1.00 39.83           O  
HETATM 3263  O   HOH A 675      25.672  -3.720 -53.598  1.00 23.31           O  
HETATM 3264  O   HOH A 676      30.911 -34.387 -63.627  1.00 23.22           O  
HETATM 3265  O   HOH A 677       6.287  -4.903 -52.583  1.00 30.05           O  
HETATM 3266  O   HOH A 678      28.625 -44.712 -48.014  1.00 33.76           O  
HETATM 3267  O   HOH A 679      -0.501 -16.844 -59.784  1.00 36.18           O  
HETATM 3268  O   HOH A 680      38.823  21.858 -63.713  1.00 25.58           O  
HETATM 3269  O   HOH A 681      27.924 -30.887 -63.962  1.00 28.04           O  
HETATM 3270  O   HOH A 682       4.132 -21.208 -43.901  1.00 36.33           O  
HETATM 3271  O   HOH A 683       9.744 -12.773 -63.662  1.00 30.60           O  
HETATM 3272  O   HOH A 684       4.411  -9.427 -79.999  1.00 36.84           O  
HETATM 3273  O   HOH A 685      29.577 -41.889 -45.562  1.00 44.07           O  
HETATM 3274  O   HOH A 686      25.762 -16.828 -58.983  1.00 41.31           O  
HETATM 3275  O   HOH A 687      35.971 -10.801 -35.773  1.00 45.33           O  
HETATM 3276  O   HOH A 688       4.173 -32.427 -36.665  1.00 46.96           O  
HETATM 3277  O   HOH A 689      22.671  -8.148 -67.334  1.00 43.85           O  
HETATM 3278  O   HOH A 690      47.098  11.191 -60.197  1.00 46.05           O  
HETATM 3279  O   HOH A 691      26.507  -7.562 -34.431  1.00 32.59           O  
HETATM 3280  O   HOH A 692       5.702 -32.264 -44.383  1.00 21.57           O  
HETATM 3281  O   HOH A 693      43.056 -11.410 -51.164  1.00 44.55           O  
HETATM 3282  O   HOH A 694       9.547 -11.529 -66.135  1.00 33.24           O  
HETATM 3283  O   HOH A 695      24.662 -31.204 -71.932  1.00 46.00           O  
HETATM 3284  O   HOH A 696      27.444 -30.016 -58.426  1.00 24.68           O  
HETATM 3285  O   HOH A 697      -0.805  -8.506 -76.126  1.00 55.21           O  
HETATM 3286  O   HOH A 698       8.166 -43.907 -49.127  1.00 37.87           O  
HETATM 3287  O   HOH A 699      15.787 -23.717 -68.562  1.00 22.81           O  
HETATM 3288  O   HOH A 700      18.265  -6.449 -34.522  1.00 35.82           O  
HETATM 3289  O   HOH A 701      13.363  -0.045 -51.529  1.00 34.91           O  
HETATM 3290  O   HOH A 702      24.648 -25.421 -33.057  1.00 43.02           O  
HETATM 3291  O   HOH A 703       5.079 -39.310 -54.257  1.00 27.98           O  
HETATM 3292  O   HOH A 704      24.189 -34.847 -56.180  1.00 21.99           O  
HETATM 3293  O   HOH A 705      27.846 -42.567 -64.689  1.00 37.79           O  
HETATM 3294  O   HOH A 706      18.562 -21.060 -49.583  1.00 23.86           O  
HETATM 3295  O   HOH A 707      27.116 -13.527 -62.226  1.00 43.54           O  
HETATM 3296  O   HOH A 708       0.808 -31.984 -55.062  1.00 22.35           O  
HETATM 3297  O   HOH A 709      33.122 -26.420 -33.904  1.00 38.48           O  
HETATM 3298  O   HOH A 710      27.841 -38.890 -55.297  1.00 23.45           O  
HETATM 3299  O   HOH A 711      37.771  -8.191 -48.588  1.00 32.23           O  
HETATM 3300  O   HOH A 712      32.159 -43.920 -52.844  1.00 32.68           O  
HETATM 3301  O   HOH A 713      17.624  -4.966 -44.885  1.00 33.54           O  
HETATM 3302  O   HOH A 714      19.486 -13.663 -67.539  1.00 24.34           O  
HETATM 3303  O   HOH A 715      40.451 -19.015 -58.485  1.00 30.61           O  
HETATM 3304  O   HOH A 716      37.589 -24.468 -55.002  1.00 28.01           O  
HETATM 3305  O   HOH A 717      41.362  -7.694 -53.932  1.00 46.94           O  
HETATM 3306  O   HOH A 718      27.674 -18.041 -30.862  1.00 40.82           O  
HETATM 3307  O   HOH A 719      20.813 -37.733 -46.158  1.00 23.14           O  
HETATM 3308  O   HOH A 720      27.994 -36.937 -69.282  1.00 31.84           O  
HETATM 3309  O   HOH A 721       8.271  -7.914 -42.197  1.00 38.55           O  
HETATM 3310  O   HOH A 722      38.193 -26.911 -51.083  1.00 54.88           O  
HETATM 3311  O   HOH A 723      38.733 -39.343 -56.176  1.00 38.10           O  
HETATM 3312  O   HOH A 724      36.536 -40.802 -49.530  1.00 48.36           O  
HETATM 3313  O   HOH A 725      15.319 -19.260 -50.786  1.00 19.29           O  
HETATM 3314  O   HOH A 726      51.364  16.317 -54.113  1.00 46.31           O  
HETATM 3315  O   HOH A 727      37.605  -2.766 -63.379  1.00 29.66           O  
HETATM 3316  O   HOH A 728      35.426 -30.174 -58.944  1.00 25.27           O  
HETATM 3317  O   HOH A 729      39.951  -3.122 -55.058  1.00 30.28           O  
HETATM 3318  O   HOH A 730      29.325 -19.173 -53.785  1.00 30.61           O  
HETATM 3319  O   HOH A 731      -0.966 -37.348 -61.275  1.00 22.61           O  
HETATM 3320  O   HOH A 732      39.843 -34.890 -50.787  1.00 32.32           O  
HETATM 3321  O   HOH A 733      20.587  -1.293 -60.886  1.00 21.98           O  
HETATM 3322  O   HOH A 734       3.444 -37.220 -54.545  1.00 28.54           O  
HETATM 3323  O   HOH A 735      -3.588 -18.821 -75.097  1.00 35.72           O  
HETATM 3324  O   HOH A 736      39.626 -27.518 -54.726  1.00 31.52           O  
