HEADER    OXIDOREDUCTASE                          27-NOV-17   6BPY              
TITLE     ASPERGILLUS FUMIGATUS THIOREDOXIN REDUCTASE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOREDOXIN REDUCTASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.8.1.9;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEOSARTORYA FUMIGATA;                           
SOURCE   3 ORGANISM_COMMON: ASPERGILLUS FUMIGATUS;                              
SOURCE   4 ORGANISM_TAXID: 746128;                                              
SOURCE   5 GENE: CDV57_04819, CDV58_04527;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-57-DEST                               
KEYWDS    REDOX HOMEOSTASIS, ROSSMANN FOLD, DITHIOL, OXIDOREDUCTASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.MARSHALL,J.B.BRUNING                                              
REVDAT   3   04-OCT-23 6BPY    1       REMARK                                   
REVDAT   2   04-SEP-19 6BPY    1       JRNL                                     
REVDAT   1   09-JAN-19 6BPY    0                                                
JRNL        AUTH   A.C.MARSHALL,S.E.KIDD,S.J.LAMONT-FRIEDRICH,G.ARENTZ,         
JRNL        AUTH 2 P.HOFFMANN,B.R.COAD,J.B.BRUNING                              
JRNL        TITL   STRUCTURE, MECHANISM, AND INHIBITION OFASPERGILLUS           
JRNL        TITL 2 FUMIGATUSTHIOREDOXIN REDUCTASE.                              
JRNL        REF    ANTIMICROB.AGENTS CHEMOTHER.  V.  63       2019              
JRNL        REFN                   ESSN 1098-6596                               
JRNL        PMID   30642940                                                     
JRNL        DOI    10.1128/AAC.02281-18                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28215                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1407                            
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 29.9750 -  6.8706    1.00     2927   158  0.1841 0.2041        
REMARK   3     2  6.8706 -  5.4642    1.00     2841   150  0.2078 0.2329        
REMARK   3     3  5.4642 -  4.7766    0.99     2797   149  0.1998 0.2631        
REMARK   3     4  4.7766 -  4.3413    0.99     2776   147  0.2067 0.2342        
REMARK   3     5  4.3413 -  4.0309    0.98     2767   148  0.2401 0.3000        
REMARK   3     6  4.0309 -  3.7938    0.96     2681   136  0.2624 0.2635        
REMARK   3     7  3.7938 -  3.6041    0.94     2611   136  0.2885 0.3044        
REMARK   3     8  3.6041 -  3.4474    0.91     2509   128  0.3242 0.3456        
REMARK   3     9  3.4474 -  3.3149    0.90     2509   129  0.3319 0.3768        
REMARK   3    10  3.3149 -  3.2006    0.86     2390   126  0.3721 0.3933        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 92.69                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 44 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -52.9751  30.0394 -43.0181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9182 T22:   0.8429                                     
REMARK   3      T33:   1.1938 T12:  -0.3267                                     
REMARK   3      T13:  -0.1317 T23:   0.2459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2306 L22:   4.4511                                     
REMARK   3      L33:   7.1947 L12:  -1.8344                                     
REMARK   3      L13:  -2.2556 L23:  -3.0454                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6779 S12:  -0.7498 S13:  -1.4157                       
REMARK   3      S21:   0.1900 S22:  -0.8226 S23:  -0.8358                       
REMARK   3      S31:   0.9388 S32:   0.6508 S33:   0.4003                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 63 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -65.2634  25.7895 -59.2630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8837 T22:   0.7323                                     
REMARK   3      T33:   0.9698 T12:  -0.0976                                     
REMARK   3      T13:  -0.0472 T23:   0.0531                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8481 L22:   6.3419                                     
REMARK   3      L33:   9.4853 L12:   1.1332                                     
REMARK   3      L13:   0.4379 L23:   2.0279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3929 S12:  -0.2042 S13:  -0.9782                       
REMARK   3      S21:   0.0580 S22:  -0.3453 S23:  -0.9045                       
REMARK   3      S31:   1.9031 S32:  -0.4995 S33:   0.0386                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -50.9211  24.7465 -39.3550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0544 T22:   0.9510                                     
REMARK   3      T33:   1.3531 T12:  -0.3187                                     
REMARK   3      T13:  -0.2613 T23:   0.3597                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3024 L22:   3.7780                                     
REMARK   3      L33:   8.2380 L12:  -0.1596                                     
REMARK   3      L13:  -0.5267 L23:  -1.4722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7170 S12:  -1.3522 S13:  -0.8562                       
REMARK   3      S21:   0.7588 S22:  -0.4422 S23:  -1.2354                       
REMARK   3      S31:   0.6307 S32:   1.0126 S33:  -0.1444                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 155 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -68.1238  17.0743 -49.8542              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1409 T22:   0.5840                                     
REMARK   3      T33:   1.1557 T12:  -0.2249                                     
REMARK   3      T13:  -0.2857 T23:   0.2042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4713 L22:   4.0409                                     
REMARK   3      L33:   2.4033 L12:   3.7051                                     
REMARK   3      L13:   1.9684 L23:   2.7190                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0766 S12:  -0.3404 S13:  -0.6969                       
REMARK   3      S21:   0.5460 S22:  -0.2061 S23:  -0.7296                       
REMARK   3      S31:  -0.0209 S32:   0.8056 S33:   0.2956                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 246 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -84.7282  10.7850 -52.8842              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8029 T22:   0.4036                                     
REMARK   3      T33:   0.9807 T12:  -0.2047                                     
REMARK   3      T13:  -0.2188 T23:   0.1835                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0039 L22:   5.8593                                     
REMARK   3      L33:   5.3179 L12:  -0.2188                                     
REMARK   3      L13:  -3.0035 L23:   0.0271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0936 S12:   0.2126 S13:   0.4489                       
REMARK   3      S21:  -0.2157 S22:   0.3023 S23:   0.4147                       
REMARK   3      S31:  -0.2322 S32:  -0.2553 S33:  -0.3062                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 247 THROUGH 278 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -71.0026  21.6425 -38.2616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3322 T22:   0.9514                                     
REMARK   3      T33:   0.9765 T12:  -0.5094                                     
REMARK   3      T13:  -0.0151 T23:   0.2295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0154 L22:   2.8144                                     
REMARK   3      L33:   1.5334 L12:   1.0802                                     
REMARK   3      L13:  -0.0737 L23:   1.9223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9773 S12:  -1.4996 S13:  -0.3530                       
REMARK   3      S21:   1.1350 S22:  -0.9510 S23:   0.5184                       
REMARK   3      S31:   0.7000 S32:  -0.7920 S33:   0.0273                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 279 THROUGH 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -63.6695  36.2124 -38.3438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0972 T22:   0.7861                                     
REMARK   3      T33:   0.7397 T12:  -0.4299                                     
REMARK   3      T13:   0.1383 T23:   0.1158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4399 L22:   2.3512                                     
REMARK   3      L33:   6.0971 L12:  -1.5424                                     
REMARK   3      L13:   3.1080 L23:   1.0584                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0352 S12:  -1.3365 S13:  -0.2124                       
REMARK   3      S21:   0.7716 S22:  -0.5851 S23:  -0.1425                       
REMARK   3      S31:  -0.1036 S32:  -0.0631 S33:  -0.3187                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 112 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -76.1036  44.1492 -62.3124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9696 T22:   0.6875                                     
REMARK   3      T33:   0.9943 T12:  -0.2080                                     
REMARK   3      T13:   0.0038 T23:   0.2891                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0812 L22:   5.6172                                     
REMARK   3      L33:   2.7790 L12:  -3.7417                                     
REMARK   3      L13:   1.1503 L23:  -0.6697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1485 S12:   0.7950 S13:   1.3492                       
REMARK   3      S21:  -0.4938 S22:  -0.0059 S23:   0.4084                       
REMARK   3      S31:  -0.0988 S32:  -0.1267 S33:  -0.1428                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 113 THROUGH 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -61.1734  54.9625 -49.0495              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9872 T22:   0.6289                                     
REMARK   3      T33:   0.8871 T12:  -0.2504                                     
REMARK   3      T13:   0.1149 T23:   0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1703 L22:   5.5831                                     
REMARK   3      L33:   0.7477 L12:   4.8460                                     
REMARK   3      L13:  -1.0129 L23:  -0.8249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3892 S12:  -0.6049 S13:   1.2716                       
REMARK   3      S21:   0.7675 S22:  -0.1844 S23:   0.8136                       
REMARK   3      S31:  -0.3878 S32:   0.0333 S33:  -0.2394                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESID 2 THROUGH 36 OR RESID   
REMARK   3                          44 OR (RESID 45 AND (NAME N OR NAME CA OR   
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID     
REMARK   3                          46 THROUGH 107 OR (RESID 108 THROUGH 110    
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB )) OR RESID 111 THROUGH 134    
REMARK   3                          OR (RESID 135 AND (NAME N OR NAME CA OR     
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID     
REMARK   3                          136 THROUGH 188 OR (RESID 189 AND (NAME N   
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESID 190 OR (RESID 191 AND (NAME N   
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESID 192 THROUGH 195 OR (RESID 196   
REMARK   3                          THROUGH 197 AND (NAME N OR NAME CA OR       
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID     
REMARK   3                          198 THROUGH 277 OR (RESID 278 AND (NAME N   
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESID 279 THROUGH 324 OR (RESID 325   
REMARK   3                          THROUGH 326 AND (NAME N OR NAME CA OR       
REMARK   3                          NAME C OR NAME O OR NAME CB ))))            
REMARK   3     SELECTION          : (CHAIN B AND ((RESID 2 AND (NAME N OR       
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 3 OR (RESID 4 THROUGH 5 AND        
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 6 THROUGH 27 OR         
REMARK   3                          (RESID 28 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 29       
REMARK   3                          THROUGH 34 OR (RESID 35 THROUGH 36 AND      
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 44 THROUGH 90 OR        
REMARK   3                          (RESID 91 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 92       
REMARK   3                          THROUGH 102 OR (RESID 103 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 104 THROUGH 270 OR (RESID 271      
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB )) OR RESID 272 THROUGH 326))  
REMARK   3     ATOM PAIRS NUMBER  : 2663                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6BPY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231256.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-AUG-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : SILICON DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.17                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28434                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.970                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 12.30                              
REMARK 200  R MERGE                    (I) : 0.19100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.30900                            
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 2.5.6                                          
REMARK 200 STARTING MODEL: 3D8X                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 77.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% TACSIMATE, PH 7.0, VAPOR             
REMARK 280  DIFFUSION, TEMPERATURE 289K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.91333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       40.45667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       40.45667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       80.91333            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 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     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     PRO A   327                                                      
REMARK 465     GLU A   328                                                      
REMARK 465     GLU A   329                                                      
REMARK 465     GLU A   330                                                      
REMARK 465     PRO A   331                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     ALA A   333                                                      
REMARK 465     VAL A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     ALA A   336                                                      
REMARK 465     GLN A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     SER A   339                                                      
REMARK 465     ALA A   340                                                      
REMARK 465     ASP A   341                                                      
REMARK 465     ASN A   342                                                      
REMARK 465     SER A   343                                                      
REMARK 465     THR A   344                                                      
REMARK 465     ILE A   345                                                      
REMARK 465     GLN A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     ALA A   348                                                      
REMARK 465     ALA A   349                                                      
REMARK 465     GLN A   350                                                      
REMARK 465     GLU A   351                                                      
REMARK 465     VAL A   352                                                      
REMARK 465     ASN A   353                                                      
REMARK 465     GLY A   354                                                      
REMARK 465     ASP A   355                                                      
REMARK 465     VAL A   356                                                      
REMARK 465     LYS A   357                                                      
REMARK 465     LYS A   358                                                      
REMARK 465     ASP A   359                                                      
REMARK 465     PRO A   360                                                      
REMARK 465     LYS A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     ALA A   363                                                      
REMARK 465     VAL A   364                                                      
REMARK 465     PRO A   365                                                      
REMARK 465     GLU A   366                                                      
REMARK 465     TYR A   367                                                      
REMARK 465     LYS A   368                                                      
REMARK 465     SER A   369                                                      
REMARK 465     ASN A   370                                                      
REMARK 465     PRO A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     LEU A   373                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     ALA B    37                                                      
REMARK 465     ASN B    38                                                      
REMARK 465     GLY B    39                                                      
REMARK 465     THR B    40                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     GLY B    43                                                      
REMARK 465     PRO B   327                                                      
REMARK 465     GLU B   328                                                      
REMARK 465     GLU B   329                                                      
REMARK 465     GLU B   330                                                      
REMARK 465     PRO B   331                                                      
REMARK 465     VAL B   332                                                      
REMARK 465     ALA B   333                                                      
REMARK 465     VAL B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     ALA B   336                                                      
REMARK 465     GLN B   337                                                      
REMARK 465     LYS B   338                                                      
REMARK 465     SER B   339                                                      
REMARK 465     ALA B   340                                                      
REMARK 465     ASP B   341                                                      
REMARK 465     ASN B   342                                                      
REMARK 465     SER B   343                                                      
REMARK 465     THR B   344                                                      
REMARK 465     ILE B   345                                                      
REMARK 465     GLN B   346                                                      
REMARK 465     PRO B   347                                                      
REMARK 465     ALA B   348                                                      
REMARK 465     ALA B   349                                                      
REMARK 465     GLN B   350                                                      
REMARK 465     GLU B   351                                                      
REMARK 465     VAL B   352                                                      
REMARK 465     ASN B   353                                                      
REMARK 465     GLY B   354                                                      
REMARK 465     ASP B   355                                                      
REMARK 465     VAL B   356                                                      
REMARK 465     LYS B   357                                                      
REMARK 465     LYS B   358                                                      
REMARK 465     ASP B   359                                                      
REMARK 465     PRO B   360                                                      
REMARK 465     LYS B   361                                                      
REMARK 465     GLY B   362                                                      
REMARK 465     ALA B   363                                                      
REMARK 465     VAL B   364                                                      
REMARK 465     PRO B   365                                                      
REMARK 465     GLU B   366                                                      
REMARK 465     TYR B   367                                                      
REMARK 465     LYS B   368                                                      
REMARK 465     SER B   369                                                      
REMARK 465     ASN B   370                                                      
REMARK 465     PRO B   371                                                      
REMARK 465     LEU B   372                                                      
REMARK 465     LEU B   373                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A   2    CG1  CG2                                            
REMARK 470     THR A   4    OG1  CG2                                            
REMARK 470     LYS A   5    CG   CD   CE   NZ                                   
REMARK 470     LYS A  28    CG   CD   CE   NZ                                   
REMARK 470     MET A  35    CG   SD   CE                                        
REMARK 470     LEU A  36    CG   CD1  CD2                                       
REMARK 470     ASN A  38    CG   OD1  ND2                                       
REMARK 470     THR A  40    OG1  CG2                                            
REMARK 470     ASP A  91    CG   OD1  OD2                                       
REMARK 470     LYS A  95    CG   CD   CE   NZ                                   
REMARK 470     LYS A  98    CG   CD   CE   NZ                                   
REMARK 470     TRP A 103    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 103    CZ3  CH2                                            
REMARK 470     LYS A 109    CG   CD   CE   NZ                                   
REMARK 470     GLU A 110    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 200    CG   CD   CE   NZ                                   
REMARK 470     LYS A 264    CG   CD   CE   NZ                                   
REMARK 470     GLU A 271    CG   CD   OE1  OE2                                  
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     LEU B  36    CG   CD1  CD2                                       
REMARK 470     GLN B  45    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  95    CG   CD   CE   NZ                                   
REMARK 470     LYS B  98    CG   CD   CE   NZ                                   
REMARK 470     ASP B 108    CG   OD1  OD2                                       
REMARK 470     LYS B 109    CG   CD   CE   NZ                                   
REMARK 470     GLU B 110    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 135    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 191    CG   CD   CE   NZ                                   
REMARK 470     LYS B 196    CG   CD   CE   NZ                                   
REMARK 470     LYS B 200    CG   CD   CE   NZ                                   
REMARK 470     LYS B 264    CG   CD   CE   NZ                                   
REMARK 470     LYS B 278    CG   CD   CE   NZ                                   
REMARK 470     GLU B 325    CG   CD   OE1  OE2                                  
REMARK 470     SER B 326    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  11       16.75   -142.06                                   
REMARK 500    LYS A  28       71.08   -119.21                                   
REMARK 500    MET A  35       48.28    -87.12                                   
REMARK 500    TRP A 103       -7.63     70.21                                   
REMARK 500    ASN A 226       64.67   -104.40                                   
REMARK 500    SER B  11       16.19   -140.96                                   
REMARK 500    MET B  35       33.17    -86.06                                   
REMARK 500    LEU B  92       59.59    -99.16                                   
REMARK 500    SER B  93      -39.32   -130.47                                   
REMARK 500    TRP B 103       -6.92     72.01                                   
REMARK 500    ASP B 105     -164.77    -79.14                                   
REMARK 500    GLN B 139       10.31     59.73                                   
REMARK 500    LYS B 191       79.02     59.62                                   
REMARK 500    LEU B 192      132.09    -34.78                                   
REMARK 500    ASN B 226       61.45     61.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAP A  407                                                       
REMARK 610     NAP B  409                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT B 410                 
DBREF1 6BPY A    1   373  UNP                  A0A229Y1X4_ASPFM                 
DBREF2 6BPY A     A0A229Y1X4                          1         373             
DBREF1 6BPY B    1   373  UNP                  A0A229Y1X4_ASPFM                 
DBREF2 6BPY B     A0A229Y1X4                          1         373             
SEQADV 6BPY GLY A    0  UNP  A0A229Y1X           EXPRESSION TAG                 
SEQADV 6BPY GLY B    0  UNP  A0A229Y1X           EXPRESSION TAG                 
SEQRES   1 A  374  GLY MET VAL HIS THR LYS VAL VAL ILE ILE GLY SER GLY          
SEQRES   2 A  374  PRO ALA ALA HIS THR ALA ALA ILE TYR LEU SER ARG ALA          
SEQRES   3 A  374  GLU LEU LYS PRO VAL LEU TYR GLU GLY MET LEU ALA ASN          
SEQRES   4 A  374  GLY THR ALA ALA GLY GLY GLN LEU THR THR THR THR ASP          
SEQRES   5 A  374  ILE GLU ASN PHE PRO GLY PHE PRO ASP GLY ILE GLY GLY          
SEQRES   6 A  374  ALA GLU LEU MET GLU ASN MET ARG LYS GLN SER ILE ARG          
SEQRES   7 A  374  PHE GLY THR GLU VAL ILE THR GLU THR ILE SER ARG VAL          
SEQRES   8 A  374  ASP LEU SER SER LYS PRO PHE LYS LEU TRP THR GLU TRP          
SEQRES   9 A  374  ASN ASP GLY PRO ASP LYS GLU PRO ALA CYS THR ALA ASP          
SEQRES  10 A  374  ALA VAL ILE ILE ALA THR GLY ALA ASN ALA ARG ARG LEU          
SEQRES  11 A  374  ASN LEU PRO GLY GLU GLU THR TYR TRP GLN ASN GLY ILE          
SEQRES  12 A  374  SER ALA CYS ALA VAL CYS ASP GLY ALA VAL PRO ILE PHE          
SEQRES  13 A  374  ARG ASN LYS PRO LEU TYR VAL ILE GLY GLY GLY ASP SER          
SEQRES  14 A  374  ALA ALA GLU GLU ALA MET PHE LEU ALA LYS TYR GLY SER          
SEQRES  15 A  374  SER VAL THR VAL LEU VAL ARG ARG ASP LYS LEU ARG ALA          
SEQRES  16 A  374  SER LYS ALA MET ALA LYS ARG LEU LEU ALA HIS PRO LYS          
SEQRES  17 A  374  VAL THR VAL ARG PHE ASN THR VAL ALA THR GLU VAL LEU          
SEQRES  18 A  374  GLY GLU LYS LYS PRO ASN GLY LEU MET THR HIS LEU ARG          
SEQRES  19 A  374  ILE LYS ASN THR VAL THR GLY GLU GLU GLU ILE VAL ASP          
SEQRES  20 A  374  ALA ASN GLY LEU PHE TYR ALA VAL GLY HIS ASP PRO ALA          
SEQRES  21 A  374  THR ALA LEU VAL LYS GLY GLN ILE ASP LEU ASP GLU ASP          
SEQRES  22 A  374  GLY TYR ILE ILE THR LYS PRO GLY THR SER TYR THR SER          
SEQRES  23 A  374  ARG GLU GLY VAL PHE ALA CYS GLY ASP VAL GLN ASP LYS          
SEQRES  24 A  374  ARG TYR ARG GLN ALA ILE THR SER ALA GLY SER GLY CYS          
SEQRES  25 A  374  ILE ALA ALA LEU GLU ALA GLU LYS PHE ILE ALA GLU ALA          
SEQRES  26 A  374  GLU SER PRO GLU GLU GLU PRO VAL ALA VAL SER ALA GLN          
SEQRES  27 A  374  LYS SER ALA ASP ASN SER THR ILE GLN PRO ALA ALA GLN          
SEQRES  28 A  374  GLU VAL ASN GLY ASP VAL LYS LYS ASP PRO LYS GLY ALA          
SEQRES  29 A  374  VAL PRO GLU TYR LYS SER ASN PRO LEU LEU                      
SEQRES   1 B  374  GLY MET VAL HIS THR LYS VAL VAL ILE ILE GLY SER GLY          
SEQRES   2 B  374  PRO ALA ALA HIS THR ALA ALA ILE TYR LEU SER ARG ALA          
SEQRES   3 B  374  GLU LEU LYS PRO VAL LEU TYR GLU GLY MET LEU ALA ASN          
SEQRES   4 B  374  GLY THR ALA ALA GLY GLY GLN LEU THR THR THR THR ASP          
SEQRES   5 B  374  ILE GLU ASN PHE PRO GLY PHE PRO ASP GLY ILE GLY GLY          
SEQRES   6 B  374  ALA GLU LEU MET GLU ASN MET ARG LYS GLN SER ILE ARG          
SEQRES   7 B  374  PHE GLY THR GLU VAL ILE THR GLU THR ILE SER ARG VAL          
SEQRES   8 B  374  ASP LEU SER SER LYS PRO PHE LYS LEU TRP THR GLU TRP          
SEQRES   9 B  374  ASN ASP GLY PRO ASP LYS GLU PRO ALA CYS THR ALA ASP          
SEQRES  10 B  374  ALA VAL ILE ILE ALA THR GLY ALA ASN ALA ARG ARG LEU          
SEQRES  11 B  374  ASN LEU PRO GLY GLU GLU THR TYR TRP GLN ASN GLY ILE          
SEQRES  12 B  374  SER ALA CYS ALA VAL CYS ASP GLY ALA VAL PRO ILE PHE          
SEQRES  13 B  374  ARG ASN LYS PRO LEU TYR VAL ILE GLY GLY GLY ASP SER          
SEQRES  14 B  374  ALA ALA GLU GLU ALA MET PHE LEU ALA LYS TYR GLY SER          
SEQRES  15 B  374  SER VAL THR VAL LEU VAL ARG ARG ASP LYS LEU ARG ALA          
SEQRES  16 B  374  SER LYS ALA MET ALA LYS ARG LEU LEU ALA HIS PRO LYS          
SEQRES  17 B  374  VAL THR VAL ARG PHE ASN THR VAL ALA THR GLU VAL LEU          
SEQRES  18 B  374  GLY GLU LYS LYS PRO ASN GLY LEU MET THR HIS LEU ARG          
SEQRES  19 B  374  ILE LYS ASN THR VAL THR GLY GLU GLU GLU ILE VAL ASP          
SEQRES  20 B  374  ALA ASN GLY LEU PHE TYR ALA VAL GLY HIS ASP PRO ALA          
SEQRES  21 B  374  THR ALA LEU VAL LYS GLY GLN ILE ASP LEU ASP GLU ASP          
SEQRES  22 B  374  GLY TYR ILE ILE THR LYS PRO GLY THR SER TYR THR SER          
SEQRES  23 B  374  ARG GLU GLY VAL PHE ALA CYS GLY ASP VAL GLN ASP LYS          
SEQRES  24 B  374  ARG TYR ARG GLN ALA ILE THR SER ALA GLY SER GLY CYS          
SEQRES  25 B  374  ILE ALA ALA LEU GLU ALA GLU LYS PHE ILE ALA GLU ALA          
SEQRES  26 B  374  GLU SER PRO GLU GLU GLU PRO VAL ALA VAL SER ALA GLN          
SEQRES  27 B  374  LYS SER ALA ASP ASN SER THR ILE GLN PRO ALA ALA GLN          
SEQRES  28 B  374  GLU VAL ASN GLY ASP VAL LYS LYS ASP PRO LYS GLY ALA          
SEQRES  29 B  374  VAL PRO GLU TYR LYS SER ASN PRO LEU LEU                      
HET    FAD  A 401      53                                                       
HET    MLI  A 402       7                                                       
HET    MLI  A 403       7                                                       
HET    MLI  A 404       7                                                       
HET    FMT  A 405       3                                                       
HET    FMT  A 406       3                                                       
HET    NAP  A 407      31                                                       
HET    ACT  A 408       4                                                       
HET    FAD  B 401      53                                                       
HET    MLI  B 402       7                                                       
HET    MLI  B 403       7                                                       
HET    FMT  B 404       3                                                       
HET    FMT  B 405       3                                                       
HET    FMT  B 406       3                                                       
HET    FMT  B 407       3                                                       
HET    FMT  B 408       3                                                       
HET    NAP  B 409      31                                                       
HET    MLT  B 410       9                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     MLI MALONATE ION                                                     
HETNAM     FMT FORMIC ACID                                                      
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     ACT ACETATE ION                                                      
HETNAM     MLT D-MALATE                                                         
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID          
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  MLI    5(C3 H2 O4 2-)                                               
FORMUL   7  FMT    7(C H2 O2)                                                   
FORMUL   9  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL  10  ACT    C2 H3 O2 1-                                                  
FORMUL  20  MLT    C4 H6 O5                                                     
FORMUL  21  HOH   *45(H2 O)                                                     
HELIX    1 AA1 GLY A   12  ALA A   25  1                                  14    
HELIX    2 AA2 GLY A   44  THR A   48  5                                   5    
HELIX    3 AA3 GLY A   63  PHE A   78  1                                  16    
HELIX    4 AA4 GLY A  133  TRP A  138  1                                   6    
HELIX    5 AA5 CYS A  145  GLY A  150  1                                   6    
HELIX    6 AA6 VAL A  152  ARG A  156  5                                   5    
HELIX    7 AA7 GLY A  166  ALA A  177  1                                  12    
HELIX    8 AA8 SER A  195  HIS A  205  1                                  11    
HELIX    9 AA9 GLY A  293  GLN A  296  5                                   4    
HELIX   10 AB1 GLN A  302  SER A  326  1                                  25    
HELIX   11 AB2 GLY B   12  ALA B   25  1                                  14    
HELIX   12 AB3 GLY B   44  THR B   48  5                                   5    
HELIX   13 AB4 GLY B   63  PHE B   78  1                                  16    
HELIX   14 AB5 GLY B  133  TRP B  138  1                                   6    
HELIX   15 AB6 CYS B  145  GLY B  150  1                                   6    
HELIX   16 AB7 VAL B  152  ARG B  156  5                                   5    
HELIX   17 AB8 GLY B  166  ALA B  177  1                                  12    
HELIX   18 AB9 SER B  195  HIS B  205  1                                  11    
HELIX   19 AC1 GLY B  293  GLN B  296  5                                   4    
HELIX   20 AC2 GLN B  302  GLU B  323  1                                  22    
SHEET    1 AA1 6 GLU A  81  ILE A  83  0                                        
SHEET    2 AA1 6 PRO A  29  TYR A  32  1  N  PRO A  29   O  GLU A  81           
SHEET    3 AA1 6 HIS A   3  ILE A   9  1  N  ILE A   8   O  VAL A  30           
SHEET    4 AA1 6 CYS A 113  ILE A 120  1  O  ILE A 119   N  VAL A   7           
SHEET    5 AA1 6 PHE A  97  THR A 101 -1  N  PHE A  97   O  ALA A 115           
SHEET    6 AA1 6 ILE A  87  ASP A  91 -1  N  SER A  88   O  TRP A 100           