HETATM 3325  O   HOH A 737      11.676 -11.441 -81.334  1.00 44.69           O  
HETATM 3326  O   HOH A 738      22.137  -1.021 -52.926  1.00 35.99           O  
HETATM 3327  O   HOH A 739      27.912  -3.496 -68.032  1.00 52.70           O  
HETATM 3328  O   HOH A 740      36.871 -43.344 -57.004  1.00 36.55           O  
HETATM 3329  O   HOH A 741      30.570  -7.550 -63.544  1.00 26.02           O  
HETATM 3330  O   HOH A 742       3.513  -0.850 -71.074  1.00 36.94           O  
HETATM 3331  O   HOH A 743      36.583 -18.854 -64.328  1.00 51.82           O  
HETATM 3332  O   HOH A 744      24.431 -44.217 -44.474  1.00 34.41           O  
HETATM 3333  O   HOH A 745      29.743 -28.495 -34.556  1.00 49.89           O  
HETATM 3334  O   HOH A 746       6.360  -6.687 -69.894  1.00 26.42           O  
HETATM 3335  O   HOH A 747      11.906 -14.158 -84.028  1.00 43.52           O  
HETATM 3336  O   HOH A 748      22.784  -2.886 -37.898  1.00 39.60           O  
HETATM 3337  O   HOH A 749      38.470 -17.252 -38.950  1.00 50.70           O  
HETATM 3338  O   HOH A 750      19.714 -13.792 -56.500  1.00 23.83           O  
HETATM 3339  O   HOH A 751       2.146   0.610 -69.269  1.00 41.54           O  
HETATM 3340  O   HOH A 752       9.356 -31.057 -44.032  1.00 23.80           O  
HETATM 3341  O   HOH A 753       3.509 -11.725 -49.595  1.00 26.23           O  
HETATM 3342  O   HOH A 754      39.902 -30.743 -49.654  1.00 54.82           O  
HETATM 3343  O   HOH A 755      38.302 -39.248 -52.532  1.00 54.44           O  
HETATM 3344  O   HOH A 756      29.253 -28.269 -38.887  1.00 31.19           O  
HETATM 3345  O   HOH A 757      41.669 -10.841 -61.748  1.00 51.01           O  
HETATM 3346  O   HOH A 758      35.500 -28.396 -39.375  1.00 47.38           O  
HETATM 3347  O   HOH A 759       5.257  -5.929 -46.961  1.00 48.90           O  
HETATM 3348  O   HOH A 760      19.716 -27.509 -49.622  1.00 26.49           O  
HETATM 3349  O   HOH A 761      42.091 -21.788 -60.185  1.00 41.75           O  
HETATM 3350  O   HOH A 762      19.851 -32.466 -55.157  1.00 22.62           O  
HETATM 3351  O   HOH A 763      10.602 -37.756 -40.437  1.00 39.98           O  
HETATM 3352  O   HOH A 764      50.197   0.455 -52.907  1.00 58.25           O  
HETATM 3353  O   HOH A 765      32.713  -2.791 -56.454  1.00 23.52           O  
HETATM 3354  O   HOH A 766      13.769  -8.100 -76.647  1.00 27.80           O  
HETATM 3355  O   HOH A 767      29.529 -31.465 -44.486  1.00 39.01           O  
HETATM 3356  O   HOH A 768      35.089 -23.034 -54.593  1.00 25.36           O  
HETATM 3357  O   HOH A 769      38.663 -22.738 -42.200  1.00 38.89           O  
HETATM 3358  O   HOH A 770       9.346 -28.810 -31.699  1.00 47.03           O  
HETATM 3359  O   HOH A 771       3.652 -26.502 -71.163  1.00 50.49           O  
HETATM 3360  O   HOH A 772      23.741 -47.590 -62.544  1.00 35.23           O  
HETATM 3361  O   HOH A 773      11.461 -14.103 -60.792  1.00 25.54           O  
HETATM 3362  O   HOH A 774      43.017  -3.379 -58.252  1.00 50.04           O  
HETATM 3363  O   HOH A 775      42.452 -14.817 -58.524  1.00 47.30           O  
HETATM 3364  O   HOH A 776      46.217   5.975 -59.395  1.00 50.27           O  
HETATM 3365  O   HOH A 777       7.723  -7.570 -45.699  1.00 46.07           O  
HETATM 3366  O   HOH A 778      16.467 -17.128 -40.943  1.00 25.60           O  
HETATM 3367  O   HOH A 779       9.820 -12.433 -34.596  1.00 41.16           O  
HETATM 3368  O   HOH A 780      34.768 -16.619 -62.017  1.00 38.84           O  
HETATM 3369  O   HOH A 781      23.274 -25.302 -55.422  1.00 21.46           O  
HETATM 3370  O   HOH A 782      18.079 -15.677 -35.678  1.00 21.89           O  
HETATM 3371  O   HOH A 783       0.412 -39.937 -43.919  1.00 42.04           O  
HETATM 3372  O   HOH A 784       4.041 -31.986 -58.382  1.00 24.86           O  
HETATM 3373  O   HOH A 785      33.102 -41.845 -51.367  1.00 37.93           O  
HETATM 3374  O   HOH A 786      -0.056 -11.810 -53.973  1.00 32.32           O  
HETATM 3375  O   HOH A 787      11.122  -6.880 -40.520  1.00 43.84           O  
HETATM 3376  O   HOH A 788      15.119  -4.131 -78.553  1.00 33.84           O  
HETATM 3377  O   HOH A 789      -1.073 -12.600 -72.021  1.00 28.82           O  
HETATM 3378  O   HOH A 790      29.404 -31.286 -39.462  1.00 50.33           O  
HETATM 3379  O   HOH A 791      21.246  -8.789 -77.922  1.00 41.33           O  
HETATM 3380  O   HOH A 792       0.145 -22.133 -72.495  1.00 49.90           O  
HETATM 3381  O   HOH A 793      31.113 -33.629 -43.867  1.00 49.61           O  
HETATM 3382  O   HOH A 794       5.541 -20.517 -34.305  1.00 49.03           O  
HETATM 3383  O   HOH A 795      10.459 -33.262 -36.701  1.00 38.94           O  
HETATM 3384  O   HOH A 796      37.927 -22.363 -51.311  1.00 25.39           O  
HETATM 3385  O   HOH A 797      19.740 -31.109 -61.699  1.00 20.48           O  
HETATM 3386  O   HOH A 798      20.897  -1.126 -39.627  1.00 26.88           O  
HETATM 3387  O   HOH A 799      22.857 -19.342 -45.487  1.00 35.27           O  
HETATM 3388  O   HOH A 800       7.165 -41.584 -44.004  1.00 35.93           O  
HETATM 3389  O   HOH A 801      23.867  -3.990 -60.485  1.00 24.50           O  
HETATM 3390  O   HOH A 802      17.008 -33.733 -72.678  1.00 50.37           O  
HETATM 3391  O   HOH A 803      14.222 -15.453 -43.813  1.00 23.29           O  
HETATM 3392  O   HOH A 804       2.946 -12.518 -82.302  1.00 50.79           O  
HETATM 3393  O   HOH A 805      15.197 -32.792 -38.951  1.00 32.23           O  
HETATM 3394  O   HOH A 806      36.153  -9.221 -44.872  1.00 34.20           O  
HETATM 3395  O   HOH A 807      34.112 -33.970 -44.708  1.00 39.09           O  
HETATM 3396  O   HOH A 808       8.413 -24.009 -67.952  1.00 34.94           O  
HETATM 3397  O   HOH A 809      15.769 -17.897 -43.574  1.00 25.40           O  
HETATM 3398  O   HOH A 810      35.472  -9.381 -58.118  1.00 25.18           O  
HETATM 3399  O   HOH A 811      32.279 -31.816 -69.946  1.00 44.26           O  
HETATM 3400  O   HOH A 812       4.689 -27.300 -39.144  1.00 48.53           O  
HETATM 3401  O   HOH A 813      39.164   7.771 -59.401  1.00 39.81           O  
HETATM 3402  O   HOH A 814       5.890  -3.535 -70.370  1.00 30.19           O  
HETATM 3403  O   HOH A 815      39.997 -16.934 -48.492  1.00 28.34           O  
HETATM 3404  O   HOH A 816       3.679 -34.757 -62.092  1.00 44.05           O  
HETATM 3405  O   HOH A 817      44.742   2.278 -59.394  1.00 46.43           O  
HETATM 3406  O   HOH A 818      44.857   0.947 -56.762  1.00 43.47           O  
HETATM 3407  O   HOH A 819      32.053 -47.854 -52.127  1.00 36.94           O  
HETATM 3408  O   HOH A 820      -2.039 -39.476 -47.147  1.00 37.61           O  
HETATM 3409  O   HOH A 821       6.206 -39.041 -61.643  1.00 48.93           O  
HETATM 3410  O   HOH A 822      16.390  -3.814 -36.003  1.00 47.28           O  
HETATM 3411  O   HOH A 823      31.176 -27.578 -37.451  1.00 26.33           O  
HETATM 3412  O   HOH A 824      30.459  -1.675 -57.621  1.00 22.82           O  
HETATM 3413  O   HOH A 825      24.134 -18.692 -33.242  1.00 23.22           O  
HETATM 3414  O   HOH A 826      31.986 -43.804 -58.071  1.00 43.23           O  
HETATM 3415  O   HOH A 827      19.645 -11.799 -74.492  1.00 30.94           O  
HETATM 3416  O   HOH A 828      31.268 -19.209 -30.868  1.00 54.60           O  
HETATM 3417  O   HOH A 829      21.851 -21.632 -29.331  1.00 41.17           O  
HETATM 3418  O   HOH A 830       5.169 -23.712 -70.461  1.00 29.39           O  
HETATM 3419  O   HOH A 831      27.169  -8.027 -69.319  1.00 52.70           O  
HETATM 3420  O   HOH A 832      -1.289 -10.856 -69.691  1.00 27.39           O  
HETATM 3421  O   HOH A 833      29.517 -30.805 -69.337  1.00 46.71           O  
HETATM 3422  O   HOH A 834      31.705 -44.944 -48.678  1.00 54.93           O  
HETATM 3423  O   HOH A 835       0.008  -8.972 -53.951  1.00 46.86           O  
HETATM 3424  O   HOH A 836       1.174 -30.838 -57.724  1.00 24.08           O  
HETATM 3425  O   HOH A 837      36.898 -37.472 -59.886  1.00 47.66           O  
HETATM 3426  O   HOH A 838      39.079 -19.466 -49.319  1.00 35.34           O  
HETATM 3427  O   HOH A 839       2.910 -23.623 -32.714  1.00 55.02           O  
HETATM 3428  O   HOH A 840      14.985   1.402 -41.936  1.00 38.99           O  
HETATM 3429  O   HOH A 841      22.929 -10.093 -39.950  1.00 24.99           O  
HETATM 3430  O   HOH A 842      41.001   2.248 -62.155  1.00 51.61           O  
HETATM 3431  O   HOH A 843       4.842 -20.535 -78.993  1.00 34.24           O  
HETATM 3432  O   HOH A 844      38.743  -9.802 -46.498  1.00 43.23           O  
HETATM 3433  O   HOH A 845      -0.665 -29.475 -54.392  1.00 23.25           O  
HETATM 3434  O   HOH A 846      -0.884 -40.415 -53.859  1.00 36.39           O  
HETATM 3435  O   HOH A 847      39.597  13.306 -66.466  1.00 45.73           O  
HETATM 3436  O   HOH A 848      27.122 -19.601 -52.181  1.00 20.60           O  
HETATM 3437  O   HOH A 849      16.148 -41.414 -40.290  1.00 33.53           O  
HETATM 3438  O   HOH A 850      35.194 -24.607 -39.500  1.00 31.21           O  
HETATM 3439  O   HOH A 851      18.750  -0.054 -38.111  1.00 34.40           O  
HETATM 3440  O   HOH A 852      35.195  -6.422 -45.170  1.00 33.81           O  
HETATM 3441  O   HOH A 853      11.648 -14.908 -34.294  1.00 28.88           O  
HETATM 3442  O   HOH A 854      16.932  -3.008 -61.289  1.00 32.04           O  
HETATM 3443  O   HOH A 855      -1.874 -24.290 -52.040  1.00 23.87           O  
HETATM 3444  O   HOH A 856       9.526  -8.198 -75.913  1.00 42.99           O  
HETATM 3445  O   HOH A 857      41.902 -17.967 -43.984  1.00 41.65           O  
HETATM 3446  O   HOH A 858       7.254 -24.340 -41.492  1.00 26.85           O  
HETATM 3447  O   HOH A 859      12.520 -19.101 -32.069  1.00 40.77           O  