SHEET    1 AA2 5 GLU A  81  ILE A  83  0                                        
SHEET    2 AA2 5 PRO A  29  TYR A  32  1  N  PRO A  29   O  GLU A  81           
SHEET    3 AA2 5 HIS A   3  ILE A   9  1  N  ILE A   8   O  VAL A  30           
SHEET    4 AA2 5 CYS A 113  ILE A 120  1  O  ILE A 119   N  VAL A   7           
SHEET    5 AA2 5 VAL A 289  ALA A 291  1  O  PHE A 290   N  ILE A 120           
SHEET    1 AA3 2 ALA A 124  ALA A 126  0                                        
SHEET    2 AA3 2 HIS A 256  PRO A 258 -1  O  ASP A 257   N  ASN A 125           
SHEET    1 AA4 5 ILE A 142  SER A 143  0                                        
SHEET    2 AA4 5 GLY A 249  TYR A 252  1  O  TYR A 252   N  SER A 143           
SHEET    3 AA4 5 PRO A 159  ILE A 163  1  N  TYR A 161   O  GLY A 249           
SHEET    4 AA4 5 SER A 182  LEU A 186  1  O  SER A 182   N  LEU A 160           
SHEET    5 AA4 5 VAL A 208  ARG A 211  1  O  ARG A 211   N  VAL A 185           
SHEET    1 AA5 3 THR A 214  GLY A 221  0                                        
SHEET    2 AA5 3 MET A 229  ASN A 236 -1  O  ARG A 233   N  THR A 217           
SHEET    3 AA5 3 GLU A 242  ASP A 246 -1  O  GLU A 243   N  ILE A 234           
SHEET    1 AA6 6 GLU B  81  ILE B  83  0                                        
SHEET    2 AA6 6 VAL B  30  TYR B  32  1  N  LEU B  31   O  GLU B  81           
SHEET    3 AA6 6 HIS B   3  ILE B   9  1  N  ILE B   8   O  TYR B  32           
SHEET    4 AA6 6 CYS B 113  ILE B 120  1  O  ILE B 119   N  ILE B   9           
SHEET    5 AA6 6 PHE B  97  THR B 101 -1  N  PHE B  97   O  ALA B 115           
SHEET    6 AA6 6 ILE B  87  ASP B  91 -1  N  SER B  88   O  TRP B 100           
SHEET    1 AA7 5 GLU B  81  ILE B  83  0                                        
SHEET    2 AA7 5 VAL B  30  TYR B  32  1  N  LEU B  31   O  GLU B  81           
SHEET    3 AA7 5 HIS B   3  ILE B   9  1  N  ILE B   8   O  TYR B  32           
SHEET    4 AA7 5 CYS B 113  ILE B 120  1  O  ILE B 119   N  ILE B   9           
SHEET    5 AA7 5 VAL B 289  ALA B 291  1  O  PHE B 290   N  ILE B 120           
SHEET    1 AA8 2 ALA B 124  ALA B 126  0                                        
SHEET    2 AA8 2 HIS B 256  PRO B 258 -1  O  ASP B 257   N  ASN B 125           
SHEET    1 AA9 5 ILE B 142  SER B 143  0                                        
SHEET    2 AA9 5 GLY B 249  TYR B 252  1  O  TYR B 252   N  SER B 143           
SHEET    3 AA9 5 PRO B 159  ILE B 163  1  N  TYR B 161   O  GLY B 249           
SHEET    4 AA9 5 SER B 182  LEU B 186  1  O  LEU B 186   N  VAL B 162           
SHEET    5 AA9 5 VAL B 208  ARG B 211  1  O  ARG B 211   N  VAL B 185           
SHEET    1 AB1 3 THR B 214  GLY B 221  0                                        
SHEET    2 AB1 3 MET B 229  ASN B 236 -1  O  ARG B 233   N  THR B 217           
SHEET    3 AB1 3 GLU B 242  ASP B 246 -1  O  VAL B 245   N  LEU B 232           
SSBOND   1 CYS A  145    CYS A  148                          1555   1555  2.03  
SSBOND   2 CYS B  145    CYS B  148                          1555   1555  2.03  
SITE     1 AC1 35 ILE A   9  GLY A  10  SER A  11  GLY A  12                    
SITE     2 AC1 35 PRO A  13  ALA A  14  TYR A  32  GLU A  33                    
SITE     3 AC1 35 GLY A  34  ALA A  37  THR A  40  ALA A  41                    
SITE     4 AC1 35 GLY A  44  GLN A  45  LEU A  46  THR A  49                    
SITE     5 AC1 35 ILE A  52  ASN A  54  GLU A  85  THR A  86                    
SITE     6 AC1 35 ILE A  87  ALA A 121  THR A 122  GLY A 123                    
SITE     7 AC1 35 TRP A 138  GLN A 139  CYS A 148  ASP A 149                    
SITE     8 AC1 35 LEU A 262  GLY A 293  ASP A 294  ARG A 301                    
SITE     9 AC1 35 GLN A 302  ALA A 303  SER A 306                               
SITE     1 AC2  8 THR A  50  GLN A 139  GLY A 141  ILE A 142                    
SITE     2 AC2  8 ASP A 149  VAL A 152  ILE A 154  PHE A 155                    
SITE     1 AC3  3 VAL A 147  GLU A 171  LEU B 315                               
SITE     1 AC4  5 LEU A 315  GLU A 318  VAL B 147  GLU B 171                    
SITE     2 AC4  5 FMT B 406                                                     
SITE     1 AC5  2 GLY A 133  THR A 136                                          
SITE     1 AC6  2 ARG A 299  LYS B 319                                          
SITE     1 AC7 10 LEU A 129  ILE A 163  GLY A 165  GLY A 166                    
SITE     2 AC7 10 ASP A 167  SER A 168  ARG A 188  ARG A 189                    
SITE     3 AC7 10 ARG A 193  VAL A 254                                          
SITE     1 AC8  2 SER A 181  SER A 182                                          
SITE     1 AC9 28 ILE B   9  GLY B  10  SER B  11  GLY B  12                    
SITE     2 AC9 28 PRO B  13  ALA B  14  TYR B  32  GLU B  33                    
SITE     3 AC9 28 GLY B  34  GLY B  44  GLN B  45  LEU B  46                    
SITE     4 AC9 28 THR B  49  ILE B  52  ASN B  54  ILE B  87                    
SITE     5 AC9 28 THR B 122  GLY B 123  TRP B 138  GLN B 139                    
SITE     6 AC9 28 CYS B 148  LEU B 262  GLY B 293  ASP B 294                    
SITE     7 AC9 28 ARG B 301  GLN B 302  ALA B 303  SER B 306                    
SITE     1 AD1  1 HOH B 503                                                     
SITE     1 AD2  6 THR B  50  GLN B 139  ASN B 140  GLY B 141                    
SITE     2 AD2  6 ASP B 149  VAL B 152                                          
SITE     1 AD3  2 GLY B 133  THR B 136                                          
SITE     1 AD4  2 SER B 181  SER B 182                                          
SITE     1 AD5  2 MLI A 404  ARG B 299                                          
SITE     1 AD6  4 ARG A  24  PHE A  78  GLU B  53  ALA B 151                    
SITE     1 AD7  4 GLU A  53  ALA A 151  ARG B  24  PHE B  78                    
SITE     1 AD8  7 LEU B 129  GLY B 165  GLY B 166  SER B 168                    
SITE     2 AD8  7 ARG B 188  ARG B 193  VAL B 254                               
SITE     1 AD9  7 THR A 305  GLY A 308  SER A 309  THR B 305                    
SITE     2 AD9  7 GLY B 308  SER B 309  ILE B 312                               
CRYST1  159.220  159.220  121.370  90.00  90.00 120.00 P 32 2 1     12          
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      0.006281  0.003626  0.000000        0.00000                         
SCALE2      0.000000  0.007252  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008239        0.00000                         
ATOM      1  N   VAL A   2     -41.295  26.881 -32.048  1.00  9.83           N  
ATOM      2  CA  VAL A   2     -41.250  28.196 -32.674  1.00 18.04           C  
ATOM      3  C   VAL A   2     -42.335  29.096 -32.094  1.00 39.64           C  
ATOM      4  O   VAL A   2     -43.001  28.735 -31.125  1.00 37.78           O  
ATOM      5  CB  VAL A   2     -41.392  28.088 -34.203  1.00 17.57           C  
ATOM      6  N   HIS A   3     -42.506  30.272 -32.695  1.00 56.05           N  
ATOM      7  CA  HIS A   3     -43.510  31.232 -32.260  1.00 51.29           C  
ATOM      8  C   HIS A   3     -43.832  32.155 -33.424  1.00 32.67           C  
ATOM      9  O   HIS A   3     -42.943  32.510 -34.203  1.00 16.36           O  
ATOM     10  CB  HIS A   3     -43.033  32.046 -31.050  1.00 50.38           C  
ATOM     11  CG  HIS A   3     -44.022  33.070 -30.583  1.00 36.23           C  
ATOM     12  ND1 HIS A   3     -45.283  32.740 -30.135  1.00 26.29           N  
ATOM     13  CD2 HIS A   3     -43.935  34.419 -30.497  1.00 28.10           C  
ATOM     14  CE1 HIS A   3     -45.929  33.840 -29.791  1.00 16.12           C  
ATOM     15  NE2 HIS A   3     -45.133  34.873 -30.002  1.00 24.13           N  
ATOM     16  N   THR A   4     -45.102  32.537 -33.539  1.00 32.67           N  
ATOM     17  CA  THR A   4     -45.544  33.410 -34.615  1.00 30.34           C  
ATOM     18  C   THR A   4     -46.630  34.346 -34.104  1.00 26.22           C  
ATOM     19  O   THR A   4     -47.123  34.213 -32.981  1.00  9.61           O  
ATOM     20  CB  THR A   4     -46.059  32.605 -35.812  1.00 13.75           C  
ATOM     21  N   LYS A   5     -46.995  35.312 -34.950  1.00 35.42           N  
ATOM     22  CA  LYS A   5     -48.041  36.265 -34.593  1.00 26.79           C  
ATOM     23  C   LYS A   5     -49.415  35.605 -34.616  1.00 20.88           C  
ATOM     24  O   LYS A   5     -50.136  35.605 -33.611  1.00 11.12           O  
ATOM     25  CB  LYS A   5     -47.998  37.467 -35.540  1.00  9.65           C  
ATOM     26  N   VAL A   6     -49.795  35.034 -35.758  1.00 24.85           N  
ATOM     27  CA  VAL A   6     -51.094  34.395 -35.932  1.00 18.88           C  
ATOM     28  C   VAL A   6     -50.887  33.020 -36.549  1.00 33.57           C  
ATOM     29  O   VAL A   6     -50.072  32.854 -37.464  1.00 29.88           O  
ATOM     30  CB  VAL A   6     -52.044  35.238 -36.813  1.00  4.79           C  
ATOM     31  CG1 VAL A   6     -53.338  34.483 -37.084  1.00 13.98           C  
ATOM     32  CG2 VAL A   6     -52.350  36.562 -36.153  1.00  3.09           C  
ATOM     33  N   VAL A   7     -51.631  32.035 -36.050  1.00 31.67           N  
ATOM     34  CA  VAL A   7     -51.647  30.688 -36.602  1.00  9.24           C  
ATOM     35  C   VAL A   7     -53.043  30.421 -37.145  1.00  7.81           C  
ATOM     36  O   VAL A   7     -54.044  30.779 -36.515  1.00 15.85           O  
ATOM     37  CB  VAL A   7     -51.245  29.632 -35.548  1.00 10.03           C  
ATOM     38  CG1 VAL A   7     -52.096  29.764 -34.294  1.00  8.60           C  
ATOM     39  CG2 VAL A   7     -51.358  28.225 -36.123  1.00 14.29           C  
ATOM     40  N   ILE A   8     -53.110  29.822 -38.330  1.00  8.50           N  
ATOM     41  CA  ILE A   8     -54.375  29.506 -38.980  1.00  7.38           C  
ATOM     42  C   ILE A   8     -54.474  27.995 -39.116  1.00  7.84           C  
ATOM     43  O   ILE A   8     -53.529  27.345 -39.580  1.00 11.34           O  
ATOM     44  CB  ILE A   8     -54.503  30.193 -40.351  1.00  7.67           C  
ATOM     45  CG1 ILE A   8     -54.059  31.653 -40.255  1.00 18.39           C  
ATOM     46  CG2 ILE A   8     -55.935  30.107 -40.854  1.00  6.31           C  
ATOM     47  CD1 ILE A   8     -54.271  32.437 -41.526  1.00 12.90           C  
ATOM     48  N   ILE A   9     -55.613  27.442 -38.716  1.00  9.74           N  
ATOM     49  CA  ILE A   9     -55.863  26.008 -38.784  1.00  6.20           C  
ATOM     50  C   ILE A   9     -56.890  25.778 -39.881  1.00  5.43           C  
ATOM     51  O   ILE A   9     -58.061  26.153 -39.742  1.00  3.91           O  
ATOM     52  CB  ILE A   9     -56.349  25.446 -37.443  1.00  5.04           C  
ATOM     53  CG1 ILE A   9     -55.392  25.841 -36.320  1.00  5.77           C  
ATOM     54  CG2 ILE A   9     -56.476  23.933 -37.520  1.00  9.40           C  
ATOM     55  CD1 ILE A   9     -55.830  25.361 -34.957  1.00  4.71           C  
ATOM     56  N   GLY A  10     -56.454  25.169 -40.968  1.00  7.82           N  
ATOM     57  CA  GLY A  10     -57.335  24.867 -42.079  1.00 11.60           C  
ATOM     58  C   GLY A  10     -56.592  24.962 -43.393  1.00  7.43           C  
ATOM     59  O   GLY A  10     -55.441  25.384 -43.462  1.00  8.97           O  
ATOM     60  N   SER A  11     -57.281  24.543 -44.455  1.00  6.94           N  
ATOM     61  CA  SER A  11     -56.717  24.637 -45.795  1.00  8.20           C  
ATOM     62  C   SER A  11     -57.764  25.016 -46.838  1.00 14.15           C  
ATOM     63  O   SER A  11     -57.525  24.828 -48.036  1.00  8.81           O  
ATOM     64  CB  SER A  11     -56.038  23.325 -46.190  1.00 18.50           C  
ATOM     65  OG  SER A  11     -56.953  22.245 -46.152  1.00 47.57           O  
ATOM     66  N   GLY A  12     -58.916  25.536 -46.420  1.00 23.39           N  
ATOM     67  CA  GLY A  12     -59.971  25.878 -47.342  1.00 22.18           C  
ATOM     68  C   GLY A  12     -59.910  27.322 -47.792  1.00 18.53           C  
ATOM     69  O   GLY A  12     -58.944  28.042 -47.516  1.00 35.15           O  
ATOM     70  N   PRO A  13     -60.945  27.773 -48.510  1.00  5.55           N  
ATOM     71  CA  PRO A  13     -60.968  29.179 -48.949  1.00  6.35           C  
ATOM     72  C   PRO A  13     -60.881  30.172 -47.804  1.00  6.07           C  
ATOM     73  O   PRO A  13     -60.218  31.208 -47.940  1.00 12.99           O  
ATOM     74  CB  PRO A  13     -62.301  29.290 -49.707  1.00  5.51           C  
ATOM     75  CG  PRO A  13     -63.088  28.074 -49.315  1.00  3.96           C  
ATOM     76  CD  PRO A  13     -62.077  27.008 -49.053  1.00  4.22           C  
ATOM     77  N   ALA A  14     -61.538  29.891 -46.678  1.00  4.60           N  
ATOM     78  CA  ALA A  14     -61.437  30.785 -45.529  1.00  4.05           C  
ATOM     79  C   ALA A  14     -60.021  30.809 -44.967  1.00 16.68           C  
ATOM     80  O   ALA A  14     -59.494  31.878 -44.640  1.00 19.42           O  
ATOM     81  CB  ALA A  14     -62.435  30.371 -44.450  1.00  2.43           C  
ATOM     82  N   ALA A  15     -59.388  29.639 -44.853  1.00 33.72           N  
ATOM     83  CA  ALA A  15     -58.059  29.572 -44.256  1.00 31.24           C  
ATOM     84  C   ALA A  15     -57.004  30.237 -45.129  1.00 18.43           C  
ATOM     85  O   ALA A  15     -56.011  30.758 -44.607  1.00 42.90           O  
ATOM     86  CB  ALA A  15     -57.678  28.117 -43.985  1.00 52.46           C  
ATOM     87  N   HIS A  16     -57.194  30.236 -46.447  1.00  9.11           N  
ATOM     88  CA  HIS A  16     -56.197  30.816 -47.337  1.00 18.88           C  
ATOM     89  C   HIS A  16     -56.413  32.307 -47.553  1.00 22.72           C  
ATOM     90  O   HIS A  16     -55.446  33.076 -47.533  1.00 11.99           O  
ATOM     91  CB  HIS A  16     -56.198  30.086 -48.682  1.00 11.95           C  
ATOM     92  CG  HIS A  16     -55.388  28.829 -48.686  1.00 12.55           C  
ATOM     93  ND1 HIS A  16     -54.033  28.818 -48.938  1.00 14.16           N  
ATOM     94  CD2 HIS A  16     -55.738  27.540 -48.460  1.00 11.54           C  
ATOM     95  CE1 HIS A  16     -53.585  27.577 -48.875  1.00 13.97           C  
ATOM     96  NE2 HIS A  16     -54.599  26.783 -48.583  1.00 12.47           N  
ATOM     97  N   THR A  17     -57.663  32.735 -47.754  1.00 23.43           N  
ATOM     98  CA  THR A  17     -57.939  34.162 -47.881  1.00 18.91           C  
ATOM     99  C   THR A  17     -57.510  34.916 -46.628  1.00 21.02           C  
ATOM    100  O   THR A  17     -56.965  36.022 -46.716  1.00 38.71           O  
ATOM    101  CB  THR A  17     -59.423  34.392 -48.169  1.00  8.30           C  
ATOM    102  OG1 THR A  17     -59.808  33.637 -49.323  1.00 10.40           O  
ATOM    103  CG2 THR A  17     -59.690  35.865 -48.433  1.00  8.39           C  
ATOM    104  N   ALA A  18     -57.741  34.328 -45.451  1.00  7.03           N  
ATOM    105  CA  ALA A  18     -57.217  34.913 -44.222  1.00  7.04           C  
ATOM    106  C   ALA A  18     -55.694  34.933 -44.233  1.00 18.48           C  
ATOM    107  O   ALA A  18     -55.072  35.910 -43.800  1.00 20.30           O  
ATOM    108  CB  ALA A  18     -57.735  34.143 -43.007  1.00  4.70           C  
ATOM    109  N   ALA A  19     -55.076  33.857 -44.728  1.00 15.60           N  
ATOM    110  CA  ALA A  19     -53.621  33.811 -44.821  1.00 21.64           C  
ATOM    111  C   ALA A  19     -53.088  34.800 -45.849  1.00 36.41           C  
ATOM    112  O   ALA A  19     -52.005  35.365 -45.657  1.00 54.99           O  
ATOM    113  CB  ALA A  19     -53.166  32.392 -45.158  1.00 28.05           C  
ATOM    114  N   ILE A  20     -53.826  35.020 -46.939  1.00 21.35           N  
ATOM    115  CA  ILE A  20     -53.378  35.948 -47.975  1.00 14.00           C  
ATOM    116  C   ILE A  20     -53.293  37.366 -47.422  1.00 12.40           C  
ATOM    117  O   ILE A  20     -52.290  38.065 -47.609  1.00 22.35           O  
ATOM    118  CB  ILE A  20     -54.302  35.874 -49.204  1.00 14.43           C  
ATOM    119  CG1 ILE A  20     -54.145  34.527 -49.912  1.00 15.79           C  
ATOM    120  CG2 ILE A  20     -54.010  37.019 -50.163  1.00 15.14           C  
ATOM    121  CD1 ILE A  20     -55.143  34.297 -51.025  1.00 14.99           C  
ATOM    122  N   TYR A  21     -54.346  37.813 -46.733  1.00 10.10           N  
ATOM    123  CA  TYR A  21     -54.361  39.182 -46.228  1.00  8.52           C  
ATOM    124  C   TYR A  21     -53.325  39.390 -45.129  1.00  9.82           C  
ATOM    125  O   TYR A  21     -52.703  40.457 -45.057  1.00 27.04           O  
ATOM    126  CB  TYR A  21     -55.762  39.550 -45.738  1.00  6.84           C  
ATOM    127  CG  TYR A  21     -56.683  40.009 -46.849  1.00 22.78           C  
ATOM    128  CD1 TYR A  21     -57.379  39.091 -47.626  1.00 19.01           C  
ATOM    129  CD2 TYR A  21     -56.849  41.360 -47.127  1.00 42.00           C  
ATOM    130  CE1 TYR A  21     -58.217  39.506 -48.645  1.00 13.41           C  
ATOM    131  CE2 TYR A  21     -57.686  41.785 -48.144  1.00 47.44           C  
ATOM    132  CZ  TYR A  21     -58.367  40.853 -48.900  1.00 28.61           C  
ATOM    133  OH  TYR A  21     -59.201  41.266 -49.914  1.00 30.60           O  
ATOM    134  N   LEU A  22     -53.118  38.392 -44.264  1.00  7.26           N  
ATOM    135  CA  LEU A  22     -52.105  38.543 -43.222  1.00  6.48           C  
ATOM    136  C   LEU A  22     -50.697  38.511 -43.795  1.00 34.29           C  
ATOM    137  O   LEU A  22     -49.807  39.200 -43.285  1.00 43.02           O  
ATOM    138  CB  LEU A  22     -52.250  37.463 -42.152  1.00  6.09           C  
ATOM    139  CG  LEU A  22     -53.160  37.756 -40.958  1.00  4.07           C  
ATOM    140  CD1 LEU A  22     -54.551  38.128 -41.397  1.00  3.38           C  
ATOM    141  CD2 LEU A  22     -53.197  36.562 -40.025  1.00 12.99           C  
ATOM    142  N   SER A  23     -50.474  37.737 -44.855  1.00 40.58           N  
ATOM    143  CA  SER A  23     -49.143  37.690 -45.442  1.00 23.40           C  
ATOM    144  C   SER A  23     -48.860  38.936 -46.272  1.00 14.66           C  
ATOM    145  O   SER A  23     -47.730  39.437 -46.273  1.00 13.06           O  
ATOM    146  CB  SER A  23     -48.991  36.428 -46.286  1.00 15.33           C  
ATOM    147  OG  SER A  23     -50.047  36.317 -47.223  1.00 38.09           O  
ATOM    148  N   ARG A  24     -49.869  39.457 -46.974  1.00 19.10           N  
ATOM    149  CA  ARG A  24     -49.686  40.721 -47.676  1.00 28.17           C  
ATOM    150  C   ARG A  24     -49.524  41.885 -46.707  1.00 22.06           C  
ATOM    151  O   ARG A  24     -48.924  42.902 -47.072  1.00  9.72           O  
ATOM    152  CB  ARG A  24     -50.855  40.986 -48.630  1.00 18.94           C  
ATOM    153  CG  ARG A  24     -50.519  41.993 -49.721  1.00 14.02           C  
ATOM    154  CD  ARG A  24     -51.709  42.331 -50.600  1.00 14.17           C  
ATOM    155  NE  ARG A  24     -51.285  42.975 -51.841  1.00 15.49           N  
ATOM    156  CZ  ARG A  24     -52.092  43.661 -52.644  1.00 38.68           C  
ATOM    157  NH1 ARG A  24     -53.374  43.801 -52.338  1.00 57.75           N  
ATOM    158  NH2 ARG A  24     -51.617  44.209 -53.755  1.00 38.10           N  
ATOM    159  N   ALA A  25     -50.039  41.753 -45.482  1.00 13.73           N  
ATOM    160  CA  ALA A  25     -49.861  42.737 -44.423  1.00 14.74           C  
ATOM    161  C   ALA A  25     -48.541  42.576 -43.681  1.00 24.07           C  
ATOM    162  O   ALA A  25     -48.409  43.089 -42.563  1.00 29.30           O  
ATOM    163  CB  ALA A  25     -51.026  42.665 -43.432  1.00  3.55           C  
ATOM    164  N   GLU A  26     -47.584  41.855 -44.266  1.00 27.85           N  
ATOM    165  CA  GLU A  26     -46.234  41.695 -43.728  1.00 30.01           C  
ATOM    166  C   GLU A  26     -46.215  40.952 -42.397  1.00 29.56           C  
ATOM    167  O   GLU A  26     -45.259  41.083 -41.625  1.00 46.92           O  
ATOM    168  CB  GLU A  26     -45.520  43.045 -43.590  1.00 31.19           C  
ATOM    169  CG  GLU A  26     -45.244  43.740 -44.913  1.00 49.95           C  
ATOM    170  CD  GLU A  26     -44.122  43.078 -45.691  1.00 63.75           C  
ATOM    171  OE1 GLU A  26     -44.155  43.109 -46.939  1.00 73.41           O  
ATOM    172  OE2 GLU A  26     -43.207  42.519 -45.051  1.00 67.21           O  
ATOM    173  N   LEU A  27     -47.251  40.173 -42.102  1.00 26.33           N  
ATOM    174  CA  LEU A  27     -47.300  39.447 -40.845  1.00 35.48           C  
ATOM    175  C   LEU A  27     -46.592  38.104 -41.018  1.00 32.93           C  
ATOM    176  O   LEU A  27     -46.036  37.796 -42.075  1.00 37.65           O  
ATOM    177  CB  LEU A  27     -48.745  39.270 -40.373  1.00 15.57           C  
ATOM    178  CG  LEU A  27     -49.194  40.174 -39.220  1.00  2.08           C  
ATOM    179  CD1 LEU A  27     -49.134  41.639 -39.626  1.00  1.95           C  
ATOM    180  CD2 LEU A  27     -50.591  39.809 -38.735  1.00  1.96           C  
ATOM    181  N   LYS A  28     -46.603  37.290 -39.964  1.00  7.74           N  
ATOM    182  CA  LYS A  28     -45.984  35.968 -39.975  1.00 10.18           C  
ATOM    183  C   LYS A  28     -47.052  34.913 -39.712  1.00 27.32           C  
ATOM    184  O   LYS A  28     -47.091  34.313 -38.631  1.00 42.69           O  
ATOM    185  CB  LYS A  28     -44.862  35.874 -38.943  1.00 27.62           C  
ATOM    186  N   PRO A  29     -47.947  34.671 -40.670  1.00 18.77           N  
ATOM    187  CA  PRO A  29     -48.973  33.649 -40.453  1.00 11.45           C  
ATOM    188  C   PRO A  29     -48.503  32.271 -40.888  1.00 19.22           C  
ATOM    189  O   PRO A  29     -47.831  32.100 -41.908  1.00 22.16           O  
ATOM    190  CB  PRO A  29     -50.132  34.140 -41.331  1.00 10.43           C  
ATOM    191  CG  PRO A  29     -49.491  35.063 -42.372  1.00 11.07           C  
ATOM    192  CD  PRO A  29     -48.034  35.243 -42.023  1.00 11.79           C  
ATOM    193  N   VAL A  30     -48.871  31.271 -40.093  1.00 13.82           N  
ATOM    194  CA  VAL A  30     -48.591  29.874 -40.396  1.00 15.20           C  
ATOM    195  C   VAL A  30     -49.914  29.179 -40.682  1.00 30.90           C  
ATOM    196  O   VAL A  30     -50.874  29.314 -39.913  1.00 28.49           O  
ATOM    197  CB  VAL A  30     -47.820  29.181 -39.257  1.00 15.76           C  
ATOM    198  CG1 VAL A  30     -46.374  29.644 -39.243  1.00 17.29           C  
ATOM    199  CG2 VAL A  30     -48.466  29.463 -37.917  1.00 14.55           C  
ATOM    200  N   LEU A  31     -49.971  28.458 -41.795  1.00 29.45           N  
ATOM    201  CA  LEU A  31     -51.188  27.789 -42.231  1.00 16.98           C  
ATOM    202  C   LEU A  31     -50.955  26.287 -42.143  1.00 25.25           C  
ATOM    203  O   LEU A  31     -50.041  25.759 -42.784  1.00 35.08           O  
ATOM    204  CB  LEU A  31     -51.562  28.209 -43.652  1.00 15.07           C  
ATOM    205  CG  LEU A  31     -52.883  27.663 -44.181  1.00 12.75           C  
ATOM    206  CD1 LEU A  31     -54.009  28.141 -43.289  1.00 10.83           C  
ATOM    207  CD2 LEU A  31     -53.106  28.120 -45.605  1.00 13.38           C  
ATOM    208  N   TYR A  32     -51.780  25.608 -41.353  1.00 24.08           N  
ATOM    209  CA  TYR A  32     -51.681  24.164 -41.151  1.00 11.63           C  
ATOM    210  C   TYR A  32     -52.726  23.465 -42.012  1.00 10.68           C  
ATOM    211  O   TYR A  32     -53.906  23.418 -41.656  1.00 31.97           O  
ATOM    212  CB  TYR A  32     -51.856  23.818 -39.676  1.00 10.74           C  
ATOM    213  CG  TYR A  32     -50.596  23.974 -38.855  1.00 11.54           C  
ATOM    214  CD1 TYR A  32     -49.641  22.967 -38.818  1.00 11.52           C  
ATOM    215  CD2 TYR A  32     -50.362  25.126 -38.117  1.00 11.97           C  
ATOM    216  CE1 TYR A  32     -48.488  23.102 -38.069  1.00 11.88           C  
ATOM    217  CE2 TYR A  32     -49.210  25.271 -37.365  1.00 21.76           C  
ATOM    218  CZ  TYR A  32     -48.277  24.255 -37.345  1.00 12.87           C  
ATOM    219  OH  TYR A  32     -47.128  24.390 -36.600  1.00 12.81           O  
ATOM    220  N   GLU A  33     -52.295  22.923 -43.154  1.00 11.10           N  
ATOM    221  CA  GLU A  33     -53.234  22.217 -44.018  1.00 10.10           C  
ATOM    222  C   GLU A  33     -53.559  20.835 -43.476  1.00 12.78           C  
ATOM    223  O   GLU A  33     -54.638  20.299 -43.751  1.00 11.05           O  
ATOM    224  CB  GLU A  33     -52.660  22.076 -45.426  1.00 10.65           C  
ATOM    225  CG  GLU A  33     -52.264  23.373 -46.080  1.00 12.05           C  
ATOM    226  CD  GLU A  33     -51.507  23.145 -47.369  1.00 30.21           C  
ATOM    227  OE1 GLU A  33     -50.933  22.047 -47.536  1.00 13.08           O  
ATOM    228  OE2 GLU A  33     -51.483  24.061 -48.218  1.00 47.74           O  
ATOM    229  N   GLY A  34     -52.644  20.248 -42.720  1.00 12.97           N  
ATOM    230  CA  GLY A  34     -52.827  18.930 -42.159  1.00  7.55           C  
ATOM    231  C   GLY A  34     -52.155  17.845 -42.983  1.00  7.03           C  
ATOM    232  O   GLY A  34     -51.785  18.033 -44.144  1.00  7.39           O  
ATOM    233  N   MET A  35     -52.003  16.687 -42.352  1.00 12.03           N  
ATOM    234  CA  MET A  35     -51.495  15.467 -42.978  1.00  4.69           C  
ATOM    235  C   MET A  35     -52.639  14.694 -43.624  1.00 15.59           C  
ATOM    236  O   MET A  35     -52.796  13.491 -43.416  1.00 33.72           O  
ATOM    237  CB  MET A  35     -50.763  14.617 -41.946  1.00  3.67           C  
ATOM    238  N   LEU A  36     -53.457  15.418 -44.396  1.00 18.74           N  
ATOM    239  CA  LEU A  36     -54.756  14.955 -44.874  1.00 26.18           C  
ATOM    240  C   LEU A  36     -55.670  14.805 -43.665  1.00 39.35           C  
ATOM    241  O   LEU A  36     -56.216  13.728 -43.406  1.00 29.05           O  
ATOM    242  CB  LEU A  36     -54.649  13.647 -45.667  1.00  5.61           C  
ATOM    243  N   ALA A  37     -55.825  15.901 -42.924  1.00 40.69           N  
ATOM    244  CA  ALA A  37     -56.558  15.890 -41.665  1.00 35.99           C  
ATOM    245  C   ALA A  37     -58.050  15.682 -41.891  1.00 44.79           C  
ATOM    246  O   ALA A  37     -58.651  16.297 -42.775  1.00 55.35           O  
ATOM    247  CB  ALA A  37     -56.328  17.203 -40.917  1.00  4.78           C  
ATOM    248  N   ASN A  38     -58.645  14.821 -41.065  1.00 25.39           N  
ATOM    249  CA  ASN A  38     -60.081  14.539 -41.094  1.00  8.70           C  
ATOM    250  C   ASN A  38     -60.563  14.115 -42.479  1.00  2.30           C  
ATOM    251  O   ASN A  38     -59.883  13.368 -43.182  1.00  1.95           O  
ATOM    252  CB  ASN A  38     -60.878  15.756 -40.615  1.00  1.95           C  
ATOM    253  N   THR A  40     -62.276  15.429 -45.661  1.00  1.95           N  
ATOM    254  CA  THR A  40     -61.612  16.260 -46.658  1.00 25.76           C  
ATOM    255  C   THR A  40     -60.114  16.356 -46.382  1.00 43.83           C  
ATOM    256  O   THR A  40     -59.700  16.751 -45.293  1.00 59.37           O  
ATOM    257  CB  THR A  40     -62.209  17.680 -46.699  1.00 26.49           C  
ATOM    258  N   ALA A  41     -59.306  16.000 -47.378  1.00 32.62           N  
ATOM    259  CA  ALA A  41     -57.859  16.011 -47.226  1.00 14.52           C  
ATOM    260  C   ALA A  41     -57.341  17.448 -47.157  1.00 21.36           C  
ATOM    261  O   ALA A  41     -58.098  18.422 -47.220  1.00 29.23           O  
ATOM    262  CB  ALA A  41     -57.200  15.248 -48.372  1.00 11.02           C  
ATOM    263  N   ALA A  42     -56.022  17.576 -47.025  1.00 28.79           N  
ATOM    264  CA  ALA A  42     -55.388  18.887 -46.953  1.00 34.35           C  
ATOM    265  C   ALA A  42     -55.574  19.628 -48.272  1.00 35.04           C  
ATOM    266  O   ALA A  42     -55.124  19.163 -49.325  1.00 46.06           O  
ATOM    267  CB  ALA A  42     -53.906  18.741 -46.620  1.00 30.79           C  
ATOM    268  N   GLY A  43     -56.234  20.781 -48.212  1.00 28.86           N  
ATOM    269  CA  GLY A  43     -56.517  21.563 -49.399  1.00 36.39           C  
ATOM    270  C   GLY A  43     -57.920  22.132 -49.397  1.00 47.64           C  
ATOM    271  O   GLY A  43     -58.227  23.052 -50.160  1.00 35.98           O  
ATOM    272  N   GLY A  44     -58.778  21.594 -48.542  1.00 54.80           N  
ATOM    273  CA  GLY A  44     -60.151  22.037 -48.425  1.00 32.83           C  
ATOM    274  C   GLY A  44     -61.130  21.013 -48.977  1.00 32.17           C  
ATOM    275  O   GLY A  44     -60.771  20.070 -49.683  1.00  7.79           O  
ATOM    276  N   GLN A  45     -62.401  21.223 -48.629  1.00 50.17           N  
ATOM    277  CA  GLN A  45     -63.472  20.378 -49.142  1.00 41.66           C  
ATOM    278  C   GLN A  45     -63.745  20.605 -50.624  1.00 35.44           C  
ATOM    279  O   GLN A  45     -64.475  19.813 -51.230  1.00 19.83           O  
ATOM    280  CB  GLN A  45     -64.751  20.606 -48.335  1.00 30.29           C  
ATOM    281  CG  GLN A  45     -65.742  19.457 -48.406  1.00 10.86           C  
ATOM    282  CD  GLN A  45     -66.971  19.695 -47.556  1.00 15.77           C  
ATOM    283  OE1 GLN A  45     -67.723  18.767 -47.261  1.00 22.71           O  
ATOM    284  NE2 GLN A  45     -67.183  20.945 -47.158  1.00  7.93           N  
ATOM    285  N   LEU A  46     -63.174  21.653 -51.223  1.00 34.34           N  
ATOM    286  CA  LEU A  46     -63.365  21.904 -52.646  1.00 20.32           C  
ATOM    287  C   LEU A  46     -62.530  20.984 -53.522  1.00 25.88           C  
ATOM    288  O   LEU A  46     -62.816  20.866 -54.718  1.00 34.93           O  
ATOM    289  CB  LEU A  46     -63.026  23.356 -52.983  1.00 12.90           C  
ATOM    290  CG  LEU A  46     -64.006  24.418 -52.494  1.00 14.15           C  
ATOM    291  CD1 LEU A  46     -63.586  25.791 -52.993  1.00 15.47           C  
ATOM    292  CD2 LEU A  46     -65.418  24.082 -52.944  1.00 15.08           C  
ATOM    293  N   THR A  47     -61.505  20.340 -52.959  1.00 22.83           N  
ATOM    294  CA  THR A  47     -60.684  19.422 -53.739  1.00 33.55           C  
ATOM    295  C   THR A  47     -61.476  18.225 -54.247  1.00 45.60           C  
ATOM    296  O   THR A  47     -61.089  17.624 -55.256  1.00 48.41           O  
ATOM    297  CB  THR A  47     -59.494  18.941 -52.905  1.00 28.33           C  
ATOM    298  OG1 THR A  47     -59.968  18.344 -51.691  1.00 29.46           O  
ATOM    299  CG2 THR A  47     -58.575  20.105 -52.567  1.00  5.07           C  
ATOM    300  N   THR A  48     -62.574  17.865 -53.578  1.00 49.52           N  
ATOM    301  CA  THR A  48     -63.375  16.732 -54.027  1.00 36.58           C  
ATOM    302  C   THR A  48     -64.292  17.102 -55.188  1.00 35.06           C  
ATOM    303  O   THR A  48     -64.583  16.250 -56.034  1.00 45.92           O  
ATOM    304  CB  THR A  48     -64.203  16.177 -52.866  1.00 17.69           C  
ATOM    305  OG1 THR A  48     -64.999  17.225 -52.297  1.00 23.83           O  
ATOM    306  CG2 THR A  48     -63.295  15.597 -51.788  1.00  1.95           C  
ATOM    307  N   THR A  49     -64.750  18.352 -55.246  1.00 15.55           N  
ATOM    308  CA  THR A  49     -65.624  18.788 -56.327  1.00 12.76           C  
ATOM    309  C   THR A  49     -64.875  18.792 -57.655  1.00 20.17           C  
ATOM    310  O   THR A  49     -63.706  19.181 -57.726  1.00 21.53           O  
ATOM    311  CB  THR A  49     -66.179  20.182 -56.033  1.00 25.67           C  
ATOM    312  OG1 THR A  49     -66.693  20.220 -54.697  1.00 33.90           O  
ATOM    313  CG2 THR A  49     -67.300  20.531 -57.006  1.00 16.15           C  
ATOM    314  N   THR A  50     -65.562  18.365 -58.716  1.00 29.81           N  
ATOM    315  CA  THR A  50     -64.919  18.270 -60.023  1.00 28.44           C  
ATOM    316  C   THR A  50     -64.848  19.629 -60.711  1.00 14.17           C  
ATOM    317  O   THR A  50     -63.794  20.015 -61.227  1.00 14.21           O  
ATOM    318  CB  THR A  50     -65.660  17.263 -60.909  1.00 25.74           C  
ATOM    319  OG1 THR A  50     -67.054  17.592 -60.951  1.00 17.76           O  
ATOM    320  CG2 THR A  50     -65.484  15.846 -60.378  1.00  8.90           C  
ATOM    321  N   ASP A  51     -65.954  20.370 -60.724  1.00 15.50           N  
ATOM    322  CA  ASP A  51     -66.007  21.662 -61.395  1.00 17.53           C  
ATOM    323  C   ASP A  51     -66.865  22.626 -60.592  1.00 24.12           C  
ATOM    324  O   ASP A  51     -68.019  22.321 -60.275  1.00 18.08           O  
ATOM    325  CB  ASP A  51     -66.559  21.527 -62.821  1.00 20.96           C  
ATOM    326  CG  ASP A  51     -65.497  21.106 -63.821  1.00 35.97           C  
ATOM    327  OD1 ASP A  51     -64.319  21.478 -63.635  1.00 41.16           O  
ATOM    328  OD2 ASP A  51     -65.841  20.406 -64.796  1.00 41.96           O  
ATOM    329  N   ILE A  52     -66.294  23.782 -60.265  1.00 28.49           N  
ATOM    330  CA  ILE A  52     -67.003  24.861 -59.586  1.00 19.18           C  
ATOM    331  C   ILE A  52     -67.377  25.906 -60.627  1.00 21.44           C  
ATOM    332  O   ILE A  52     -66.501  26.486 -61.281  1.00 21.31           O  
ATOM    333  CB  ILE A  52     -66.150  25.481 -58.468  1.00 18.53           C  
ATOM    334  CG1 ILE A  52     -65.737  24.417 -57.451  1.00 24.26           C  
ATOM    335  CG2 ILE A  52     -66.899  26.617 -57.790  1.00 18.52           C  
ATOM    336  CD1 ILE A  52     -64.757  24.921 -56.420  1.00 28.86           C  
ATOM    337  N   GLU A  53     -68.677  26.169 -60.767  1.00 20.86           N  
ATOM    338  CA  GLU A  53     -69.167  27.103 -61.767  1.00 21.99           C  
ATOM    339  C   GLU A  53     -69.800  28.349 -61.167  1.00 20.84           C  
ATOM    340  O   GLU A  53     -70.052  29.309 -61.903  1.00 21.21           O  
ATOM    341  CB  GLU A  53     -70.199  26.415 -62.677  1.00 21.61           C  
ATOM    342  CG  GLU A  53     -69.770  25.068 -63.249  1.00 21.60           C  
ATOM    343  CD  GLU A  53     -68.702  25.189 -64.318  1.00 29.48           C  
ATOM    344  OE1 GLU A  53     -67.629  24.569 -64.163  1.00 43.83           O  
ATOM    345  OE2 GLU A  53     -68.936  25.903 -65.315  1.00 32.83           O  
ATOM    346  N   ASN A  54     -70.046  28.369 -59.856  1.00 22.33           N  
ATOM    347  CA  ASN A  54     -70.666  29.502 -59.184  1.00 16.78           C  
ATOM    348  C   ASN A  54     -69.658  30.354 -58.421  1.00 18.03           C  
ATOM    349  O   ASN A  54     -70.042  31.077 -57.495  1.00 14.54           O  
ATOM    350  CB  ASN A  54     -71.774  29.018 -58.245  1.00 33.48           C  
ATOM    351  CG  ASN A  54     -71.252  28.132 -57.131  1.00 33.40           C  
ATOM    352  OD1 ASN A  54     -70.151  27.588 -57.216  1.00 46.93           O  
ATOM    353  ND2 ASN A  54     -72.047  27.978 -56.078  1.00 19.05           N  
ATOM    354  N   PHE A  55     -68.374  30.278 -58.784  1.00 32.77           N  
ATOM    355  CA  PHE A  55     -67.381  31.137 -58.153  1.00 25.11           C  
ATOM    356  C   PHE A  55     -67.104  32.335 -59.045  1.00 33.46           C  
ATOM    357  O   PHE A  55     -66.773  32.154 -60.226  1.00 50.81           O  