HETATM 3448  O   HOH A 860      20.319 -25.954 -70.227  1.00 29.20           O  
HETATM 3449  O   HOH A 861      40.664 -29.144 -64.575  1.00 47.20           O  
HETATM 3450  O   HOH A 862      10.237  -1.315 -58.480  1.00 38.61           O  
HETATM 3451  O   HOH A 863       1.219  -7.256 -55.643  1.00 34.45           O  
HETATM 3452  O   HOH A 864       9.542 -10.220 -77.242  1.00 33.76           O  
HETATM 3453  O   HOH A 865      16.148 -12.800 -29.020  1.00 37.71           O  
HETATM 3454  O   HOH A 866      20.569 -16.264 -68.150  1.00 24.80           O  
HETATM 3455  O   HOH A 867      40.964 -15.912 -60.653  1.00 48.97           O  
HETATM 3456  O   HOH A 868      19.734 -21.044 -68.548  1.00 26.15           O  
HETATM 3457  O   HOH A 869       2.739 -14.348 -46.983  1.00 31.72           O  
HETATM 3458  O   HOH A 870      40.006 -19.213 -42.344  1.00 36.87           O  
HETATM 3459  O   HOH A 871      19.154 -29.086 -59.911  1.00 21.95           O  
HETATM 3460  O   HOH A 872      38.485 -11.060 -63.324  1.00 40.95           O  
HETATM 3461  O   HOH A 873      21.857 -32.642 -42.623  1.00 51.52           O  
HETATM 3462  O   HOH A 874      25.002 -37.759 -69.759  1.00 55.65           O  
HETATM 3463  O   HOH A 875       4.127  -5.497 -50.218  1.00 37.51           O  
HETATM 3464  O   HOH A 876      12.507  -4.751 -39.216  1.00 45.47           O  
HETATM 3465  O   HOH A 877      14.132 -21.287 -71.992  1.00 32.16           O  
HETATM 3466  O   HOH A 878      18.137 -36.795 -70.218  1.00 37.18           O  
HETATM 3467  O   HOH A 879      22.414 -40.059 -43.300  1.00 36.39           O  
HETATM 3468  O   HOH A 880       8.582 -35.727 -67.860  1.00 23.36           O  
HETATM 3469  O   HOH A 881      15.978 -35.322 -71.707  1.00 43.62           O  
HETATM 3470  O   HOH A 882      28.127 -18.488 -56.190  1.00 24.21           O  
HETATM 3471  O   HOH A 883      22.805 -19.593 -65.047  1.00 37.57           O  
HETATM 3472  O   HOH A 884      38.252 -17.569 -64.421  1.00 40.01           O  
HETATM 3473  O   HOH A 885      41.226 -23.257 -53.604  1.00 40.88           O  
HETATM 3474  O   HOH A 886       3.500 -29.175 -41.169  1.00 50.65           O  
HETATM 3475  O   HOH A 887      11.688 -21.560 -32.744  1.00 51.71           O  
HETATM 3476  O   HOH A 888      36.820  -5.872 -47.452  1.00 22.66           O  
HETATM 3477  O   HOH A 889       6.260 -22.873 -32.290  1.00 50.47           O  
HETATM 3478  O   HOH A 890      19.417 -18.305 -69.602  1.00 30.47           O  
HETATM 3479  O   HOH A 891      22.227 -27.378 -73.452  1.00 48.95           O  
HETATM 3480  O   HOH A 892      12.744   1.221 -45.912  1.00 47.27           O  
HETATM 3481  O   HOH A 893      25.310 -20.992 -65.246  1.00 34.86           O  
HETATM 3482  O   HOH A 894      10.747 -17.342 -33.502  1.00 46.62           O  
HETATM 3483  O   HOH A 895      16.753 -20.682 -71.994  1.00 29.84           O  
HETATM 3484  O   HOH A 896      33.559 -40.667 -46.214  1.00 52.64           O  
HETATM 3485  O   HOH A 897       2.274  -7.388 -49.114  1.00 42.69           O  
HETATM 3486  O   HOH A 898      17.144  -0.564 -51.038  1.00 33.82           O  
HETATM 3487  O   HOH A 899      -3.651 -32.328 -66.366  1.00 37.70           O  
HETATM 3488  O   HOH A 900       5.914 -34.455 -39.264  1.00 27.88           O  
HETATM 3489  O   HOH A 901      33.761  -6.645 -65.916  1.00 27.68           O  
HETATM 3490  O   HOH A 902      23.115 -15.573 -26.811  1.00 47.28           O  
HETATM 3491  O   HOH A 903      22.217 -51.771 -61.708  1.00 29.86           O  
HETATM 3492  O   HOH A 904      24.947 -35.322 -70.067  1.00 40.27           O  
HETATM 3493  O   HOH A 905      12.276 -10.200 -78.474  1.00 17.89           O  
HETATM 3494  O   HOH A 906      29.372 -29.663 -66.116  1.00 51.38           O  
HETATM 3495  O   HOH A 907      26.849 -41.233 -68.502  1.00 36.62           O  
HETATM 3496  O   HOH A 908      42.480 -17.111 -46.338  1.00 52.80           O  
HETATM 3497  O   HOH A 909      25.597 -52.095 -53.506  1.00 35.82           O  
HETATM 3498  O   HOH A 910      39.112 -30.568 -43.666  1.00 48.35           O  
HETATM 3499  O   HOH A 911      16.518 -15.580 -83.915  1.00 55.99           O  
HETATM 3500  O   HOH A 912       7.638 -34.384 -70.802  1.00 27.76           O  
HETATM 3501  O   HOH A 913      -3.065 -39.169 -42.920  1.00 59.77           O  
HETATM 3502  O   HOH A 914      19.914 -23.414 -71.117  1.00 45.12           O  
HETATM 3503  O   HOH A 915      31.369  -5.340 -39.934  1.00 23.97           O  
HETATM 3504  O   HOH A 916       1.360 -22.220 -39.763  1.00 26.96           O  
HETATM 3505  O   HOH A 917      27.495 -10.601 -67.830  1.00 39.98           O  
HETATM 3506  O   HOH A 918      30.014 -39.271 -45.660  1.00 40.13           O  
HETATM 3507  O   HOH A 919      24.289 -18.324 -30.630  1.00 38.64           O  
HETATM 3508  O   HOH A 920      41.687 -17.500 -56.521  1.00 46.01           O  
HETATM 3509  O   HOH A 921      37.329 -13.611 -39.055  1.00 27.08           O  