ATOM    358  CB  PHE A  55     -66.086  30.372 -57.891  1.00 19.26           C  
ATOM    359  CG  PHE A  55     -65.198  31.018 -56.864  1.00 17.81           C  
ATOM    360  CD1 PHE A  55     -65.384  30.768 -55.513  1.00 26.75           C  
ATOM    361  CD2 PHE A  55     -64.179  31.875 -57.246  1.00 15.96           C  
ATOM    362  CE1 PHE A  55     -64.571  31.360 -54.564  1.00 15.72           C  
ATOM    363  CE2 PHE A  55     -63.362  32.469 -56.300  1.00 14.18           C  
ATOM    364  CZ  PHE A  55     -63.559  32.212 -54.958  1.00 14.63           C  
ATOM    365  N   PRO A  56     -67.230  33.557 -58.532  1.00 29.29           N  
ATOM    366  CA  PRO A  56     -67.084  34.737 -59.393  1.00 17.22           C  
ATOM    367  C   PRO A  56     -65.645  34.945 -59.838  1.00 16.66           C  
ATOM    368  O   PRO A  56     -64.701  34.788 -59.059  1.00 28.29           O  
ATOM    369  CB  PRO A  56     -67.559  35.884 -58.498  1.00 10.10           C  
ATOM    370  CG  PRO A  56     -67.277  35.403 -57.114  1.00  9.93           C  
ATOM    371  CD  PRO A  56     -67.518  33.922 -57.134  1.00 12.11           C  
ATOM    372  N   GLY A  57     -65.486  35.307 -61.109  1.00 11.83           N  
ATOM    373  CA  GLY A  57     -64.184  35.502 -61.714  1.00 19.63           C  
ATOM    374  C   GLY A  57     -63.775  34.404 -62.668  1.00 41.76           C  
ATOM    375  O   GLY A  57     -62.786  34.572 -63.394  1.00 42.44           O  
ATOM    376  N   PHE A  58     -64.503  33.285 -62.689  1.00 41.04           N  
ATOM    377  CA  PHE A  58     -64.230  32.153 -63.571  1.00 16.80           C  
ATOM    378  C   PHE A  58     -65.502  31.871 -64.362  1.00 19.84           C  
ATOM    379  O   PHE A  58     -66.292  30.987 -63.996  1.00 27.57           O  
ATOM    380  CB  PHE A  58     -63.780  30.927 -62.779  1.00 17.52           C  
ATOM    381  CG  PHE A  58     -62.600  31.185 -61.886  1.00 14.82           C  
ATOM    382  CD1 PHE A  58     -61.308  31.060 -62.367  1.00 24.52           C  
ATOM    383  CD2 PHE A  58     -62.785  31.551 -60.563  1.00 14.79           C  
ATOM    384  CE1 PHE A  58     -60.221  31.298 -61.547  1.00 10.21           C  
ATOM    385  CE2 PHE A  58     -61.701  31.789 -59.737  1.00 12.60           C  
ATOM    386  CZ  PHE A  58     -60.418  31.662 -60.231  1.00 10.35           C  
ATOM    387  N   PRO A  59     -65.736  32.606 -65.453  1.00 20.27           N  
ATOM    388  CA  PRO A  59     -67.001  32.438 -66.184  1.00 25.21           C  
ATOM    389  C   PRO A  59     -67.134  31.084 -66.853  1.00 26.95           C  
ATOM    390  O   PRO A  59     -68.261  30.618 -67.059  1.00 28.73           O  
ATOM    391  CB  PRO A  59     -66.963  33.576 -67.212  1.00 33.32           C  
ATOM    392  CG  PRO A  59     -65.505  33.835 -67.419  1.00 38.14           C  
ATOM    393  CD  PRO A  59     -64.856  33.605 -66.082  1.00 35.18           C  
ATOM    394  N   ASP A  60     -66.025  30.439 -67.201  1.00 23.51           N  
ATOM    395  CA  ASP A  60     -66.055  29.110 -67.793  1.00 36.68           C  
ATOM    396  C   ASP A  60     -65.916  28.008 -66.752  1.00 51.72           C  
ATOM    397  O   ASP A  60     -65.656  26.856 -67.115  1.00 70.68           O  
ATOM    398  CB  ASP A  60     -64.953  28.976 -68.847  1.00 50.51           C  
ATOM    399  CG  ASP A  60     -65.142  29.930 -70.011  1.00 63.86           C  
ATOM    400  OD1 ASP A  60     -66.305  30.247 -70.339  1.00 64.90           O  
ATOM    401  OD2 ASP A  60     -64.127  30.363 -70.597  1.00 67.79           O  
ATOM    402  N   GLY A  61     -66.083  28.335 -65.472  1.00 41.08           N  
ATOM    403  CA  GLY A  61     -65.926  27.363 -64.409  1.00 23.18           C  
ATOM    404  C   GLY A  61     -64.478  27.017 -64.133  1.00 20.57           C  
ATOM    405  O   GLY A  61     -63.605  27.258 -64.972  1.00 19.11           O  
ATOM    406  N   ILE A  62     -64.208  26.455 -62.958  1.00 19.62           N  
ATOM    407  CA  ILE A  62     -62.855  26.051 -62.590  1.00 17.14           C  
ATOM    408  C   ILE A  62     -62.943  24.819 -61.702  1.00 21.20           C  
ATOM    409  O   ILE A  62     -63.843  24.700 -60.866  1.00 39.36           O  
ATOM    410  CB  ILE A  62     -62.089  27.201 -61.897  1.00 15.84           C  
ATOM    411  CG1 ILE A  62     -60.646  26.786 -61.602  1.00 13.13           C  
ATOM    412  CG2 ILE A  62     -62.802  27.642 -60.625  1.00 17.11           C  
ATOM    413  CD1 ILE A  62     -59.837  27.851 -60.897  1.00 23.14           C  
ATOM    414  N   GLY A  63     -62.010  23.892 -61.900  1.00 14.84           N  
ATOM    415  CA  GLY A  63     -61.963  22.707 -61.064  1.00 14.99           C  
ATOM    416  C   GLY A  63     -61.603  23.059 -59.631  1.00 13.30           C  
ATOM    417  O   GLY A  63     -60.727  23.886 -59.373  1.00 12.42           O  
ATOM    418  N   GLY A  64     -62.305  22.426 -58.688  1.00 13.72           N  
ATOM    419  CA  GLY A  64     -62.042  22.684 -57.282  1.00 13.00           C  
ATOM    420  C   GLY A  64     -60.611  22.388 -56.883  1.00 23.76           C  
ATOM    421  O   GLY A  64     -60.067  23.033 -55.982  1.00 13.28           O  
ATOM    422  N   ALA A  65     -59.980  21.421 -57.550  1.00 41.77           N  
ATOM    423  CA  ALA A  65     -58.581  21.121 -57.271  1.00 30.48           C  
ATOM    424  C   ALA A  65     -57.683  22.274 -57.698  1.00 18.97           C  
ATOM    425  O   ALA A  65     -56.801  22.700 -56.945  1.00 29.81           O  
ATOM    426  CB  ALA A  65     -58.171  19.825 -57.972  1.00 41.14           C  
ATOM    427  N   GLU A  66     -57.901  22.799 -58.908  1.00 23.82           N  
ATOM    428  CA  GLU A  66     -57.056  23.877 -59.411  1.00 16.22           C  
ATOM    429  C   GLU A  66     -57.342  25.199 -58.708  1.00 18.53           C  
ATOM    430  O   GLU A  66     -56.430  26.017 -58.540  1.00 35.43           O  
ATOM    431  CB  GLU A  66     -57.251  24.029 -60.922  1.00 13.34           C  
ATOM    432  CG  GLU A  66     -56.418  25.133 -61.562  1.00 45.70           C  
ATOM    433  CD  GLU A  66     -56.783  25.378 -63.016  1.00 50.60           C  
ATOM    434  OE1 GLU A  66     -57.617  24.622 -63.558  1.00 47.76           O  
ATOM    435  OE2 GLU A  66     -56.238  26.330 -63.615  1.00 39.43           O  
ATOM    436  N   LEU A  67     -58.587  25.424 -58.283  1.00 25.51           N  
ATOM    437  CA  LEU A  67     -58.910  26.655 -57.567  1.00 31.44           C  
ATOM    438  C   LEU A  67     -58.159  26.739 -56.246  1.00 25.42           C  
ATOM    439  O   LEU A  67     -57.546  27.766 -55.929  1.00 50.26           O  
ATOM    440  CB  LEU A  67     -60.418  26.750 -57.332  1.00 36.08           C  
ATOM    441  CG  LEU A  67     -60.887  27.996 -56.577  1.00 13.39           C  
ATOM    442  CD1 LEU A  67     -60.448  29.257 -57.306  1.00 14.13           C  
ATOM    443  CD2 LEU A  67     -62.394  27.981 -56.383  1.00 13.53           C  
ATOM    444  N   MET A  68     -58.193  25.663 -55.458  1.00 13.40           N  
ATOM    445  CA  MET A  68     -57.479  25.652 -54.189  1.00 13.53           C  
ATOM    446  C   MET A  68     -55.968  25.585 -54.367  1.00 16.89           C  
ATOM    447  O   MET A  68     -55.235  26.006 -53.465  1.00 31.18           O  
ATOM    448  CB  MET A  68     -57.961  24.488 -53.324  1.00 21.11           C  
ATOM    449  CG  MET A  68     -59.410  24.619 -52.877  1.00 37.44           C  
ATOM    450  SD  MET A  68     -59.764  26.191 -52.066  1.00 37.73           S  
ATOM    451  CE  MET A  68     -58.524  26.204 -50.776  1.00 11.47           C  
ATOM    452  N   GLU A  69     -55.483  25.072 -55.500  1.00 26.06           N  
ATOM    453  CA  GLU A  69     -54.046  25.106 -55.754  1.00 24.11           C  
ATOM    454  C   GLU A  69     -53.595  26.511 -56.126  1.00 31.56           C  
ATOM    455  O   GLU A  69     -52.522  26.958 -55.703  1.00 30.75           O  
ATOM    456  CB  GLU A  69     -53.675  24.108 -56.851  1.00 15.27           C  
ATOM    457  CG  GLU A  69     -52.176  23.964 -57.081  1.00 40.72           C  
ATOM    458  CD  GLU A  69     -51.460  23.296 -55.919  1.00 66.01           C  
ATOM    459  OE1 GLU A  69     -52.128  22.610 -55.117  1.00 74.03           O  
ATOM    460  OE2 GLU A  69     -50.226  23.459 -55.807  1.00 70.36           O  
ATOM    461  N   ASN A  70     -54.401  27.222 -56.920  1.00 31.29           N  
ATOM    462  CA  ASN A  70     -54.145  28.638 -57.159  1.00 15.26           C  
ATOM    463  C   ASN A  70     -54.214  29.423 -55.858  1.00 14.77           C  
ATOM    464  O   ASN A  70     -53.361  30.278 -55.589  1.00 16.55           O  
ATOM    465  CB  ASN A  70     -55.148  29.190 -58.173  1.00 14.63           C  
ATOM    466  CG  ASN A  70     -54.885  28.699 -59.580  1.00 14.88           C  
ATOM    467  OD1 ASN A  70     -54.030  27.842 -59.803  1.00 15.19           O  
ATOM    468  ND2 ASN A  70     -55.627  29.238 -60.542  1.00 29.94           N  
ATOM    469  N   MET A  71     -55.229  29.147 -55.039  1.00 14.04           N  
ATOM    470  CA  MET A  71     -55.360  29.826 -53.757  1.00 13.49           C  
ATOM    471  C   MET A  71     -54.231  29.451 -52.804  1.00 14.48           C  
ATOM    472  O   MET A  71     -53.883  30.240 -51.918  1.00 37.88           O  
ATOM    473  CB  MET A  71     -56.721  29.506 -53.143  1.00 12.76           C  
ATOM    474  CG  MET A  71     -57.260  30.582 -52.226  1.00 37.90           C  
ATOM    475  SD  MET A  71     -58.878  30.144 -51.574  1.00 26.47           S  
ATOM    476  CE  MET A  71     -59.818  29.983 -53.089  1.00 11.31           C  
ATOM    477  N   ARG A  72     -53.650  28.260 -52.964  1.00 15.47           N  
ATOM    478  CA  ARG A  72     -52.518  27.875 -52.128  1.00 19.48           C  
ATOM    479  C   ARG A  72     -51.273  28.680 -52.477  1.00 18.96           C  
ATOM    480  O   ARG A  72     -50.647  29.284 -51.598  1.00 19.97           O  
ATOM    481  CB  ARG A  72     -52.234  26.379 -52.266  1.00 27.24           C  
ATOM    482  CG  ARG A  72     -50.949  25.948 -51.571  1.00 32.12           C  
ATOM    483  CD  ARG A  72     -50.602  24.498 -51.862  1.00 35.11           C  
ATOM    484  NE  ARG A  72     -49.174  24.240 -51.690  1.00 41.80           N  
ATOM    485  CZ  ARG A  72     -48.609  23.865 -50.547  1.00 29.43           C  
ATOM    486  NH1 ARG A  72     -49.350  23.705 -49.461  1.00 20.48           N  
ATOM    487  NH2 ARG A  72     -47.301  23.653 -50.489  1.00 23.92           N  
ATOM    488  N   LYS A  73     -50.896  28.700 -53.759  1.00 18.18           N  
ATOM    489  CA  LYS A  73     -49.715  29.457 -54.161  1.00 19.25           C  
ATOM    490  C   LYS A  73     -49.906  30.952 -53.941  1.00 18.48           C  
ATOM    491  O   LYS A  73     -48.926  31.675 -53.727  1.00 21.93           O  
ATOM    492  CB  LYS A  73     -49.356  29.163 -55.620  1.00 24.50           C  
ATOM    493  CG  LYS A  73     -50.495  29.309 -56.608  1.00 31.76           C  
ATOM    494  CD  LYS A  73     -50.003  29.137 -58.039  1.00 26.73           C  
ATOM    495  CE  LYS A  73     -49.321  27.790 -58.244  1.00 29.56           C  
ATOM    496  NZ  LYS A  73     -50.248  26.645 -58.019  1.00 26.12           N  
ATOM    497  N   GLN A  74     -51.150  31.434 -53.987  1.00 25.32           N  
ATOM    498  CA  GLN A  74     -51.399  32.837 -53.673  1.00 28.82           C  
ATOM    499  C   GLN A  74     -51.135  33.135 -52.204  1.00 34.94           C  
ATOM    500  O   GLN A  74     -50.737  34.254 -51.861  1.00 45.28           O  
ATOM    501  CB  GLN A  74     -52.833  33.217 -54.034  1.00 13.59           C  
ATOM    502  CG  GLN A  74     -53.084  34.715 -54.037  1.00 17.05           C  
ATOM    503  CD  GLN A  74     -54.415  35.079 -54.653  1.00 18.44           C  
ATOM    504  OE1 GLN A  74     -55.196  34.205 -55.029  1.00 22.06           O  
ATOM    505  NE2 GLN A  74     -54.681  36.375 -54.764  1.00 17.43           N  
ATOM    506  N   SER A  75     -51.347  32.154 -51.327  1.00 18.82           N  
ATOM    507  CA  SER A  75     -51.038  32.349 -49.916  1.00 15.33           C  
ATOM    508  C   SER A  75     -49.532  32.346 -49.679  1.00 16.26           C  
ATOM    509  O   SER A  75     -49.004  33.211 -48.970  1.00 15.76           O  
ATOM    510  CB  SER A  75     -51.725  31.268 -49.081  1.00 15.26           C  
ATOM    511  OG  SER A  75     -51.432  31.418 -47.704  1.00 16.28           O  
ATOM    512  N   ILE A  76     -48.820  31.384 -50.272  1.00 17.68           N  
ATOM    513  CA  ILE A  76     -47.378  31.295 -50.070  1.00 18.91           C  
ATOM    514  C   ILE A  76     -46.636  32.398 -50.811  1.00 34.74           C  
ATOM    515  O   ILE A  76     -45.488  32.704 -50.466  1.00 52.84           O  
ATOM    516  CB  ILE A  76     -46.841  29.912 -50.490  1.00 21.19           C  
ATOM    517  CG1 ILE A  76     -46.862  29.758 -52.012  1.00 32.10           C  
ATOM    518  CG2 ILE A  76     -47.639  28.800 -49.825  1.00 21.29           C  
ATOM    519  CD1 ILE A  76     -46.365  28.412 -52.501  1.00 28.20           C  
ATOM    520  N   ARG A  77     -47.256  32.992 -51.834  1.00 23.35           N  
ATOM    521  CA  ARG A  77     -46.622  34.089 -52.562  1.00 16.50           C  
ATOM    522  C   ARG A  77     -46.291  35.247 -51.629  1.00 15.20           C  
ATOM    523  O   ARG A  77     -45.168  35.766 -51.637  1.00 15.04           O  
ATOM    524  CB  ARG A  77     -47.534  34.558 -53.697  1.00 15.31           C  
ATOM    525  CG  ARG A  77     -47.062  35.819 -54.403  1.00 13.84           C  
ATOM    526  CD  ARG A  77     -48.206  36.478 -55.160  1.00 20.67           C  
ATOM    527  NE  ARG A  77     -47.749  37.558 -56.030  1.00 10.93           N  
ATOM    528  CZ  ARG A  77     -48.560  38.389 -56.679  1.00 19.21           C  
ATOM    529  NH1 ARG A  77     -49.875  38.268 -56.555  1.00 26.29           N  
ATOM    530  NH2 ARG A  77     -48.056  39.342 -57.450  1.00 41.50           N  
ATOM    531  N   PHE A  78     -47.261  35.672 -50.823  1.00 14.31           N  
ATOM    532  CA  PHE A  78     -47.059  36.790 -49.912  1.00 13.17           C  
ATOM    533  C   PHE A  78     -46.374  36.384 -48.611  1.00 13.72           C  
ATOM    534  O   PHE A  78     -46.201  37.235 -47.732  1.00 33.98           O  
ATOM    535  CB  PHE A  78     -48.398  37.472 -49.617  1.00 11.26           C  
ATOM    536  CG  PHE A  78     -49.101  37.989 -50.844  1.00 10.06           C  
ATOM    537  CD1 PHE A  78     -48.629  39.107 -51.513  1.00  8.74           C  
ATOM    538  CD2 PHE A  78     -50.235  37.357 -51.327  1.00 20.37           C  
ATOM    539  CE1 PHE A  78     -49.274  39.582 -52.640  1.00  7.85           C  
ATOM    540  CE2 PHE A  78     -50.883  37.828 -52.454  1.00 26.56           C  
ATOM    541  CZ  PHE A  78     -50.401  38.942 -53.111  1.00 15.28           C  
ATOM    542  N   GLY A  79     -45.980  35.120 -48.463  1.00 15.06           N  
ATOM    543  CA  GLY A  79     -45.123  34.730 -47.359  1.00 27.12           C  
ATOM    544  C   GLY A  79     -45.770  34.031 -46.181  1.00 25.82           C  
ATOM    545  O   GLY A  79     -45.436  34.323 -45.029  1.00 32.69           O  
ATOM    546  N   THR A  80     -46.695  33.111 -46.440  1.00 20.14           N  
ATOM    547  CA  THR A  80     -47.265  32.280 -45.387  1.00 27.78           C  
ATOM    548  C   THR A  80     -46.430  31.017 -45.228  1.00 17.88           C  
ATOM    549  O   THR A  80     -46.138  30.331 -46.214  1.00 30.99           O  
ATOM    550  CB  THR A  80     -48.716  31.902 -45.686  1.00 37.43           C  
ATOM    551  OG1 THR A  80     -48.810  31.353 -47.005  1.00 71.48           O  
ATOM    552  CG2 THR A  80     -49.625  33.107 -45.569  1.00 13.91           C  
ATOM    553  N   GLU A  81     -46.045  30.715 -43.992  1.00 17.94           N  
ATOM    554  CA  GLU A  81     -45.334  29.475 -43.696  1.00 19.97           C  
ATOM    555  C   GLU A  81     -46.374  28.368 -43.606  1.00 28.62           C  
ATOM    556  O   GLU A  81     -46.995  28.161 -42.562  1.00 42.52           O  
ATOM    557  CB  GLU A  81     -44.532  29.597 -42.406  1.00 19.49           C  
ATOM    558  CG  GLU A  81     -43.733  28.349 -42.059  1.00 21.50           C  
ATOM    559  CD  GLU A  81     -42.955  28.491 -40.766  1.00 42.06           C  
ATOM    560  OE1 GLU A  81     -42.870  29.622 -40.242  1.00 47.44           O  
ATOM    561  OE2 GLU A  81     -42.430  27.470 -40.272  1.00 53.37           O  
ATOM    562  N   VAL A  82     -46.572  27.655 -44.710  1.00 22.54           N  
ATOM    563  CA  VAL A  82     -47.594  26.620 -44.800  1.00 21.90           C  
ATOM    564  C   VAL A  82     -46.947  25.279 -44.471  1.00 31.16           C  
ATOM    565  O   VAL A  82     -46.108  24.781 -45.225  1.00 48.25           O  
ATOM    566  CB  VAL A  82     -48.245  26.598 -46.187  1.00 22.42           C  
ATOM    567  CG1 VAL A  82     -49.243  25.461 -46.280  1.00 20.25           C  
ATOM    568  CG2 VAL A  82     -48.919  27.930 -46.474  1.00 34.61           C  
ATOM    569  N   ILE A  83     -47.341  24.694 -43.343  1.00 25.83           N  
ATOM    570  CA  ILE A  83     -46.842  23.397 -42.903  1.00 25.19           C  
ATOM    571  C   ILE A  83     -47.975  22.388 -43.023  1.00 22.24           C  
ATOM    572  O   ILE A  83     -49.084  22.628 -42.530  1.00 22.40           O  
ATOM    573  CB  ILE A  83     -46.312  23.458 -41.460  1.00 26.47           C  
ATOM    574  CG1 ILE A  83     -45.267  24.569 -41.315  1.00 33.70           C  
ATOM    575  CG2 ILE A  83     -45.732  22.115 -41.044  1.00 25.23           C  
ATOM    576  CD1 ILE A  83     -44.021  24.361 -42.152  1.00 34.24           C  
ATOM    577  N   THR A  84     -47.697  21.262 -43.681  1.00 21.60           N  
ATOM    578  CA  THR A  84     -48.717  20.246 -43.944  1.00 25.09           C  
ATOM    579  C   THR A  84     -48.757  19.249 -42.784  1.00 20.56           C  
ATOM    580  O   THR A  84     -48.412  18.072 -42.908  1.00 16.15           O  
ATOM    581  CB  THR A  84     -48.448  19.552 -45.274  1.00 23.63           C  
ATOM    582  OG1 THR A  84     -47.276  18.736 -45.161  1.00 37.26           O  
ATOM    583  CG2 THR A  84     -48.231  20.582 -46.374  1.00 19.98           C  
ATOM    584  N   GLU A  85     -49.196  19.750 -41.631  1.00 24.66           N  
ATOM    585  CA  GLU A  85     -49.297  18.944 -40.423  1.00 17.60           C  
ATOM    586  C   GLU A  85     -50.623  19.237 -39.735  1.00 20.00           C  
ATOM    587  O   GLU A  85     -51.165  20.340 -39.841  1.00 26.64           O  
ATOM    588  CB  GLU A  85     -48.126  19.207 -39.464  1.00 17.48           C  
ATOM    589  CG  GLU A  85     -46.781  18.713 -39.983  1.00 21.15           C  
ATOM    590  CD  GLU A  85     -45.631  19.034 -39.046  1.00 31.91           C  
ATOM    591  OE1 GLU A  85     -45.887  19.550 -37.937  1.00 41.29           O  
ATOM    592  OE2 GLU A  85     -44.469  18.769 -39.420  1.00 30.74           O  
ATOM    593  N   THR A  86     -51.139  18.235 -39.031  1.00 23.86           N  
ATOM    594  CA  THR A  86     -52.449  18.312 -38.396  1.00 16.49           C  
ATOM    595  C   THR A  86     -52.305  18.708 -36.933  1.00 19.93           C  
ATOM    596  O   THR A  86     -51.453  18.169 -36.219  1.00 39.26           O  
ATOM    597  CB  THR A  86     -53.181  16.974 -38.507  1.00  7.55           C  
ATOM    598  OG1 THR A  86     -53.328  16.619 -39.888  1.00  7.43           O  
ATOM    599  CG2 THR A  86     -54.552  17.051 -37.846  1.00  5.69           C  
ATOM    600  N   ILE A  87     -53.137  19.649 -36.496  1.00  9.98           N  
ATOM    601  CA  ILE A  87     -53.163  20.067 -35.100  1.00  9.82           C  
ATOM    602  C   ILE A  87     -53.978  19.060 -34.300  1.00  8.74           C  
ATOM    603  O   ILE A  87     -55.096  18.700 -34.688  1.00  8.47           O  
ATOM    604  CB  ILE A  87     -53.743  21.484 -34.970  1.00 13.64           C  
ATOM    605  CG1 ILE A  87     -52.879  22.488 -35.735  1.00 13.16           C  
ATOM    606  CG2 ILE A  87     -53.845  21.885 -33.511  1.00 29.54           C  
ATOM    607  CD1 ILE A  87     -51.469  22.614 -35.201  1.00 15.31           C  
ATOM    608  N   SER A  88     -53.422  18.601 -33.177  1.00 14.93           N  
ATOM    609  CA  SER A  88     -54.075  17.601 -32.335  1.00 16.04           C  
ATOM    610  C   SER A  88     -54.787  18.232 -31.143  1.00 15.61           C  
ATOM    611  O   SER A  88     -55.985  18.016 -30.943  1.00  8.15           O  
ATOM    612  CB  SER A  88     -53.050  16.568 -31.849  1.00 23.45           C  
ATOM    613  OG  SER A  88     -53.667  15.587 -31.033  1.00 26.04           O  
ATOM    614  N   ARG A  89     -54.063  19.001 -30.335  1.00 20.45           N  
ATOM    615  CA  ARG A  89     -54.638  19.665 -29.177  1.00 18.16           C  
ATOM    616  C   ARG A  89     -54.253  21.136 -29.197  1.00  8.78           C  
ATOM    617  O   ARG A  89     -53.212  21.515 -29.740  1.00  6.86           O  
ATOM    618  CB  ARG A  89     -54.163  19.029 -27.860  1.00 18.30           C  
ATOM    619  CG  ARG A  89     -55.003  19.407 -26.647  1.00 11.58           C  
ATOM    620  CD  ARG A  89     -54.136  19.637 -25.419  1.00  1.95           C  
ATOM    621  NE  ARG A  89     -53.027  18.691 -25.341  1.00  1.95           N  
ATOM    622  CZ  ARG A  89     -52.025  18.788 -24.474  1.00  1.96           C  
ATOM    623  NH1 ARG A  89     -51.992  19.791 -23.608  1.00  1.95           N  
ATOM    624  NH2 ARG A  89     -51.057  17.882 -24.471  1.00  1.95           N  
ATOM    625  N   VAL A  90     -55.106  21.960 -28.595  1.00  6.19           N  
ATOM    626  CA  VAL A  90     -54.886  23.396 -28.485  1.00 12.21           C  
ATOM    627  C   VAL A  90     -55.180  23.814 -27.051  1.00 27.18           C  
ATOM    628  O   VAL A  90     -56.172  23.373 -26.459  1.00 37.89           O  
ATOM    629  CB  VAL A  90     -55.749  24.189 -29.488  1.00 11.01           C  
ATOM    630  CG1 VAL A  90     -55.312  23.906 -30.910  1.00 13.49           C  
ATOM    631  CG2 VAL A  90     -57.221  23.834 -29.327  1.00  4.68           C  
ATOM    632  N   ASP A  91     -54.298  24.630 -26.480  1.00 20.31           N  
ATOM    633  CA  ASP A  91     -54.426  25.104 -25.103  1.00  5.81           C  
ATOM    634  C   ASP A  91     -54.613  26.621 -25.118  1.00  4.03           C  
ATOM    635  O   ASP A  91     -53.640  27.378 -25.068  1.00 25.62           O  
ATOM    636  CB  ASP A  91     -53.211  24.698 -24.274  1.00  1.95           C  
ATOM    637  N   LEU A  92     -55.862  27.063 -25.186  1.00  2.65           N  
ATOM    638  CA  LEU A  92     -56.186  28.488 -25.136  1.00  9.45           C  
ATOM    639  C   LEU A  92     -56.637  28.883 -23.731  1.00 24.05           C  
ATOM    640  O   LEU A  92     -57.790  29.250 -23.481  1.00 35.99           O  
ATOM    641  CB  LEU A  92     -57.234  28.852 -26.185  1.00  3.95           C  
ATOM    642  CG  LEU A  92     -57.036  28.619 -27.691  1.00  6.22           C  
ATOM    643  CD1 LEU A  92     -56.862  27.170 -28.064  1.00  5.96           C  
ATOM    644  CD2 LEU A  92     -58.214  29.206 -28.446  1.00  7.81           C  
ATOM    645  N   SER A  93     -55.708  28.768 -22.805  1.00 20.40           N  
ATOM    646  CA  SER A  93     -55.875  29.200 -21.422  1.00 11.48           C  
ATOM    647  C   SER A  93     -54.767  30.143 -20.976  1.00 23.87           C  
ATOM    648  O   SER A  93     -55.044  31.114 -20.266  1.00 27.72           O  
ATOM    649  CB  SER A  93     -55.937  27.973 -20.499  1.00  1.95           C  
ATOM    650  OG  SER A  93     -55.264  26.867 -21.078  1.00  1.95           O  
ATOM    651  N   SER A  94     -53.525  29.888 -21.382  1.00 31.09           N  
ATOM    652  CA  SER A  94     -52.405  30.750 -21.040  1.00 38.35           C  
ATOM    653  C   SER A  94     -52.365  31.959 -21.977  1.00 30.91           C  
ATOM    654  O   SER A  94     -53.162  32.083 -22.912  1.00  2.00           O  
ATOM    655  CB  SER A  94     -51.098  29.963 -21.098  1.00 41.65           C  
ATOM    656  OG  SER A  94     -50.762  29.626 -22.434  1.00 40.79           O  
ATOM    657  N   LYS A  95     -51.427  32.875 -21.710  1.00 35.38           N  
ATOM    658  CA  LYS A  95     -51.260  34.049 -22.568  1.00 20.12           C  
ATOM    659  C   LYS A  95     -50.941  33.674 -24.010  1.00 25.27           C  
ATOM    660  O   LYS A  95     -51.661  34.125 -24.919  1.00 25.20           O  
ATOM    661  CB  LYS A  95     -50.210  34.985 -21.959  1.00  1.95           C  
ATOM    662  N   PRO A  96     -49.892  32.876 -24.308  1.00 22.04           N  
ATOM    663  CA  PRO A  96     -49.687  32.453 -25.698  1.00 14.54           C  
ATOM    664  C   PRO A  96     -50.414  31.152 -26.010  1.00 25.96           C  
ATOM    665  O   PRO A  96     -50.312  30.175 -25.262  1.00 20.19           O  
ATOM    666  CB  PRO A  96     -48.164  32.302 -25.790  1.00  5.12           C  
ATOM    667  CG  PRO A  96     -47.726  31.959 -24.379  1.00  2.71           C  
ATOM    668  CD  PRO A  96     -48.854  32.308 -23.426  1.00 14.04           C  
ATOM    669  N   PHE A  97     -51.168  31.138 -27.107  1.00 29.47           N  
ATOM    670  CA  PHE A  97     -51.900  29.942 -27.505  1.00 26.82           C  
ATOM    671  C   PHE A  97     -50.931  28.845 -27.931  1.00 32.27           C  
ATOM    672  O   PHE A  97     -50.050  29.072 -28.764  1.00 38.99           O  
ATOM    673  CB  PHE A  97     -52.860  30.276 -28.646  1.00 24.45           C  
ATOM    674  CG  PHE A  97     -53.939  31.253 -28.265  1.00 14.21           C  
ATOM    675  CD1 PHE A  97     -54.354  31.377 -26.949  1.00 14.72           C  
ATOM    676  CD2 PHE A  97     -54.521  32.066 -29.224  1.00 12.61           C  
ATOM    677  CE1 PHE A  97     -55.341  32.281 -26.600  1.00 16.34           C  
ATOM    678  CE2 PHE A  97     -55.508  32.972 -28.881  1.00 13.55           C  
ATOM    679  CZ  PHE A  97     -55.917  33.080 -27.568  1.00 11.08           C  
ATOM    680  N   LYS A  98     -51.097  27.651 -27.367  1.00 21.39           N  
ATOM    681  CA  LYS A  98     -50.227  26.519 -27.655  1.00 16.71           C  
ATOM    682  C   LYS A  98     -50.958  25.497 -28.518  1.00 16.41           C  
ATOM    683  O   LYS A  98     -52.149  25.240 -28.320  1.00  9.15           O  
ATOM    684  CB  LYS A  98     -49.739  25.858 -26.363  1.00 12.30           C  
ATOM    685  N   LEU A  99     -50.235  24.924 -29.481  1.00 26.80           N  
ATOM    686  CA  LEU A  99     -50.778  23.931 -30.398  1.00 19.70           C  
ATOM    687  C   LEU A  99     -49.822  22.751 -30.495  1.00 11.71           C  
ATOM    688  O   LEU A  99     -48.601  22.912 -30.418  1.00 12.06           O  
ATOM    689  CB  LEU A  99     -51.026  24.512 -31.801  1.00 25.56           C  
ATOM    690  CG  LEU A  99     -51.976  25.703 -31.965  1.00 25.97           C  
ATOM    691  CD1 LEU A  99     -51.291  27.023 -31.635  1.00 33.53           C  
ATOM    692  CD2 LEU A  99     -52.541  25.733 -33.376  1.00 23.49           C  
ATOM    693  N   TRP A 100     -50.388  21.560 -30.679  1.00 10.43           N  
ATOM    694  CA  TRP A 100     -49.619  20.326 -30.764  1.00 10.28           C  
ATOM    695  C   TRP A 100     -49.979  19.571 -32.036  1.00 10.02           C  
ATOM    696  O   TRP A 100     -51.151  19.504 -32.419  1.00  9.38           O  
ATOM    697  CB  TRP A 100     -49.863  19.435 -29.540  1.00 18.94           C  
ATOM    698  CG  TRP A 100     -49.197  19.931 -28.292  1.00 10.44           C  
ATOM    699  CD1 TRP A 100     -47.928  19.650 -27.876  1.00 11.55           C  
ATOM    700  CD2 TRP A 100     -49.761  20.798 -27.300  1.00  6.87           C  
ATOM    701  NE1 TRP A 100     -47.669  20.284 -26.685  1.00 26.59           N  
ATOM    702  CE2 TRP A 100     -48.778  20.997 -26.310  1.00 21.21           C  
ATOM    703  CE3 TRP A 100     -51.003  21.425 -27.151  1.00  4.64           C  
ATOM    704  CZ2 TRP A 100     -48.996  21.795 -25.189  1.00 16.86           C  
ATOM    705  CZ3 TRP A 100     -51.217  22.218 -26.036  1.00  3.43           C  
ATOM    706  CH2 TRP A 100     -50.219  22.395 -25.071  1.00  2.25           C  
ATOM    707  N   THR A 101     -48.963  19.007 -32.687  1.00 10.70           N  
ATOM    708  CA  THR A 101     -49.177  18.192 -33.874  1.00 10.67           C  
ATOM    709  C   THR A 101     -49.737  16.823 -33.489  1.00 19.23           C  
ATOM    710  O   THR A 101     -49.560  16.343 -32.365  1.00 29.40           O  
ATOM    711  CB  THR A 101     -47.867  18.027 -34.649  1.00 12.07           C  
ATOM    712  OG1 THR A 101     -47.156  19.271 -34.656  1.00 14.29           O  
ATOM    713  CG2 THR A 101     -48.137  17.614 -36.091  1.00 12.54           C  
ATOM    714  N   GLU A 102     -50.418  16.188 -34.444  1.00 21.25           N  
ATOM    715  CA  GLU A 102     -50.958  14.855 -34.215  1.00 23.51           C  
ATOM    716  C   GLU A 102     -49.843  13.818 -34.151  1.00 20.54           C  
ATOM    717  O   GLU A 102     -48.826  13.930 -34.843  1.00  9.57           O  
ATOM    718  CB  GLU A 102     -51.957  14.481 -35.310  1.00 25.25           C  
ATOM    719  CG  GLU A 102     -51.359  14.352 -36.701  1.00 34.96           C  
ATOM    720  CD  GLU A 102     -52.064  13.303 -37.540  1.00 29.64           C  
ATOM    721  OE1 GLU A 102     -52.369  12.218 -37.000  1.00 26.22           O  
ATOM    722  OE2 GLU A 102     -52.319  13.562 -38.735  1.00 23.75           O  
ATOM    723  N   TRP A 103     -50.030  12.828 -33.272  1.00 17.32           N  
ATOM    724  CA  TRP A 103     -49.083  11.747 -33.004  1.00 10.97           C  
ATOM    725  C   TRP A 103     -47.853  12.274 -32.273  1.00 24.35           C  
ATOM    726  O   TRP A 103     -47.002  11.495 -31.832  1.00 22.03           O  
ATOM    727  CB  TRP A 103     -48.678  11.029 -34.297  1.00  1.95           C  
ATOM    728  N   ASN A 104     -47.757  13.598 -32.142  1.00 32.31           N  
ATOM    729  CA  ASN A 104     -46.731  14.269 -31.354  1.00 26.68           C  
ATOM    730  C   ASN A 104     -47.352  15.103 -30.240  1.00 26.68           C  
ATOM    731  O   ASN A 104     -46.761  16.086 -29.788  1.00 17.36           O  
ATOM    732  CB  ASN A 104     -45.844  15.141 -32.242  1.00  8.79           C  
ATOM    733  CG  ASN A 104     -45.001  14.328 -33.203  1.00 20.12           C  
ATOM    734  OD1 ASN A 104     -45.096  13.102 -33.247  1.00 34.11           O  
ATOM    735  ND2 ASN A 104     -44.165  15.009 -33.977  1.00 14.40           N  
ATOM    736  N   ASP A 105     -48.550  14.727 -29.793  1.00 24.71           N  
ATOM    737  CA  ASP A 105     -49.232  15.506 -28.760  1.00 15.94           C  
ATOM    738  C   ASP A 105     -48.613  15.261 -27.388  1.00 20.98           C  
ATOM    739  O   ASP A 105     -48.019  16.165 -26.794  1.00 38.73           O  
ATOM    740  CB  ASP A 105     -50.725  15.161 -28.756  1.00 11.20           C  
ATOM    741  CG  ASP A 105     -51.558  16.171 -27.994  1.00 13.58           C  
ATOM    742  OD1 ASP A 105     -50.988  17.163 -27.494  1.00  2.97           O  
ATOM    743  OD2 ASP A 105     -52.786  15.967 -27.893  1.00 17.02           O  
ATOM    744  N   GLY A 106     -48.742  14.041 -26.871  1.00  1.95           N  
ATOM    745  CA  GLY A 106     -48.142  13.681 -25.609  1.00  2.18           C  
ATOM    746  C   GLY A 106     -48.800  14.376 -24.433  1.00  8.02           C  
ATOM    747  O   GLY A 106     -49.412  15.439 -24.574  1.00  1.95           O  
ATOM    748  N   PRO A 107     -48.703  13.783 -23.245  1.00 16.01           N  
ATOM    749  CA  PRO A 107     -49.285  14.437 -22.066  1.00 12.97           C  
ATOM    750  C   PRO A 107     -48.401  15.562 -21.548  1.00 11.39           C  
ATOM    751  O   PRO A 107     -48.889  16.522 -20.943  1.00  1.95           O  
ATOM    752  CB  PRO A 107     -49.396  13.292 -21.053  1.00  6.87           C  
ATOM    753  CG  PRO A 107     -48.291  12.361 -21.437  1.00  7.00           C  
ATOM    754  CD  PRO A 107     -48.196  12.433 -22.939  1.00  9.76           C  
ATOM    755  N   ASP A 108     -47.096  15.450 -21.794  1.00 19.27           N  
ATOM    756  CA  ASP A 108     -46.097  16.398 -21.304  1.00 14.92           C  
ATOM    757  C   ASP A 108     -45.088  16.732 -22.397  1.00  8.43           C  
ATOM    758  O   ASP A 108     -43.881  16.810 -22.145  1.00  4.84           O  
ATOM    759  CB  ASP A 108     -45.384  15.862 -20.061  1.00  8.18           C  
ATOM    760  CG  ASP A 108     -46.235  15.966 -18.807  1.00  1.95           C  
ATOM    761  OD1 ASP A 108     -47.099  16.865 -18.742  1.00  7.82           O  
ATOM    762  OD2 ASP A 108     -46.032  15.153 -17.880  1.00  1.96           O  
ATOM    763  N   LYS A 109     -45.558  16.936 -23.622  1.00  1.95           N  
ATOM    764  CA  LYS A 109     -44.677  17.262 -24.734  1.00  1.95           C  
ATOM    765  C   LYS A 109     -44.743  18.750 -25.066  1.00  9.44           C  
ATOM    766  O   LYS A 109     -45.707  19.445 -24.737  1.00 22.75           O  
ATOM    767  CB  LYS A 109     -45.031  16.433 -25.971  1.00  1.95           C  
ATOM    768  N   GLU A 110     -43.689  19.230 -25.733  1.00  2.69           N  
ATOM    769  CA  GLU A 110     -43.568  20.640 -26.077  1.00  6.30           C  
ATOM    770  C   GLU A 110     -44.378  20.959 -27.334  1.00 15.78           C  
ATOM    771  O   GLU A 110     -44.358  20.189 -28.298  1.00 27.28           O  
ATOM    772  CB  GLU A 110     -42.103  21.014 -26.297  1.00  1.95           C  
ATOM    773  N   PRO A 111     -45.103  22.078 -27.338  1.00  5.73           N  
ATOM    774  CA  PRO A 111     -45.898  22.442 -28.516  1.00  8.25           C  
ATOM    775  C   PRO A 111     -45.025  22.689 -29.737  1.00 13.09           C  
ATOM    776  O   PRO A 111     -43.877  23.129 -29.632  1.00 13.96           O  
ATOM    777  CB  PRO A 111     -46.621  23.720 -28.074  1.00  8.31           C  
ATOM    778  CG  PRO A 111     -45.780  24.274 -26.976  1.00  6.25           C  
ATOM    779  CD  PRO A 111     -45.201  23.085 -26.268  1.00  4.32           C  
ATOM    780  N   ALA A 112     -45.585  22.388 -30.910  1.00 25.81           N  
ATOM    781  CA  ALA A 112     -44.856  22.583 -32.158  1.00 23.71           C  
ATOM    782  C   ALA A 112     -44.878  24.037 -32.609  1.00 25.19           C  
ATOM    783  O   ALA A 112     -43.926  24.498 -33.249  1.00 34.35           O  
ATOM    784  CB  ALA A 112     -45.432  21.686 -33.254  1.00 15.52           C  
ATOM    785  N   CYS A 113     -45.945  24.768 -32.294  1.00 18.48           N  
ATOM    786  CA  CYS A 113     -46.042  26.176 -32.645  1.00 25.93           C  
ATOM    787  C   CYS A 113     -46.955  26.873 -31.648  1.00 21.63           C  
ATOM    788  O   CYS A 113     -47.968  26.311 -31.225  1.00  3.87           O  
ATOM    789  CB  CYS A 113     -46.569  26.368 -34.071  1.00 24.15           C  
ATOM    790  SG  CYS A 113     -46.407  28.056 -34.699  1.00 12.49           S  
ATOM    791  N   THR A 114     -46.584  28.095 -31.276  1.00 28.48           N  
ATOM    792  CA  THR A 114     -47.390  28.930 -30.400  1.00 19.63           C  
ATOM    793  C   THR A 114     -47.574  30.302 -31.033  1.00 11.47           C  
ATOM    794  O   THR A 114     -46.740  30.755 -31.822  1.00 14.13           O  
ATOM    795  CB  THR A 114     -46.758  29.074 -29.005  1.00 10.46           C  