HETATM 3510  O   HOH A 922       6.036 -21.650 -76.178  1.00 21.83           O  
HETATM 3511  O   HOH A 923      32.322  -2.364 -43.481  1.00 37.48           O  
HETATM 3512  O   HOH A 924       1.032 -38.557 -62.456  1.00 42.38           O  
HETATM 3513  O   HOH A 925      14.026 -21.397 -81.464  1.00 50.84           O  
HETATM 3514  O   HOH A 926      40.019  -8.022 -50.062  1.00 44.66           O  
HETATM 3515  O   HOH A 927      21.235 -23.704 -76.241  1.00 47.08           O  
HETATM 3516  O   HOH A 928      24.889 -15.789 -69.405  1.00 49.80           O  
HETATM 3517  O   HOH A 929       4.172 -39.775 -41.637  1.00 36.66           O  
HETATM 3518  O   HOH A 930      36.736  -6.912 -64.975  1.00 32.43           O  
HETATM 3519  O   HOH A 931      25.422 -27.479 -35.665  1.00 35.22           O  
HETATM 3520  O   HOH A 932      45.208   6.278 -52.366  1.00 37.82           O  
HETATM 3521  O   HOH A 933      13.869  -5.284 -42.045  1.00 13.91           O  
HETATM 3522  O   HOH A 934      36.441 -10.616 -67.224  1.00 50.72           O  
HETATM 3523  O   HOH A 935      21.225 -12.324 -76.845  1.00 36.66           O  
HETATM 3524  O   HOH A 936      24.613 -28.788 -40.158  1.00 35.59           O  
HETATM 3525  O   HOH A 937       3.700 -30.610 -43.383  1.00 44.87           O  
HETATM 3526  O   HOH A 938      30.784 -45.466 -60.148  0.50 36.41           O  
HETATM 3527  O   HOH A 939      14.170  -2.437 -80.600  1.00 43.41           O  
HETATM 3528  O   HOH A 940      26.957 -13.410 -68.791  1.00 35.38           O  
HETATM 3529  O   HOH A 941      35.331 -39.998 -52.714  1.00 16.11           O  
HETATM 3530  O   HOH A 942       8.182 -24.417 -70.759  1.00 38.48           O  
HETATM 3531  O   HOH A 943      23.250 -19.723 -28.956  1.00 47.57           O  
HETATM 3532  O   HOH A 944      21.520 -37.251 -43.428  1.00 17.71           O  
HETATM 3533  O   HOH A 945      12.887  -5.419 -44.693  1.00 39.89           O  
HETATM 3534  O   HOH A 946      -2.949 -21.806 -71.426  1.00 49.62           O  
HETATM 3535  O   HOH A 947      -2.229 -20.508 -72.852  1.00 42.22           O  
HETATM 3536  O   HOH A 948      12.214 -19.898 -79.681  1.00 29.36           O  
HETATM 3537  O   HOH A 949      21.716 -32.271 -39.583  1.00 51.90           O  
HETATM 3538  O   HOH A 950      16.689  -2.827 -82.293  1.00 52.37           O  
HETATM 3539  O   HOH A 951      16.629  -0.725 -48.339  1.00 37.12           O  
HETATM 3540  O   HOH A 952       9.785 -40.824 -43.952  1.00 43.78           O  
HETATM 3541  O   HOH A 953       8.593 -24.209 -73.489  1.00 41.63           O  
HETATM 3542  O   HOH A 954      25.709 -33.702 -71.183  1.00 44.40           O  
HETATM 3543  O   HOH A 955      15.738   3.623 -43.261  1.00 37.76           O  
HETATM 3544  O   HOH A 956      31.719 -17.051 -62.101  1.00 39.10           O  
HETATM 3545  O   HOH A 957      23.543 -25.678 -68.920  1.00 46.84           O  
HETATM 3546  O   HOH A 958      14.001   0.082 -81.770  1.00 34.18           O  
HETATM 3547  O   HOH A 959      11.848  -3.936 -80.888  1.00 53.25           O  
HETATM 3548  O   HOH A 960      -5.309 -39.757 -44.368  1.00 50.74           O  
HETATM 3549  O   HOH A 961      37.375 -35.443 -64.402  1.00 56.12           O  
HETATM 3550  O   HOH A 962      26.335 -28.357 -37.775  1.00 39.43           O  
HETATM 3551  O   HOH A 963      38.730 -24.794 -52.515  1.00 46.96           O  
HETATM 3552  O   HOH A 964      39.119  14.337 -69.003  1.00 55.55           O  
HETATM 3553  O   HOH A 965      37.873 -35.923 -62.054  1.00 46.90           O  
HETATM 3554  O   HOH A 966      38.034  -4.953 -66.486  1.00 46.66           O  
HETATM 3555  O   HOH A 967      43.565  -1.713 -56.355  1.00 50.76           O  
HETATM 3556  O   HOH A 968      21.103  -2.980 -35.751  1.00 49.84           O  
HETATM 3557  O   HOH A 969      11.308   0.748 -49.961  1.00 36.07           O  
HETATM 3558  O   HOH A 970      26.657 -13.612 -31.341  1.00 44.84           O  
HETATM 3559  O   HOH A 971      30.040  -7.018 -66.008  1.00 43.07           O  
HETATM 3560  O   HOH A 972      38.976 -32.633 -45.222  1.00 58.06           O  
HETATM 3561  O   HOH A 973      36.431  -9.062 -42.042  1.00 32.26           O  
HETATM 3562  O   HOH A 974      22.794 -14.513 -76.813  1.00 47.44           O  
HETATM 3563  O   HOH A 975      16.230  -4.962 -34.485  1.00 55.09           O  
HETATM 3564  O   HOH A 976      39.268 -37.413 -49.823  1.00 50.53           O  
HETATM 3565  O   HOH A 977      29.696 -19.959 -64.326  1.00 47.08           O  
HETATM 3566  O   HOH A 978      12.843  -5.747 -78.250  1.00 41.60           O  
HETATM 3567  O   HOH A 979      38.151  -9.309 -65.224  1.00 46.28           O  
HETATM 3568  O   HOH A 980      -4.769 -33.756 -41.271  1.00 50.15           O  
HETATM 3569  O   HOH A 981      18.705  -2.122 -36.098  1.00 51.04           O  
HETATM 3570  O   HOH A 982      -2.621 -34.572 -39.998  1.00 51.12           O  
HETATM 3571  O   HOH A 983      34.816 -39.621 -66.805  1.00 44.92           O  