ATOM    796  OG1 THR A 114     -47.556  29.958 -28.207  1.00 11.12           O  
ATOM    797  CG2 THR A 114     -45.343  29.619 -29.105  1.00  1.95           C  
ATOM    798  N   ALA A 115     -48.681  30.957 -30.689  1.00  1.95           N  
ATOM    799  CA  ALA A 115     -49.002  32.246 -31.282  1.00  5.35           C  
ATOM    800  C   ALA A 115     -49.886  33.050 -30.340  1.00  6.37           C  
ATOM    801  O   ALA A 115     -50.494  32.512 -29.411  1.00  1.95           O  
ATOM    802  CB  ALA A 115     -49.691  32.081 -32.641  1.00  3.96           C  
ATOM    803  N   ASP A 116     -49.943  34.357 -30.598  1.00 14.77           N  
ATOM    804  CA  ASP A 116     -50.751  35.286 -29.820  1.00 10.42           C  
ATOM    805  C   ASP A 116     -52.176  35.421 -30.341  1.00  7.64           C  
ATOM    806  O   ASP A 116     -53.007  36.045 -29.672  1.00 16.19           O  
ATOM    807  CB  ASP A 116     -50.087  36.667 -29.793  1.00  9.18           C  
ATOM    808  CG  ASP A 116     -48.703  36.635 -29.174  1.00 21.29           C  
ATOM    809  OD1 ASP A 116     -48.551  36.045 -28.084  1.00 29.91           O  
ATOM    810  OD2 ASP A 116     -47.769  37.202 -29.779  1.00 20.93           O  
ATOM    811  N   ALA A 117     -52.472  34.868 -31.514  1.00  7.48           N  
ATOM    812  CA  ALA A 117     -53.815  34.882 -32.071  1.00  7.98           C  
ATOM    813  C   ALA A 117     -53.950  33.691 -33.006  1.00 10.26           C  
ATOM    814  O   ALA A 117     -52.984  33.290 -33.660  1.00 28.25           O  
ATOM    815  CB  ALA A 117     -54.115  36.189 -32.813  1.00  2.10           C  
ATOM    816  N   VAL A 118     -55.148  33.117 -33.056  1.00  1.95           N  
ATOM    817  CA  VAL A 118     -55.401  31.935 -33.868  1.00  1.95           C  
ATOM    818  C   VAL A 118     -56.688  32.122 -34.660  1.00  1.95           C  
ATOM    819  O   VAL A 118     -57.684  32.639 -34.141  1.00  1.95           O  
ATOM    820  CB  VAL A 118     -55.459  30.660 -32.996  1.00  4.40           C  
ATOM    821  CG1 VAL A 118     -56.480  30.813 -31.884  1.00  5.59           C  
ATOM    822  CG2 VAL A 118     -55.758  29.432 -33.846  1.00 24.08           C  
ATOM    823  N   ILE A 119     -56.660  31.704 -35.924  1.00  1.95           N  
ATOM    824  CA  ILE A 119     -57.814  31.744 -36.815  1.00  1.95           C  
ATOM    825  C   ILE A 119     -58.282  30.314 -37.029  1.00 18.86           C  
ATOM    826  O   ILE A 119     -57.483  29.442 -37.393  1.00 25.66           O  
ATOM    827  CB  ILE A 119     -57.475  32.408 -38.161  1.00  2.45           C  
ATOM    828  CG1 ILE A 119     -56.841  33.783 -37.950  1.00  1.95           C  
ATOM    829  CG2 ILE A 119     -58.721  32.525 -39.021  1.00  3.47           C  
ATOM    830  CD1 ILE A 119     -57.800  34.820 -37.436  1.00  1.95           C  
ATOM    831  N   ILE A 120     -59.568  30.073 -36.809  1.00 30.13           N  
ATOM    832  CA  ILE A 120     -60.155  28.748 -36.962  1.00  2.47           C  
ATOM    833  C   ILE A 120     -60.941  28.733 -38.265  1.00  3.67           C  
ATOM    834  O   ILE A 120     -62.018  29.332 -38.362  1.00  5.51           O  
ATOM    835  CB  ILE A 120     -61.043  28.380 -35.768  1.00  1.96           C  
ATOM    836  CG1 ILE A 120     -60.202  28.274 -34.495  1.00  1.95           C  
ATOM    837  CG2 ILE A 120     -61.775  27.073 -36.032  1.00  2.04           C  
ATOM    838  CD1 ILE A 120     -60.996  27.880 -33.274  1.00  1.95           C  
ATOM    839  N   ALA A 121     -60.399  28.056 -39.272  1.00  4.37           N  
ATOM    840  CA  ALA A 121     -61.052  27.874 -40.564  1.00 15.38           C  
ATOM    841  C   ALA A 121     -61.011  26.406 -40.959  1.00 14.80           C  
ATOM    842  O   ALA A 121     -60.673  26.041 -42.087  1.00 30.67           O  
ATOM    843  CB  ALA A 121     -60.404  28.748 -41.632  1.00 12.02           C  
ATOM    844  N   THR A 122     -61.368  25.541 -40.014  1.00  5.09           N  
ATOM    845  CA  THR A 122     -61.240  24.098 -40.168  1.00  5.29           C  
ATOM    846  C   THR A 122     -62.409  23.468 -40.921  1.00  5.82           C  
ATOM    847  O   THR A 122     -62.495  22.237 -40.985  1.00  5.86           O  
ATOM    848  CB  THR A 122     -61.085  23.447 -38.792  1.00  3.91           C  
ATOM    849  OG1 THR A 122     -60.893  22.036 -38.944  1.00 11.61           O  
ATOM    850  CG2 THR A 122     -62.316  23.704 -37.941  1.00  3.15           C  
ATOM    851  N   GLY A 123     -63.297  24.277 -41.490  1.00 17.03           N  
ATOM    852  CA  GLY A 123     -64.368  23.773 -42.329  1.00 21.42           C  
ATOM    853  C   GLY A 123     -65.444  23.009 -41.574  1.00  5.93           C  
ATOM    854  O   GLY A 123     -65.393  22.800 -40.363  1.00  5.13           O  
ATOM    855  N   ALA A 124     -66.454  22.592 -42.342  1.00  9.65           N  
ATOM    856  CA  ALA A 124     -67.560  21.783 -41.827  1.00 12.43           C  
ATOM    857  C   ALA A 124     -68.028  20.896 -42.977  1.00 13.16           C  
ATOM    858  O   ALA A 124     -68.820  21.334 -43.817  1.00 26.82           O  
ATOM    859  CB  ALA A 124     -68.688  22.656 -41.295  1.00  7.55           C  
ATOM    860  N   ASN A 125     -67.534  19.660 -43.008  1.00  6.46           N  
ATOM    861  CA  ASN A 125     -67.825  18.762 -44.116  1.00  7.09           C  
ATOM    862  C   ASN A 125     -69.249  18.225 -44.039  1.00  6.93           C  
ATOM    863  O   ASN A 125     -69.820  18.055 -42.959  1.00  8.52           O  
ATOM    864  CB  ASN A 125     -66.836  17.594 -44.135  1.00  9.48           C  
ATOM    865  CG  ASN A 125     -65.412  18.034 -44.422  1.00 43.96           C  
ATOM    866  OD1 ASN A 125     -65.171  19.160 -44.858  1.00 64.99           O  
ATOM    867  ND2 ASN A 125     -64.459  17.142 -44.179  1.00 50.05           N  
ATOM    868  N   ALA A 126     -69.824  17.961 -45.211  1.00 10.65           N  
ATOM    869  CA  ALA A 126     -71.129  17.322 -45.291  1.00  8.99           C  
ATOM    870  C   ALA A 126     -70.994  15.823 -45.055  1.00  6.79           C  
ATOM    871  O   ALA A 126     -70.047  15.188 -45.528  1.00  7.26           O  
ATOM    872  CB  ALA A 126     -71.776  17.587 -46.651  1.00  7.36           C  
ATOM    873  N   ARG A 127     -71.950  15.261 -44.322  1.00  6.17           N  
ATOM    874  CA  ARG A 127     -71.893  13.849 -43.970  1.00  5.76           C  
ATOM    875  C   ARG A 127     -72.195  12.971 -45.179  1.00  6.29           C  
ATOM    876  O   ARG A 127     -73.125  13.235 -45.946  1.00  7.04           O  
ATOM    877  CB  ARG A 127     -72.881  13.536 -42.846  1.00  4.96           C  
ATOM    878  CG  ARG A 127     -72.490  14.075 -41.483  1.00  4.29           C  
ATOM    879  CD  ARG A 127     -73.625  13.891 -40.487  1.00 23.43           C  
ATOM    880  NE  ARG A 127     -73.293  14.418 -39.166  1.00 36.94           N  
ATOM    881  CZ  ARG A 127     -74.169  14.557 -38.176  1.00 50.92           C  
ATOM    882  NH1 ARG A 127     -75.436  14.211 -38.357  1.00 57.50           N  
ATOM    883  NH2 ARG A 127     -73.778  15.045 -37.007  1.00 52.15           N  
ATOM    884  N   ARG A 128     -71.392  11.926 -45.350  1.00  6.35           N  
ATOM    885  CA  ARG A 128     -71.616  10.917 -46.372  1.00 12.99           C  
ATOM    886  C   ARG A 128     -72.096   9.628 -45.718  1.00 19.60           C  
ATOM    887  O   ARG A 128     -71.956   9.427 -44.509  1.00 27.24           O  
ATOM    888  CB  ARG A 128     -70.345  10.648 -47.184  1.00 19.13           C  
ATOM    889  CG  ARG A 128     -69.792  11.850 -47.931  1.00  9.67           C  
ATOM    890  CD  ARG A 128     -68.785  11.398 -48.975  1.00 11.07           C  
ATOM    891  NE  ARG A 128     -67.896  12.471 -49.405  1.00 29.14           N  
ATOM    892  CZ  ARG A 128     -66.889  12.303 -50.256  1.00 44.60           C  
ATOM    893  NH1 ARG A 128     -66.646  11.104 -50.769  1.00 19.72           N  
ATOM    894  NH2 ARG A 128     -66.125  13.333 -50.594  1.00 67.43           N  
ATOM    895  N   LEU A 129     -72.667   8.747 -46.538  1.00 14.96           N  
ATOM    896  CA  LEU A 129     -73.239   7.501 -46.048  1.00 14.15           C  
ATOM    897  C   LEU A 129     -72.338   6.294 -46.271  1.00 21.25           C  
ATOM    898  O   LEU A 129     -72.645   5.214 -45.755  1.00 15.12           O  
ATOM    899  CB  LEU A 129     -74.596   7.249 -46.713  1.00  5.50           C  
ATOM    900  CG  LEU A 129     -75.663   8.307 -46.436  1.00  6.13           C  
ATOM    901  CD1 LEU A 129     -77.036   7.791 -46.828  1.00 23.42           C  
ATOM    902  CD2 LEU A 129     -75.634   8.739 -44.977  1.00 17.35           C  
ATOM    903  N   ASN A 130     -71.245   6.453 -47.019  1.00 31.72           N  
ATOM    904  CA  ASN A 130     -70.294   5.372 -47.287  1.00 45.26           C  
ATOM    905  C   ASN A 130     -70.989   4.167 -47.918  1.00 43.31           C  
ATOM    906  O   ASN A 130     -70.695   3.014 -47.594  1.00 38.73           O  
ATOM    907  CB  ASN A 130     -69.546   4.963 -46.015  1.00 49.53           C  
ATOM    908  CG  ASN A 130     -68.874   6.138 -45.330  1.00 45.08           C  
ATOM    909  OD1 ASN A 130     -68.523   7.130 -45.970  1.00 14.76           O  
ATOM    910  ND2 ASN A 130     -68.690   6.030 -44.019  1.00 56.88           N  
ATOM    911  N   LEU A 131     -71.925   4.438 -48.823  1.00 24.87           N  
ATOM    912  CA  LEU A 131     -72.614   3.372 -49.529  1.00  6.18           C  
ATOM    913  C   LEU A 131     -71.651   2.643 -50.465  1.00 28.03           C  
ATOM    914  O   LEU A 131     -70.643   3.208 -50.895  1.00 56.70           O  
ATOM    915  CB  LEU A 131     -73.783   3.934 -50.333  1.00  6.70           C  
ATOM    916  CG  LEU A 131     -74.927   4.565 -49.538  1.00  6.24           C  
ATOM    917  CD1 LEU A 131     -76.009   5.071 -50.479  1.00  6.67           C  
ATOM    918  CD2 LEU A 131     -75.497   3.576 -48.531  1.00  5.17           C  
ATOM    919  N   PRO A 132     -71.932   1.382 -50.784  1.00 14.71           N  
ATOM    920  CA  PRO A 132     -71.165   0.708 -51.839  1.00  6.48           C  
ATOM    921  C   PRO A 132     -71.378   1.402 -53.176  1.00 12.20           C  
ATOM    922  O   PRO A 132     -72.504   1.742 -53.548  1.00  7.74           O  
ATOM    923  CB  PRO A 132     -71.729  -0.717 -51.838  1.00  5.22           C  
ATOM    924  CG  PRO A 132     -73.048  -0.616 -51.141  1.00  4.60           C  
ATOM    925  CD  PRO A 132     -72.890   0.475 -50.133  1.00  4.78           C  
ATOM    926  N   GLY A 133     -70.280   1.623 -53.896  1.00 23.38           N  
ATOM    927  CA  GLY A 133     -70.320   2.383 -55.125  1.00 12.34           C  
ATOM    928  C   GLY A 133     -70.263   3.882 -54.949  1.00 13.96           C  
ATOM    929  O   GLY A 133     -70.169   4.602 -55.951  1.00 25.56           O  
ATOM    930  N   GLU A 134     -70.324   4.382 -53.712  1.00 10.63           N  
ATOM    931  CA  GLU A 134     -70.228   5.821 -53.491  1.00 11.28           C  
ATOM    932  C   GLU A 134     -68.874   6.355 -53.938  1.00 12.85           C  
ATOM    933  O   GLU A 134     -68.796   7.404 -54.589  1.00 21.90           O  
ATOM    934  CB  GLU A 134     -70.473   6.139 -52.018  1.00 10.16           C  
ATOM    935  CG  GLU A 134     -70.208   7.580 -51.632  1.00 18.91           C  
ATOM    936  CD  GLU A 134     -70.425   7.827 -50.155  1.00 20.64           C  
ATOM    937  OE1 GLU A 134     -71.520   7.501 -49.652  1.00 12.80           O  
ATOM    938  OE2 GLU A 134     -69.495   8.335 -49.495  1.00 21.27           O  
ATOM    939  N   GLU A 135     -67.795   5.642 -53.605  1.00 13.02           N  
ATOM    940  CA  GLU A 135     -66.465   6.056 -54.038  1.00 14.74           C  
ATOM    941  C   GLU A 135     -66.343   6.049 -55.557  1.00 16.27           C  
ATOM    942  O   GLU A 135     -65.597   6.855 -56.125  1.00 41.93           O  
ATOM    943  CB  GLU A 135     -65.408   5.143 -53.410  1.00 20.93           C  
ATOM    944  CG  GLU A 135     -63.972   5.453 -53.812  1.00 26.02           C  
ATOM    945  CD  GLU A 135     -62.980   4.441 -53.263  1.00 42.98           C  
ATOM    946  OE1 GLU A 135     -63.376   3.619 -52.409  1.00 42.83           O  
ATOM    947  OE2 GLU A 135     -61.805   4.466 -53.688  1.00 48.92           O  
ATOM    948  N   THR A 136     -67.078   5.163 -56.232  1.00 15.63           N  
ATOM    949  CA  THR A 136     -66.979   5.056 -57.683  1.00 18.17           C  
ATOM    950  C   THR A 136     -67.767   6.147 -58.399  1.00 17.16           C  
ATOM    951  O   THR A 136     -67.395   6.545 -59.509  1.00 18.37           O  
ATOM    952  CB  THR A 136     -67.464   3.675 -58.138  1.00 20.84           C  
ATOM    953  OG1 THR A 136     -66.884   2.665 -57.302  1.00 14.74           O  
ATOM    954  CG2 THR A 136     -67.069   3.411 -59.586  1.00 23.33           C  
ATOM    955  N   TYR A 137     -68.840   6.649 -57.789  1.00 15.92           N  
ATOM    956  CA  TYR A 137     -69.708   7.626 -58.436  1.00 15.82           C  
ATOM    957  C   TYR A 137     -69.815   8.935 -57.664  1.00 15.61           C  
ATOM    958  O   TYR A 137     -70.710   9.738 -57.952  1.00 22.38           O  
ATOM    959  CB  TYR A 137     -71.098   7.024 -58.666  1.00 17.36           C  
ATOM    960  CG  TYR A 137     -71.056   5.752 -59.482  1.00 14.31           C  
ATOM    961  CD1 TYR A 137     -70.971   5.794 -60.868  1.00 15.06           C  
ATOM    962  CD2 TYR A 137     -71.086   4.509 -58.867  1.00 13.38           C  
ATOM    963  CE1 TYR A 137     -70.923   4.631 -61.616  1.00 16.99           C  
ATOM    964  CE2 TYR A 137     -71.039   3.343 -59.606  1.00 23.53           C  
ATOM    965  CZ  TYR A 137     -70.957   3.410 -60.980  1.00 16.22           C  
ATOM    966  OH  TYR A 137     -70.911   2.248 -61.716  1.00 29.24           O  
ATOM    967  N   TRP A 138     -68.937   9.172 -56.691  1.00 19.82           N  
ATOM    968  CA  TRP A 138     -68.898  10.468 -56.026  1.00 20.56           C  
ATOM    969  C   TRP A 138     -68.425  11.535 -57.005  1.00 16.85           C  
ATOM    970  O   TRP A 138     -67.419  11.353 -57.698  1.00 18.27           O  
ATOM    971  CB  TRP A 138     -67.977  10.430 -54.810  1.00 15.63           C  
ATOM    972  CG  TRP A 138     -67.892  11.750 -54.119  1.00 15.25           C  
ATOM    973  CD1 TRP A 138     -66.844  12.621 -54.142  1.00 16.26           C  
ATOM    974  CD2 TRP A 138     -68.902  12.358 -53.305  1.00 20.84           C  
ATOM    975  NE1 TRP A 138     -67.138  13.734 -53.392  1.00 15.25           N  
ATOM    976  CE2 TRP A 138     -68.395  13.596 -52.866  1.00 13.68           C  
ATOM    977  CE3 TRP A 138     -70.185  11.973 -52.903  1.00 35.99           C  
ATOM    978  CZ2 TRP A 138     -69.125  14.453 -52.045  1.00 13.50           C  
ATOM    979  CZ3 TRP A 138     -70.909  12.825 -52.088  1.00 36.24           C  
ATOM    980  CH2 TRP A 138     -70.377  14.050 -51.668  1.00 25.02           C  
ATOM    981  N   GLN A 139     -69.162  12.643 -57.069  1.00 16.07           N  
ATOM    982  CA  GLN A 139     -68.966  13.716 -58.041  1.00 16.59           C  
ATOM    983  C   GLN A 139     -69.123  13.240 -59.480  1.00 17.22           C  
ATOM    984  O   GLN A 139     -68.801  13.982 -60.416  1.00 17.65           O  
ATOM    985  CB  GLN A 139     -67.608  14.406 -57.855  1.00 17.61           C  
ATOM    986  CG  GLN A 139     -67.573  15.350 -56.669  1.00 30.47           C  
ATOM    987  CD  GLN A 139     -68.546  16.506 -56.820  1.00 53.13           C  
ATOM    988  OE1 GLN A 139     -68.413  17.332 -57.724  1.00 68.20           O  
ATOM    989  NE2 GLN A 139     -69.540  16.560 -55.942  1.00 40.54           N  
ATOM    990  N   ASN A 140     -69.604  12.014 -59.676  1.00 22.48           N  
ATOM    991  CA  ASN A 140     -70.011  11.507 -60.979  1.00 18.19           C  
ATOM    992  C   ASN A 140     -71.477  11.092 -60.945  1.00 15.62           C  
ATOM    993  O   ASN A 140     -71.890  10.165 -61.644  1.00 15.33           O  
ATOM    994  CB  ASN A 140     -69.124  10.342 -61.414  1.00 17.98           C  
ATOM    995  CG  ASN A 140     -67.706  10.777 -61.720  1.00 25.67           C  
ATOM    996  OD1 ASN A 140     -67.486  11.802 -62.365  1.00 42.87           O  
ATOM    997  ND2 ASN A 140     -66.734   9.998 -61.259  1.00 21.15           N  
ATOM    998  N   GLY A 141     -72.270  11.783 -60.130  1.00 14.58           N  
ATOM    999  CA  GLY A 141     -73.662  11.439 -59.932  1.00 13.13           C  
ATOM   1000  C   GLY A 141     -74.104  11.629 -58.496  1.00 12.93           C  
ATOM   1001  O   GLY A 141     -75.290  11.842 -58.229  1.00 44.34           O  
ATOM   1002  N   ILE A 142     -73.160  11.554 -57.561  1.00 12.63           N  
ATOM   1003  CA  ILE A 142     -73.431  11.749 -56.142  1.00 11.68           C  
ATOM   1004  C   ILE A 142     -72.872  13.102 -55.722  1.00 11.73           C  
ATOM   1005  O   ILE A 142     -71.795  13.506 -56.176  1.00 38.58           O  
ATOM   1006  CB  ILE A 142     -72.827  10.615 -55.291  1.00 11.76           C  
ATOM   1007  CG1 ILE A 142     -73.154   9.256 -55.912  1.00 13.12           C  
ATOM   1008  CG2 ILE A 142     -73.350  10.678 -53.864  1.00 10.59           C  
ATOM   1009  CD1 ILE A 142     -72.590   8.081 -55.148  1.00 22.96           C  
ATOM   1010  N   SER A 143     -73.606  13.800 -54.858  1.00 10.52           N  
ATOM   1011  CA  SER A 143     -73.191  15.109 -54.373  1.00 16.55           C  
ATOM   1012  C   SER A 143     -73.833  15.355 -53.013  1.00 18.51           C  
ATOM   1013  O   SER A 143     -74.598  14.531 -52.506  1.00 24.11           O  
ATOM   1014  CB  SER A 143     -73.559  16.212 -55.372  1.00 13.43           C  
ATOM   1015  OG  SER A 143     -73.193  17.490 -54.878  1.00 21.01           O  
ATOM   1016  N   ALA A 144     -73.505  16.504 -52.417  1.00  8.80           N  
ATOM   1017  CA  ALA A 144     -74.046  16.867 -51.115  1.00  7.94           C  
ATOM   1018  C   ALA A 144     -74.518  18.312 -51.029  1.00  8.34           C  
ATOM   1019  O   ALA A 144     -74.992  18.722 -49.964  1.00  7.62           O  
ATOM   1020  CB  ALA A 144     -73.006  16.609 -50.013  1.00  8.23           C  
ATOM   1021  N   CYS A 145     -74.392  19.097 -52.097  1.00  7.19           N  
ATOM   1022  CA  CYS A 145     -74.854  20.482 -52.122  1.00 14.31           C  
ATOM   1023  C   CYS A 145     -75.765  20.659 -53.329  1.00 14.99           C  
ATOM   1024  O   CYS A 145     -75.314  20.540 -54.473  1.00 19.89           O  
ATOM   1025  CB  CYS A 145     -73.680  21.459 -52.176  1.00 32.78           C  
ATOM   1026  SG  CYS A 145     -74.155  23.134 -52.649  1.00 96.93           S  
ATOM   1027  N   ALA A 146     -77.046  20.938 -53.075  1.00 13.56           N  
ATOM   1028  CA  ALA A 146     -77.989  21.135 -54.172  1.00  8.12           C  
ATOM   1029  C   ALA A 146     -77.749  22.453 -54.896  1.00 11.07           C  
ATOM   1030  O   ALA A 146     -77.987  22.546 -56.105  1.00  2.37           O  
ATOM   1031  CB  ALA A 146     -79.423  21.071 -53.653  1.00 17.86           C  
ATOM   1032  N   VAL A 147     -77.295  23.482 -54.177  1.00 27.44           N  
ATOM   1033  CA  VAL A 147     -77.039  24.773 -54.808  1.00 13.50           C  
ATOM   1034  C   VAL A 147     -75.816  24.692 -55.712  1.00 17.13           C  
ATOM   1035  O   VAL A 147     -75.778  25.302 -56.788  1.00 33.26           O  
ATOM   1036  CB  VAL A 147     -76.874  25.862 -53.732  1.00  1.95           C  
ATOM   1037  CG1 VAL A 147     -76.682  27.227 -54.374  1.00  7.83           C  
ATOM   1038  CG2 VAL A 147     -78.074  25.870 -52.799  1.00  1.95           C  
ATOM   1039  N   CYS A 148     -74.804  23.931 -55.297  1.00 27.83           N  
ATOM   1040  CA  CYS A 148     -73.551  23.876 -56.037  1.00 24.65           C  
ATOM   1041  C   CYS A 148     -73.684  23.037 -57.304  1.00 27.49           C  
ATOM   1042  O   CYS A 148     -73.358  23.500 -58.402  1.00 25.21           O  
ATOM   1043  CB  CYS A 148     -72.445  23.315 -55.143  1.00 24.15           C  
ATOM   1044  SG  CYS A 148     -72.457  23.922 -53.436  1.00 54.50           S  
ATOM   1045  N   ASP A 149     -74.163  21.801 -57.169  1.00 19.53           N  
ATOM   1046  CA  ASP A 149     -74.143  20.831 -58.255  1.00  7.01           C  
ATOM   1047  C   ASP A 149     -75.521  20.519 -58.823  1.00  5.97           C  
ATOM   1048  O   ASP A 149     -75.624  19.681 -59.725  1.00  6.57           O  
ATOM   1049  CB  ASP A 149     -73.480  19.530 -57.785  1.00  8.60           C  
ATOM   1050  CG  ASP A 149     -72.077  19.750 -57.247  1.00 41.38           C  
ATOM   1051  OD1 ASP A 149     -71.344  20.592 -57.809  1.00 60.74           O  
ATOM   1052  OD2 ASP A 149     -71.706  19.076 -56.262  1.00 50.62           O  
ATOM   1053  N   GLY A 150     -76.580  21.162 -58.328  1.00  4.48           N  
ATOM   1054  CA  GLY A 150     -77.915  20.845 -58.807  1.00  3.45           C  
ATOM   1055  C   GLY A 150     -78.139  21.201 -60.262  1.00  2.78           C  
ATOM   1056  O   GLY A 150     -78.939  20.555 -60.946  1.00 16.06           O  
ATOM   1057  N   ALA A 151     -77.435  22.214 -60.761  1.00 21.40           N  
ATOM   1058  CA  ALA A 151     -77.630  22.695 -62.121  1.00 12.19           C  
ATOM   1059  C   ALA A 151     -76.777  21.966 -63.151  1.00 14.96           C  
ATOM   1060  O   ALA A 151     -76.932  22.229 -64.349  1.00 19.52           O  
ATOM   1061  CB  ALA A 151     -77.333  24.198 -62.195  1.00  8.39           C  
ATOM   1062  N   VAL A 152     -75.892  21.071 -62.720  1.00  4.70           N  
ATOM   1063  CA  VAL A 152     -75.014  20.315 -63.614  1.00  6.13           C  
ATOM   1064  C   VAL A 152     -75.861  19.612 -64.671  1.00 19.14           C  
ATOM   1065  O   VAL A 152     -76.909  19.038 -64.339  1.00 32.22           O  
ATOM   1066  CB  VAL A 152     -74.148  19.323 -62.819  1.00 12.64           C  
ATOM   1067  CG1 VAL A 152     -73.325  18.439 -63.747  1.00  9.73           C  
ATOM   1068  CG2 VAL A 152     -73.236  20.077 -61.860  1.00  8.43           C  
ATOM   1069  N   PRO A 153     -75.464  19.651 -65.947  1.00 20.65           N  
ATOM   1070  CA  PRO A 153     -76.326  19.097 -67.008  1.00 39.93           C  
ATOM   1071  C   PRO A 153     -76.617  17.610 -66.876  1.00 40.64           C  
ATOM   1072  O   PRO A 153     -77.626  17.148 -67.426  1.00 23.47           O  
ATOM   1073  CB  PRO A 153     -75.540  19.400 -68.293  1.00 19.08           C  
ATOM   1074  CG  PRO A 153     -74.133  19.648 -67.841  1.00  5.72           C  
ATOM   1075  CD  PRO A 153     -74.262  20.295 -66.501  1.00  5.68           C  
ATOM   1076  N   ILE A 154     -75.776  16.839 -66.181  1.00 38.37           N  
ATOM   1077  CA  ILE A 154     -76.024  15.407 -66.056  1.00 12.79           C  
ATOM   1078  C   ILE A 154     -77.232  15.096 -65.187  1.00 20.16           C  
ATOM   1079  O   ILE A 154     -77.702  13.953 -65.184  1.00 32.67           O  
ATOM   1080  CB  ILE A 154     -74.790  14.669 -65.496  1.00 11.48           C  
ATOM   1081  CG1 ILE A 154     -74.599  14.985 -64.012  1.00 11.83           C  
ATOM   1082  CG2 ILE A 154     -73.543  15.038 -66.285  1.00 16.99           C  
ATOM   1083  CD1 ILE A 154     -73.451  14.232 -63.377  1.00 13.77           C  
ATOM   1084  N   PHE A 155     -77.752  16.083 -64.453  1.00 13.53           N  
ATOM   1085  CA  PHE A 155     -78.931  15.890 -63.624  1.00  6.39           C  
ATOM   1086  C   PHE A 155     -80.190  16.511 -64.209  1.00 17.89           C  
ATOM   1087  O   PHE A 155     -81.285  16.234 -63.707  1.00 27.31           O  
ATOM   1088  CB  PHE A 155     -78.703  16.474 -62.220  1.00  6.13           C  
ATOM   1089  CG  PHE A 155     -77.467  15.963 -61.538  1.00  7.78           C  
ATOM   1090  CD1 PHE A 155     -77.319  14.616 -61.254  1.00 23.93           C  
ATOM   1091  CD2 PHE A 155     -76.457  16.834 -61.167  1.00  8.13           C  
ATOM   1092  CE1 PHE A 155     -76.181  14.147 -60.624  1.00 32.95           C  
ATOM   1093  CE2 PHE A 155     -75.318  16.371 -60.536  1.00  9.59           C  
ATOM   1094  CZ  PHE A 155     -75.181  15.026 -60.263  1.00 19.44           C  
ATOM   1095  N   ARG A 156     -80.072  17.332 -65.250  1.00 26.68           N  
ATOM   1096  CA  ARG A 156     -81.237  18.011 -65.801  1.00 13.88           C  
ATOM   1097  C   ARG A 156     -82.093  17.026 -66.586  1.00 13.54           C  
ATOM   1098  O   ARG A 156     -81.578  16.244 -67.392  1.00  9.33           O  
ATOM   1099  CB  ARG A 156     -80.810  19.184 -66.684  1.00  4.59           C  
ATOM   1100  CG  ARG A 156     -79.959  20.218 -65.953  1.00 10.40           C  
ATOM   1101  CD  ARG A 156     -79.980  21.581 -66.634  1.00 10.69           C  
ATOM   1102  NE  ARG A 156     -81.233  22.295 -66.404  1.00 41.63           N  
ATOM   1103  CZ  ARG A 156     -82.167  22.491 -67.330  1.00 66.41           C  
ATOM   1104  NH1 ARG A 156     -81.992  22.031 -68.561  1.00 75.52           N  
ATOM   1105  NH2 ARG A 156     -83.276  23.153 -67.026  1.00 67.56           N  
ATOM   1106  N   ASN A 157     -83.403  17.064 -66.335  1.00 13.34           N  
ATOM   1107  CA  ASN A 157     -84.368  16.169 -66.977  1.00 13.70           C  
ATOM   1108  C   ASN A 157     -84.025  14.703 -66.711  1.00 28.21           C  
ATOM   1109  O   ASN A 157     -84.122  13.850 -67.595  1.00 45.28           O  
ATOM   1110  CB  ASN A 157     -84.469  16.445 -68.479  1.00 20.17           C  
ATOM   1111  CG  ASN A 157     -85.898  16.406 -68.984  1.00 37.59           C  
ATOM   1112  OD1 ASN A 157     -86.842  16.634 -68.228  1.00 38.63           O  
ATOM   1113  ND2 ASN A 157     -86.064  16.116 -70.270  1.00 47.60           N  
ATOM   1114  N   LYS A 158     -83.624  14.413 -65.480  1.00 26.40           N  
ATOM   1115  CA  LYS A 158     -83.278  13.074 -65.032  1.00 10.09           C  
ATOM   1116  C   LYS A 158     -83.910  12.835 -63.670  1.00 11.43           C  
ATOM   1117  O   LYS A 158     -84.209  13.787 -62.942  1.00  7.26           O  
ATOM   1118  CB  LYS A 158     -81.758  12.882 -64.936  1.00  8.51           C  
ATOM   1119  CG  LYS A 158     -81.015  12.936 -66.262  1.00 19.04           C  
ATOM   1120  CD  LYS A 158     -81.468  11.827 -67.199  1.00 15.63           C  
ATOM   1121  CE  LYS A 158     -80.564  11.727 -68.419  1.00 11.28           C  
ATOM   1122  NZ  LYS A 158     -80.470  13.019 -69.152  1.00 46.38           N  
ATOM   1123  N   PRO A 159     -84.138  11.574 -63.302  1.00 21.55           N  
ATOM   1124  CA  PRO A 159     -84.664  11.287 -61.960  1.00  8.16           C  
ATOM   1125  C   PRO A 159     -83.591  11.515 -60.905  1.00  6.86           C  
ATOM   1126  O   PRO A 159     -82.491  10.964 -60.989  1.00  7.55           O  
ATOM   1127  CB  PRO A 159     -85.071   9.810 -62.041  1.00  9.06           C  
ATOM   1128  CG  PRO A 159     -85.179   9.514 -63.508  1.00 30.58           C  
ATOM   1129  CD  PRO A 159     -84.143  10.378 -64.159  1.00 37.71           C  
ATOM   1130  N   LEU A 160     -83.923  12.325 -59.904  1.00  6.05           N  
ATOM   1131  CA  LEU A 160     -83.002  12.668 -58.832  1.00  7.61           C  
ATOM   1132  C   LEU A 160     -83.540  12.160 -57.502  1.00  4.84           C  
ATOM   1133  O   LEU A 160     -84.754  12.105 -57.285  1.00  4.98           O  
ATOM   1134  CB  LEU A 160     -82.777  14.182 -58.754  1.00 25.55           C  
ATOM   1135  CG  LEU A 160     -82.295  14.860 -60.037  1.00  5.01           C  
ATOM   1136  CD1 LEU A 160     -82.088  16.351 -59.810  1.00  4.40           C  
ATOM   1137  CD2 LEU A 160     -81.020  14.204 -60.536  1.00  5.42           C  
ATOM   1138  N   TYR A 161     -82.623  11.787 -56.611  1.00  4.59           N  
ATOM   1139  CA  TYR A 161     -82.979  11.256 -55.303  1.00  6.45           C  
ATOM   1140  C   TYR A 161     -82.264  12.036 -54.209  1.00  4.47           C  
ATOM   1141  O   TYR A 161     -81.094  12.403 -54.355  1.00  4.70           O  
ATOM   1142  CB  TYR A 161     -82.648   9.758 -55.191  1.00  4.57           C  
ATOM   1143  CG  TYR A 161     -83.681   8.858 -55.835  1.00  4.60           C  
ATOM   1144  CD1 TYR A 161     -83.869   8.855 -57.210  1.00 25.99           C  
ATOM   1145  CD2 TYR A 161     -84.477   8.019 -55.065  1.00  4.42           C  
ATOM   1146  CE1 TYR A 161     -84.815   8.040 -57.803  1.00 23.19           C  
ATOM   1147  CE2 TYR A 161     -85.426   7.198 -55.649  1.00 14.04           C  
ATOM   1148  CZ  TYR A 161     -85.590   7.213 -57.019  1.00 18.26           C  
ATOM   1149  OH  TYR A 161     -86.532   6.401 -57.611  1.00 10.92           O  
ATOM   1150  N   VAL A 162     -82.982  12.290 -53.117  1.00  4.51           N  
ATOM   1151  CA  VAL A 162     -82.471  13.021 -51.964  1.00  4.95           C  
ATOM   1152  C   VAL A 162     -82.586  12.127 -50.738  1.00 14.50           C  
ATOM   1153  O   VAL A 162     -83.576  11.404 -50.577  1.00 26.03           O  
ATOM   1154  CB  VAL A 162     -83.237  14.344 -51.749  1.00  4.78           C  
ATOM   1155  CG1 VAL A 162     -82.604  15.158 -50.633  1.00  5.42           C  
ATOM   1156  CG2 VAL A 162     -83.293  15.145 -53.040  1.00  4.25           C  
ATOM   1157  N   ILE A 163     -81.573  12.170 -49.878  1.00 11.65           N  
ATOM   1158  CA  ILE A 163     -81.534  11.372 -48.657  1.00  7.84           C  
ATOM   1159  C   ILE A 163     -81.584  12.319 -47.466  1.00 10.44           C  
ATOM   1160  O   ILE A 163     -80.731  13.204 -47.333  1.00 25.67           O  
ATOM   1161  CB  ILE A 163     -80.284  10.483 -48.602  1.00  8.87           C  
ATOM   1162  CG1 ILE A 163     -80.290   9.488 -49.761  1.00  7.93           C  
ATOM   1163  CG2 ILE A 163     -80.205   9.757 -47.270  1.00 10.67           C  
ATOM   1164  CD1 ILE A 163     -79.075   8.592 -49.792  1.00 18.76           C  
ATOM   1165  N   GLY A 164     -82.564  12.128 -46.599  1.00  9.46           N  
ATOM   1166  CA  GLY A 164     -82.713  12.933 -45.401  1.00 10.88           C  
ATOM   1167  C   GLY A 164     -84.168  13.282 -45.151  1.00 23.61           C  
ATOM   1168  O   GLY A 164     -85.013  13.249 -46.045  1.00 28.74           O  
ATOM   1169  N   GLY A 165     -84.467  13.618 -43.898  1.00 18.21           N  
ATOM   1170  CA  GLY A 165     -85.821  13.976 -43.525  1.00 12.26           C  
ATOM   1171  C   GLY A 165     -85.939  15.324 -42.843  1.00 14.59           C  
ATOM   1172  O   GLY A 165     -87.039  15.737 -42.463  1.00 13.64           O  
ATOM   1173  N   GLY A 166     -84.817  16.020 -42.684  1.00 51.84           N  
ATOM   1174  CA  GLY A 166     -84.801  17.304 -42.019  1.00 52.69           C  
ATOM   1175  C   GLY A 166     -85.195  18.441 -42.944  1.00 36.74           C  
ATOM   1176  O   GLY A 166     -85.688  18.247 -44.057  1.00 30.65           O  
ATOM   1177  N   ASP A 167     -84.967  19.663 -42.456  1.00 29.00           N  
ATOM   1178  CA  ASP A 167     -85.294  20.842 -43.252  1.00 10.96           C  
ATOM   1179  C   ASP A 167     -84.344  20.987 -44.433  1.00  9.89           C  
ATOM   1180  O   ASP A 167     -84.758  21.413 -45.518  1.00  9.19           O  
ATOM   1181  CB  ASP A 167     -85.260  22.098 -42.381  1.00 19.34           C  
ATOM   1182  CG  ASP A 167     -86.359  22.116 -41.338  1.00 38.46           C  
ATOM   1183  OD1 ASP A 167     -86.281  21.323 -40.377  1.00 47.39           O  
ATOM   1184  OD2 ASP A 167     -87.299  22.927 -41.480  1.00 37.93           O  
ATOM   1185  N   SER A 168     -83.067  20.642 -44.240  1.00 10.68           N  
ATOM   1186  CA  SER A 168     -82.112  20.698 -45.343  1.00  9.36           C  
ATOM   1187  C   SER A 168     -82.526  19.780 -46.482  1.00  9.24           C  
ATOM   1188  O   SER A 168     -82.287  20.096 -47.653  1.00 10.11           O  
ATOM   1189  CB  SER A 168     -80.711  20.330 -44.849  1.00 11.04           C  
ATOM   1190  OG  SER A 168     -80.281  21.201 -43.817  1.00 45.86           O  
ATOM   1191  N   ALA A 169     -83.148  18.644 -46.162  1.00 16.61           N  
ATOM   1192  CA  ALA A 169     -83.614  17.736 -47.203  1.00  9.94           C  
ATOM   1193  C   ALA A 169     -84.745  18.361 -48.008  1.00  6.78           C  
ATOM   1194  O   ALA A 169     -84.693  18.403 -49.242  1.00 11.75           O  
ATOM   1195  CB  ALA A 169     -84.055  16.410 -46.585  1.00 10.47           C  
ATOM   1196  N   ALA A 170     -85.780  18.851 -47.320  1.00  7.23           N  
ATOM   1197  CA  ALA A 170     -86.917  19.449 -48.013  1.00  6.36           C  
ATOM   1198  C   ALA A 170     -86.499  20.688 -48.793  1.00 17.02           C  
ATOM   1199  O   ALA A 170     -87.007  20.943 -49.892  1.00 14.68           O  
ATOM   1200  CB  ALA A 170     -88.019  19.791 -47.011  1.00  6.96           C  
ATOM   1201  N   GLU A 171     -85.572  21.472 -48.239  1.00 23.89           N  
ATOM   1202  CA  GLU A 171     -85.110  22.672 -48.927  1.00  4.65           C  
ATOM   1203  C   GLU A 171     -84.321  22.318 -50.183  1.00  4.11           C  
ATOM   1204  O   GLU A 171     -84.520  22.928 -51.240  1.00  3.24           O  
ATOM   1205  CB  GLU A 171     -84.272  23.528 -47.976  1.00  4.80           C  
ATOM   1206  CG  GLU A 171     -83.962  24.923 -48.491  1.00 40.88           C  
ATOM   1207  CD  GLU A 171     -83.183  25.752 -47.487  1.00 62.52           C  
ATOM   1208  OE1 GLU A 171     -82.767  25.195 -46.450  1.00 57.26           O  
ATOM   1209  OE2 GLU A 171     -82.988  26.962 -47.736  1.00 72.71           O  
ATOM   1210  N   GLU A 172     -83.423  21.333 -50.088  1.00 16.46           N  
ATOM   1211  CA  GLU A 172     -82.627  20.943 -51.248  1.00 17.35           C  
ATOM   1212  C   GLU A 172     -83.440  20.137 -52.255  1.00 17.75           C  
ATOM   1213  O   GLU A 172     -83.146  20.177 -53.456  1.00  3.32           O  
ATOM   1214  CB  GLU A 172     -81.397  20.148 -50.805  1.00  4.66           C  
ATOM   1215  CG  GLU A 172     -80.337  20.979 -50.091  1.00 42.37           C  
ATOM   1216  CD  GLU A 172     -78.979  20.296 -50.053  1.00 43.17           C  
ATOM   1217  OE1 GLU A 172     -78.881  19.135 -50.506  1.00 14.87           O  
ATOM   1218  OE2 GLU A 172     -78.011  20.922 -49.569  1.00 36.86           O  
ATOM   1219  N   ALA A 173     -84.455  19.402 -51.793  1.00 23.10           N  
ATOM   1220  CA  ALA A 173     -85.279  18.619 -52.711  1.00  7.58           C  
ATOM   1221  C   ALA A 173     -86.063  19.522 -53.654  1.00 18.89           C  
ATOM   1222  O   ALA A 173     -86.068  19.310 -54.873  1.00 25.52           O  
ATOM   1223  CB  ALA A 173     -86.224  17.707 -51.928  1.00  5.17           C  
ATOM   1224  N   MET A 174     -86.742  20.534 -53.105  1.00 22.48           N  
ATOM   1225  CA  MET A 174     -87.490  21.466 -53.944  1.00  4.73           C  
ATOM   1226  C   MET A 174     -86.568  22.291 -54.833  1.00  9.06           C  
ATOM   1227  O   MET A 174     -86.979  22.726 -55.915  1.00 27.22           O  
ATOM   1228  CB  MET A 174     -88.355  22.379 -53.075  1.00  2.72           C  
ATOM   1229  CG  MET A 174     -89.420  21.639 -52.282  1.00  3.39           C  
ATOM   1230  SD  MET A 174     -90.472  22.731 -51.307  1.00 13.31           S  
ATOM   1231  CE  MET A 174     -89.289  23.396 -50.139  1.00  8.16           C  
ATOM   1232  N   PHE A 175     -85.325  22.518 -54.399  1.00  2.26           N  
ATOM   1233  CA  PHE A 175     -84.368  23.220 -55.248  1.00  1.95           C  
ATOM   1234  C   PHE A 175     -83.959  22.356 -56.435  1.00  8.26           C  
ATOM   1235  O   PHE A 175     -83.821  22.859 -57.557  1.00  1.95           O  
ATOM   1236  CB  PHE A 175     -83.145  23.632 -54.427  1.00  1.95           C  
ATOM   1237  CG  PHE A 175     -82.189  24.531 -55.163  1.00  1.96           C  
ATOM   1238  CD1 PHE A 175     -81.186  23.999 -55.957  1.00  4.00           C  
ATOM   1239  CD2 PHE A 175     -82.284  25.907 -55.048  1.00  1.95           C  
ATOM   1240  CE1 PHE A 175     -80.303  24.821 -56.631  1.00  1.95           C  
ATOM   1241  CE2 PHE A 175     -81.402  26.735 -55.718  1.00  1.95           C  
ATOM   1242  CZ  PHE A 175     -80.412  26.191 -56.511  1.00  1.95           C  
ATOM   1243  N   LEU A 176     -83.767  21.053 -56.208  1.00 18.38           N  
ATOM   1244  CA  LEU A 176     -83.417  20.147 -57.295  1.00  4.98           C  
ATOM   1245  C   LEU A 176     -84.564  19.948 -58.273  1.00  9.39           C  
ATOM   1246  O   LEU A 176     -84.332  19.492 -59.398  1.00  9.26           O  
ATOM   1247  CB  LEU A 176     -82.976  18.795 -56.734  1.00  3.19           C  
ATOM   1248  CG  LEU A 176     -81.631  18.765 -56.011  1.00  3.27           C  
ATOM   1249  CD1 LEU A 176     -81.477  17.468 -55.238  1.00  3.65           C  
ATOM   1250  CD2 LEU A 176     -80.498  18.933 -57.005  1.00  3.31           C  
ATOM   1251  N   ALA A 177     -85.794  20.281 -57.873  1.00  6.78           N  
ATOM   1252  CA  ALA A 177     -86.930  20.164 -58.777  1.00  3.05           C  
ATOM   1253  C   ALA A 177     -86.839  21.135 -59.944  1.00  2.56           C  
ATOM   1254  O   ALA A 177     -87.532  20.946 -60.948  1.00 18.55           O  
ATOM   1255  CB  ALA A 177     -88.234  20.386 -58.013  1.00  3.08           C  
ATOM   1256  N   LYS A 178     -85.993  22.162 -59.841  1.00  1.95           N  
ATOM   1257  CA  LYS A 178     -85.819  23.100 -60.942  1.00  8.63           C  
ATOM   1258  C   LYS A 178     -85.168  22.449 -62.155  1.00  1.95           C  
ATOM   1259  O   LYS A 178     -85.359  22.930 -63.277  1.00  1.95           O  
ATOM   1260  CB  LYS A 178     -84.974  24.292 -60.486  1.00 15.33           C  
ATOM   1261  CG  LYS A 178     -85.599  25.124 -59.378  1.00  3.00           C  
ATOM   1262  CD  LYS A 178     -84.685  26.273 -58.983  1.00  1.95           C  
ATOM   1263  CE  LYS A 178     -85.324  27.160 -57.926  1.00  1.95           C  
ATOM   1264  NZ  LYS A 178     -86.531  27.865 -58.438  1.00  7.56           N  
ATOM   1265  N   TYR A 179     -84.411  21.370 -61.956  1.00  2.52           N  
ATOM   1266  CA  TYR A 179     -83.623  20.761 -63.020  1.00  6.17           C  
ATOM   1267  C   TYR A 179     -84.058  19.342 -63.349  1.00 20.21           C  
ATOM   1268  O   TYR A 179     -84.263  19.019 -64.525  1.00 45.90           O  
ATOM   1269  CB  TYR A 179     -82.136  20.772 -62.631  1.00  3.02           C  
ATOM   1270  CG  TYR A 179     -81.674  22.080 -62.032  1.00 15.78           C  
ATOM   1271  CD1 TYR A 179     -81.326  23.154 -62.840  1.00 12.83           C  
ATOM   1272  CD2 TYR A 179     -81.585  22.241 -60.655  1.00  7.28           C  
ATOM   1273  CE1 TYR A 179     -80.905  24.353 -62.293  1.00  1.95           C  
ATOM   1274  CE2 TYR A 179     -81.164  23.434 -60.099  1.00  1.95           C  
ATOM   1275  CZ  TYR A 179     -80.824  24.487 -60.922  1.00  1.95           C  
ATOM   1276  OH  TYR A 179     -80.404  25.677 -60.372  1.00  1.95           O  
ATOM   1277  N   GLY A 180     -84.203  18.481 -62.343  1.00  4.20           N  
ATOM   1278  CA  GLY A 180     -84.478  17.083 -62.601  1.00 17.00           C  
ATOM   1279  C   GLY A 180     -85.893  16.830 -63.086  1.00 37.42           C  
ATOM   1280  O   GLY A 180     -86.815  17.617 -62.870  1.00 50.08           O  
ATOM   1281  N   SER A 181     -86.056  15.690 -63.766  1.00 28.59           N  
ATOM   1282  CA  SER A 181     -87.381  15.277 -64.220  1.00 19.02           C  
ATOM   1283  C   SER A 181     -88.282  14.926 -63.044  1.00  7.57           C  
ATOM   1284  O   SER A 181     -89.479  15.236 -63.055  1.00  7.56           O  
ATOM   1285  CB  SER A 181     -87.267  14.085 -65.171  1.00 24.69           C  
ATOM   1286  OG  SER A 181     -87.043  14.508 -66.502  1.00 56.23           O  
ATOM   1287  N   SER A 182     -87.726  14.276 -62.027  1.00  7.62           N  
ATOM   1288  CA  SER A 182     -88.478  13.922 -60.835  1.00  7.71           C  
ATOM   1289  C   SER A 182     -87.509  13.829 -59.668  1.00 10.51           C  
ATOM   1290  O   SER A 182     -86.397  13.314 -59.815  1.00 39.90           O  
ATOM   1291  CB  SER A 182     -89.236  12.600 -61.016  1.00 33.67           C  
ATOM   1292  OG  SER A 182     -88.356  11.540 -61.351  1.00 47.63           O  
ATOM   1293  N   VAL A 183     -87.935  14.335 -58.516  1.00  6.12           N  
ATOM   1294  CA  VAL A 183     -87.132  14.323 -57.301  1.00  9.15           C  
ATOM   1295  C   VAL A 183     -87.846  13.460 -56.273  1.00 16.08           C  
ATOM   1296  O   VAL A 183     -89.029  13.675 -55.989  1.00 15.86           O  
ATOM   1297  CB  VAL A 183     -86.898  15.744 -56.756  1.00 21.52           C  
ATOM   1298  CG1 VAL A 183     -86.116  15.689 -55.452  1.00 19.21           C  
ATOM   1299  CG2 VAL A 183     -86.174  16.597 -57.787  1.00 18.29           C  
ATOM   1300  N   THR A 184     -87.134  12.480 -55.728  1.00 25.18           N  
ATOM   1301  CA  THR A 184     -87.662  11.610 -54.688  1.00 21.77           C  
ATOM   1302  C   THR A 184     -86.775  11.722 -53.458  1.00  4.59           C  
ATOM   1303  O   THR A 184     -85.547  11.659 -53.567  1.00 16.40           O  
ATOM   1304  CB  THR A 184     -87.725  10.155 -55.164  1.00 16.42           C  
ATOM   1305  OG1 THR A 184     -88.394  10.091 -56.430  1.00  9.44           O  
ATOM   1306  CG2 THR A 184     -88.474   9.297 -54.157  1.00  5.19           C  
ATOM   1307  N   VAL A 185     -87.392  11.895 -52.294  1.00  4.75           N  
ATOM   1308  CA  VAL A 185     -86.673  12.010 -51.031  1.00  7.28           C  
ATOM   1309  C   VAL A 185     -86.922  10.740 -50.226  1.00 11.02           C  
ATOM   1310  O   VAL A 185     -88.066  10.283 -50.108  1.00 13.00           O  
ATOM   1311  CB  VAL A 185     -87.078  13.279 -50.259  1.00  5.27           C  
ATOM   1312  CG1 VAL A 185     -88.581  13.390 -50.145  1.00 10.60           C  
ATOM   1313  CG2 VAL A 185     -86.424  13.306 -48.889  1.00 24.54           C  
ATOM   1314  N   LEU A 186     -85.849  10.161 -49.693  1.00 13.79           N  
ATOM   1315  CA  LEU A 186     -85.873   8.866 -49.012  1.00  7.24           C  
ATOM   1316  C   LEU A 186     -85.709   9.099 -47.512  1.00  9.30           C  
ATOM   1317  O   LEU A 186     -84.593   9.147 -46.992  1.00 10.18           O  
ATOM   1318  CB  LEU A 186     -84.783   7.947 -49.554  1.00  5.57           C  
ATOM   1319  CG  LEU A 186     -84.680   7.837 -51.075  1.00  4.82           C  
ATOM   1320  CD1 LEU A 186     -83.524   6.932 -51.467  1.00  5.01           C  
ATOM   1321  CD2 LEU A 186     -85.985   7.328 -51.662  1.00  4.38           C  
ATOM   1322  N   VAL A 187     -86.833   9.242 -46.818  1.00  7.19           N  
ATOM   1323  CA  VAL A 187     -86.819   9.387 -45.368  1.00 14.47           C  
ATOM   1324  C   VAL A 187     -86.607   8.019 -44.735  1.00 32.19           C  
ATOM   1325  O   VAL A 187     -87.246   7.033 -45.123  1.00 39.13           O  
ATOM   1326  CB  VAL A 187     -88.125  10.031 -44.876  1.00 30.97           C  
ATOM   1327  CG1 VAL A 187     -88.076  10.263 -43.371  1.00 46.72           C  
ATOM   1328  CG2 VAL A 187     -88.382  11.331 -45.618  1.00 41.71           C  
ATOM   1329  N   ARG A 188     -85.707   7.958 -43.752  1.00 38.61           N  
ATOM   1330  CA  ARG A 188     -85.365   6.683 -43.131  1.00 11.45           C  
ATOM   1331  C   ARG A 188     -86.481   6.197 -42.216  1.00 11.75           C  
ATOM   1332  O   ARG A 188     -86.867   5.024 -42.259  1.00 10.89           O  
ATOM   1333  CB  ARG A 188     -84.053   6.821 -42.359  1.00 22.71           C  
ATOM   1334  CG  ARG A 188     -83.889   5.832 -41.222  1.00 29.72           C  
ATOM   1335  CD  ARG A 188     -83.075   6.434 -40.088  1.00 41.56           C  
ATOM   1336  NE  ARG A 188     -81.647   6.481 -40.389  1.00 36.85           N  
ATOM   1337  CZ  ARG A 188     -80.744   7.081 -39.621  1.00 50.22           C  
ATOM   1338  NH1 ARG A 188     -81.120   7.693 -38.506  1.00 49.52           N  
ATOM   1339  NH2 ARG A 188     -79.463   7.070 -39.965  1.00 62.23           N  
ATOM   1340  N   ARG A 189     -87.021   7.089 -41.393  1.00 30.07           N  
ATOM   1341  CA  ARG A 189     -88.094   6.743 -40.476  1.00 14.46           C  
ATOM   1342  C   ARG A 189     -89.446   7.030 -41.130  1.00 12.10           C  
ATOM   1343  O   ARG A 189     -89.546   7.239 -42.342  1.00 22.80           O  
ATOM   1344  CB  ARG A 189     -87.911   7.465 -39.144  1.00 41.25           C  
ATOM   1345  CG  ARG A 189     -87.911   8.977 -39.211  1.00 55.40           C  
ATOM   1346  CD  ARG A 189     -87.645   9.544 -37.826  1.00 51.92           C  
ATOM   1347  NE  ARG A 189     -87.919  10.973 -37.738  1.00 55.48           N  
ATOM   1348  CZ  ARG A 189     -87.851  11.672 -36.611  1.00 49.34           C  
ATOM   1349  NH1 ARG A 189     -87.517  11.072 -35.476  1.00 42.66           N  
ATOM   1350  NH2 ARG A 189     -88.120  12.970 -36.616  1.00 47.44           N  
ATOM   1351  N   ASP A 190     -90.506   7.034 -40.326  1.00 12.52           N  
ATOM   1352  CA  ASP A 190     -91.873   7.134 -40.819  1.00 13.47           C  
ATOM   1353  C   ASP A 190     -92.436   8.550 -40.846  1.00 31.79           C  
ATOM   1354  O   ASP A 190     -93.573   8.727 -41.295  1.00 44.78           O  
ATOM   1355  CB  ASP A 190     -92.792   6.261 -39.957  1.00 17.70           C  
ATOM   1356  CG  ASP A 190     -92.914   6.774 -38.527  1.00 16.72           C  
ATOM   1357  OD1 ASP A 190     -91.940   7.367 -38.013  1.00 14.08           O  
ATOM   1358  OD2 ASP A 190     -93.988   6.586 -37.917  1.00 15.53           O  
ATOM   1359  N   LYS A 191     -91.697   9.562 -40.396  1.00 24.22           N  
ATOM   1360  CA  LYS A 191     -92.218  10.919 -40.480  1.00 12.88           C  
ATOM   1361  C   LYS A 191     -91.093  11.943 -40.565  1.00 13.77           C  
ATOM   1362  O   LYS A 191     -90.069  11.825 -39.884  1.00 15.49           O  
ATOM   1363  CB  LYS A 191     -93.125  11.231 -39.284  1.00 13.73           C  
ATOM   1364  CG  LYS A 191     -92.583  10.764 -37.946  1.00 15.40           C  
ATOM   1365  CD  LYS A 191     -93.639  10.908 -36.858  1.00 26.93           C  
ATOM   1366  CE  LYS A 191     -93.231  10.187 -35.581  1.00 47.88           C  
ATOM   1367  NZ  LYS A 191     -94.310  10.231 -34.554  1.00 39.17           N  
ATOM   1368  N   LEU A 192     -91.296  12.930 -41.438  1.00 21.24           N  
ATOM   1369  CA  LEU A 192     -90.354  14.024 -41.639  1.00 17.76           C  
ATOM   1370  C   LEU A 192     -89.935  14.667 -40.322  1.00 17.14           C  
ATOM   1371  O   LEU A 192     -90.776  14.996 -39.479  1.00 15.53           O  
ATOM   1372  CB  LEU A 192     -90.983  15.080 -42.547  1.00 11.63           C  
ATOM   1373  CG  LEU A 192     -91.115  14.714 -44.024  1.00  9.98           C  
ATOM   1374  CD1 LEU A 192     -92.013  15.714 -44.732  1.00  9.19           C  
ATOM   1375  CD2 LEU A 192     -89.748  14.656 -44.675  1.00  9.59           C  
ATOM   1376  N   ARG A 193     -88.625  14.836 -40.147  1.00 29.50           N  
ATOM   1377  CA  ARG A 193     -88.085  15.559 -39.003  1.00 24.27           C  
ATOM   1378  C   ARG A 193     -88.158  17.071 -39.187  1.00 31.54           C  
ATOM   1379  O   ARG A 193     -87.864  17.813 -38.243  1.00 41.96           O  
ATOM   1380  CB  ARG A 193     -86.632  15.134 -38.755  1.00 19.72           C  
ATOM   1381  CG  ARG A 193     -86.089  15.457 -37.365  1.00 29.69           C  
ATOM   1382  CD  ARG A 193     -84.595  15.174 -37.271  1.00 44.24           C  
ATOM   1383  NE  ARG A 193     -84.079  15.366 -35.917  1.00 44.99           N  
ATOM   1384  CZ  ARG A 193     -83.883  14.384 -35.041  1.00 48.75           C  
ATOM   1385  NH1 ARG A 193     -84.156  13.130 -35.373  1.00 52.51           N  
ATOM   1386  NH2 ARG A 193     -83.410  14.657 -33.832  1.00 37.66           N  
ATOM   1387  N   ALA A 194     -88.564  17.540 -40.366  1.00 17.95           N  
ATOM   1388  CA  ALA A 194     -88.494  18.951 -40.712  1.00 15.58           C  
ATOM   1389  C   ALA A 194     -89.625  19.743 -40.060  1.00 23.23           C  
ATOM   1390  O   ALA A 194     -90.486  19.204 -39.358  1.00 14.27           O  
ATOM   1391  CB  ALA A 194     -88.524  19.124 -42.229  1.00 12.04           C  
ATOM   1392  N   SER A 195     -89.615  21.051 -40.306  1.00 30.89           N  
ATOM   1393  CA  SER A 195     -90.615  21.954 -39.763  1.00 21.96           C  
ATOM   1394  C   SER A 195     -91.976  21.702 -40.405  1.00 42.83           C  
ATOM   1395  O   SER A 195     -92.085  21.162 -41.509  1.00 54.50           O  
ATOM   1396  CB  SER A 195     -90.196  23.408 -39.981  1.00 10.26           C  
ATOM   1397  OG  SER A 195     -91.175  24.302 -39.479  1.00 38.64           O  
ATOM   1398  N   LYS A 196     -93.027  22.101 -39.684  1.00 35.18           N  
ATOM   1399  CA  LYS A 196     -94.384  21.870 -40.167  1.00 12.89           C  
ATOM   1400  C   LYS A 196     -94.669  22.694 -41.415  1.00  8.50           C  
ATOM   1401  O   LYS A 196     -95.373  22.236 -42.323  1.00  8.12           O  
ATOM   1402  CB  LYS A 196     -95.392  22.197 -39.066  1.00 12.13           C  
ATOM   1403  CG  LYS A 196     -95.050  21.595 -37.713  1.00 20.57           C  
ATOM   1404  CD  LYS A 196     -95.978  22.121 -36.629  1.00 26.85           C  
ATOM   1405  CE  LYS A 196     -95.561  21.629 -35.253  1.00 24.40           C  
ATOM   1406  NZ  LYS A 196     -96.436  22.177 -34.180  1.00 14.89           N  
ATOM   1407  N   ALA A 197     -94.124  23.910 -41.483  1.00  7.47           N  
ATOM   1408  CA  ALA A 197     -94.347  24.762 -42.644  1.00 15.92           C  
ATOM   1409  C   ALA A 197     -93.471  24.337 -43.815  1.00 22.14           C  
ATOM   1410  O   ALA A 197     -93.916  24.361 -44.969  1.00 23.52           O  
ATOM   1411  CB  ALA A 197     -94.088  26.225 -42.284  1.00 12.53           C  
ATOM   1412  N   MET A 198     -92.223  23.949 -43.538  1.00 25.48           N  
ATOM   1413  CA  MET A 198     -91.348  23.471 -44.601  1.00 19.13           C  
ATOM   1414  C   MET A 198     -91.829  22.138 -45.160  1.00 19.72           C  
ATOM   1415  O   MET A 198     -91.686  21.884 -46.362  1.00 27.69           O  
ATOM   1416  CB  MET A 198     -89.915  23.347 -44.080  1.00  8.85           C  
ATOM   1417  CG  MET A 198     -88.880  23.025 -45.145  1.00 13.17           C  
ATOM   1418  SD  MET A 198     -88.698  24.336 -46.368  1.00 38.56           S  
ATOM   1419  CE  MET A 198     -88.388  25.752 -45.315  1.00 47.61           C  
ATOM   1420  N   ALA A 199     -92.403  21.280 -44.312  1.00 16.15           N  
ATOM   1421  CA  ALA A 199     -92.992  20.041 -44.806  1.00 17.84           C  
ATOM   1422  C   ALA A 199     -94.254  20.306 -45.615  1.00  7.35           C  
ATOM   1423  O   ALA A 199     -94.583  19.531 -46.520  1.00  7.33           O  
ATOM   1424  CB  ALA A 199     -93.295  19.096 -43.643  1.00 23.59           C  
ATOM   1425  N   LYS A 200     -94.975  21.384 -45.297  1.00  6.95           N  
ATOM   1426  CA  LYS A 200     -96.172  21.733 -46.056  1.00 12.06           C  
ATOM   1427  C   LYS A 200     -95.832  22.019 -47.513  1.00 20.54           C  
ATOM   1428  O   LYS A 200     -96.467  21.483 -48.429  1.00 17.08           O  
ATOM   1429  CB  LYS A 200     -96.869  22.935 -45.415  1.00  5.86           C  
ATOM   1430  N   ARG A 201     -94.821  22.860 -47.747  1.00 16.41           N  
ATOM   1431  CA  ARG A 201     -94.414  23.170 -49.111  1.00  7.47           C  
ATOM   1432  C   ARG A 201     -93.731  21.992 -49.793  1.00 13.53           C  
ATOM   1433  O   ARG A 201     -93.717  21.930 -51.027  1.00 11.75           O  
ATOM   1434  CB  ARG A 201     -93.485  24.387 -49.115  1.00  2.87           C  
ATOM   1435  CG  ARG A 201     -94.159  25.681 -48.677  1.00 11.66           C  
ATOM   1436  CD  ARG A 201     -93.160  26.819 -48.487  1.00 13.59           C  
ATOM   1437  NE  ARG A 201     -92.261  26.976 -49.627  1.00 13.06           N  
ATOM   1438  CZ  ARG A 201     -90.952  26.749 -49.584  1.00 18.62           C  
ATOM   1439  NH1 ARG A 201     -90.382  26.362 -48.451  1.00 41.46           N  
ATOM   1440  NH2 ARG A 201     -90.210  26.916 -50.670  1.00  4.80           N  
ATOM   1441  N   LEU A 202     -93.174  21.057 -49.022  1.00 28.73           N  
ATOM   1442  CA  LEU A 202     -92.541  19.883 -49.615  1.00 30.22           C  
ATOM   1443  C   LEU A 202     -93.584  18.936 -50.196  1.00 34.21           C  
ATOM   1444  O   LEU A 202     -93.555  18.609 -51.388  1.00 48.07           O  
ATOM   1445  CB  LEU A 202     -91.678  19.167 -48.576  1.00  6.07           C  
ATOM   1446  CG  LEU A 202     -91.010  17.882 -49.066  1.00  6.10           C  
ATOM   1447  CD1 LEU A 202     -90.011  18.187 -50.173  1.00  5.39           C  
ATOM   1448  CD2 LEU A 202     -90.338  17.148 -47.917  1.00  9.47           C  
ATOM   1449  N   LEU A 203     -94.520  18.481 -49.359  1.00 26.92           N  
ATOM   1450  CA  LEU A 203     -95.552  17.553 -49.806  1.00 29.44           C  
ATOM   1451  C   LEU A 203     -96.491  18.167 -50.839  1.00 34.42           C  
ATOM   1452  O   LEU A 203     -97.224  17.429 -51.507  1.00 27.42           O  
ATOM   1453  CB  LEU A 203     -96.356  17.061 -48.602  1.00 13.78           C  
ATOM   1454  CG  LEU A 203     -95.625  16.129 -47.633  1.00  8.55           C  
ATOM   1455  CD1 LEU A 203     -96.410  15.980 -46.340  1.00 20.88           C  
ATOM   1456  CD2 LEU A 203     -95.386  14.773 -48.273  1.00 17.56           C  
ATOM   1457  N   ALA A 204     -96.490  19.493 -50.984  1.00 22.12           N  
ATOM   1458  CA  ALA A 204     -97.329  20.158 -51.973  1.00 15.52           C  
ATOM   1459  C   ALA A 204     -96.645  20.344 -53.320  1.00 16.35           C  
ATOM   1460  O   ALA A 204     -97.338  20.537 -54.327  1.00 22.39           O  
ATOM   1461  CB  ALA A 204     -97.786  21.523 -51.448  1.00 19.41           C  
ATOM   1462  N   HIS A 205     -95.318  20.304 -53.365  1.00 13.13           N  
ATOM   1463  CA  HIS A 205     -94.605  20.489 -54.626  1.00 20.74           C  
ATOM   1464  C   HIS A 205     -94.909  19.325 -55.565  1.00 25.46           C  
ATOM   1465  O   HIS A 205     -94.849  18.164 -55.144  1.00 41.75           O  
ATOM   1466  CB  HIS A 205     -93.102  20.600 -54.373  1.00 20.12           C  
ATOM   1467  CG  HIS A 205     -92.345  21.259 -55.485  1.00 22.92           C  
ATOM   1468  ND1 HIS A 205     -92.120  20.648 -56.700  1.00 26.86           N  
ATOM   1469  CD2 HIS A 205     -91.755  22.476 -55.561  1.00 21.92           C  
ATOM   1470  CE1 HIS A 205     -91.430  21.462 -57.479  1.00 25.64           C  
ATOM   1471  NE2 HIS A 205     -91.193  22.577 -56.811  1.00 22.31           N  
ATOM   1472  N   PRO A 206     -95.241  19.589 -56.833  1.00 11.40           N  
ATOM   1473  CA  PRO A 206     -95.717  18.492 -57.695  1.00 21.32           C  
ATOM   1474  C   PRO A 206     -94.631  17.514 -58.110  1.00 28.71           C  
ATOM   1475  O   PRO A 206     -94.880  16.302 -58.132  1.00 53.72           O  
ATOM   1476  CB  PRO A 206     -96.305  19.236 -58.902  1.00  5.17           C  
ATOM   1477  CG  PRO A 206     -95.549  20.524 -58.947  1.00  3.82           C  
ATOM   1478  CD  PRO A 206     -95.291  20.895 -57.513  1.00  3.87           C  
ATOM   1479  N   LYS A 207     -93.433  17.994 -58.438  1.00  6.01           N  
ATOM   1480  CA  LYS A 207     -92.398  17.129 -58.992  1.00  6.41           C  
ATOM   1481  C   LYS A 207     -91.587  16.401 -57.927  1.00  6.55           C  
ATOM   1482  O   LYS A 207     -90.580  15.770 -58.266  1.00  6.56           O  
ATOM   1483  CB  LYS A 207     -91.464  17.927 -59.906  1.00  5.47           C  
ATOM   1484  CG  LYS A 207     -92.098  18.320 -61.229  1.00 10.95           C  
ATOM   1485  CD  LYS A 207     -91.064  18.857 -62.201  1.00  8.79           C  
ATOM   1486  CE  LYS A 207     -90.458  20.151 -61.702  1.00 38.34           C  
ATOM   1487  NZ  LYS A 207     -89.365  20.621 -62.598  1.00 60.79           N  
ATOM   1488  N   VAL A 208     -91.988  16.467 -56.662  1.00 18.61           N  
ATOM   1489  CA  VAL A 208     -91.303  15.742 -55.601  1.00 20.03           C  
ATOM   1490  C   VAL A 208     -92.286  14.776 -54.955  1.00 18.74           C  
ATOM   1491  O   VAL A 208     -93.490  15.040 -54.868  1.00 28.65           O  
ATOM   1492  CB  VAL A 208     -90.677  16.677 -54.541  1.00 14.68           C  
ATOM   1493  CG1 VAL A 208     -89.768  17.702 -55.205  1.00 14.31           C  
ATOM   1494  CG2 VAL A 208     -91.750  17.356 -53.715  1.00 27.72           C  
ATOM   1495  N   THR A 209     -91.760  13.632 -54.524  1.00 10.34           N  
ATOM   1496  CA  THR A 209     -92.545  12.617 -53.837  1.00 32.66           C  
ATOM   1497  C   THR A 209     -91.737  12.102 -52.658  1.00 23.63           C  
ATOM   1498  O   THR A 209     -90.567  11.741 -52.814  1.00  6.08           O  
ATOM   1499  CB  THR A 209     -92.918  11.457 -54.773  1.00 21.50           C  
ATOM   1500  OG1 THR A 209     -91.735  10.935 -55.390  1.00 34.32           O  
ATOM   1501  CG2 THR A 209     -93.889  11.924 -55.853  1.00 10.56           C  
ATOM   1502  N   VAL A 210     -92.355  12.084 -51.483  1.00 17.79           N  
ATOM   1503  CA  VAL A 210     -91.688  11.645 -50.264  1.00  6.43           C  
ATOM   1504  C   VAL A 210     -91.970  10.163 -50.064  1.00  7.68           C  
ATOM   1505  O   VAL A 210     -93.131   9.742 -50.019  1.00 21.43           O  
ATOM   1506  CB  VAL A 210     -92.154  12.464 -49.051  1.00  6.86           C  
ATOM   1507  CG1 VAL A 210     -91.389  12.049 -47.804  1.00  6.95           C  
ATOM   1508  CG2 VAL A 210     -91.992  13.953 -49.317  1.00  6.77           C  
ATOM   1509  N   ARG A 211     -90.909   9.369 -49.949  1.00  6.76           N  
ATOM   1510  CA  ARG A 211     -91.018   7.931 -49.718  1.00  5.92           C  
ATOM   1511  C   ARG A 211     -90.535   7.649 -48.300  1.00 10.06           C  
ATOM   1512  O   ARG A 211     -89.331   7.516 -48.058  1.00  5.64           O  
ATOM   1513  CB  ARG A 211     -90.217   7.144 -50.751  1.00  4.95           C  
ATOM   1514  CG  ARG A 211     -90.770   7.248 -52.161  1.00 33.86           C  
ATOM   1515  CD  ARG A 211     -90.207   6.161 -53.061  1.00 39.57           C  
ATOM   1516  NE  ARG A 211     -90.367   4.835 -52.473  1.00 43.47           N  
ATOM   1517  CZ  ARG A 211     -90.097   3.700 -53.109  1.00 40.34           C  
ATOM   1518  NH1 ARG A 211     -89.659   3.729 -54.360  1.00 35.28           N  
ATOM   1519  NH2 ARG A 211     -90.271   2.536 -52.497  1.00 39.90           N  
ATOM   1520  N   PHE A 212     -91.477   7.559 -47.365  1.00 11.73           N  
ATOM   1521  CA  PHE A 212     -91.128   7.264 -45.987  1.00  6.76           C  
ATOM   1522  C   PHE A 212     -90.677   5.813 -45.852  1.00  6.61           C  
ATOM   1523  O   PHE A 212     -91.039   4.943 -46.651  1.00 33.54           O  
ATOM   1524  CB  PHE A 212     -92.309   7.542 -45.055  1.00  7.44           C  
ATOM   1525  CG  PHE A 212     -92.778   8.970 -45.076  1.00  7.92           C  
ATOM   1526  CD1 PHE A 212     -92.137   9.934 -44.314  1.00  8.76           C  
ATOM   1527  CD2 PHE A 212     -93.863   9.348 -45.850  1.00 13.48           C  
ATOM   1528  CE1 PHE A 212     -92.566  11.249 -44.326  1.00 13.67           C  
ATOM   1529  CE2 PHE A 212     -94.297  10.663 -45.867  1.00 28.75           C  
ATOM   1530  CZ  PHE A 212     -93.648  11.614 -45.103  1.00 25.66           C  
ATOM   1531  N   ASN A 213     -89.866   5.564 -44.822  1.00  7.20           N  
ATOM   1532  CA  ASN A 213     -89.351   4.230 -44.518  1.00  7.08           C  
ATOM   1533  C   ASN A 213     -88.590   3.649 -45.709  1.00  6.15           C  
ATOM   1534  O   ASN A 213     -88.873   2.546 -46.183  1.00 16.45           O  
ATOM   1535  CB  ASN A 213     -90.484   3.297 -44.081  1.00  6.72           C  
ATOM   1536  CG  ASN A 213     -91.015   3.633 -42.704  1.00  8.27           C  
ATOM   1537  OD1 ASN A 213     -90.248   3.926 -41.786  1.00 24.82           O  
ATOM   1538  ND2 ASN A 213     -92.335   3.602 -42.554  1.00  7.45           N  
ATOM   1539  N   THR A 214     -87.604   4.403 -46.188  1.00  6.32           N  
ATOM   1540  CA  THR A 214     -86.816   3.993 -47.342  1.00  5.65           C  
ATOM   1541  C   THR A 214     -85.384   4.465 -47.149  1.00  6.50           C  
ATOM   1542  O   THR A 214     -85.153   5.613 -46.755  1.00  8.18           O  
ATOM   1543  CB  THR A 214     -87.395   4.557 -48.646  1.00 10.95           C  
ATOM   1544  OG1 THR A 214     -88.775   4.191 -48.756  1.00 18.13           O  
ATOM   1545  CG2 THR A 214     -86.639   4.006 -49.845  1.00  7.01           C  
ATOM   1546  N   VAL A 215     -84.431   3.578 -47.424  1.00 13.49           N  
ATOM   1547  CA  VAL A 215     -83.011   3.850 -47.248  1.00 19.11           C  
ATOM   1548  C   VAL A 215     -82.278   3.411 -48.507  1.00 18.98           C  
ATOM   1549  O   VAL A 215     -82.563   2.344 -49.061  1.00 40.94           O  
ATOM   1550  CB  VAL A 215     -82.444   3.123 -46.008  1.00 11.53           C  
ATOM   1551  CG1 VAL A 215     -80.950   3.375 -45.869  1.00 61.24           C  
ATOM   1552  CG2 VAL A 215     -83.183   3.552 -44.746  1.00  9.90           C  
ATOM   1553  N   ALA A 216     -81.336   4.235 -48.962  1.00  7.90           N  
ATOM   1554  CA  ALA A 216     -80.506   3.868 -50.101  1.00  7.82           C  
ATOM   1555  C   ALA A 216     -79.411   2.910 -49.647  1.00  9.57           C  
ATOM   1556  O   ALA A 216     -78.711   3.174 -48.664  1.00 11.30           O  
ATOM   1557  CB  ALA A 216     -79.896   5.113 -50.743  1.00  9.73           C  
ATOM   1558  N   THR A 217     -79.261   1.802 -50.369  1.00 14.93           N  
ATOM   1559  CA  THR A 217     -78.340   0.732 -49.998  1.00 11.28           C  
ATOM   1560  C   THR A 217     -77.112   0.636 -50.888  1.00 10.96           C  
ATOM   1561  O   THR A 217     -76.033   0.306 -50.395  1.00 12.62           O  
ATOM   1562  CB  THR A 217     -79.060  -0.622 -49.998  1.00 15.71           C  
ATOM   1563  OG1 THR A 217     -79.830  -0.762 -51.198  1.00 48.41           O  
ATOM   1564  CG2 THR A 217     -79.973  -0.739 -48.791  1.00  8.35           C  
ATOM   1565  N   GLU A 218     -77.240   0.899 -52.187  1.00 10.19           N  
ATOM   1566  CA  GLU A 218     -76.099   0.771 -53.082  1.00 11.34           C  
ATOM   1567  C   GLU A 218     -76.303   1.670 -54.293  1.00 10.57           C  
ATOM   1568  O   GLU A 218     -77.434   1.901 -54.730  1.00  8.98           O  
ATOM   1569  CB  GLU A 218     -75.916  -0.695 -53.504  1.00 15.99           C  
ATOM   1570  CG  GLU A 218     -74.848  -0.962 -54.553  1.00 31.48           C  
ATOM   1571  CD  GLU A 218     -74.699  -2.444 -54.856  1.00 49.94           C  
ATOM   1572  OE1 GLU A 218     -73.862  -3.107 -54.208  1.00 48.13           O  
ATOM   1573  OE2 GLU A 218     -75.433  -2.951 -55.730  1.00 60.09           O  
ATOM   1574  N   VAL A 219     -75.192   2.174 -54.825  1.00 14.99           N  
ATOM   1575  CA  VAL A 219     -75.184   3.073 -55.973  1.00 11.53           C  
ATOM   1576  C   VAL A 219     -74.677   2.294 -57.179  1.00 12.01           C  
ATOM   1577  O   VAL A 219     -73.585   1.713 -57.139  1.00 13.80           O  
ATOM   1578  CB  VAL A 219     -74.318   4.315 -55.710  1.00 12.29           C  
ATOM   1579  CG1 VAL A 219     -74.168   5.140 -56.974  1.00 11.87           C  
ATOM   1580  CG2 VAL A 219     -74.921   5.152 -54.591  1.00 11.60           C  
ATOM   1581  N   LEU A 220     -75.466   2.283 -58.249  1.00 10.87           N  
ATOM   1582  CA  LEU A 220     -75.132   1.566 -59.469  1.00 14.27           C  
ATOM   1583  C   LEU A 220     -74.968   2.542 -60.625  1.00 11.60           C  
ATOM   1584  O   LEU A 220     -75.561   3.625 -60.634  1.00 10.73           O  
ATOM   1585  CB  LEU A 220     -76.208   0.531 -59.806  1.00 16.13           C  
ATOM   1586  CG  LEU A 220     -76.408  -0.528 -58.723  1.00 10.08           C  
ATOM   1587  CD1 LEU A 220     -77.468  -1.533 -59.140  1.00 30.88           C  
ATOM   1588  CD2 LEU A 220     -75.088  -1.218 -58.414  1.00 11.80           C  
ATOM   1589  N   GLY A 221     -74.157   2.153 -61.599  1.00 12.75           N  
ATOM   1590  CA  GLY A 221     -73.949   2.999 -62.756  1.00 13.04           C  
ATOM   1591  C   GLY A 221     -73.073   2.328 -63.787  1.00 27.77           C  
ATOM   1592  O   GLY A 221     -72.861   1.114 -63.752  1.00 34.74           O  
ATOM   1593  N   GLU A 222     -72.569   3.142 -64.711  1.00 28.58           N  
ATOM   1594  CA  GLU A 222     -71.665   2.666 -65.745  1.00 22.65           C  
ATOM   1595  C   GLU A 222     -70.350   2.192 -65.133  1.00 28.40           C  
ATOM   1596  O   GLU A 222     -69.949   2.610 -64.044  1.00 26.11           O  
ATOM   1597  CB  GLU A 222     -71.388   3.767 -66.771  1.00 16.31           C  
ATOM   1598  CG  GLU A 222     -72.625   4.504 -67.259  1.00 26.94           C  
ATOM   1599  CD  GLU A 222     -72.284   5.724 -68.099  1.00 33.39           C  
ATOM   1600  OE1 GLU A 222     -71.381   6.490 -67.699  1.00 34.76           O  
ATOM   1601  OE2 GLU A 222     -72.916   5.917 -69.159  1.00 23.19           O  
ATOM   1602  N   LYS A 223     -69.674   1.303 -65.856  1.00 30.51           N  
ATOM   1603  CA  LYS A 223     -68.336   0.839 -65.500  1.00 21.33           C  
ATOM   1604  C   LYS A 223     -67.400   1.240 -66.637  1.00 20.48           C  
ATOM   1605  O   LYS A 223     -67.123   0.461 -67.550  1.00 22.63           O  
ATOM   1606  CB  LYS A 223     -68.314  -0.674 -65.239  1.00 26.86           C  
ATOM   1607  CG  LYS A 223     -67.025  -1.171 -64.595  1.00 28.52           C  
ATOM   1608  CD  LYS A 223     -67.080  -2.665 -64.317  1.00 23.90           C  
ATOM   1609  CE  LYS A 223     -68.208  -3.014 -63.357  1.00 27.88           C  
ATOM   1610  NZ  LYS A 223     -68.277  -4.480 -63.096  1.00 26.48           N  
ATOM   1611  N   LYS A 224     -66.921   2.475 -66.567  1.00 20.74           N  
ATOM   1612  CA  LYS A 224     -65.951   3.076 -67.472  1.00 26.87           C  
ATOM   1613  C   LYS A 224     -65.081   3.969 -66.590  1.00 37.67           C  
ATOM   1614  O   LYS A 224     -65.342   4.045 -65.383  1.00 32.56           O  
ATOM   1615  CB  LYS A 224     -66.652   3.838 -68.601  1.00 20.37           C  
ATOM   1616  CG  LYS A 224     -67.404   5.070 -68.157  1.00 19.03           C  
ATOM   1617  CD  LYS A 224     -68.012   5.796 -69.340  1.00 18.27           C  
ATOM   1618  CE  LYS A 224     -68.957   4.894 -70.116  1.00 18.59           C  
ATOM   1619  NZ  LYS A 224     -69.535   5.598 -71.293  1.00 18.35           N  
ATOM   1620  N   PRO A 225     -64.022   4.632 -67.110  1.00 44.73           N  
ATOM   1621  CA  PRO A 225     -63.228   5.521 -66.241  1.00 42.09           C  
ATOM   1622  C   PRO A 225     -64.034   6.599 -65.525  1.00 35.04           C  
ATOM   1623  O   PRO A 225     -64.032   6.659 -64.291  1.00 36.93           O  
ATOM   1624  CB  PRO A 225     -62.215   6.151 -67.211  1.00 37.83           C  
ATOM   1625  CG  PRO A 225     -62.671   5.768 -68.595  1.00 26.06           C  
ATOM   1626  CD  PRO A 225     -63.395   4.480 -68.433  1.00 32.94           C  
ATOM   1627  N   ASN A 226     -64.692   7.475 -66.276  1.00 21.83           N  
ATOM   1628  CA  ASN A 226     -65.546   8.521 -65.703  1.00 20.91           C  
ATOM   1629  C   ASN A 226     -67.019   8.167 -65.868  1.00 29.00           C  
ATOM   1630  O   ASN A 226     -67.787   8.837 -66.562  1.00 31.41           O  
ATOM   1631  CB  ASN A 226     -65.231   9.883 -66.310  1.00 31.17           C  
ATOM   1632  CG  ASN A 226     -64.608  10.828 -65.309  1.00 41.02           C  
ATOM   1633  OD1 ASN A 226     -64.913  10.765 -64.115  1.00 56.78           O  
ATOM   1634  ND2 ASN A 226     -63.765  11.731 -65.785  1.00 20.93           N  
ATOM   1635  N   GLY A 227     -67.401   7.083 -65.200  1.00 31.21           N  
ATOM   1636  CA  GLY A 227     -68.752   6.577 -65.318  1.00 25.33           C  
ATOM   1637  C   GLY A 227     -69.722   7.333 -64.427  1.00 27.87           C  
ATOM   1638  O   GLY A 227     -69.453   7.603 -63.256  1.00 28.59           O  
ATOM   1639  N   LEU A 228     -70.867   7.670 -65.006  1.00 38.74           N  
ATOM   1640  CA  LEU A 228     -71.914   8.367 -64.286  1.00 36.23           C  
ATOM   1641  C   LEU A 228     -72.791   7.366 -63.542  1.00 34.97           C  
ATOM   1642  O   LEU A 228     -72.719   6.152 -63.752  1.00 32.40           O  
ATOM   1643  CB  LEU A 228     -72.756   9.209 -65.242  1.00 16.19           C  
ATOM   1644  CG  LEU A 228     -72.202  10.540 -65.759  1.00 12.15           C  
ATOM   1645  CD1 LEU A 228     -71.008  10.372 -66.697  1.00 13.04           C  
ATOM   1646  CD2 LEU A 228     -73.318  11.317 -66.437  1.00 22.70           C  
ATOM   1647  N   MET A 229     -73.637   7.893 -62.667  1.00 26.96           N  
ATOM   1648  CA  MET A 229     -74.554   7.069 -61.896  1.00 11.06           C  
ATOM   1649  C   MET A 229     -75.818   6.819 -62.707  1.00 10.46           C  
ATOM   1650  O   MET A 229     -76.384   7.750 -63.288  1.00 23.76           O  
ATOM   1651  CB  MET A 229     -74.892   7.740 -60.566  1.00 10.13           C  
ATOM   1652  CG  MET A 229     -75.796   6.910 -59.683  1.00  9.39           C  
ATOM   1653  SD  MET A 229     -76.265   7.762 -58.169  1.00 18.40           S  
ATOM   1654  CE  MET A 229     -77.874   8.385 -58.618  1.00  7.15           C  
ATOM   1655  N   THR A 230     -76.253   5.560 -62.747  1.00 12.26           N  
ATOM   1656  CA  THR A 230     -77.412   5.159 -63.533  1.00 10.43           C  
ATOM   1657  C   THR A 230     -78.549   4.578 -62.707  1.00  9.42           C  
ATOM   1658  O   THR A 230     -79.712   4.773 -63.069  1.00  9.34           O  
ATOM   1659  CB  THR A 230     -77.007   4.121 -64.595  1.00 11.50           C  
ATOM   1660  OG1 THR A 230     -75.775   4.517 -65.209  1.00 45.20           O  
ATOM   1661  CG2 THR A 230     -78.077   4.004 -65.669  1.00 12.08           C  
ATOM   1662  N   HIS A 231     -78.256   3.881 -61.612  1.00  8.92           N  
ATOM   1663  CA  HIS A 231     -79.294   3.232 -60.826  1.00  9.27           C  
ATOM   1664  C   HIS A 231     -78.973   3.344 -59.344  1.00 11.70           C  
ATOM   1665  O   HIS A 231     -77.810   3.441 -58.946  1.00 28.25           O  
ATOM   1666  CB  HIS A 231     -79.454   1.760 -61.226  1.00  8.04           C  
ATOM   1667  CG  HIS A 231     -79.965   1.569 -62.619  1.00  8.57           C  
ATOM   1668  ND1 HIS A 231     -79.132   1.344 -63.694  1.00  9.64           N  
ATOM   1669  CD2 HIS A 231     -81.225   1.574 -63.115  1.00  8.89           C  
ATOM   1670  CE1 HIS A 231     -79.857   1.217 -64.791  1.00 11.09           C  