HETATM 3572  O   HOH A 984       9.370 -35.177 -73.042  1.00 46.78           O  
HETATM 3573  O   HOH A 985       6.183  -2.512 -50.805  1.00 55.18           O  
HETATM 3574  O   HOH A 986      47.311  -0.027 -53.697  1.00 50.21           O  
HETATM 3575  O   HOH A 987      22.158 -22.091 -70.062  1.00 38.68           O  
HETATM 3576  O   HOH A 988      33.856 -42.691 -48.636  1.00 46.37           O  
HETATM 3577  O   HOH A 989       6.677 -37.547 -66.167  1.00 50.61           O  
HETATM 3578  O   HOH A 990      21.301 -17.008 -76.952  1.00 41.82           O  
HETATM 3579  O   HOH A 991      19.984 -38.725 -39.285  1.00 51.15           O  
HETATM 3580  O   HOH A 992      41.749 -13.865 -62.773  1.00 51.96           O  
HETATM 3581  O   HOH A 993      40.357 -31.725 -57.146  1.00 40.50           O  
HETATM 3582  O   HOH A 994      33.598 -28.999 -37.362  1.00 47.93           O  
HETATM 3583  O   HOH A 995      15.741 -32.477 -28.378  1.00 42.35           O  
HETATM 3584  O   HOH A 996      28.129 -19.184 -28.107  1.00 47.54           O  
HETATM 3585  O   HOH A 997      11.428 -40.904 -41.615  1.00 48.98           O  
HETATM 3586  O   HOH A 998      22.520 -18.122 -69.859  1.00 47.97           O  
HETATM 3587  O   HOH A 999       2.552  -4.394 -73.615  1.00 53.73           O  
HETATM 3588  O   HOH A1000      26.549 -36.777 -41.484  1.00 46.66           O  
HETATM 3589  O   HOH A1001       5.533 -23.042 -45.496  1.00 34.78           O  
HETATM 3590  O   HOH A1002      40.562 -28.830 -51.227  1.00 50.93           O  
HETATM 3591  O   HOH A1003       6.660 -34.313 -29.277  1.00 51.24           O  
HETATM 3592  O   HOH A1004      42.394 -18.751 -61.085  1.00 43.69           O  
HETATM 3593  O   HOH A1005      26.726 -29.829 -72.279  1.00 54.99           O  
HETATM 3594  O   HOH A1006      24.187 -37.925 -41.518  1.00 47.27           O  
HETATM 3595  O   HOH A1007      -1.522 -12.119 -60.716  1.00 31.31           O  
HETATM 3596  O   HOH A1008       0.000   0.000 -70.578  0.25 43.25           O  
HETATM 3597  O   HOH A1009      36.882 -25.557 -37.241  1.00 50.00           O  
HETATM 3598  O   HOH A1010      34.553 -25.019 -31.947  1.00 47.34           O  
HETATM 3599  O   HOH A1011      17.682 -22.432 -69.930  1.00 30.50           O  
HETATM 3600  O   HOH A1012      -1.798 -35.605 -65.626  1.00 39.98           O  
HETATM 3601  O   HOH A1013      14.115 -45.865 -45.741  1.00 44.32           O  
HETATM 3602  O   HOH A1014       5.040 -33.913 -71.980  1.00 50.84           O  
HETATM 3603  O   HOH A1015       3.818 -32.192 -39.384  1.00 41.45           O  
HETATM 3604  O   HOH A1016      41.301 -29.622 -55.721  1.00 33.88           O  
HETATM 3605  O   HOH A1017      23.776 -19.462 -71.734  1.00 46.53           O  
HETATM 3606  O   HOH A1018      47.548  15.121 -47.644  1.00 47.92           O  
HETATM 3607  O   HOH A1019      43.657 -28.692 -57.179  1.00 42.50           O  
HETATM 3608  O   HOH A1020      45.466 -30.854 -60.078  0.50 49.17           O  
CONECT   88 2635                                                                
CONECT  341  379                                                                
CONECT  379  341                                                                
CONECT  515 3174                                                                
CONECT  762  895                                                                
CONECT  819 1192                                                                
CONECT  895  762                                                                
CONECT  944 3069                                                                
CONECT 1192  819                                                                
CONECT 1205 1240                                                                
CONECT 1240 1205                                                                
CONECT 1567 1660                                                                
CONECT 1579 1647                                                                
CONECT 1647 1579                                                                
CONECT 1660 1567                                                                
CONECT 1675 3188                                                                
CONECT 1714 3188                                                                
CONECT 1878 2012                                                                
CONECT 1921 3188                                                                
CONECT 2012 1878                                                                
CONECT 2086 3188                                                                
CONECT 2635   88                                                                
CONECT 2669 2889                                                                
CONECT 2889 2669                                                                
CONECT 3069  944 3070 3080                                                      