ATOM   1671  NE2 HIS A 231     -81.131   1.352 -64.467  1.00 10.90           N  
ATOM   1672  N   LEU A 232     -80.026   3.325 -58.530  1.00  6.60           N  
ATOM   1673  CA  LEU A 232     -79.907   3.359 -57.080  1.00  6.35           C  
ATOM   1674  C   LEU A 232     -80.737   2.224 -56.503  1.00  5.81           C  
ATOM   1675  O   LEU A 232     -81.898   2.046 -56.883  1.00 13.96           O  
ATOM   1676  CB  LEU A 232     -80.379   4.704 -56.515  1.00 11.37           C  
ATOM   1677  CG  LEU A 232     -80.301   4.875 -54.997  1.00  5.92           C  
ATOM   1678  CD1 LEU A 232     -78.852   4.927 -54.541  1.00  7.14           C  
ATOM   1679  CD2 LEU A 232     -81.056   6.117 -54.547  1.00  5.39           C  
ATOM   1680  N   ARG A 233     -80.140   1.455 -55.596  1.00 15.88           N  
ATOM   1681  CA  ARG A 233     -80.823   0.354 -54.926  1.00  5.77           C  
ATOM   1682  C   ARG A 233     -81.341   0.852 -53.580  1.00 11.24           C  
ATOM   1683  O   ARG A 233     -80.553   1.179 -52.686  1.00 25.43           O  
ATOM   1684  CB  ARG A 233     -79.893  -0.846 -54.757  1.00  6.55           C  
ATOM   1685  CG  ARG A 233     -80.522  -2.021 -54.023  1.00 11.01           C  
ATOM   1686  CD  ARG A 233     -79.540  -3.170 -53.881  1.00  6.86           C  
ATOM   1687  NE  ARG A 233     -79.312  -3.844 -55.155  1.00 17.81           N  
ATOM   1688  CZ  ARG A 233     -78.373  -4.761 -55.357  1.00 33.09           C  
ATOM   1689  NH1 ARG A 233     -77.565  -5.114 -54.367  1.00 47.98           N  
ATOM   1690  NH2 ARG A 233     -78.239  -5.323 -56.550  1.00 43.35           N  
ATOM   1691  N   ILE A 234     -82.662   0.923 -53.444  1.00  5.13           N  
ATOM   1692  CA  ILE A 234     -83.304   1.379 -52.220  1.00 15.64           C  
ATOM   1693  C   ILE A 234     -83.955   0.191 -51.522  1.00 15.75           C  
ATOM   1694  O   ILE A 234     -84.282  -0.828 -52.138  1.00 18.15           O  
ATOM   1695  CB  ILE A 234     -84.337   2.489 -52.495  1.00 14.14           C  
ATOM   1696  CG1 ILE A 234     -85.450   1.967 -53.405  1.00 13.48           C  
ATOM   1697  CG2 ILE A 234     -83.660   3.697 -53.121  1.00 28.16           C  
ATOM   1698  CD1 ILE A 234     -86.446   3.024 -53.817  1.00  7.95           C  
ATOM   1699  N   LYS A 235     -84.156   0.335 -50.212  1.00  6.98           N  
ATOM   1700  CA  LYS A 235     -84.656  -0.753 -49.377  1.00  4.49           C  
ATOM   1701  C   LYS A 235     -85.697  -0.214 -48.411  1.00  4.49           C  
ATOM   1702  O   LYS A 235     -85.402   0.683 -47.616  1.00  5.26           O  
ATOM   1703  CB  LYS A 235     -83.519  -1.424 -48.602  1.00  5.34           C  
ATOM   1704  CG  LYS A 235     -83.996  -2.376 -47.514  1.00 21.74           C  
ATOM   1705  CD  LYS A 235     -82.829  -2.976 -46.744  1.00 15.88           C  
ATOM   1706  CE  LYS A 235     -82.070  -1.907 -45.975  1.00  9.12           C  
ATOM   1707  NZ  LYS A 235     -80.900  -2.463 -45.244  1.00 10.33           N  
ATOM   1708  N   ASN A 236     -86.908  -0.764 -48.477  1.00  3.81           N  
ATOM   1709  CA  ASN A 236     -87.923  -0.455 -47.479  1.00  3.97           C  
ATOM   1710  C   ASN A 236     -87.459  -0.931 -46.109  1.00  4.68           C  
ATOM   1711  O   ASN A 236     -86.994  -2.064 -45.957  1.00 43.39           O  
ATOM   1712  CB  ASN A 236     -89.250  -1.116 -47.855  1.00  3.20           C  
ATOM   1713  CG  ASN A 236     -90.328  -0.901 -46.810  1.00  8.50           C  
ATOM   1714  OD1 ASN A 236     -90.426  -1.649 -45.838  1.00 31.06           O  
ATOM   1715  ND2 ASN A 236     -91.147   0.125 -47.009  1.00 21.46           N  
ATOM   1716  N   THR A 237     -87.589  -0.064 -45.108  1.00  5.57           N  
ATOM   1717  CA  THR A 237     -87.016  -0.317 -43.793  1.00  6.64           C  
ATOM   1718  C   THR A 237     -87.952  -1.094 -42.874  1.00  6.49           C  
ATOM   1719  O   THR A 237     -87.547  -1.455 -41.764  1.00  7.31           O  
ATOM   1720  CB  THR A 237     -86.611   1.003 -43.124  1.00  8.03           C  
ATOM   1721  OG1 THR A 237     -85.665   0.741 -42.081  1.00 39.21           O  
ATOM   1722  CG2 THR A 237     -87.818   1.680 -42.513  1.00  8.36           C  
ATOM   1723  N   VAL A 238     -89.179  -1.367 -43.303  1.00  5.46           N  
ATOM   1724  CA  VAL A 238     -90.131  -2.139 -42.511  1.00  4.97           C  
ATOM   1725  C   VAL A 238     -90.212  -3.582 -42.989  1.00  3.71           C  
ATOM   1726  O   VAL A 238     -90.165  -4.513 -42.186  1.00  3.20           O  
ATOM   1727  CB  VAL A 238     -91.521  -1.464 -42.542  1.00  4.71           C  
ATOM   1728  CG1 VAL A 238     -92.456  -2.125 -41.543  1.00  4.12           C  
ATOM   1729  CG2 VAL A 238     -91.396   0.026 -42.268  1.00  5.91           C  
ATOM   1730  N   THR A 239     -90.335  -3.785 -44.302  1.00  3.03           N  
ATOM   1731  CA  THR A 239     -90.368  -5.137 -44.849  1.00  2.00           C  
ATOM   1732  C   THR A 239     -88.964  -5.698 -45.046  1.00  9.69           C  
ATOM   1733  O   THR A 239     -88.729  -6.889 -44.809  1.00 26.12           O  
ATOM   1734  CB  THR A 239     -91.128  -5.153 -46.176  1.00  1.95           C  
ATOM   1735  OG1 THR A 239     -90.375  -4.449 -47.171  1.00  1.95           O  
ATOM   1736  CG2 THR A 239     -92.488  -4.492 -46.018  1.00 11.04           C  
ATOM   1737  N   GLY A 240     -88.028  -4.863 -45.488  1.00  3.10           N  
ATOM   1738  CA  GLY A 240     -86.680  -5.296 -45.782  1.00  3.46           C  
ATOM   1739  C   GLY A 240     -86.441  -5.614 -47.240  1.00  2.96           C  
ATOM   1740  O   GLY A 240     -85.326  -6.012 -47.596  1.00 14.39           O  
ATOM   1741  N   GLU A 241     -87.452  -5.448 -48.088  1.00  2.29           N  
ATOM   1742  CA  GLU A 241     -87.346  -5.764 -49.506  1.00  1.95           C  
ATOM   1743  C   GLU A 241     -86.583  -4.656 -50.222  1.00  2.38           C  
ATOM   1744  O   GLU A 241     -86.982  -3.488 -50.175  1.00 21.38           O  
ATOM   1745  CB  GLU A 241     -88.737  -5.948 -50.108  1.00  1.95           C  
ATOM   1746  CG  GLU A 241     -89.620  -6.917 -49.327  1.00 28.21           C  
ATOM   1747  CD  GLU A 241     -90.948  -7.188 -50.010  1.00 46.14           C  
ATOM   1748  OE1 GLU A 241     -91.238  -6.531 -51.033  1.00 48.35           O  
ATOM   1749  OE2 GLU A 241     -91.702  -8.060 -49.523  1.00 36.47           O  
ATOM   1750  N   GLU A 242     -85.481  -5.020 -50.872  1.00  2.69           N  
ATOM   1751  CA  GLU A 242     -84.674  -4.071 -51.624  1.00  3.20           C  
ATOM   1752  C   GLU A 242     -85.126  -4.028 -53.078  1.00  2.76           C  
ATOM   1753  O   GLU A 242     -85.638  -5.010 -53.622  1.00 16.02           O  
ATOM   1754  CB  GLU A 242     -83.190  -4.435 -51.545  1.00  4.05           C  
ATOM   1755  CG  GLU A 242     -82.669  -4.591 -50.124  1.00 36.42           C  
ATOM   1756  CD  GLU A 242     -81.154  -4.586 -50.047  1.00 58.40           C  
ATOM   1757  OE1 GLU A 242     -80.510  -4.034 -50.963  1.00 59.03           O  
ATOM   1758  OE2 GLU A 242     -80.608  -5.139 -49.069  1.00 67.16           O  
ATOM   1759  N   GLU A 243     -84.925  -2.872 -53.706  1.00 12.20           N  
ATOM   1760  CA  GLU A 243     -85.394  -2.633 -55.061  1.00  2.83           C  
ATOM   1761  C   GLU A 243     -84.388  -1.741 -55.776  1.00 12.59           C  
ATOM   1762  O   GLU A 243     -83.665  -0.971 -55.140  1.00 23.31           O  
ATOM   1763  CB  GLU A 243     -86.786  -1.984 -55.029  1.00  2.48           C  
ATOM   1764  CG  GLU A 243     -87.390  -1.635 -56.374  1.00 35.31           C  
ATOM   1765  CD  GLU A 243     -88.567  -0.685 -56.245  1.00 39.00           C  
ATOM   1766  OE1 GLU A 243     -88.836  -0.222 -55.114  1.00 19.14           O  
ATOM   1767  OE2 GLU A 243     -89.219  -0.400 -57.271  1.00 39.42           O  
ATOM   1768  N   ILE A 244     -84.351  -1.846 -57.102  1.00  3.64           N  
ATOM   1769  CA  ILE A 244     -83.451  -1.056 -57.935  1.00  4.37           C  
ATOM   1770  C   ILE A 244     -84.291  -0.115 -58.789  1.00 22.66           C  
ATOM   1771  O   ILE A 244     -85.164  -0.562 -59.545  1.00 13.90           O  
ATOM   1772  CB  ILE A 244     -82.553  -1.947 -58.807  1.00  4.85           C  
ATOM   1773  CG1 ILE A 244     -81.725  -2.885 -57.928  1.00  5.02           C  
ATOM   1774  CG2 ILE A 244     -81.648  -1.096 -59.683  1.00  6.61           C  
ATOM   1775  CD1 ILE A 244     -80.683  -3.670 -58.688  1.00  5.72           C  
ATOM   1776  N   VAL A 245     -84.028   1.185 -58.671  1.00 21.74           N  
ATOM   1777  CA  VAL A 245     -84.770   2.203 -59.400  1.00 12.49           C  
ATOM   1778  C   VAL A 245     -83.798   3.038 -60.223  1.00  6.23           C  
ATOM   1779  O   VAL A 245     -82.606   3.133 -59.921  1.00  6.23           O  
ATOM   1780  CB  VAL A 245     -85.596   3.106 -58.460  1.00  7.40           C  
ATOM   1781  CG1 VAL A 245     -86.755   2.328 -57.857  1.00 25.75           C  
ATOM   1782  CG2 VAL A 245     -84.711   3.690 -57.368  1.00  4.72           C  
ATOM   1783  N   ASP A 246     -84.328   3.640 -61.287  1.00  7.22           N  
ATOM   1784  CA  ASP A 246     -83.531   4.530 -62.121  1.00  8.25           C  
ATOM   1785  C   ASP A 246     -83.192   5.797 -61.348  1.00 15.84           C  
ATOM   1786  O   ASP A 246     -84.065   6.406 -60.721  1.00 27.36           O  
ATOM   1787  CB  ASP A 246     -84.284   4.877 -63.404  1.00  9.91           C  
ATOM   1788  CG  ASP A 246     -84.697   3.650 -64.189  1.00 20.82           C  
ATOM   1789  OD1 ASP A 246     -83.884   2.709 -64.294  1.00 43.72           O  
ATOM   1790  OD2 ASP A 246     -85.836   3.626 -64.702  1.00 20.22           O  
ATOM   1791  N   ALA A 247     -81.923   6.197 -61.392  1.00  1.95           N  
ATOM   1792  CA  ALA A 247     -81.482   7.375 -60.650  1.00  1.95           C  
ATOM   1793  C   ALA A 247     -80.188   7.887 -61.258  1.00 15.97           C  
ATOM   1794  O   ALA A 247     -79.182   7.171 -61.264  1.00 38.46           O  
ATOM   1795  CB  ALA A 247     -81.289   7.045 -59.170  1.00  1.95           C  
ATOM   1796  N   ASN A 248     -80.215   9.117 -61.774  1.00 10.92           N  
ATOM   1797  CA  ASN A 248     -79.016   9.750 -62.304  1.00  1.95           C  
ATOM   1798  C   ASN A 248     -78.313  10.634 -61.284  1.00  6.07           C  
ATOM   1799  O   ASN A 248     -77.140  10.968 -61.480  1.00  7.08           O  
ATOM   1800  CB  ASN A 248     -79.354  10.592 -63.538  1.00  8.94           C  
ATOM   1801  CG  ASN A 248     -79.811   9.751 -64.709  1.00 19.41           C  
ATOM   1802  OD1 ASN A 248     -80.989   9.414 -64.824  1.00 15.03           O  
ATOM   1803  ND2 ASN A 248     -78.878   9.404 -65.586  1.00 38.15           N  
ATOM   1804  N   GLY A 249     -78.997  11.017 -60.209  1.00 10.57           N  
ATOM   1805  CA  GLY A 249     -78.405  11.880 -59.207  1.00  9.95           C  
ATOM   1806  C   GLY A 249     -78.818  11.542 -57.790  1.00  9.21           C  
ATOM   1807  O   GLY A 249     -80.007  11.368 -57.503  1.00  5.31           O  
ATOM   1808  N   LEU A 250     -77.839  11.449 -56.893  1.00  6.26           N  
ATOM   1809  CA  LEU A 250     -78.073  11.171 -55.481  1.00  1.95           C  
ATOM   1810  C   LEU A 250     -77.439  12.284 -54.661  1.00  1.95           C  
ATOM   1811  O   LEU A 250     -76.215  12.454 -54.682  1.00  8.24           O  
ATOM   1812  CB  LEU A 250     -77.496   9.811 -55.086  1.00  1.95           C  
ATOM   1813  CG  LEU A 250     -77.749   9.355 -53.648  1.00  1.95           C  
ATOM   1814  CD1 LEU A 250     -79.240   9.232 -53.383  1.00  1.95           C  
ATOM   1815  CD2 LEU A 250     -77.040   8.040 -53.368  1.00  1.95           C  
ATOM   1816  N   PHE A 251     -78.266  13.033 -53.937  1.00  1.95           N  
ATOM   1817  CA  PHE A 251     -77.822  14.189 -53.165  1.00  1.95           C  
ATOM   1818  C   PHE A 251     -78.009  13.898 -51.681  1.00  2.59           C  
ATOM   1819  O   PHE A 251     -79.141  13.740 -51.211  1.00  4.89           O  
ATOM   1820  CB  PHE A 251     -78.588  15.442 -53.581  1.00  4.50           C  
ATOM   1821  CG  PHE A 251     -78.154  15.999 -54.902  1.00  2.67           C  
ATOM   1822  CD1 PHE A 251     -78.710  15.532 -56.080  1.00  2.18           C  
ATOM   1823  CD2 PHE A 251     -77.185  16.985 -54.967  1.00 15.11           C  
ATOM   1824  CE1 PHE A 251     -78.311  16.041 -57.300  1.00  1.95           C  
ATOM   1825  CE2 PHE A 251     -76.783  17.498 -56.184  1.00 21.06           C  
ATOM   1826  CZ  PHE A 251     -77.347  17.024 -57.352  1.00  2.43           C  
ATOM   1827  N   TYR A 252     -76.900  13.824 -50.951  1.00  1.95           N  
ATOM   1828  CA  TYR A 252     -76.964  13.670 -49.504  1.00  1.95           C  
ATOM   1829  C   TYR A 252     -77.470  14.956 -48.863  1.00  3.54           C  
ATOM   1830  O   TYR A 252     -76.963  16.046 -49.147  1.00  8.08           O  
ATOM   1831  CB  TYR A 252     -75.589  13.309 -48.945  1.00  1.95           C  
ATOM   1832  CG  TYR A 252     -75.046  11.978 -49.418  1.00  1.95           C  
ATOM   1833  CD1 TYR A 252     -75.899  10.956 -49.814  1.00 17.61           C  
ATOM   1834  CD2 TYR A 252     -73.678  11.743 -49.466  1.00  1.95           C  
ATOM   1835  CE1 TYR A 252     -75.404   9.737 -50.244  1.00 18.54           C  
ATOM   1836  CE2 TYR A 252     -73.175  10.530 -49.894  1.00  1.95           C  
ATOM   1837  CZ  TYR A 252     -74.040   9.531 -50.282  1.00 11.90           C  
ATOM   1838  OH  TYR A 252     -73.541   8.323 -50.710  1.00 26.60           O  
ATOM   1839  N   ALA A 253     -78.474  14.828 -47.995  1.00  5.13           N  
ATOM   1840  CA  ALA A 253     -79.066  15.973 -47.315  1.00  7.65           C  
ATOM   1841  C   ALA A 253     -79.208  15.705 -45.822  1.00  6.61           C  
ATOM   1842  O   ALA A 253     -80.142  16.193 -45.179  1.00  8.06           O  
ATOM   1843  CB  ALA A 253     -80.414  16.341 -47.929  1.00 10.56           C  
ATOM   1844  N   VAL A 254     -78.294  14.916 -45.264  1.00  3.63           N  
ATOM   1845  CA  VAL A 254     -78.138  14.793 -43.820  1.00  2.06           C  
ATOM   1846  C   VAL A 254     -77.304  15.975 -43.347  1.00 39.22           C  
ATOM   1847  O   VAL A 254     -76.752  16.720 -44.165  1.00 53.97           O  
ATOM   1848  CB  VAL A 254     -77.496  13.450 -43.437  1.00  1.95           C  
ATOM   1849  CG1 VAL A 254     -78.436  12.310 -43.783  1.00  1.95           C  
ATOM   1850  CG2 VAL A 254     -76.178  13.274 -44.158  1.00  1.95           C  
ATOM   1851  N   GLY A 255     -77.208  16.162 -42.034  1.00 42.76           N  
ATOM   1852  CA  GLY A 255     -76.525  17.323 -41.496  1.00 54.95           C  
ATOM   1853  C   GLY A 255     -75.046  17.393 -41.821  1.00 25.74           C  
ATOM   1854  O   GLY A 255     -74.525  16.577 -42.588  1.00  9.06           O  
ATOM   1855  N   HIS A 256     -74.357  18.369 -41.239  1.00  1.95           N  
ATOM   1856  CA  HIS A 256     -72.942  18.585 -41.492  1.00  1.95           C  
ATOM   1857  C   HIS A 256     -72.145  18.381 -40.211  1.00  1.96           C  
ATOM   1858  O   HIS A 256     -72.689  18.403 -39.103  1.00 10.03           O  
ATOM   1859  CB  HIS A 256     -72.690  19.989 -42.051  1.00 10.56           C  
ATOM   1860  CG  HIS A 256     -73.458  20.290 -43.300  1.00 18.55           C  
ATOM   1861  ND1 HIS A 256     -72.906  20.183 -44.559  1.00 13.91           N  
ATOM   1862  CD2 HIS A 256     -74.737  20.694 -43.484  1.00 19.20           C  
ATOM   1863  CE1 HIS A 256     -73.811  20.509 -45.464  1.00 16.59           C  
ATOM   1864  NE2 HIS A 256     -74.931  20.823 -44.838  1.00 25.40           N  
ATOM   1865  N   ASP A 257     -70.838  18.192 -40.377  1.00  1.95           N  
ATOM   1866  CA  ASP A 257     -69.927  17.924 -39.264  1.00  1.95           C  
ATOM   1867  C   ASP A 257     -68.875  19.018 -39.172  1.00 10.41           C  
ATOM   1868  O   ASP A 257     -67.870  18.981 -39.906  1.00 12.31           O  
ATOM   1869  CB  ASP A 257     -69.255  16.561 -39.427  1.00  1.96           C  
ATOM   1870  CG  ASP A 257     -70.176  15.412 -39.083  1.00 36.38           C  
ATOM   1871  OD1 ASP A 257     -71.285  15.670 -38.571  1.00 55.46           O  
ATOM   1872  OD2 ASP A 257     -69.789  14.250 -39.326  1.00 49.92           O  
ATOM   1873  N   PRO A 258     -69.055  20.013 -38.306  1.00  4.79           N  
ATOM   1874  CA  PRO A 258     -67.986  20.995 -38.095  1.00  1.95           C  
ATOM   1875  C   PRO A 258     -66.785  20.337 -37.438  1.00 13.84           C  
ATOM   1876  O   PRO A 258     -66.924  19.542 -36.506  1.00 44.51           O  
ATOM   1877  CB  PRO A 258     -68.630  22.036 -37.170  1.00  1.95           C  
ATOM   1878  CG  PRO A 258     -70.108  21.792 -37.264  1.00  1.95           C  
ATOM   1879  CD  PRO A 258     -70.259  20.327 -37.520  1.00  1.96           C  
ATOM   1880  N   ALA A 259     -65.595  20.675 -37.930  1.00  2.52           N  
ATOM   1881  CA  ALA A 259     -64.381  20.089 -37.378  1.00 21.72           C  
ATOM   1882  C   ALA A 259     -63.952  20.848 -36.129  1.00 17.51           C  
ATOM   1883  O   ALA A 259     -62.792  21.252 -36.000  1.00 33.12           O  
ATOM   1884  CB  ALA A 259     -63.264  20.081 -38.421  1.00 22.20           C  
ATOM   1885  N   THR A 260     -64.885  21.024 -35.193  1.00  1.95           N  
ATOM   1886  CA  THR A 260     -64.649  21.729 -33.940  1.00  1.95           C  
ATOM   1887  C   THR A 260     -64.181  20.805 -32.820  1.00 34.34           C  
ATOM   1888  O   THR A 260     -64.390  21.113 -31.637  1.00 38.54           O  
ATOM   1889  CB  THR A 260     -65.921  22.465 -33.523  1.00  1.95           C  
ATOM   1890  OG1 THR A 260     -65.758  23.006 -32.206  1.00 21.13           O  
ATOM   1891  CG2 THR A 260     -67.093  21.504 -33.537  1.00  1.95           C  
ATOM   1892  N   ALA A 261     -63.558  19.674 -33.160  1.00 36.07           N  
ATOM   1893  CA  ALA A 261     -63.151  18.717 -32.137  1.00 26.03           C  
ATOM   1894  C   ALA A 261     -62.026  19.258 -31.265  1.00 29.18           C  
ATOM   1895  O   ALA A 261     -61.952  18.926 -30.076  1.00 15.58           O  
ATOM   1896  CB  ALA A 261     -62.730  17.399 -32.790  1.00 24.66           C  
ATOM   1897  N   LEU A 262     -61.140  20.082 -31.832  1.00 33.76           N  
ATOM   1898  CA  LEU A 262     -59.968  20.536 -31.089  1.00 19.31           C  
ATOM   1899  C   LEU A 262     -60.339  21.487 -29.956  1.00 20.70           C  
ATOM   1900  O   LEU A 262     -59.653  21.519 -28.928  1.00 43.79           O  
ATOM   1901  CB  LEU A 262     -58.971  21.210 -32.032  1.00  1.95           C  
ATOM   1902  CG  LEU A 262     -58.610  20.463 -33.318  1.00 13.86           C  
ATOM   1903  CD1 LEU A 262     -57.503  21.195 -34.065  1.00  1.95           C  
ATOM   1904  CD2 LEU A 262     -58.213  19.024 -33.029  1.00 35.50           C  
ATOM   1905  N   VAL A 263     -61.407  22.264 -30.119  1.00  1.95           N  
ATOM   1906  CA  VAL A 263     -61.787  23.250 -29.114  1.00  1.95           C  
ATOM   1907  C   VAL A 263     -62.542  22.570 -27.979  1.00 12.93           C  
ATOM   1908  O   VAL A 263     -62.051  22.506 -26.846  1.00  9.07           O  
ATOM   1909  CB  VAL A 263     -62.630  24.370 -29.749  1.00  1.95           C  
ATOM   1910  CG1 VAL A 263     -63.244  25.242 -28.682  1.00  1.95           C  
ATOM   1911  CG2 VAL A 263     -61.778  25.200 -30.697  1.00  1.95           C  
ATOM   1912  N   LYS A 264     -63.722  22.040 -28.289  1.00 12.80           N  
ATOM   1913  CA  LYS A 264     -64.540  21.255 -27.363  1.00 13.56           C  
ATOM   1914  C   LYS A 264     -64.635  21.895 -25.974  1.00 27.78           C  
ATOM   1915  O   LYS A 264     -64.214  21.323 -24.969  1.00 53.43           O  
ATOM   1916  CB  LYS A 264     -64.009  19.826 -27.261  1.00  9.17           C  
ATOM   1917  N   GLY A 265     -65.190  23.108 -25.924  1.00 12.10           N  
ATOM   1918  CA  GLY A 265     -65.472  23.787 -24.668  1.00 17.10           C  
ATOM   1919  C   GLY A 265     -64.721  25.090 -24.463  1.00 22.67           C  
ATOM   1920  O   GLY A 265     -65.212  25.972 -23.749  1.00  8.66           O  
ATOM   1921  N   GLN A 266     -63.527  25.220 -25.047  1.00 27.62           N  
ATOM   1922  CA  GLN A 266     -62.746  26.442 -24.858  1.00 17.01           C  
ATOM   1923  C   GLN A 266     -63.460  27.651 -25.454  1.00 14.74           C  
ATOM   1924  O   GLN A 266     -63.542  28.713 -24.827  1.00 12.38           O  
ATOM   1925  CB  GLN A 266     -61.353  26.271 -25.466  1.00  8.30           C  
ATOM   1926  CG  GLN A 266     -60.707  24.930 -25.149  1.00  9.61           C  
ATOM   1927  CD  GLN A 266     -59.196  24.964 -25.267  1.00 18.08           C  
ATOM   1928  OE1 GLN A 266     -58.553  25.956 -24.922  1.00 34.55           O  
ATOM   1929  NE2 GLN A 266     -58.619  23.875 -25.764  1.00  4.20           N  
ATOM   1930  N   ILE A 267     -63.977  27.507 -26.670  1.00 22.93           N  
ATOM   1931  CA  ILE A 267     -64.798  28.520 -27.322  1.00 22.28           C  
ATOM   1932  C   ILE A 267     -66.226  27.995 -27.353  1.00 11.76           C  
ATOM   1933  O   ILE A 267     -66.447  26.788 -27.488  1.00  8.07           O  
ATOM   1934  CB  ILE A 267     -64.289  28.851 -28.742  1.00 10.10           C  
ATOM   1935  CG1 ILE A 267     -62.896  29.485 -28.685  1.00  7.73           C  
ATOM   1936  CG2 ILE A 267     -65.250  29.780 -29.473  1.00  5.21           C  
ATOM   1937  CD1 ILE A 267     -61.755  28.499 -28.768  1.00  4.36           C  
ATOM   1938  N   ASP A 268     -67.191  28.896 -27.199  1.00  7.63           N  
ATOM   1939  CA  ASP A 268     -68.592  28.498 -27.184  1.00 17.65           C  
ATOM   1940  C   ASP A 268     -69.031  27.969 -28.548  1.00 20.87           C  
ATOM   1941  O   ASP A 268     -68.648  28.501 -29.594  1.00 34.92           O  
ATOM   1942  CB  ASP A 268     -69.469  29.677 -26.765  1.00 23.19           C  
ATOM   1943  CG  ASP A 268     -69.144  30.180 -25.370  1.00 38.22           C  
ATOM   1944  OD1 ASP A 268     -68.263  29.587 -24.711  1.00 46.77           O  
ATOM   1945  OD2 ASP A 268     -69.766  31.171 -24.933  1.00 39.08           O  
ATOM   1946  N   LEU A 269     -69.819  26.897 -28.527  1.00  2.11           N  
ATOM   1947  CA  LEU A 269     -70.421  26.303 -29.712  1.00  1.95           C  
ATOM   1948  C   LEU A 269     -71.938  26.420 -29.626  1.00 19.53           C  
ATOM   1949  O   LEU A 269     -72.499  26.816 -28.601  1.00 43.81           O  
ATOM   1950  CB  LEU A 269     -70.031  24.827 -29.881  1.00  1.95           C  
ATOM   1951  CG  LEU A 269     -68.620  24.372 -30.261  1.00  1.95           C  
ATOM   1952  CD1 LEU A 269     -67.635  24.563 -29.138  1.00  1.95           C  
ATOM   1953  CD2 LEU A 269     -68.664  22.912 -30.660  1.00 22.76           C  
ATOM   1954  N   ASP A 270     -72.602  26.067 -30.723  1.00 18.62           N  
ATOM   1955  CA  ASP A 270     -74.051  26.099 -30.803  1.00 17.89           C  
ATOM   1956  C   ASP A 270     -74.601  24.680 -30.648  1.00  4.77           C  
ATOM   1957  O   ASP A 270     -73.869  23.736 -30.336  1.00  1.95           O  
ATOM   1958  CB  ASP A 270     -74.496  26.759 -32.112  1.00 21.23           C  
ATOM   1959  CG  ASP A 270     -74.198  25.908 -33.332  1.00 31.70           C  
ATOM   1960  OD1 ASP A 270     -73.287  25.058 -33.262  1.00 42.68           O  
ATOM   1961  OD2 ASP A 270     -74.876  26.094 -34.365  1.00 32.25           O  
ATOM   1962  N   GLU A 271     -75.911  24.526 -30.862  1.00  1.95           N  
ATOM   1963  CA  GLU A 271     -76.546  23.225 -30.668  1.00  1.96           C  
ATOM   1964  C   GLU A 271     -76.038  22.193 -31.669  1.00  7.81           C  
ATOM   1965  O   GLU A 271     -75.886  21.015 -31.326  1.00  8.52           O  
ATOM   1966  CB  GLU A 271     -78.065  23.366 -30.768  1.00  1.95           C  
ATOM   1967  N   ASP A 272     -75.770  22.610 -32.905  1.00 23.29           N  
ATOM   1968  CA  ASP A 272     -75.344  21.686 -33.949  1.00 23.07           C  
ATOM   1969  C   ASP A 272     -73.834  21.495 -34.010  1.00  9.18           C  
ATOM   1970  O   ASP A 272     -73.370  20.599 -34.723  1.00  8.80           O  
ATOM   1971  CB  ASP A 272     -75.854  22.158 -35.317  1.00 34.67           C  
ATOM   1972  CG  ASP A 272     -77.367  22.093 -35.433  1.00 33.63           C  
ATOM   1973  OD1 ASP A 272     -77.958  21.103 -34.952  1.00 30.42           O  
ATOM   1974  OD2 ASP A 272     -77.963  23.027 -36.010  1.00 27.94           O  
ATOM   1975  N   GLY A 273     -73.059  22.296 -33.281  1.00  2.02           N  
ATOM   1976  CA  GLY A 273     -71.619  22.139 -33.221  1.00  7.19           C  
ATOM   1977  C   GLY A 273     -70.822  23.261 -33.850  1.00 15.60           C  
ATOM   1978  O   GLY A 273     -69.595  23.277 -33.704  1.00  4.10           O  
ATOM   1979  N   TYR A 274     -71.464  24.196 -34.543  1.00 28.52           N  
ATOM   1980  CA  TYR A 274     -70.728  25.285 -35.167  1.00 10.89           C  
ATOM   1981  C   TYR A 274     -70.239  26.278 -34.113  1.00  8.31           C  
ATOM   1982  O   TYR A 274     -70.795  26.390 -33.016  1.00 24.08           O  
ATOM   1983  CB  TYR A 274     -71.606  25.999 -36.196  1.00  3.57           C  
ATOM   1984  CG  TYR A 274     -71.988  25.150 -37.391  1.00  4.19           C  
ATOM   1985  CD1 TYR A 274     -73.084  24.297 -37.344  1.00  3.94           C  
ATOM   1986  CD2 TYR A 274     -71.258  25.210 -38.571  1.00  8.21           C  
ATOM   1987  CE1 TYR A 274     -73.436  23.524 -38.437  1.00  4.73           C  
ATOM   1988  CE2 TYR A 274     -71.602  24.442 -39.668  1.00  4.98           C  
ATOM   1989  CZ  TYR A 274     -72.692  23.603 -39.597  1.00 10.79           C  
ATOM   1990  OH  TYR A 274     -73.035  22.841 -40.688  1.00 18.15           O  
ATOM   1991  N   ILE A 275     -69.182  27.007 -34.459  1.00  9.17           N  
ATOM   1992  CA  ILE A 275     -68.639  28.030 -33.571  1.00  1.95           C  
ATOM   1993  C   ILE A 275     -69.521  29.268 -33.639  1.00  2.77           C  
ATOM   1994  O   ILE A 275     -69.766  29.815 -34.721  1.00  5.00           O  
ATOM   1995  CB  ILE A 275     -67.187  28.367 -33.946  1.00  1.95           C  
ATOM   1996  CG1 ILE A 275     -66.254  27.216 -33.569  1.00  3.69           C  
ATOM   1997  CG2 ILE A 275     -66.747  29.655 -33.263  1.00  1.95           C  
ATOM   1998  CD1 ILE A 275     -64.793  27.517 -33.821  1.00  1.95           C  
ATOM   1999  N   ILE A 276     -69.991  29.722 -32.482  1.00 13.55           N  
ATOM   2000  CA  ILE A 276     -70.804  30.930 -32.423  1.00 13.85           C  
ATOM   2001  C   ILE A 276     -69.889  32.142 -32.525  1.00  9.15           C  
ATOM   2002  O   ILE A 276     -68.849  32.213 -31.858  1.00  2.82           O  
ATOM   2003  CB  ILE A 276     -71.654  30.961 -31.141  1.00 12.74           C  
ATOM   2004  CG1 ILE A 276     -70.779  30.873 -29.889  1.00 36.26           C  
ATOM   2005  CG2 ILE A 276     -72.672  29.830 -31.153  1.00  1.96           C  
ATOM   2006  CD1 ILE A 276     -70.571  32.202 -29.182  1.00 41.04           C  
ATOM   2007  N   THR A 277     -70.254  33.083 -33.392  1.00 22.33           N  
ATOM   2008  CA  THR A 277     -69.492  34.308 -33.575  1.00 14.83           C  
ATOM   2009  C   THR A 277     -70.446  35.488 -33.652  1.00 17.88           C  
ATOM   2010  O   THR A 277     -71.607  35.343 -34.046  1.00 22.89           O  
ATOM   2011  CB  THR A 277     -68.624  34.265 -34.844  1.00  9.01           C  
ATOM   2012  OG1 THR A 277     -69.436  33.911 -35.971  1.00 10.70           O  
ATOM   2013  CG2 THR A 277     -67.486  33.263 -34.694  1.00  7.13           C  
ATOM   2014  N   LYS A 278     -69.944  36.655 -33.261  1.00  9.21           N  
ATOM   2015  CA  LYS A 278     -70.718  37.881 -33.381  1.00 10.59           C  
ATOM   2016  C   LYS A 278     -71.102  38.091 -34.843  1.00 19.74           C  
ATOM   2017  O   LYS A 278     -70.234  38.005 -35.724  1.00 31.79           O  
ATOM   2018  CB  LYS A 278     -69.912  39.067 -32.850  1.00 14.23           C  
ATOM   2019  CG  LYS A 278     -70.727  40.305 -32.511  1.00 10.55           C  
ATOM   2020  CD  LYS A 278     -69.868  41.322 -31.770  1.00 14.39           C  
ATOM   2021  CE  LYS A 278     -70.673  42.541 -31.345  1.00 27.40           C  
ATOM   2022  NZ  LYS A 278     -71.174  43.316 -32.512  1.00 29.66           N  
ATOM   2023  N   PRO A 279     -72.375  38.349 -35.143  1.00 12.83           N  
ATOM   2024  CA  PRO A 279     -72.818  38.388 -36.544  1.00 15.73           C  
ATOM   2025  C   PRO A 279     -72.070  39.431 -37.364  1.00 35.85           C  
ATOM   2026  O   PRO A 279     -71.760  40.525 -36.887  1.00 46.46           O  
ATOM   2027  CB  PRO A 279     -74.309  38.724 -36.433  1.00 14.10           C  
ATOM   2028  CG  PRO A 279     -74.696  38.276 -35.059  1.00 12.50           C  
ATOM   2029  CD  PRO A 279     -73.493  38.532 -34.203  1.00 11.95           C  
ATOM   2030  N   GLY A 280     -71.781  39.071 -38.614  1.00 44.68           N  
ATOM   2031  CA  GLY A 280     -70.999  39.895 -39.514  1.00 44.03           C  
ATOM   2032  C   GLY A 280     -69.530  40.010 -39.178  1.00 21.64           C  
ATOM   2033  O   GLY A 280     -68.809  40.732 -39.875  1.00 14.92           O  
ATOM   2034  N   THR A 281     -69.062  39.320 -38.141  1.00 13.11           N  
ATOM   2035  CA  THR A 281     -67.678  39.378 -37.698  1.00 12.20           C  
ATOM   2036  C   THR A 281     -67.175  37.961 -37.457  1.00 16.02           C  
ATOM   2037  O   THR A 281     -67.940  36.993 -37.464  1.00 16.04           O  
ATOM   2038  CB  THR A 281     -67.513  40.210 -36.417  1.00 22.31           C  
ATOM   2039  OG1 THR A 281     -68.097  39.506 -35.315  1.00 21.91           O  
ATOM   2040  CG2 THR A 281     -68.181  41.571 -36.556  1.00 29.19           C  
ATOM   2041  N   SER A 282     -65.867  37.850 -37.242  1.00 13.54           N  
ATOM   2042  CA  SER A 282     -65.235  36.594 -36.871  1.00  9.73           C  
ATOM   2043  C   SER A 282     -64.942  36.515 -35.380  1.00  9.37           C  
ATOM   2044  O   SER A 282     -64.205  35.623 -34.948  1.00  8.97           O  
ATOM   2045  CB  SER A 282     -63.945  36.400 -37.665  1.00  9.91           C  
ATOM   2046  OG  SER A 282     -62.981  37.365 -37.285  1.00 10.03           O  
ATOM   2047  N   TYR A 283     -65.498  37.429 -34.590  1.00  9.81           N  
ATOM   2048  CA  TYR A 283     -65.239  37.458 -33.158  1.00 11.02           C  
ATOM   2049  C   TYR A 283     -65.914  36.266 -32.487  1.00  8.70           C  
ATOM   2050  O   TYR A 283     -67.144  36.152 -32.501  1.00  8.41           O  
ATOM   2051  CB  TYR A 283     -65.746  38.771 -32.564  1.00 30.05           C  
ATOM   2052  CG  TYR A 283     -64.983  40.000 -33.019  1.00 30.95           C  
ATOM   2053  CD1 TYR A 283     -63.674  39.904 -33.471  1.00 26.93           C  
ATOM   2054  CD2 TYR A 283     -65.577  41.257 -32.999  1.00 35.15           C  
ATOM   2055  CE1 TYR A 283     -62.975  41.025 -33.884  1.00 22.21           C  
ATOM   2056  CE2 TYR A 283     -64.886  42.384 -33.413  1.00 26.64           C  
ATOM   2057  CZ  TYR A 283     -63.586  42.261 -33.855  1.00 21.72           C  
ATOM   2058  OH  TYR A 283     -62.895  43.378 -34.267  1.00 24.91           O  
ATOM   2059  N   THR A 284     -65.112  35.378 -31.904  1.00  8.14           N  
ATOM   2060  CA  THR A 284     -65.629  34.223 -31.178  1.00  6.90           C  
ATOM   2061  C   THR A 284     -65.999  34.630 -29.754  1.00  6.68           C  
ATOM   2062  O   THR A 284     -66.091  35.815 -29.423  1.00 22.38           O  
ATOM   2063  CB  THR A 284     -64.612  33.087 -31.184  1.00  7.60           C  
ATOM   2064  OG1 THR A 284     -63.408  33.515 -30.535  1.00  9.93           O  
ATOM   2065  CG2 THR A 284     -64.289  32.670 -32.609  1.00 18.83           C  
ATOM   2066  N   SER A 285     -66.222  33.639 -28.887  1.00 14.20           N  
ATOM   2067  CA  SER A 285     -66.563  33.921 -27.499  1.00 24.07           C  
ATOM   2068  C   SER A 285     -65.339  34.194 -26.635  1.00 28.21           C  
ATOM   2069  O   SER A 285     -65.468  34.844 -25.591  1.00 16.60           O  
ATOM   2070  CB  SER A 285     -67.360  32.759 -26.906  1.00  2.79           C  
ATOM   2071  OG  SER A 285     -67.667  32.997 -25.543  1.00  7.91           O  
ATOM   2072  N   ARG A 286     -64.165  33.714 -27.038  1.00 24.52           N  
ATOM   2073  CA  ARG A 286     -62.915  33.988 -26.342  1.00 15.85           C  
ATOM   2074  C   ARG A 286     -62.136  35.066 -27.083  1.00 13.92           C  
ATOM   2075  O   ARG A 286     -61.866  34.928 -28.280  1.00  9.66           O  
ATOM   2076  CB  ARG A 286     -62.063  32.726 -26.211  1.00 15.24           C  
ATOM   2077  CG  ARG A 286     -60.648  33.015 -25.742  1.00 14.13           C  
ATOM   2078  CD  ARG A 286     -60.577  33.060 -24.225  1.00 34.40           C  
ATOM   2079  NE  ARG A 286     -59.252  33.438 -23.738  1.00 44.66           N  
ATOM   2080  CZ  ARG A 286     -58.208  32.617 -23.699  1.00 33.95           C  
ATOM   2081  NH1 ARG A 286     -58.331  31.370 -24.128  1.00 27.15           N  
ATOM   2082  NH2 ARG A 286     -57.041  33.043 -23.236  1.00 19.89           N  
ATOM   2083  N   GLU A 287     -61.778  36.133 -26.372  1.00 35.91           N  
ATOM   2084  CA  GLU A 287     -61.021  37.221 -26.980  1.00 36.28           C  
ATOM   2085  C   GLU A 287     -59.615  36.747 -27.329  1.00 28.48           C  
ATOM   2086  O   GLU A 287     -58.861  36.314 -26.451  1.00 27.72           O  
ATOM   2087  CB  GLU A 287     -60.967  38.420 -26.034  1.00 23.40           C  
ATOM   2088  CG  GLU A 287     -60.200  39.616 -26.582  1.00 16.22           C  
ATOM   2089  CD  GLU A 287     -60.168  40.786 -25.616  1.00 16.44           C  
ATOM   2090  OE1 GLU A 287     -60.827  40.705 -24.558  1.00 15.20           O  
ATOM   2091  OE2 GLU A 287     -59.482  41.786 -25.914  1.00 17.03           O  
ATOM   2092  N   GLY A 288     -59.265  36.825 -28.611  1.00 13.59           N  
ATOM   2093  CA  GLY A 288     -57.979  36.376 -29.111  1.00 14.28           C  
ATOM   2094  C   GLY A 288     -58.057  35.307 -30.179  1.00 13.26           C  
ATOM   2095  O   GLY A 288     -57.086  35.123 -30.928  1.00 13.96           O  
ATOM   2096  N   VAL A 289     -59.176  34.596 -30.283  1.00 38.19           N  
ATOM   2097  CA  VAL A 289     -59.366  33.549 -31.280  1.00 36.58           C  
ATOM   2098  C   VAL A 289     -60.526  33.940 -32.185  1.00 25.52           C  
ATOM   2099  O   VAL A 289     -61.576  34.385 -31.706  1.00  9.42           O  
ATOM   2100  CB  VAL A 289     -59.607  32.177 -30.619  1.00 14.79           C  
ATOM   2101  CG1 VAL A 289     -60.626  32.288 -29.503  1.00  9.11           C  
ATOM   2102  CG2 VAL A 289     -60.062  31.154 -31.650  1.00 12.84           C  
ATOM   2103  N   PHE A 290     -60.325  33.792 -33.493  1.00 19.82           N  
ATOM   2104  CA  PHE A 290     -61.327  34.115 -34.495  1.00 14.02           C  
ATOM   2105  C   PHE A 290     -61.682  32.861 -35.283  1.00 16.44           C  
ATOM   2106  O   PHE A 290     -60.899  31.911 -35.366  1.00 27.05           O  
ATOM   2107  CB  PHE A 290     -60.826  35.207 -35.454  1.00 10.26           C  
ATOM   2108  CG  PHE A 290     -60.163  36.369 -34.766  1.00 10.62           C  
ATOM   2109  CD1 PHE A 290     -58.820  36.321 -34.429  1.00 11.43           C  
ATOM   2110  CD2 PHE A 290     -60.882  37.512 -34.466  1.00 13.89           C  
ATOM   2111  CE1 PHE A 290     -58.211  37.389 -33.800  1.00 11.82           C  
ATOM   2112  CE2 PHE A 290     -60.277  38.584 -33.838  1.00 11.05           C  
ATOM   2113  CZ  PHE A 290     -58.941  38.522 -33.504  1.00 11.57           C  
ATOM   2114  N   ALA A 291     -62.879  32.868 -35.867  1.00  9.00           N  
ATOM   2115  CA  ALA A 291     -63.384  31.724 -36.620  1.00  8.91           C  
ATOM   2116  C   ALA A 291     -64.016  32.219 -37.911  1.00  9.48           C  
ATOM   2117  O   ALA A 291     -64.920  33.059 -37.877  1.00 27.27           O  
ATOM   2118  CB  ALA A 291     -64.396  30.921 -35.799  1.00 24.56           C  
ATOM   2119  N   CYS A 292     -63.541  31.705 -39.043  1.00 10.46           N  
ATOM   2120  CA  CYS A 292     -64.088  32.049 -40.347  1.00 11.27           C  
ATOM   2121  C   CYS A 292     -64.420  30.778 -41.116  1.00 35.13           C  
ATOM   2122  O   CYS A 292     -63.895  29.698 -40.833  1.00 69.46           O  
ATOM   2123  CB  CYS A 292     -63.114  32.904 -41.163  1.00 12.34           C  
ATOM   2124  SG  CYS A 292     -61.487  32.159 -41.369  1.00 27.36           S  
ATOM   2125  N   GLY A 293     -65.307  30.919 -42.097  1.00 22.00           N  
ATOM   2126  CA  GLY A 293     -65.642  29.812 -42.969  1.00 30.40           C  
ATOM   2127  C   GLY A 293     -66.839  29.015 -42.500  1.00 34.24           C  
ATOM   2128  O   GLY A 293     -67.719  29.548 -41.818  1.00 60.06           O  
ATOM   2129  N   ASP A 294     -66.883  27.730 -42.861  1.00 11.02           N  
ATOM   2130  CA  ASP A 294     -68.014  26.883 -42.505  1.00  9.88           C  
ATOM   2131  C   ASP A 294     -68.038  26.504 -41.032  1.00 15.68           C  
ATOM   2132  O   ASP A 294     -69.041  25.947 -40.575  1.00 39.04           O  
ATOM   2133  CB  ASP A 294     -68.022  25.612 -43.355  1.00 20.88           C  
ATOM   2134  CG  ASP A 294     -68.553  25.848 -44.753  1.00 36.61           C  
ATOM   2135  OD1 ASP A 294     -68.670  27.024 -45.157  1.00 43.08           O  
ATOM   2136  OD2 ASP A 294     -68.867  24.854 -45.443  1.00 42.97           O  
ATOM   2137  N   VAL A 295     -66.965  26.769 -40.284  1.00 15.72           N  
ATOM   2138  CA  VAL A 295     -66.981  26.468 -38.857  1.00  7.81           C  
ATOM   2139  C   VAL A 295     -67.993  27.349 -38.138  1.00  6.24           C  
ATOM   2140  O   VAL A 295     -68.559  26.951 -37.113  1.00  4.82           O  
ATOM   2141  CB  VAL A 295     -65.573  26.636 -38.261  1.00 22.53           C  
ATOM   2142  CG1 VAL A 295     -65.452  25.857 -36.959  1.00  5.46           C  
ATOM   2143  CG2 VAL A 295     -64.521  26.217 -39.265  1.00 38.38           C  
ATOM   2144  N   GLN A 296     -68.236  28.554 -38.657  1.00 21.73           N  
ATOM   2145  CA  GLN A 296     -69.217  29.471 -38.100  1.00  7.38           C  
ATOM   2146  C   GLN A 296     -70.463  29.622 -38.956  1.00  8.38           C  
ATOM   2147  O   GLN A 296     -71.492  30.071 -38.442  1.00 17.10           O  
ATOM   2148  CB  GLN A 296     -68.599  30.862 -37.908  1.00 19.11           C  
ATOM   2149  CG  GLN A 296     -68.165  31.515 -39.210  1.00  9.48           C  
ATOM   2150  CD  GLN A 296     -67.952  33.003 -39.067  1.00 52.18           C  
ATOM   2151  OE1 GLN A 296     -67.970  33.539 -37.961  1.00 63.85           O  
ATOM   2152  NE2 GLN A 296     -67.751  33.684 -40.190  1.00 96.56           N  
ATOM   2153  N   ASP A 297     -70.398  29.261 -40.234  1.00  9.46           N  
ATOM   2154  CA  ASP A 297     -71.487  29.481 -41.175  1.00 10.89           C  
ATOM   2155  C   ASP A 297     -72.277  28.191 -41.347  1.00 18.42           C  
ATOM   2156  O   ASP A 297     -71.724  27.165 -41.756  1.00 33.56           O  
ATOM   2157  CB  ASP A 297     -70.948  29.971 -42.520  1.00 46.05           C  
ATOM   2158  CG  ASP A 297     -71.999  29.956 -43.611  1.00 44.07           C  
ATOM   2159  OD1 ASP A 297     -73.141  30.382 -43.340  1.00 46.92           O  
ATOM   2160  OD2 ASP A 297     -71.680  29.534 -44.743  1.00 37.80           O  
ATOM   2161  N   LYS A 298     -73.571  28.253 -41.036  1.00 20.97           N  
ATOM   2162  CA  LYS A 298     -74.489  27.145 -41.237  1.00  9.86           C  
ATOM   2163  C   LYS A 298     -75.605  27.475 -42.217  1.00 12.00           C  
ATOM   2164  O   LYS A 298     -76.317  26.562 -42.652  1.00 47.34           O  
ATOM   2165  CB  LYS A 298     -75.103  26.728 -39.889  1.00  7.88           C  
ATOM   2166  CG  LYS A 298     -75.913  25.441 -39.897  1.00 30.34           C  
ATOM   2167  CD  LYS A 298     -76.925  25.435 -38.761  1.00 40.43           C  
ATOM   2168  CE  LYS A 298     -76.273  25.793 -37.435  1.00 20.98           C  
ATOM   2169  NZ  LYS A 298     -77.266  25.866 -36.329  1.00 24.11           N  
ATOM   2170  N   ARG A 299     -75.748  28.741 -42.612  1.00 14.05           N  
ATOM   2171  CA  ARG A 299     -76.858  29.173 -43.449  1.00 16.41           C  
ATOM   2172  C   ARG A 299     -76.521  29.228 -44.933  1.00 20.51           C  
ATOM   2173  O   ARG A 299     -77.435  29.133 -45.759  1.00 48.03           O  
ATOM   2174  CB  ARG A 299     -77.341  30.558 -42.991  1.00 22.76           C  
ATOM   2175  CG  ARG A 299     -78.802  30.866 -43.288  1.00 34.51           C  
ATOM   2176  CD  ARG A 299     -79.190  32.264 -42.810  1.00 30.54           C  
ATOM   2177  NE  ARG A 299     -78.788  32.516 -41.427  1.00 32.25           N  
ATOM   2178  CZ  ARG A 299     -77.809  33.343 -41.069  1.00 43.27           C  
ATOM   2179  NH1 ARG A 299     -77.130  34.010 -41.991  1.00 42.82           N  
ATOM   2180  NH2 ARG A 299     -77.511  33.508 -39.787  1.00 41.33           N  
ATOM   2181  N   TYR A 300     -75.245  29.363 -45.296  1.00 17.16           N  
ATOM   2182  CA  TYR A 300     -74.854  29.510 -46.694  1.00 17.64           C  
ATOM   2183  C   TYR A 300     -73.974  28.372 -47.183  1.00 23.65           C  
ATOM   2184  O   TYR A 300     -74.285  27.756 -48.211  1.00 30.03           O  
ATOM   2185  CB  TYR A 300     -74.142  30.857 -46.895  1.00 17.89           C  
ATOM   2186  CG  TYR A 300     -74.868  32.002 -46.230  1.00 18.77           C  
ATOM   2187  CD1 TYR A 300     -76.080  32.463 -46.726  1.00 27.24           C  
ATOM   2188  CD2 TYR A 300     -74.349  32.611 -45.096  1.00 19.88           C  
ATOM   2189  CE1 TYR A 300     -76.752  33.502 -46.111  1.00 30.30           C  
ATOM   2190  CE2 TYR A 300     -75.011  33.651 -44.476  1.00 18.91           C  
ATOM   2191  CZ  TYR A 300     -76.212  34.093 -44.987  1.00 20.65           C  
ATOM   2192  OH  TYR A 300     -76.873  35.128 -44.369  1.00 21.85           O  
ATOM   2193  N   ARG A 301     -72.880  28.079 -46.477  1.00 28.89           N  
ATOM   2194  CA  ARG A 301     -71.997  26.955 -46.800  1.00 23.09           C  
ATOM   2195  C   ARG A 301     -71.503  27.036 -48.245  1.00 13.89           C  
ATOM   2196  O   ARG A 301     -71.593  26.077 -49.015  1.00 23.04           O  
ATOM   2197  CB  ARG A 301     -72.685  25.614 -46.522  1.00 22.89           C  
ATOM   2198  CG  ARG A 301     -72.971  25.348 -45.046  1.00 10.62           C  
ATOM   2199  CD  ARG A 301     -73.943  24.188 -44.852  1.00 36.15           C  
ATOM   2200  NE  ARG A 301     -75.301  24.526 -45.270  1.00 57.01           N  
ATOM   2201  CZ  ARG A 301     -75.843  24.161 -46.429  1.00 42.95           C  
ATOM   2202  NH1 ARG A 301     -75.143  23.438 -47.294  1.00 24.87           N  
ATOM   2203  NH2 ARG A 301     -77.086  24.518 -46.723  1.00 32.80           N  
ATOM   2204  N   GLN A 302     -70.979  28.201 -48.611  1.00 20.77           N  
ATOM   2205  CA  GLN A 302     -70.429  28.440 -49.935  1.00 24.65           C  
ATOM   2206  C   GLN A 302     -68.964  28.837 -49.820  1.00 47.44           C  
ATOM   2207  O   GLN A 302     -68.518  29.356 -48.793  1.00 81.39           O  
ATOM   2208  CB  GLN A 302     -71.210  29.534 -50.676  1.00 11.54           C  
ATOM   2209  CG  GLN A 302     -72.646  29.162 -51.000  1.00 11.16           C  
ATOM   2210  CD  GLN A 302     -72.739  28.030 -52.002  1.00 11.42           C  
ATOM   2211  OE1 GLN A 302     -71.876  27.882 -52.868  1.00 23.91           O  
ATOM   2212  NE2 GLN A 302     -73.788  27.224 -51.891  1.00  8.11           N  
ATOM   2213  N   ALA A 303     -68.212  28.587 -50.894  1.00 27.56           N  
ATOM   2214  CA  ALA A 303     -66.799  28.955 -50.896  1.00 23.63           C  
ATOM   2215  C   ALA A 303     -66.625  30.462 -51.011  1.00 37.56           C  
ATOM   2216  O   ALA A 303     -65.742  31.041 -50.368  1.00 61.53           O  
ATOM   2217  CB  ALA A 303     -66.064  28.243 -52.029  1.00 17.13           C  
ATOM   2218  N   ILE A 304     -67.457  31.116 -51.825  1.00 30.93           N  
ATOM   2219  CA  ILE A 304     -67.360  32.565 -51.961  1.00 12.13           C  
ATOM   2220  C   ILE A 304     -67.710  33.254 -50.648  1.00 13.06           C  
ATOM   2221  O   ILE A 304     -67.168  34.321 -50.336  1.00 20.95           O  
ATOM   2222  CB  ILE A 304     -68.248  33.053 -53.122  1.00 17.59           C  
ATOM   2223  CG1 ILE A 304     -68.011  34.540 -53.385  1.00  7.64           C  
ATOM   2224  CG2 ILE A 304     -69.720  32.780 -52.837  1.00 20.66           C  
ATOM   2225  CD1 ILE A 304     -66.560  34.876 -53.633  1.00  8.45           C  
ATOM   2226  N   THR A 305     -68.598  32.659 -49.848  1.00 13.88           N  
ATOM   2227  CA  THR A 305     -68.930  33.235 -48.549  1.00 15.01           C  
ATOM   2228  C   THR A 305     -67.862  32.915 -47.510  1.00 15.45           C  
ATOM   2229  O   THR A 305     -67.565  33.747 -46.646  1.00 15.32           O  
ATOM   2230  CB  THR A 305     -70.296  32.735 -48.077  1.00 15.52           C  
ATOM   2231  OG1 THR A 305     -70.256  31.312 -47.907  1.00 23.35           O  
ATOM   2232  CG2 THR A 305     -71.375  33.100 -49.089  1.00 14.83           C  
ATOM   2233  N   SER A 306     -67.292  31.710 -47.565  1.00 27.27           N  
ATOM   2234  CA  SER A 306     -66.198  31.377 -46.659  1.00 25.47           C  
ATOM   2235  C   SER A 306     -64.950  32.186 -46.985  1.00 27.70           C  
ATOM   2236  O   SER A 306     -64.243  32.637 -46.076  1.00 44.23           O  
ATOM   2237  CB  SER A 306     -65.902  29.879 -46.721  1.00 18.15           C  
ATOM   2238  OG  SER A 306     -67.028  29.125 -46.307  1.00 33.04           O  
ATOM   2239  N   ALA A 307     -64.662  32.380 -48.275  1.00 32.02           N  
ATOM   2240  CA  ALA A 307     -63.540  33.230 -48.660  1.00 18.36           C  
ATOM   2241  C   ALA A 307     -63.748  34.657 -48.175  1.00 16.57           C  
ATOM   2242  O   ALA A 307     -62.810  35.300 -47.690  1.00 34.31           O  
ATOM   2243  CB  ALA A 307     -63.348  33.200 -50.176  1.00 16.56           C  
ATOM   2244  N   GLY A 308     -64.974  35.166 -48.292  1.00 15.70           N  
ATOM   2245  CA  GLY A 308     -65.267  36.487 -47.763  1.00 14.99           C  
ATOM   2246  C   GLY A 308     -65.102  36.547 -46.258  1.00 14.51           C  
ATOM   2247  O   GLY A 308     -64.458  37.454 -45.726  1.00 32.73           O  
ATOM   2248  N   SER A 309     -65.682  35.573 -45.551  1.00 22.09           N  
ATOM   2249  CA  SER A 309     -65.549  35.535 -44.099  1.00 22.79           C  
ATOM   2250  C   SER A 309     -64.101  35.330 -43.677  1.00 13.52           C  
ATOM   2251  O   SER A 309     -63.713  35.741 -42.577  1.00 12.64           O  
ATOM   2252  CB  SER A 309     -66.435  34.435 -43.515  1.00 31.11           C  
ATOM   2253  OG  SER A 309     -66.383  34.447 -42.100  1.00 41.46           O  
ATOM   2254  N   GLY A 310     -63.288  34.701 -44.529  1.00 14.68           N  
ATOM   2255  CA  GLY A 310     -61.875  34.570 -44.219  1.00 15.16           C  
ATOM   2256  C   GLY A 310     -61.161  35.907 -44.226  1.00 14.79           C  
ATOM   2257  O   GLY A 310     -60.276  36.154 -43.403  1.00 14.42           O  
ATOM   2258  N   CYS A 311     -61.535  36.788 -45.157  1.00 24.27           N  
ATOM   2259  CA  CYS A 311     -61.017  38.151 -45.141  1.00 13.89           C  
ATOM   2260  C   CYS A 311     -61.489  38.909 -43.906  1.00 12.40           C  
ATOM   2261  O   CYS A 311     -60.752  39.749 -43.379  1.00 11.73           O  
ATOM   2262  CB  CYS A 311     -61.433  38.891 -46.412  1.00 13.97           C  
ATOM   2263  SG  CYS A 311     -60.907  40.615 -46.479  1.00 14.85           S  
ATOM   2264  N   ILE A 312     -62.712  38.637 -43.442  1.00 15.98           N  
ATOM   2265  CA  ILE A 312     -63.212  39.281 -42.230  1.00 11.35           C  
ATOM   2266  C   ILE A 312     -62.353  38.886 -41.037  1.00 10.95           C  
ATOM   2267  O   ILE A 312     -61.964  39.727 -40.218  1.00 10.52           O  
ATOM   2268  CB  ILE A 312     -64.690  38.916 -41.999  1.00 12.34           C  
ATOM   2269  CG1 ILE A 312     -65.537  39.286 -43.216  1.00 12.31           C  
ATOM   2270  CG2 ILE A 312     -65.218  39.608 -40.750  1.00 11.45           C  
ATOM   2271  CD1 ILE A 312     -65.295  40.669 -43.737  1.00 12.15           C  
ATOM   2272  N   ALA A 313     -62.047  37.591 -40.921  1.00 11.58           N  
ATOM   2273  CA  ALA A 313     -61.165  37.129 -39.856  1.00 11.15           C  
ATOM   2274  C   ALA A 313     -59.762  37.689 -40.016  1.00 11.51           C  
ATOM   2275  O   ALA A 313     -59.035  37.838 -39.028  1.00 11.37           O  
ATOM   2276  CB  ALA A 313     -61.125  35.601 -39.827  1.00 22.36           C  
ATOM   2277  N   ALA A 314     -59.369  38.008 -41.248  1.00 12.92           N  
ATOM   2278  CA  ALA A 314     -58.026  38.518 -41.492  1.00 12.52           C  
ATOM   2279  C   ALA A 314     -57.875  39.948 -40.989  1.00 11.29           C  
ATOM   2280  O   ALA A 314     -56.919  40.267 -40.273  1.00 11.18           O  
ATOM   2281  CB  ALA A 314     -57.703  38.433 -42.983  1.00 20.71           C  
ATOM   2282  N   LEU A 315     -58.812  40.826 -41.355  1.00 11.47           N  
ATOM   2283  CA  LEU A 315     -58.710  42.225 -40.953  1.00  9.75           C  
ATOM   2284  C   LEU A 315     -58.859  42.381 -39.445  1.00 16.26           C  
ATOM   2285  O   LEU A 315     -58.115  43.145 -38.819  1.00 50.57           O  
ATOM   2286  CB  LEU A 315     -59.753  43.065 -41.691  1.00  9.50           C  
ATOM   2287  CG  LEU A 315     -59.666  43.021 -43.219  1.00  9.77           C  
ATOM   2288  CD1 LEU A 315     -60.698  43.939 -43.858  1.00  9.55           C  
ATOM   2289  CD2 LEU A 315     -58.264  43.380 -43.686  1.00  9.65           C  
ATOM   2290  N   GLU A 316     -59.811  41.667 -38.842  1.00 18.95           N  
ATOM   2291  CA  GLU A 316     -60.021  41.793 -37.406  1.00 28.92           C  
ATOM   2292  C   GLU A 316     -58.920  41.127 -36.591  1.00 19.25           C  
ATOM   2293  O   GLU A 316     -58.749  41.468 -35.416  1.00 19.59           O  
ATOM   2294  CB  GLU A 316     -61.384  41.217 -37.022  1.00 29.92           C  
ATOM   2295  CG  GLU A 316     -62.553  42.081 -37.467  1.00 30.60           C  
ATOM   2296  CD  GLU A 316     -63.880  41.360 -37.377  1.00 41.72           C  
ATOM   2297  OE1 GLU A 316     -64.924  42.011 -37.592  1.00 50.34           O  
ATOM   2298  OE2 GLU A 316     -63.881  40.146 -37.081  1.00 47.89           O  
ATOM   2299  N   ALA A 317     -58.174  40.187 -37.177  1.00 10.54           N  
ATOM   2300  CA  ALA A 317     -57.000  39.656 -36.493  1.00 11.15           C  
ATOM   2301  C   ALA A 317     -55.827  40.626 -36.565  1.00 32.15           C  
ATOM   2302  O   ALA A 317     -55.098  40.798 -35.582  1.00 33.60           O  
ATOM   2303  CB  ALA A 317     -56.608  38.301 -37.082  1.00 12.01           C  
ATOM   2304  N   GLU A 318     -55.627  41.263 -37.722  1.00 35.37           N  
ATOM   2305  CA  GLU A 318     -54.560  42.250 -37.849  1.00 15.45           C  
ATOM   2306  C   GLU A 318     -54.858  43.495 -37.023  1.00 11.63           C  
ATOM   2307  O   GLU A 318     -53.939  44.104 -36.463  1.00 18.04           O  
ATOM   2308  CB  GLU A 318     -54.357  42.609 -39.323  1.00 10.95           C  
ATOM   2309  CG  GLU A 318     -53.214  43.574 -39.594  1.00 30.45           C  
ATOM   2310  CD  GLU A 318     -53.698  44.962 -39.968  1.00 37.18           C  
ATOM   2311  OE1 GLU A 318     -54.893  45.104 -40.305  1.00 35.88           O  
ATOM   2312  OE2 GLU A 318     -52.885  45.909 -39.924  1.00 34.90           O  
ATOM   2313  N   LYS A 319     -56.134  43.877 -36.926  1.00 14.85           N  
ATOM   2314  CA  LYS A 319     -56.524  44.977 -36.051  1.00 15.18           C  
ATOM   2315  C   LYS A 319     -56.322  44.612 -34.585  1.00 20.12           C  
ATOM   2316  O   LYS A 319     -55.953  45.466 -33.771  1.00 29.72           O  
ATOM   2317  CB  LYS A 319     -57.981  45.358 -36.319  1.00 29.25           C  
ATOM   2318  CG  LYS A 319     -58.598  46.295 -35.293  1.00 43.67           C  
ATOM   2319  CD  LYS A 319     -59.967  46.780 -35.744  1.00 44.51           C  
ATOM   2320  CE  LYS A 319     -60.633  47.628 -34.673  1.00 39.48           C  
ATOM   2321  NZ  LYS A 319     -62.001  48.060 -35.075  1.00 35.51           N  
ATOM   2322  N   PHE A 320     -56.548  43.343 -34.234  1.00 27.81           N  
ATOM   2323  CA  PHE A 320     -56.376  42.905 -32.851  1.00 19.67           C  
ATOM   2324  C   PHE A 320     -54.917  42.976 -32.416  1.00 11.56           C  
ATOM   2325  O   PHE A 320     -54.623  43.366 -31.280  1.00 11.94           O  
ATOM   2326  CB  PHE A 320     -56.926  41.487 -32.682  1.00 12.18           C  
ATOM   2327  CG  PHE A 320     -56.550  40.837 -31.379  1.00 13.28           C  
ATOM   2328  CD1 PHE A 320     -57.199  41.184 -30.204  1.00 14.30           C  
ATOM   2329  CD2 PHE A 320     -55.559  39.869 -31.330  1.00 15.96           C  
ATOM   2330  CE1 PHE A 320     -56.859  40.585 -29.004  1.00 15.50           C  
ATOM   2331  CE2 PHE A 320     -55.214  39.267 -30.134  1.00 14.91           C  
ATOM   2332  CZ  PHE A 320     -55.865  39.626 -28.969  1.00 15.71           C  
ATOM   2333  N   ILE A 321     -53.988  42.592 -33.296  1.00 11.24           N  
ATOM   2334  CA  ILE A 321     -52.573  42.625 -32.934  1.00 11.65           C  
ATOM   2335  C   ILE A 321     -52.078  44.062 -32.832  1.00 13.33           C  
ATOM   2336  O   ILE A 321     -51.293  44.400 -31.937  1.00 10.10           O  
ATOM   2337  CB  ILE A 321     -51.739  41.811 -33.938  1.00 11.83           C  
ATOM   2338  CG1 ILE A 321     -52.020  40.319 -33.781  1.00 13.19           C  
ATOM   2339  CG2 ILE A 321     -50.251  42.088 -33.761  1.00 19.19           C  
ATOM   2340  CD1 ILE A 321     -51.161  39.466 -34.667  1.00 29.86           C  
ATOM   2341  N   ALA A 322     -52.532  44.930 -33.738  1.00  9.27           N  
ATOM   2342  CA  ALA A 322     -52.094  46.322 -33.721  1.00  8.09           C  
ATOM   2343  C   ALA A 322     -52.456  46.994 -32.402  1.00 11.39           C  
ATOM   2344  O   ALA A 322     -51.622  47.664 -31.782  1.00 33.01           O  
ATOM   2345  CB  ALA A 322     -52.704  47.079 -34.901  1.00  7.27           C  
ATOM   2346  N   GLU A 323     -53.698  46.820 -31.953  1.00  9.00           N  
ATOM   2347  CA  GLU A 323     -54.145  47.422 -30.703  1.00 27.77           C  
ATOM   2348  C   GLU A 323     -53.585  46.731 -29.464  1.00 31.32           C  
ATOM   2349  O   GLU A 323     -53.911  47.156 -28.350  1.00 31.17           O  
ATOM   2350  CB  GLU A 323     -55.674  47.424 -30.645  1.00 33.97           C  
ATOM   2351  CG  GLU A 323     -56.336  48.140 -31.810  1.00 33.39           C  
ATOM   2352  CD  GLU A 323     -57.847  48.147 -31.705  1.00 39.71           C  
ATOM   2353  OE1 GLU A 323     -58.392  47.360 -30.902  1.00 30.31           O  
ATOM   2354  OE2 GLU A 323     -58.490  48.939 -32.426  1.00 42.03           O  
ATOM   2355  N   ALA A 324     -52.759  45.696 -29.614  1.00 30.86           N  
ATOM   2356  CA  ALA A 324     -52.211  44.981 -28.467  1.00 28.84           C  
ATOM   2357  C   ALA A 324     -50.777  45.377 -28.147  1.00 27.64           C  
ATOM   2358  O   ALA A 324     -50.419  45.484 -26.970  1.00 27.87           O  
ATOM   2359  CB  ALA A 324     -52.280  43.469 -28.703  1.00 15.39           C  
ATOM   2360  N   GLU A 325     -49.945  45.595 -29.166  1.00 19.68           N  
ATOM   2361  CA  GLU A 325     -48.557  45.985 -28.949  1.00 23.75           C  
ATOM   2362  C   GLU A 325     -48.364  47.495 -28.899  1.00 35.95           C  
ATOM   2363  O   GLU A 325     -47.358  47.958 -28.349  1.00 27.31           O  
ATOM   2364  CB  GLU A 325     -47.657  45.385 -30.036  1.00 29.45           C  
ATOM   2365  CG  GLU A 325     -48.251  45.406 -31.436  1.00 41.12           C  
ATOM   2366  CD  GLU A 325     -47.312  44.824 -32.478  1.00 41.95           C  
ATOM   2367  OE1 GLU A 325     -46.605  45.606 -33.148  1.00 40.27           O  
ATOM   2368  OE2 GLU A 325     -47.274  43.584 -32.620  1.00 37.54           O  
ATOM   2369  N   SER A 326     -49.293  48.266 -29.457  1.00 56.83           N  
ATOM   2370  CA  SER A 326     -49.184  49.721 -29.465  1.00 51.49           C  
ATOM   2371  C   SER A 326     -50.136  50.347 -28.451  1.00 45.95           C  
ATOM   2372  O   SER A 326     -50.779  49.643 -27.672  1.00 39.58           O  
ATOM   2373  CB  SER A 326     -49.465  50.276 -30.864  1.00 31.25           C  
ATOM   2374  OG  SER A 326     -50.782  49.965 -31.286  1.00  6.43           O  
TER    2375      SER A 326                                                      
ATOM   2376  N   MET B   1     -86.823  44.551 -68.209  1.00 15.88           N  
ATOM   2377  CA  MET B   1     -87.980  43.929 -68.843  1.00 44.16           C  
ATOM   2378  C   MET B   1     -89.282  44.432 -68.226  1.00 63.06           C  
ATOM   2379  O   MET B   1     -89.271  45.322 -67.376  1.00 62.29           O  
ATOM   2380  CB  MET B   1     -87.898  42.405 -68.732  1.00 33.33           C  
ATOM   2381  N   VAL B   2     -90.406  43.856 -68.661  1.00 69.57           N  
ATOM   2382  CA  VAL B   2     -91.705  44.267 -68.135  1.00 58.95           C  
ATOM   2383  C   VAL B   2     -91.833  43.880 -66.667  1.00 70.47           C  
ATOM   2384  O   VAL B   2     -92.203  44.703 -65.822  1.00 70.54           O  
ATOM   2385  CB  VAL B   2     -92.844  43.666 -68.978  1.00 30.45           C  
ATOM   2386  CG1 VAL B   2     -94.189  43.939 -68.319  1.00 19.32           C  
ATOM   2387  CG2 VAL B   2     -92.816  44.232 -70.389  1.00 23.88           C  
ATOM   2388  N   HIS B   3     -91.527  42.625 -66.340  1.00 73.33           N  
ATOM   2389  CA  HIS B   3     -91.604  42.156 -64.964  1.00 58.22           C  
ATOM   2390  C   HIS B   3     -90.703  40.941 -64.798  1.00 40.52           C  
ATOM   2391  O   HIS B   3     -90.611  40.102 -65.698  1.00 43.38           O  
ATOM   2392  CB  HIS B   3     -93.045  41.804 -64.570  1.00 45.21           C  
ATOM   2393  CG  HIS B   3     -93.182  41.293 -63.169  1.00 43.18           C  
ATOM   2394  ND1 HIS B   3     -92.834  42.042 -62.065  1.00 42.31           N  
ATOM   2395  CD2 HIS B   3     -93.629  40.107 -62.692  1.00 39.29           C  
ATOM   2396  CE1 HIS B   3     -93.061  41.340 -60.969  1.00 35.25           C  
ATOM   2397  NE2 HIS B   3     -93.543  40.162 -61.322  1.00 37.55           N  
ATOM   2398  N   THR B   4     -90.049  40.856 -63.640  1.00 19.42           N  
ATOM   2399  CA  THR B   4     -89.154  39.755 -63.311  1.00 25.93           C  
ATOM   2400  C   THR B   4     -89.286  39.439 -61.829  1.00 24.48           C  
ATOM   2401  O   THR B   4     -89.944  40.158 -61.072  1.00  7.58           O  
ATOM   2402  CB  THR B   4     -87.690  40.076 -63.645  1.00 15.91           C  
ATOM   2403  OG1 THR B   4     -87.336  41.342 -63.075  1.00  9.81           O  
ATOM   2404  CG2 THR B   4     -87.465  40.105 -65.151  1.00 12.17           C  
ATOM   2405  N   LYS B   5     -88.641  38.347 -61.415  1.00 33.20           N  
ATOM   2406  CA  LYS B   5     -88.683  37.945 -60.014  1.00 31.50           C  
ATOM   2407  C   LYS B   5     -87.867  38.897 -59.148  1.00  6.00           C  
ATOM   2408  O   LYS B   5     -88.384  39.490 -58.193  1.00  5.79           O  
ATOM   2409  CB  LYS B   5     -88.170  36.511 -59.865  1.00 38.25           C  
ATOM   2410  CG  LYS B   5     -88.859  35.494 -60.761  1.00 12.97           C  
ATOM   2411  CD  LYS B   5     -90.304  35.272 -60.354  1.00  4.13           C  
ATOM   2412  CE  LYS B   5     -90.975  34.254 -61.263  1.00 14.04           C  
ATOM   2413  NZ  LYS B   5     -90.238  32.959 -61.285  1.00 33.32           N  
ATOM   2414  N   VAL B   6     -86.586  39.053 -59.467  1.00  6.37           N  
ATOM   2415  CA  VAL B   6     -85.679  39.898 -58.702  1.00 12.49           C  
ATOM   2416  C   VAL B   6     -84.917  40.800 -59.665  1.00 12.54           C  
ATOM   2417  O   VAL B   6     -84.504  40.365 -60.747  1.00  7.36           O  
ATOM   2418  CB  VAL B   6     -84.717  39.049 -57.842  1.00 14.32           C  
ATOM   2419  CG1 VAL B   6     -84.047  37.976 -58.687  1.00 25.97           C  
ATOM   2420  CG2 VAL B   6     -83.683  39.925 -57.146  1.00 18.58           C  
ATOM   2421  N   VAL B   7     -84.757  42.065 -59.282  1.00 12.82           N  
ATOM   2422  CA  VAL B   7     -83.969  43.036 -60.030  1.00  7.13           C  
ATOM   2423  C   VAL B   7     -82.794  43.466 -59.163  1.00  6.66           C  
ATOM   2424  O   VAL B   7     -82.944  43.668 -57.953  1.00  6.61           O  
ATOM   2425  CB  VAL B   7     -84.822  44.249 -60.463  1.00  7.64           C  
ATOM   2426  CG1 VAL B   7     -85.524  44.874 -59.267  1.00  7.64           C  
ATOM   2427  CG2 VAL B   7     -83.967  45.272 -61.194  1.00  7.62           C  
ATOM   2428  N   ILE B   8     -81.618  43.581 -59.775  1.00  6.50           N  
ATOM   2429  CA  ILE B   8     -80.395  43.957 -59.075  1.00 14.13           C  
ATOM   2430  C   ILE B   8     -79.906  45.289 -59.625  1.00 28.43           C  
ATOM   2431  O   ILE B   8     -79.824  45.471 -60.845  1.00 42.48           O  
ATOM   2432  CB  ILE B   8     -79.306  42.877 -59.213  1.00 11.99           C  
ATOM   2433  CG1 ILE B   8     -79.897  41.486 -58.980  1.00 12.18           C  
ATOM   2434  CG2 ILE B   8     -78.161  43.149 -58.248  1.00  7.81           C  
ATOM   2435  CD1 ILE B   8     -78.867  40.382 -58.980  1.00  6.68           C  
ATOM   2436  N   ILE B   9     -79.586  46.214 -58.725  1.00  8.97           N  
ATOM   2437  CA  ILE B   9     -79.089  47.539 -59.078  1.00  8.37           C  
ATOM   2438  C   ILE B   9     -77.620  47.604 -58.676  1.00  8.36           C  
ATOM   2439  O   ILE B   9     -77.293  47.607 -57.482  1.00  4.83           O  
ATOM   2440  CB  ILE B   9     -79.902  48.653 -58.404  1.00 15.90           C  
ATOM   2441  CG1 ILE B   9     -81.396  48.476 -58.689  1.00  5.87           C  
ATOM   2442  CG2 ILE B   9     -79.432  50.018 -58.877  1.00 24.15           C  
ATOM   2443  CD1 ILE B   9     -82.272  49.515 -58.020  1.00  6.40           C  
ATOM   2444  N   GLY B  10     -76.740  47.660 -59.661  1.00  4.12           N  
ATOM   2445  CA  GLY B  10     -75.313  47.748 -59.411  1.00  3.76           C  
ATOM   2446  C   GLY B  10     -74.525  47.029 -60.485  1.00  4.73           C  
ATOM   2447  O   GLY B  10     -75.072  46.346 -61.348  1.00  4.35           O  
ATOM   2448  N   SER B  11     -73.198  47.196 -60.415  1.00 10.88           N  
ATOM   2449  CA  SER B  11     -72.310  46.522 -61.356  1.00 25.18           C  
ATOM   2450  C   SER B  11     -71.029  46.017 -60.699  1.00 38.67           C  
ATOM   2451  O   SER B  11     -70.064  45.703 -61.408  1.00 35.34           O  
ATOM   2452  CB  SER B  11     -71.947  47.447 -62.523  1.00 39.04           C  
ATOM   2453  OG  SER B  11     -71.018  46.824 -63.393  1.00 41.79           O  
ATOM   2454  N   GLY B  12     -70.989  45.930 -59.373  1.00 42.24           N  
ATOM   2455  CA  GLY B  12     -69.803  45.489 -58.680  1.00  5.30           C  
ATOM   2456  C   GLY B  12     -69.813  44.003 -58.395  1.00  6.61           C  
ATOM   2457  O   GLY B  12     -70.672  43.258 -58.878  1.00 25.49           O  
ATOM   2458  N   PRO B  13     -68.837  43.540 -57.607  1.00  9.71           N  
ATOM   2459  CA  PRO B  13     -68.807  42.113 -57.243  1.00 15.10           C  
ATOM   2460  C   PRO B  13     -70.064  41.639 -56.532  1.00  8.71           C  
ATOM   2461  O   PRO B  13     -70.525  40.520 -56.782  1.00  8.82           O  
ATOM   2462  CB  PRO B  13     -67.569  42.014 -56.341  1.00  8.98           C  
ATOM   2463  CG  PRO B  13     -66.698  43.139 -56.784  1.00  8.90           C  
ATOM   2464  CD  PRO B  13     -67.636  44.255 -57.144  1.00  7.36           C  
ATOM   2465  N   ALA B  14     -70.633  42.462 -55.649  1.00  8.00           N  
ATOM   2466  CA  ALA B  14     -71.868  42.074 -54.973  1.00  7.88           C  
ATOM   2467  C   ALA B  14     -73.023  41.950 -55.959  1.00  7.70           C  
ATOM   2468  O   ALA B  14     -73.820  41.008 -55.878  1.00 12.60           O  
ATOM   2469  CB  ALA B  14     -72.205  43.080 -53.874  1.00  7.84           C  
ATOM   2470  N   ALA B  15     -73.133  42.895 -56.894  1.00  7.03           N  
ATOM   2471  CA  ALA B  15     -74.249  42.873 -57.832  1.00  8.55           C  
ATOM   2472  C   ALA B  15     -74.159  41.698 -58.797  1.00  9.04           C  
ATOM   2473  O   ALA B  15     -75.192  41.199 -59.260  1.00 18.13           O  
ATOM   2474  CB  ALA B  15     -74.313  44.189 -58.605  1.00  7.63           C  
ATOM   2475  N   HIS B  16     -72.947  41.237 -59.108  1.00  7.07           N  
ATOM   2476  CA  HIS B  16     -72.783  40.159 -60.075  1.00  7.40           C  
ATOM   2477  C   HIS B  16     -72.853  38.776 -59.435  1.00 10.18           C  
ATOM   2478  O   HIS B  16     -73.471  37.870 -60.005  1.00 24.04           O  
ATOM   2479  CB  HIS B  16     -71.464  40.327 -60.834  1.00  7.72           C  
ATOM   2480  CG  HIS B  16     -71.549  41.294 -61.974  1.00 17.85           C  
ATOM   2481  ND1 HIS B  16     -71.982  40.929 -63.231  1.00 15.08           N  
ATOM   2482  CD2 HIS B  16     -71.263  42.616 -62.045  1.00 18.28           C  
ATOM   2483  CE1 HIS B  16     -71.958  41.983 -64.027  1.00  7.32           C  
ATOM   2484  NE2 HIS B  16     -71.525  43.019 -63.332  1.00 15.92           N  
ATOM   2485  N   THR B  17     -72.226  38.583 -58.271  1.00  7.67           N  
ATOM   2486  CA  THR B  17     -72.353  37.303 -57.576  1.00  7.66           C  
ATOM   2487  C   THR B  17     -73.809  37.003 -57.250  1.00 16.34           C  
ATOM   2488  O   THR B  17     -74.248  35.850 -57.336  1.00 13.17           O  
ATOM   2489  CB  THR B  17     -71.515  37.295 -56.298  1.00 14.75           C  
ATOM   2490  OG1 THR B  17     -71.919  38.375 -55.449  1.00 73.46           O  
ATOM   2491  CG2 THR B  17     -70.056  37.443 -56.629  1.00  8.49           C  
ATOM   2492  N   ALA B  18     -74.572  38.028 -56.864  1.00 18.48           N  
ATOM   2493  CA  ALA B  18     -76.007  37.848 -56.682  1.00  7.06           C  
ATOM   2494  C   ALA B  18     -76.674  37.451 -57.991  1.00  7.00           C  
ATOM   2495  O   ALA B  18     -77.556  36.584 -58.009  1.00  6.89           O  
ATOM   2496  CB  ALA B  18     -76.634  39.125 -56.124  1.00  7.39           C  
ATOM   2497  N   ALA B  19     -76.257  38.064 -59.101  1.00 11.89           N  
ATOM   2498  CA  ALA B  19     -76.821  37.705 -60.398  1.00  7.51           C  
ATOM   2499  C   ALA B  19     -76.422  36.292 -60.806  1.00  7.96           C  
ATOM   2500  O   ALA B  19     -77.209  35.581 -61.437  1.00  8.39           O  
ATOM   2501  CB  ALA B  19     -76.386  38.715 -61.460  1.00  7.76           C  
ATOM   2502  N   ILE B  20     -75.204  35.869 -60.455  1.00 14.64           N  
ATOM   2503  CA  ILE B  20     -74.749  34.527 -60.815  1.00  8.56           C  
ATOM   2504  C   ILE B  20     -75.592  33.472 -60.109  1.00  8.09           C  
ATOM   2505  O   ILE B  20     -76.105  32.537 -60.736  1.00  8.54           O  
ATOM   2506  CB  ILE B  20     -73.254  34.361 -60.488  1.00  9.26           C  
ATOM   2507  CG1 ILE B  20     -72.401  35.247 -61.400  1.00  9.20           C  
ATOM   2508  CG2 ILE B  20     -72.842  32.901 -60.614  1.00 11.06           C  
ATOM   2509  CD1 ILE B  20     -70.935  35.281 -61.019  1.00  9.45           C  
ATOM   2510  N   TYR B  21     -75.744  33.606 -58.790  1.00  7.30           N  
ATOM   2511  CA  TYR B  21     -76.507  32.622 -58.029  1.00  6.74           C  
ATOM   2512  C   TYR B  21     -77.995  32.692 -58.354  1.00 29.76           C  
ATOM   2513  O   TYR B  21     -78.669  31.658 -58.423  1.00 64.62           O  
ATOM   2514  CB  TYR B  21     -76.273  32.823 -56.531  1.00  6.28           C  
ATOM   2515  CG  TYR B  21     -75.016  32.163 -56.006  1.00  8.59           C  
ATOM   2516  CD1 TYR B  21     -73.782  32.791 -56.106  1.00  6.88           C  
ATOM   2517  CD2 TYR B  21     -75.066  30.911 -55.406  1.00 57.64           C  
ATOM   2518  CE1 TYR B  21     -72.632  32.190 -55.627  1.00  7.21           C  
ATOM   2519  CE2 TYR B  21     -73.923  30.302 -54.924  1.00 62.42           C  
ATOM   2520  CZ  TYR B  21     -72.708  30.945 -55.037  1.00 40.84           C  
ATOM   2521  OH  TYR B  21     -71.568  30.340 -54.557  1.00 50.80           O  
ATOM   2522  N   LEU B  22     -78.523  33.902 -58.558  1.00 20.08           N  
ATOM   2523  CA  LEU B  22     -79.944  34.047 -58.858  1.00  6.63           C  
ATOM   2524  C   LEU B  22     -80.283  33.550 -60.258  1.00  7.23           C  
ATOM   2525  O   LEU B  22     -81.372  33.006 -60.472  1.00 24.72           O  
ATOM   2526  CB  LEU B  22     -80.360  35.508 -58.693  1.00  6.66           C  
ATOM   2527  CG  LEU B  22     -80.729  35.949 -57.274  1.00  6.50           C  
ATOM   2528  CD1 LEU B  22     -80.788  37.468 -57.175  1.00  6.63           C  
ATOM   2529  CD2 LEU B  22     -82.043  35.332 -56.832  1.00  6.13           C  
ATOM   2530  N   SER B  23     -79.372  33.721 -61.220  1.00  8.12           N  
ATOM   2531  CA  SER B  23     -79.633  33.258 -62.580  1.00  9.37           C  
ATOM   2532  C   SER B  23     -79.434  31.754 -62.711  1.00  9.65           C  
ATOM   2533  O   SER B  23     -80.155  31.097 -63.470  1.00 17.92           O  
ATOM   2534  CB  SER B  23     -78.742  33.997 -63.577  1.00 10.51           C  
ATOM   2535  OG  SER B  23     -77.379  33.903 -63.207  1.00 24.30           O  
ATOM   2536  N   ARG B  24     -78.459  31.195 -61.990  1.00  9.18           N  
ATOM   2537  CA  ARG B  24     -78.276  29.749 -61.999  1.00 21.06           C  
ATOM   2538  C   ARG B  24     -79.441  29.019 -61.343  1.00 21.51           C  
ATOM   2539  O   ARG B  24     -79.676  27.847 -61.656  1.00  7.91           O  
ATOM   2540  CB  ARG B  24     -76.965  29.376 -61.303  1.00 12.03           C  
ATOM   2541  CG  ARG B  24     -76.463  27.987 -61.659  1.00 21.21           C  
ATOM   2542  CD  ARG B  24     -75.226  27.607 -60.866  1.00  9.46           C  
ATOM   2543  NE  ARG B  24     -74.542  26.460 -61.456  1.00 10.53           N  
ATOM   2544  CZ  ARG B  24     -73.646  25.715 -60.817  1.00 13.87           C  
ATOM   2545  NH1 ARG B  24     -73.326  25.993 -59.560  1.00 29.28           N  
ATOM   2546  NH2 ARG B  24     -73.075  24.690 -61.432  1.00 13.15           N  