CONECT 3070 3069 3071 3077                                                      
CONECT 3071 3070 3072 3078                                                      
CONECT 3072 3071 3073 3079                                                      
CONECT 3073 3072 3074 3080                                                      
CONECT 3074 3073 3081                                                           
CONECT 3075 3076 3077 3082                                                      
CONECT 3076 3075                                                                
CONECT 3077 3070 3075                                                           
CONECT 3078 3071                                                                
CONECT 3079 3072 3083                                                           
CONECT 3080 3069 3073                                                           
CONECT 3081 3074                                                                
CONECT 3082 3075                                                                
CONECT 3083 3079 3084 3094                                                      
CONECT 3084 3083 3085 3091                                                      
CONECT 3085 3084 3086 3092                                                      
CONECT 3086 3085 3087 3093                                                      
CONECT 3087 3086 3088 3094                                                      
CONECT 3088 3087 3095                                                           
CONECT 3089 3090 3091 3096                                                      
CONECT 3090 3089                                                                
CONECT 3091 3084 3089                                                           
CONECT 3092 3085                                                                
CONECT 3093 3086 3097                                                           
CONECT 3094 3083 3087                                                           
CONECT 3095 3088                                                                
CONECT 3096 3089                                                                
CONECT 3097 3093 3098 3106                                                      
CONECT 3098 3097 3099 3103                                                      
CONECT 3099 3098 3100 3104                                                      
CONECT 3100 3099 3101 3105                                                      
CONECT 3101 3100 3102 3106                                                      
CONECT 3102 3101 3107                                                           
CONECT 3103 3098                                                                
CONECT 3104 3099 3108                                                           
CONECT 3105 3100                                                                
CONECT 3106 3097 3101                                                           
CONECT 3107 3102 3141                                                           
CONECT 3108 3104 3109 3117                                                      
CONECT 3109 3108 3110 3114                                                      
CONECT 3110 3109 3111 3115                                                      
CONECT 3111 3110 3112 3116                                                      
CONECT 3112 3111 3113 3117                                                      
CONECT 3113 3112 3118                                                           
CONECT 3114 3109 3119                                                           
CONECT 3115 3110                                                                
CONECT 3116 3111                                                                
CONECT 3117 3108 3112                                                           
CONECT 3118 3113                                                                
CONECT 3119 3114 3120 3128                                                      
CONECT 3120 3119 3121 3125                                                      
CONECT 3121 3120 3122 3126                                                      
CONECT 3122 3121 3123 3127                                                      
CONECT 3123 3122 3124 3128                                                      
CONECT 3124 3123 3129                                                           
CONECT 3125 3120 3130                                                           
CONECT 3126 3121                                                                
CONECT 3127 3122                                                                
CONECT 3128 3119 3123                                                           
CONECT 3129 3124                                                                
CONECT 3130 3125 3131 3139                                                      
CONECT 3131 3130 3132 3136                                                      
CONECT 3132 3131 3133 3137                                                      
CONECT 3133 3132 3134 3138                                                      
CONECT 3134 3133 3135 3139                                                      
CONECT 3135 3134 3140                                                           
CONECT 3136 3131                                                                
CONECT 3137 3132                                                                
CONECT 3138 3133                                                                
CONECT 3139 3130 3134                                                           
CONECT 3140 3135                                                                
CONECT 3141 3107 3142 3150                                                      
CONECT 3142 3141 3143 3147                                                      
CONECT 3143 3142 3144 3148                                                      
CONECT 3144 3143 3145 3149                                                      
CONECT 3145 3144 3146 3150                                                      
CONECT 3146 3145 3151                                                           
CONECT 3147 3142                                                                
CONECT 3148 3143 3152                                                           
CONECT 3149 3144                                                                
CONECT 3150 3141 3145                                                           
CONECT 3151 3146 3163                                                           
CONECT 3152 3148 3153 3161                                                      
CONECT 3153 3152 3154 3158                                                      
CONECT 3154 3153 3155 3159                                                      
CONECT 3155 3154 3156 3160                                                      
CONECT 3156 3155 3157 3161                                                      
CONECT 3157 3156 3162                                                           
CONECT 3158 3153                                                                
CONECT 3159 3154                                                                
CONECT 3160 3155                                                                
CONECT 3161 3152 3156                                                           
CONECT 3162 3157                                                                
CONECT 3163 3151 3164 3172                                                      
CONECT 3164 3163 3165 3169                                                      
CONECT 3165 3164 3166 3170                                                      
CONECT 3166 3165 3167 3171                                                      
CONECT 3167 3166 3168 3172                                                      
CONECT 3168 3167 3173                                                           
CONECT 3169 3164                                                                
CONECT 3170 3165                                                                
CONECT 3171 3166                                                                
CONECT 3172 3163 3167                                                           
CONECT 3173 3168                                                                
CONECT 3174  515 3175 3185                                                      
CONECT 3175 3174 3176 3182                                                      
CONECT 3176 3175 3177 3183                                                      
CONECT 3177 3176 3178 3184                                                      
CONECT 3178 3177 3179 3185                                                      
CONECT 3179 3178 3186                                                           
CONECT 3180 3181 3182 3187                                                      
CONECT 3181 3180                                                                
CONECT 3182 3175 3180                                                           
CONECT 3183 3176                                                                
CONECT 3184 3177                                                                
CONECT 3185 3174 3178                                                           
CONECT 3186 3179                                                                
CONECT 3187 3180                                                                
CONECT 3188 1675 1714 1921 2086                                                 
CONECT 3188 3252 3269                                                           
CONECT 3252 3188                                                                
CONECT 3269 3188                                                                
MASTER      645    0   11    4   25    0    0    6 3595    1  147   31          
END                                                                             