ATOM   2547  N   ALA B  25     -80.172  29.681 -60.447  1.00 20.72           N  
ATOM   2548  CA  ALA B  25     -81.377  29.121 -59.853  1.00  5.89           C  
ATOM   2549  C   ALA B  25     -82.612  29.308 -60.729  1.00 12.54           C  
ATOM   2550  O   ALA B  25     -83.733  29.156 -60.228  1.00 44.10           O  
ATOM   2551  CB  ALA B  25     -81.619  29.734 -58.471  1.00  5.20           C  
ATOM   2552  N   GLU B  26     -82.428  29.640 -62.009  1.00  7.34           N  
ATOM   2553  CA  GLU B  26     -83.506  29.740 -62.994  1.00 32.09           C  
ATOM   2554  C   GLU B  26     -84.504  30.852 -62.666  1.00 31.10           C  
ATOM   2555  O   GLU B  26     -85.656  30.803 -63.109  1.00 19.83           O  
ATOM   2556  CB  GLU B  26     -84.244  28.401 -63.141  1.00 52.38           C  
ATOM   2557  CG  GLU B  26     -83.387  27.257 -63.677  1.00 53.30           C  
ATOM   2558  CD  GLU B  26     -83.090  27.373 -65.161  1.00 53.32           C  
ATOM   2559  OE1 GLU B  26     -83.932  27.925 -65.900  1.00 64.29           O  
ATOM   2560  OE2 GLU B  26     -82.012  26.908 -65.590  1.00 47.54           O  
ATOM   2561  N   LEU B  27     -84.098  31.857 -61.889  1.00 29.01           N  
ATOM   2562  CA  LEU B  27     -85.016  32.905 -61.456  1.00 24.26           C  
ATOM   2563  C   LEU B  27     -85.117  34.086 -62.417  1.00 29.55           C  
ATOM   2564  O   LEU B  27     -85.940  34.978 -62.179  1.00 49.60           O  
ATOM   2565  CB  LEU B  27     -84.619  33.416 -60.068  1.00  5.84           C  
ATOM   2566  CG  LEU B  27     -85.511  32.940 -58.918  1.00  4.73           C  
ATOM   2567  CD1 LEU B  27     -85.460  31.427 -58.777  1.00 29.04           C  
ATOM   2568  CD2 LEU B  27     -85.114  33.610 -57.616  1.00  4.68           C  
ATOM   2569  N   LYS B  28     -84.310  34.122 -63.481  1.00  9.19           N  
ATOM   2570  CA  LYS B  28     -84.348  35.183 -64.487  1.00 10.66           C  
ATOM   2571  C   LYS B  28     -84.175  36.563 -63.860  1.00 13.26           C  
ATOM   2572  O   LYS B  28     -85.127  37.354 -63.829  1.00  9.92           O  
ATOM   2573  CB  LYS B  28     -85.662  35.133 -65.273  1.00 11.42           C  
ATOM   2574  CG  LYS B  28     -86.017  33.762 -65.824  1.00 11.66           C  
ATOM   2575  CD  LYS B  28     -87.445  33.735 -66.348  1.00 12.11           C  
ATOM   2576  CE  LYS B  28     -87.875  32.324 -66.721  1.00 22.24           C  
ATOM   2577  NZ  LYS B  28     -89.309  32.266 -67.121  1.00 18.87           N  
ATOM   2578  N   PRO B  29     -82.989  36.891 -63.355  1.00 17.87           N  
ATOM   2579  CA  PRO B  29     -82.759  38.211 -62.764  1.00 10.21           C  
ATOM   2580  C   PRO B  29     -82.305  39.237 -63.790  1.00 19.51           C  
ATOM   2581  O   PRO B  29     -81.600  38.931 -64.754  1.00 30.84           O  
ATOM   2582  CB  PRO B  29     -81.651  37.938 -61.735  1.00  8.00           C  
ATOM   2583  CG  PRO B  29     -80.980  36.651 -62.195  1.00  8.51           C  
ATOM   2584  CD  PRO B  29     -81.759  36.085 -63.358  1.00 17.11           C  
ATOM   2585  N   VAL B  30     -82.730  40.479 -63.568  1.00 18.97           N  
ATOM   2586  CA  VAL B  30     -82.350  41.612 -64.406  1.00 12.16           C  
ATOM   2587  C   VAL B  30     -81.386  42.490 -63.620  1.00  8.55           C  
ATOM   2588  O   VAL B  30     -81.645  42.829 -62.458  1.00  7.73           O  
ATOM   2589  CB  VAL B  30     -83.577  42.416 -64.874  1.00 10.56           C  
ATOM   2590  CG1 VAL B  30     -84.323  41.659 -65.955  1.00 12.31           C  
ATOM   2591  CG2 VAL B  30     -84.504  42.701 -63.711  1.00  9.72           C  
ATOM   2592  N   LEU B  31     -80.270  42.843 -64.251  1.00  8.50           N  
ATOM   2593  CA  LEU B  31     -79.195  43.598 -63.619  1.00  7.41           C  
ATOM   2594  C   LEU B  31     -79.095  44.981 -64.249  1.00 16.55           C  
ATOM   2595  O   LEU B  31     -78.897  45.102 -65.463  1.00  7.60           O  
ATOM   2596  CB  LEU B  31     -77.865  42.857 -63.757  1.00  7.43           C  
ATOM   2597  CG  LEU B  31     -76.626  43.482 -63.109  1.00  6.55           C  
ATOM   2598  CD1 LEU B  31     -76.809  43.628 -61.614  1.00  6.05           C  
ATOM   2599  CD2 LEU B  31     -75.381  42.665 -63.422  1.00  6.91           C  
ATOM   2600  N   TYR B  32     -79.224  46.017 -63.423  1.00 15.56           N  
ATOM   2601  CA  TYR B  32     -79.069  47.399 -63.869  1.00  5.68           C  
ATOM   2602  C   TYR B  32     -77.657  47.823 -63.488  1.00 12.91           C  
ATOM   2603  O   TYR B  32     -77.400  48.225 -62.350  1.00 39.72           O  
ATOM   2604  CB  TYR B  32     -80.118  48.310 -63.242  1.00  5.62           C  
ATOM   2605  CG  TYR B  32     -81.439  48.317 -63.971  1.00  6.71           C  
ATOM   2606  CD1 TYR B  32     -81.630  49.121 -65.086  1.00  6.99           C  
ATOM   2607  CD2 TYR B  32     -82.497  47.524 -63.546  1.00 17.71           C  
ATOM   2608  CE1 TYR B  32     -82.834  49.137 -65.756  1.00  8.27           C  
ATOM   2609  CE2 TYR B  32     -83.708  47.532 -64.214  1.00 11.40           C  
ATOM   2610  CZ  TYR B  32     -83.870  48.342 -65.318  1.00  9.26           C  
ATOM   2611  OH  TYR B  32     -85.068  48.359 -65.993  1.00 10.75           O  
ATOM   2612  N   GLU B  33     -76.743  47.734 -64.452  1.00  4.56           N  
ATOM   2613  CA  GLU B  33     -75.350  48.086 -64.216  1.00  3.68           C  
ATOM   2614  C   GLU B  33     -75.103  49.587 -64.232  1.00  9.69           C  
ATOM   2615  O   GLU B  33     -74.087  50.036 -63.691  1.00 34.98           O  
ATOM   2616  CB  GLU B  33     -74.448  47.395 -65.242  1.00  4.08           C  
ATOM   2617  CG  GLU B  33     -74.853  47.603 -66.686  1.00 22.81           C  
ATOM   2618  CD  GLU B  33     -73.946  46.862 -67.652  1.00 37.89           C  
ATOM   2619  OE1 GLU B  33     -74.093  47.055 -68.877  1.00 46.82           O  
ATOM   2620  OE2 GLU B  33     -73.087  46.085 -67.184  1.00 26.73           O  
ATOM   2621  N   GLY B  34     -75.985  50.370 -64.841  1.00  2.47           N  
ATOM   2622  CA  GLY B  34     -75.749  51.789 -64.991  1.00  1.95           C  
ATOM   2623  C   GLY B  34     -75.282  52.123 -66.395  1.00 13.76           C  
ATOM   2624  O   GLY B  34     -74.989  51.252 -67.216  1.00 17.78           O  
ATOM   2625  N   MET B  35     -75.218  53.425 -66.674  1.00 25.97           N  
ATOM   2626  CA  MET B  35     -74.769  53.906 -67.975  1.00  1.96           C  
ATOM   2627  C   MET B  35     -73.253  54.042 -68.053  1.00  1.95           C  
ATOM   2628  O   MET B  35     -72.746  54.921 -68.762  1.00 48.48           O  
ATOM   2629  CB  MET B  35     -75.437  55.246 -68.289  1.00  1.95           C  
ATOM   2630  CG  MET B  35     -75.711  55.492 -69.766  1.00  1.95           C  
ATOM   2631  SD  MET B  35     -75.678  57.249 -70.184  1.00 29.37           S  
ATOM   2632  CE  MET B  35     -76.230  57.987 -68.649  1.00 40.65           C  
ATOM   2633  N   LEU B  36     -72.520  53.172 -67.362  1.00  1.95           N  
ATOM   2634  CA  LEU B  36     -71.072  53.284 -67.210  1.00  9.93           C  
ATOM   2635  C   LEU B  36     -70.530  52.099 -66.413  1.00 19.22           C  
ATOM   2636  O   LEU B  36     -71.187  51.062 -66.286  1.00  1.95           O  
ATOM   2637  CB  LEU B  36     -70.693  54.595 -66.519  1.00 10.50           C  
ATOM   2638  N   GLY B  44     -68.479  49.324 -61.829  1.00 53.49           N  
ATOM   2639  CA  GLY B  44     -68.048  49.383 -60.445  1.00 58.79           C  
ATOM   2640  C   GLY B  44     -66.795  50.209 -60.243  1.00 82.86           C  
ATOM   2641  O   GLY B  44     -66.100  50.537 -61.204  1.00 98.71           O  
ATOM   2642  N   GLN B  45     -66.502  50.548 -58.985  1.00 87.15           N  
ATOM   2643  CA  GLN B  45     -65.267  51.255 -58.671  1.00 65.74           C  
ATOM   2644  C   GLN B  45     -64.038  50.381 -58.865  1.00 72.97           C  
ATOM   2645  O   GLN B  45     -62.915  50.896 -58.819  1.00 43.82           O  
ATOM   2646  CB  GLN B  45     -65.303  51.775 -57.234  1.00 19.95           C  
ATOM   2647  N   LEU B  46     -64.229  49.078 -59.070  1.00 86.89           N  
ATOM   2648  CA  LEU B  46     -63.124  48.162 -59.304  1.00 55.42           C  
ATOM   2649  C   LEU B  46     -62.584  48.240 -60.726  1.00 52.80           C  
ATOM   2650  O   LEU B  46     -61.460  47.790 -60.973  1.00 48.05           O  
ATOM   2651  CB  LEU B  46     -63.574  46.736 -58.992  1.00  5.06           C  
ATOM   2652  CG  LEU B  46     -62.510  45.829 -58.390  1.00  6.94           C  
ATOM   2653  CD1 LEU B  46     -61.736  46.559 -57.304  1.00 21.05           C  
ATOM   2654  CD2 LEU B  46     -63.154  44.581 -57.832  1.00  8.38           C  
ATOM   2655  N   THR B  47     -63.361  48.793 -61.662  1.00 63.24           N  
ATOM   2656  CA  THR B  47     -62.897  48.951 -63.036  1.00 58.63           C  
ATOM   2657  C   THR B  47     -61.716  49.910 -63.134  1.00 49.79           C  
ATOM   2658  O   THR B  47     -60.920  49.807 -64.074  1.00 48.95           O  
ATOM   2659  CB  THR B  47     -64.050  49.437 -63.921  1.00 48.55           C  
ATOM   2660  OG1 THR B  47     -65.220  48.654 -63.655  1.00 46.65           O  
ATOM   2661  CG2 THR B  47     -63.696  49.307 -65.397  1.00 38.58           C  
ATOM   2662  N   THR B  48     -61.573  50.825 -62.173  1.00 39.86           N  
ATOM   2663  CA  THR B  48     -60.470  51.778 -62.200  1.00 56.10           C  
ATOM   2664  C   THR B  48     -59.163  51.156 -61.722  1.00 64.81           C  
ATOM   2665  O   THR B  48     -58.087  51.586 -62.153  1.00 34.35           O  
ATOM   2666  CB  THR B  48     -60.805  53.003 -61.344  1.00 51.68           C  
ATOM   2667  OG1 THR B  48     -61.139  52.586 -60.014  1.00 58.63           O  
ATOM   2668  CG2 THR B  48     -61.979  53.768 -61.940  1.00 36.29           C  
ATOM   2669  N   THR B  49     -59.235  50.151 -60.849  1.00 70.65           N  
ATOM   2670  CA  THR B  49     -58.029  49.516 -60.333  1.00 51.49           C  
ATOM   2671  C   THR B  49     -57.272  48.815 -61.455  1.00 30.62           C  
ATOM   2672  O   THR B  49     -57.867  48.178 -62.328  1.00 12.37           O  
ATOM   2673  CB  THR B  49     -58.390  48.512 -59.235  1.00 35.06           C  
ATOM   2674  OG1 THR B  49     -59.279  49.127 -58.294  1.00 23.31           O  
ATOM   2675  CG2 THR B  49     -57.138  48.034 -58.506  1.00 17.68           C  
ATOM   2676  N   THR B  50     -55.944  48.936 -61.424  1.00 33.22           N  
ATOM   2677  CA  THR B  50     -55.120  48.367 -62.485  1.00 35.22           C  
ATOM   2678  C   THR B  50     -54.885  46.875 -62.275  1.00 20.68           C  
ATOM   2679  O   THR B  50     -55.042  46.080 -63.208  1.00 39.95           O  
ATOM   2680  CB  THR B  50     -53.788  49.116 -62.575  1.00 28.31           C  
ATOM   2681  OG1 THR B  50     -53.163  49.142 -61.287  1.00  7.53           O  
ATOM   2682  CG2 THR B  50     -54.012  50.544 -63.055  1.00  1.95           C  
ATOM   2683  N   ASP B  51     -54.512  46.475 -61.060  1.00  6.38           N  
ATOM   2684  CA  ASP B  51     -54.213  45.079 -60.764  1.00 13.23           C  
ATOM   2685  C   ASP B  51     -54.694  44.736 -59.364  1.00 23.37           C  
ATOM   2686  O   ASP B  51     -54.324  45.407 -58.395  1.00 12.46           O  
ATOM   2687  CB  ASP B  51     -52.711  44.794 -60.887  1.00 20.83           C  
ATOM   2688  CG  ASP B  51     -52.281  44.540 -62.318  1.00 44.48           C  
ATOM   2689  OD1 ASP B  51     -53.089  43.991 -63.097  1.00 48.95           O  
ATOM   2690  OD2 ASP B  51     -51.134  44.892 -62.666  1.00 54.81           O  
ATOM   2691  N   ILE B  52     -55.516  43.694 -59.265  1.00 29.22           N  
ATOM   2692  CA  ILE B  52     -55.994  43.173 -57.990  1.00 13.98           C  
ATOM   2693  C   ILE B  52     -55.192  41.924 -57.660  1.00 23.16           C  
ATOM   2694  O   ILE B  52     -55.220  40.945 -58.415  1.00 40.31           O  
ATOM   2695  CB  ILE B  52     -57.493  42.849 -58.044  1.00 13.82           C  
ATOM   2696  CG1 ILE B  52     -58.289  44.081 -58.458  1.00 14.17           C  
ATOM   2697  CG2 ILE B  52     -57.969  42.325 -56.698  1.00 14.54           C  
ATOM   2698  CD1 ILE B  52     -59.727  43.776 -58.715  1.00 16.57           C  
ATOM   2699  N   GLU B  53     -54.493  41.944 -56.529  1.00 28.24           N  
ATOM   2700  CA  GLU B  53     -53.658  40.822 -56.135  1.00 30.05           C  
ATOM   2701  C   GLU B  53     -54.105  40.138 -54.852  1.00 20.06           C  
ATOM   2702  O   GLU B  53     -53.576  39.069 -54.530  1.00 21.87           O  
ATOM   2703  CB  GLU B  53     -52.195  41.270 -55.999  1.00 22.55           C  
ATOM   2704  CG  GLU B  53     -51.698  42.031 -57.217  1.00 18.51           C  
ATOM   2705  CD  GLU B  53     -50.192  42.151 -57.260  1.00 46.76           C  
ATOM   2706  OE1 GLU B  53     -49.568  42.191 -56.181  1.00 61.10           O  
ATOM   2707  OE2 GLU B  53     -49.632  42.197 -58.376  1.00 61.56           O  
ATOM   2708  N   ASN B  54     -55.062  40.709 -54.119  1.00 17.61           N  
ATOM   2709  CA  ASN B  54     -55.546  40.129 -52.874  1.00 16.33           C  
ATOM   2710  C   ASN B  54     -56.880  39.409 -53.045  1.00 16.54           C  
ATOM   2711  O   ASN B  54     -57.617  39.246 -52.067  1.00 14.58           O  
ATOM   2712  CB  ASN B  54     -55.667  41.207 -51.796  1.00 13.21           C  
ATOM   2713  CG  ASN B  54     -56.688  42.266 -52.147  1.00 12.05           C  
ATOM   2714  OD1 ASN B  54     -57.068  42.419 -53.307  1.00 25.89           O  
ATOM   2715  ND2 ASN B  54     -57.144  43.003 -51.140  1.00  9.64           N  
ATOM   2716  N   PHE B  55     -57.217  38.991 -54.279  1.00 18.22           N  
ATOM   2717  CA  PHE B  55     -58.429  38.219 -54.534  1.00 17.93           C  
ATOM   2718  C   PHE B  55     -58.086  36.742 -54.629  1.00 32.44           C  
ATOM   2719  O   PHE B  55     -57.221  36.367 -55.434  1.00 59.82           O  
ATOM   2720  CB  PHE B  55     -59.097  38.682 -55.827  1.00 24.72           C  
ATOM   2721  CG  PHE B  55     -60.544  38.281 -55.947  1.00 16.16           C  
ATOM   2722  CD1 PHE B  55     -60.898  37.062 -56.503  1.00 16.70           C  
ATOM   2723  CD2 PHE B  55     -61.550  39.130 -55.513  1.00 14.39           C  
ATOM   2724  CE1 PHE B  55     -62.228  36.695 -56.617  1.00 15.32           C  
ATOM   2725  CE2 PHE B  55     -62.880  38.768 -55.624  1.00 13.27           C  
ATOM   2726  CZ  PHE B  55     -63.219  37.549 -56.177  1.00 13.66           C  
ATOM   2727  N   PRO B  56     -58.725  35.877 -53.841  1.00 26.90           N  
ATOM   2728  CA  PRO B  56     -58.336  34.461 -53.838  1.00 14.58           C  
ATOM   2729  C   PRO B  56     -58.742  33.764 -55.128  1.00 16.15           C  
ATOM   2730  O   PRO B  56     -59.845  33.960 -55.644  1.00 30.60           O  
ATOM   2731  CB  PRO B  56     -59.085  33.891 -52.629  1.00 10.20           C  
ATOM   2732  CG  PRO B  56     -60.279  34.772 -52.493  1.00 16.14           C  
ATOM   2733  CD  PRO B  56     -59.824  36.150 -52.898  1.00 20.07           C  
ATOM   2734  N   GLY B  57     -57.835  32.934 -55.639  1.00 16.44           N  
ATOM   2735  CA  GLY B  57     -58.026  32.230 -56.891  1.00 16.37           C  
ATOM   2736  C   GLY B  57     -57.199  32.768 -58.038  1.00 27.25           C  
ATOM   2737  O   GLY B  57     -57.108  32.106 -59.080  1.00 17.90           O  
ATOM   2738  N   PHE B  58     -56.585  33.943 -57.878  1.00 31.96           N  
ATOM   2739  CA  PHE B  58     -55.739  34.562 -58.896  1.00 25.93           C  
ATOM   2740  C   PHE B  58     -54.379  34.837 -58.264  1.00 29.07           C  
ATOM   2741  O   PHE B  58     -54.107  35.958 -57.808  1.00 38.44           O  
ATOM   2742  CB  PHE B  58     -56.371  35.839 -59.448  1.00 23.83           C  
ATOM   2743  CG  PHE B  58     -57.756  35.640 -59.998  1.00 21.16           C  
ATOM   2744  CD1 PHE B  58     -57.945  35.260 -61.317  1.00 19.29           C  
ATOM   2745  CD2 PHE B  58     -58.869  35.833 -59.195  1.00 20.22           C  
ATOM   2746  CE1 PHE B  58     -59.217  35.075 -61.826  1.00 17.04           C  
ATOM   2747  CE2 PHE B  58     -60.144  35.651 -59.699  1.00 18.11           C  
ATOM   2748  CZ  PHE B  58     -60.318  35.272 -61.017  1.00 16.70           C  
ATOM   2749  N   PRO B  59     -53.501  33.831 -58.214  1.00 30.09           N  
ATOM   2750  CA  PRO B  59     -52.220  34.018 -57.516  1.00 33.61           C  
ATOM   2751  C   PRO B  59     -51.293  35.006 -58.196  1.00 34.32           C  
ATOM   2752  O   PRO B  59     -50.467  35.628 -57.517  1.00 37.49           O  
ATOM   2753  CB  PRO B  59     -51.622  32.605 -57.503  1.00 29.51           C  
ATOM   2754  CG  PRO B  59     -52.231  31.940 -58.697  1.00 26.39           C  
ATOM   2755  CD  PRO B  59     -53.625  32.488 -58.804  1.00 25.07           C  
ATOM   2756  N   ASP B  60     -51.405  35.178 -59.512  1.00 31.78           N  
ATOM   2757  CA  ASP B  60     -50.583  36.128 -60.246  1.00 30.25           C  
ATOM   2758  C   ASP B  60     -51.251  37.489 -60.389  1.00 27.22           C  
ATOM   2759  O   ASP B  60     -50.812  38.303 -61.209  1.00 38.40           O  
ATOM   2760  CB  ASP B  60     -50.232  35.565 -61.625  1.00 28.29           C  
ATOM   2761  CG  ASP B  60     -49.394  34.301 -61.545  1.00 46.54           C  
ATOM   2762  OD1 ASP B  60     -48.609  34.166 -60.582  1.00 55.61           O  
ATOM   2763  OD2 ASP B  60     -49.518  33.445 -62.445  1.00 55.49           O  
ATOM   2764  N   GLY B  61     -52.296  37.754 -59.608  1.00 26.96           N  
ATOM   2765  CA  GLY B  61     -53.026  39.000 -59.720  1.00 23.75           C  
ATOM   2766  C   GLY B  61     -53.916  39.034 -60.945  1.00 21.80           C  
ATOM   2767  O   GLY B  61     -53.724  38.252 -61.880  1.00 22.01           O  
ATOM   2768  N   ILE B  62     -54.898  39.931 -60.951  1.00 19.49           N  
ATOM   2769  CA  ILE B  62     -55.807  40.077 -62.083  1.00 17.52           C  
ATOM   2770  C   ILE B  62     -56.204  41.542 -62.191  1.00 14.68           C  
ATOM   2771  O   ILE B  62     -56.386  42.226 -61.179  1.00 14.17           O  
ATOM   2772  CB  ILE B  62     -57.039  39.152 -61.942  1.00 18.30           C  
ATOM   2773  CG1 ILE B  62     -57.946  39.258 -63.173  1.00 16.26           C  
ATOM   2774  CG2 ILE B  62     -57.806  39.452 -60.658  1.00 20.95           C  
ATOM   2775  CD1 ILE B  62     -59.194  38.404 -63.093  1.00 16.00           C  
ATOM   2776  N   GLY B  63     -56.310  42.029 -63.424  1.00 12.63           N  
ATOM   2777  CA  GLY B  63     -56.746  43.397 -63.637  1.00  9.97           C  
ATOM   2778  C   GLY B  63     -58.195  43.588 -63.223  1.00  9.58           C  
ATOM   2779  O   GLY B  63     -59.059  42.753 -63.495  1.00 21.04           O  
ATOM   2780  N   GLY B  64     -58.455  44.702 -62.537  1.00  8.09           N  
ATOM   2781  CA  GLY B  64     -59.809  44.992 -62.099  1.00  7.49           C  
ATOM   2782  C   GLY B  64     -60.800  45.100 -63.240  1.00  6.50           C  
ATOM   2783  O   GLY B  64     -61.980  44.779 -63.074  1.00 11.82           O  
ATOM   2784  N   ALA B  65     -60.339  45.545 -64.411  1.00  5.26           N  
ATOM   2785  CA  ALA B  65     -61.226  45.652 -65.564  1.00  4.38           C  
ATOM   2786  C   ALA B  65     -61.668  44.279 -66.057  1.00 19.69           C  
ATOM   2787  O   ALA B  65     -62.861  44.045 -66.284  1.00  6.08           O  
ATOM   2788  CB  ALA B  65     -60.535  46.431 -66.684  1.00 17.83           C  
ATOM   2789  N   GLU B  66     -60.718  43.355 -66.231  1.00 43.66           N  
ATOM   2790  CA  GLU B  66     -61.068  42.033 -66.742  1.00 22.65           C  
ATOM   2791  C   GLU B  66     -61.774  41.186 -65.691  1.00 22.16           C  
ATOM   2792  O   GLU B  66     -62.580  40.316 -66.043  1.00 57.51           O  
ATOM   2793  CB  GLU B  66     -59.826  41.312 -67.269  1.00  8.80           C  
ATOM   2794  CG  GLU B  66     -58.736  41.068 -66.247  1.00 36.21           C  
ATOM   2795  CD  GLU B  66     -57.624  40.195 -66.795  1.00 49.47           C  
ATOM   2796  OE1 GLU B  66     -57.904  39.374 -67.694  1.00 47.34           O  
ATOM   2797  OE2 GLU B  66     -56.471  40.333 -66.334  1.00 55.24           O  
ATOM   2798  N   LEU B  67     -61.483  41.409 -64.407  1.00 10.81           N  
ATOM   2799  CA  LEU B  67     -62.182  40.675 -63.356  1.00 11.94           C  
ATOM   2800  C   LEU B  67     -63.676  40.969 -63.395  1.00 14.60           C  
ATOM   2801  O   LEU B  67     -64.503  40.053 -63.313  1.00 29.69           O  
ATOM   2802  CB  LEU B  67     -61.599  41.019 -61.987  1.00 12.73           C  
ATOM   2803  CG  LEU B  67     -62.279  40.303 -60.818  1.00 13.13           C  
ATOM   2804  CD1 LEU B  67     -62.223  38.793 -61.001  1.00 13.93           C  
ATOM   2805  CD2 LEU B  67     -61.652  40.708 -59.497  1.00 13.80           C  
ATOM   2806  N   MET B  68     -64.041  42.248 -63.512  1.00  9.27           N  
ATOM   2807  CA  MET B  68     -65.449  42.601 -63.643  1.00  8.30           C  
ATOM   2808  C   MET B  68     -66.023  42.166 -64.983  1.00 16.29           C  
ATOM   2809  O   MET B  68     -67.240  41.985 -65.092  1.00 27.34           O  
ATOM   2810  CB  MET B  68     -65.644  44.107 -63.462  1.00 19.84           C  
ATOM   2811  CG  MET B  68     -65.372  44.609 -62.056  1.00 36.13           C  
ATOM   2812  SD  MET B  68     -66.333  43.708 -60.824  1.00 17.55           S  
ATOM   2813  CE  MET B  68     -65.074  42.647 -60.123  1.00 33.18           C  
ATOM   2814  N   GLU B  69     -65.178  41.997 -66.001  1.00  8.23           N  
ATOM   2815  CA  GLU B  69     -65.647  41.446 -67.266  1.00  8.14           C  
ATOM   2816  C   GLU B  69     -65.872  39.943 -67.159  1.00 19.57           C  
ATOM   2817  O   GLU B  69     -66.834  39.414 -67.729  1.00 40.02           O  
ATOM   2818  CB  GLU B  69     -64.651  41.762 -68.383  1.00 15.80           C  
ATOM   2819  CG  GLU B  69     -65.129  41.366 -69.773  1.00 44.37           C  
ATOM   2820  CD  GLU B  69     -66.288  42.218 -70.263  1.00 67.35           C  
ATOM   2821  OE1 GLU B  69     -66.480  43.332 -69.731  1.00 69.25           O  
ATOM   2822  OE2 GLU B  69     -67.008  41.773 -71.183  1.00 73.87           O  
ATOM   2823  N   ASN B  70     -64.995  39.241 -66.437  1.00 23.52           N  
ATOM   2824  CA  ASN B  70     -65.230  37.829 -66.153  1.00 10.07           C  
ATOM   2825  C   ASN B  70     -66.510  37.639 -65.352  1.00 10.03           C  
ATOM   2826  O   ASN B  70     -67.334  36.775 -65.675  1.00 43.27           O  
ATOM   2827  CB  ASN B  70     -64.036  37.234 -65.404  1.00 10.90           C  
ATOM   2828  CG  ASN B  70     -62.821  37.055 -66.290  1.00 10.90           C  
ATOM   2829  OD1 ASN B  70     -62.806  37.491 -67.441  1.00 10.20           O  
ATOM   2830  ND2 ASN B  70     -61.792  36.409 -65.754  1.00 11.69           N  
ATOM   2831  N   MET B  71     -66.703  38.446 -64.304  1.00 10.08           N  
ATOM   2832  CA  MET B  71     -67.926  38.327 -63.518  1.00  9.80           C  
ATOM   2833  C   MET B  71     -69.151  38.733 -64.323  1.00  9.32           C  
ATOM   2834  O   MET B  71     -70.253  38.239 -64.061  1.00 29.94           O  
ATOM   2835  CB  MET B  71     -67.837  39.166 -62.244  1.00  9.56           C  
ATOM   2836  CG  MET B  71     -66.903  38.605 -61.191  1.00 10.28           C  
ATOM   2837  SD  MET B  71     -66.879  39.627 -59.709  1.00 11.29           S  
ATOM   2838  CE  MET B  71     -65.552  38.860 -58.784  1.00 30.16           C  
ATOM   2839  N   ARG B  72     -68.983  39.619 -65.306  1.00  8.99           N  
ATOM   2840  CA  ARG B  72     -70.111  39.993 -66.151  1.00  8.74           C  
ATOM   2841  C   ARG B  72     -70.513  38.836 -67.055  1.00  9.22           C  
ATOM   2842  O   ARG B  72     -71.690  38.458 -67.109  1.00  9.57           O  
ATOM   2843  CB  ARG B  72     -69.772  41.236 -66.973  1.00  8.08           C  
ATOM   2844  CG  ARG B  72     -70.843  41.615 -67.981  1.00  7.96           C  
ATOM   2845  CD  ARG B  72     -70.384  42.754 -68.870  1.00  7.08           C  
ATOM   2846  NE  ARG B  72     -71.125  42.796 -70.126  1.00 12.19           N  
ATOM   2847  CZ  ARG B  72     -72.251  43.478 -70.304  1.00 22.08           C  
ATOM   2848  NH1 ARG B  72     -72.767  44.177 -69.302  1.00 17.83           N  
ATOM   2849  NH2 ARG B  72     -72.861  43.462 -71.481  1.00 26.30           N  
ATOM   2850  N   LYS B  73     -69.546  38.258 -67.774  1.00  9.12           N  
ATOM   2851  CA  LYS B  73     -69.859  37.123 -68.636  1.00  8.98           C  
ATOM   2852  C   LYS B  73     -70.330  35.925 -67.826  1.00 19.99           C  
ATOM   2853  O   LYS B  73     -71.131  35.121 -68.316  1.00  9.70           O  
ATOM   2854  CB  LYS B  73     -68.642  36.743 -69.481  1.00  8.18           C  
ATOM   2855  CG  LYS B  73     -68.226  37.803 -70.489  1.00 46.31           C  
ATOM   2856  CD  LYS B  73     -67.252  37.240 -71.516  1.00 60.81           C  
ATOM   2857  CE  LYS B  73     -65.967  36.747 -70.867  1.00 62.65           C  
ATOM   2858  NZ  LYS B  73     -65.157  37.861 -70.300  1.00 61.83           N  
ATOM   2859  N   GLN B  74     -69.856  35.794 -66.585  1.00 26.90           N  
ATOM   2860  CA  GLN B  74     -70.348  34.728 -65.722  1.00 10.01           C  
ATOM   2861  C   GLN B  74     -71.795  34.969 -65.311  1.00 10.46           C  
ATOM   2862  O   GLN B  74     -72.546  34.011 -65.101  1.00 10.86           O  
ATOM   2863  CB  GLN B  74     -69.450  34.591 -64.496  1.00 10.10           C  
ATOM   2864  CG  GLN B  74     -69.660  33.310 -63.718  1.00 10.20           C  
ATOM   2865  CD  GLN B  74     -68.574  33.082 -62.692  1.00 31.49           C  
ATOM   2866  OE1 GLN B  74     -67.687  33.918 -62.516  1.00 19.65           O  
ATOM   2867  NE2 GLN B  74     -68.635  31.946 -62.008  1.00 56.30           N  
ATOM   2868  N   SER B  75     -72.204  36.234 -65.191  1.00 10.24           N  
ATOM   2869  CA  SER B  75     -73.604  36.531 -64.905  1.00 10.30           C  
ATOM   2870  C   SER B  75     -74.476  36.275 -66.126  1.00 11.10           C  
ATOM   2871  O   SER B  75     -75.549  35.671 -66.014  1.00 22.47           O  
ATOM   2872  CB  SER B  75     -73.757  37.978 -64.436  1.00  9.51           C  
ATOM   2873  OG  SER B  75     -73.096  38.192 -63.202  1.00  8.88           O  
ATOM   2874  N   ILE B  76     -74.029  36.723 -67.302  1.00 11.00           N  
ATOM   2875  CA  ILE B  76     -74.811  36.541 -68.517  1.00 11.49           C  
ATOM   2876  C   ILE B  76     -74.808  35.085 -68.966  1.00 17.51           C  
ATOM   2877  O   ILE B  76     -75.723  34.657 -69.679  1.00 25.43           O  
ATOM   2878  CB  ILE B  76     -74.277  37.471 -69.623  1.00 10.71           C  
ATOM   2879  CG1 ILE B  76     -74.160  38.903 -69.097  1.00 10.34           C  
ATOM   2880  CG2 ILE B  76     -75.183  37.444 -70.847  1.00 11.16           C  
ATOM   2881  CD1 ILE B  76     -73.604  39.886 -70.106  1.00 18.81           C  
ATOM   2882  N   ARG B  77     -73.808  34.305 -68.547  1.00 17.19           N  
ATOM   2883  CA  ARG B  77     -73.769  32.889 -68.903  1.00 30.07           C  
ATOM   2884  C   ARG B  77     -75.008  32.158 -68.400  1.00 20.20           C  
ATOM   2885  O   ARG B  77     -75.682  31.455 -69.162  1.00 16.49           O  
ATOM   2886  CB  ARG B  77     -72.502  32.243 -68.340  1.00 40.29           C  
ATOM   2887  CG  ARG B  77     -72.455  30.731 -68.493  1.00 28.86           C  
ATOM   2888  CD  ARG B  77     -71.450  30.117 -67.534  1.00 25.28           C  
ATOM   2889  NE  ARG B  77     -71.214  28.703 -67.808  1.00 26.90           N  
ATOM   2890  CZ  ARG B  77     -70.496  27.904 -67.025  1.00 25.73           C  
ATOM   2891  NH1 ARG B  77     -69.946  28.381 -65.917  1.00 39.49           N  
ATOM   2892  NH2 ARG B  77     -70.328  26.629 -67.348  1.00 17.86           N  
ATOM   2893  N   PHE B  78     -75.331  32.324 -67.118  1.00 12.84           N  
ATOM   2894  CA  PHE B  78     -76.468  31.643 -66.513  1.00 13.89           C  
ATOM   2895  C   PHE B  78     -77.797  32.343 -66.774  1.00 22.17           C  
ATOM   2896  O   PHE B  78     -78.822  31.901 -66.243  1.00 27.00           O  
ATOM   2897  CB  PHE B  78     -76.245  31.493 -65.006  1.00 12.92           C  
ATOM   2898  CG  PHE B  78     -75.001  30.728 -64.651  1.00 13.83           C  
ATOM   2899  CD1 PHE B  78     -74.933  29.359 -64.849  1.00 28.07           C  
ATOM   2900  CD2 PHE B  78     -73.900  31.376 -64.117  1.00 26.34           C  
ATOM   2901  CE1 PHE B  78     -73.792  28.652 -64.525  1.00 24.39           C  
ATOM   2902  CE2 PHE B  78     -72.755  30.673 -63.790  1.00 28.91           C  
ATOM   2903  CZ  PHE B  78     -72.701  29.310 -63.995  1.00 23.00           C  
ATOM   2904  N   GLY B  79     -77.805  33.417 -67.560  1.00 36.26           N  
ATOM   2905  CA  GLY B  79     -79.046  34.003 -68.029  1.00 30.32           C  
ATOM   2906  C   GLY B  79     -79.499  35.247 -67.293  1.00 26.99           C  
ATOM   2907  O   GLY B  79     -80.694  35.413 -67.028  1.00 32.05           O  
ATOM   2908  N   THR B  80     -78.567  36.139 -66.970  1.00 13.59           N  
ATOM   2909  CA  THR B  80     -78.914  37.418 -66.366  1.00 12.34           C  
ATOM   2910  C   THR B  80     -79.167  38.442 -67.464  1.00 20.60           C  
ATOM   2911  O   THR B  80     -78.328  38.629 -68.352  1.00 42.91           O  
ATOM   2912  CB  THR B  80     -77.800  37.904 -65.437  1.00 10.93           C  
ATOM   2913  OG1 THR B  80     -77.501  36.888 -64.471  1.00 10.48           O  
ATOM   2914  CG2 THR B  80     -78.224  39.171 -64.712  1.00  9.85           C  
ATOM   2915  N   GLU B  81     -80.323  39.098 -67.403  1.00 17.29           N  
ATOM   2916  CA  GLU B  81     -80.659  40.165 -68.344  1.00 13.49           C  
ATOM   2917  C   GLU B  81     -80.013  41.453 -67.851  1.00 17.90           C  
ATOM   2918  O   GLU B  81     -80.562  42.173 -67.017  1.00 17.52           O  
ATOM   2919  CB  GLU B  81     -82.171  40.307 -68.483  1.00 14.56           C  
ATOM   2920  CG  GLU B  81     -82.614  41.375 -69.475  1.00 39.51           C  
ATOM   2921  CD  GLU B  81     -84.125  41.489 -69.583  1.00 42.58           C  
ATOM   2922  OE1 GLU B  81     -84.834  40.609 -69.049  1.00 36.16           O  
ATOM   2923  OE2 GLU B  81     -84.605  42.464 -70.201  1.00 35.19           O  
ATOM   2924  N   VAL B  82     -78.823  41.741 -68.369  1.00 32.06           N  
ATOM   2925  CA  VAL B  82     -78.053  42.916 -67.976  1.00 12.05           C  
ATOM   2926  C   VAL B  82     -78.332  44.013 -68.994  1.00  9.84           C  
ATOM   2927  O   VAL B  82     -77.925  43.912 -70.156  1.00  9.97           O  
ATOM   2928  CB  VAL B  82     -76.552  42.608 -67.889  1.00  9.31           C  
ATOM   2929  CG1 VAL B  82     -75.775  43.869 -67.548  1.00  7.96           C  
ATOM   2930  CG2 VAL B  82     -76.287  41.516 -66.865  1.00 12.92           C  
ATOM   2931  N   ILE B  83     -79.023  45.066 -68.564  1.00  9.41           N  
ATOM   2932  CA  ILE B  83     -79.333  46.212 -69.411  1.00 29.45           C  
ATOM   2933  C   ILE B  83     -78.534  47.409 -68.911  1.00 18.14           C  
ATOM   2934  O   ILE B  83     -78.511  47.692 -67.706  1.00  6.81           O  
ATOM   2935  CB  ILE B  83     -80.843  46.509 -69.446  1.00 30.23           C  
ATOM   2936  CG1 ILE B  83     -81.436  46.504 -68.037  1.00 18.50           C  
ATOM   2937  CG2 ILE B  83     -81.562  45.496 -70.332  1.00 38.92           C  
ATOM   2938  CD1 ILE B  83     -82.947  46.521 -68.028  1.00 20.65           C  
ATOM   2939  N   THR B  84     -77.880  48.106 -69.841  1.00  9.06           N  
ATOM   2940  CA  THR B  84     -76.954  49.194 -69.517  1.00  5.10           C  
ATOM   2941  C   THR B  84     -77.723  50.511 -69.377  1.00  4.53           C  
ATOM   2942  O   THR B  84     -77.611  51.436 -70.184  1.00  3.79           O  
ATOM   2943  CB  THR B  84     -75.869  49.291 -70.584  1.00  4.41           C  
ATOM   2944  OG1 THR B  84     -75.401  47.976 -70.909  1.00  5.27           O  
ATOM   2945  CG2 THR B  84     -74.697  50.124 -70.093  1.00 12.16           C  
ATOM   2946  N   GLU B  85     -78.526  50.577 -68.315  1.00 12.71           N  
ATOM   2947  CA  GLU B  85     -79.333  51.752 -68.020  1.00  4.51           C  
ATOM   2948  C   GLU B  85     -79.243  52.076 -66.536  1.00  3.82           C  
ATOM   2949  O   GLU B  85     -79.046  51.191 -65.700  1.00  4.07           O  
ATOM   2950  CB  GLU B  85     -80.801  51.545 -68.424  1.00  6.03           C  
ATOM   2951  CG  GLU B  85     -81.034  51.465 -69.925  1.00  6.81           C  
ATOM   2952  CD  GLU B  85     -82.485  51.189 -70.276  1.00 32.36           C  
ATOM   2953  OE1 GLU B  85     -82.784  51.002 -71.475  1.00 43.68           O  
ATOM   2954  OE2 GLU B  85     -83.327  51.161 -69.353  1.00 38.78           O  
ATOM   2955  N   THR B  86     -79.385  53.360 -66.220  1.00  2.98           N  
ATOM   2956  CA  THR B  86     -79.258  53.862 -64.858  1.00  4.28           C  
ATOM   2957  C   THR B  86     -80.641  54.002 -64.233  1.00 15.13           C  
ATOM   2958  O   THR B  86     -81.567  54.506 -64.876  1.00 54.32           O  
ATOM   2959  CB  THR B  86     -78.530  55.210 -64.848  1.00  1.95           C  
ATOM   2960  OG1 THR B  86     -77.236  55.060 -65.447  1.00 10.45           O  
ATOM   2961  CG2 THR B  86     -78.367  55.731 -63.429  1.00  1.95           C  
ATOM   2962  N   ILE B  87     -80.780  53.549 -62.989  1.00  3.67           N  
ATOM   2963  CA  ILE B  87     -82.037  53.697 -62.260  1.00  4.68           C  
ATOM   2964  C   ILE B  87     -82.131  55.112 -61.709  1.00 14.74           C  
ATOM   2965  O   ILE B  87     -81.189  55.613 -61.083  1.00  3.21           O  
ATOM   2966  CB  ILE B  87     -82.148  52.658 -61.132  1.00  5.20           C  
ATOM   2967  CG1 ILE B  87     -82.159  51.241 -61.703  1.00 21.63           C  
ATOM   2968  CG2 ILE B  87     -83.399  52.906 -60.302  1.00  6.27           C  
ATOM   2969  CD1 ILE B  87     -83.357  50.952 -62.579  1.00  6.82           C  
ATOM   2970  N   SER B  88     -83.274  55.759 -61.936  1.00 33.02           N  
ATOM   2971  CA  SER B  88     -83.495  57.133 -61.499  1.00  4.55           C  
ATOM   2972  C   SER B  88     -84.283  57.194 -60.194  1.00  5.59           C  
ATOM   2973  O   SER B  88     -83.826  57.794 -59.216  1.00  9.94           O  
ATOM   2974  CB  SER B  88     -84.216  57.921 -62.601  1.00  4.68           C  
ATOM   2975  OG  SER B  88     -84.439  59.263 -62.205  1.00  4.39           O  
ATOM   2976  N   ARG B  89     -85.466  56.584 -60.161  1.00  8.89           N  
ATOM   2977  CA  ARG B  89     -86.307  56.577 -58.974  1.00  8.25           C  
ATOM   2978  C   ARG B  89     -86.766  55.157 -58.676  1.00  9.32           C  
ATOM   2979  O   ARG B  89     -86.857  54.315 -59.573  1.00  9.43           O  
ATOM   2980  CB  ARG B  89     -87.527  57.496 -59.145  1.00  9.04           C  
ATOM   2981  CG  ARG B  89     -88.231  57.852 -57.845  1.00 11.23           C  
ATOM   2982  CD  ARG B  89     -89.738  57.883 -58.023  1.00 21.77           C  
ATOM   2983  NE  ARG B  89     -90.122  58.449 -59.312  1.00 11.69           N  
ATOM   2984  CZ  ARG B  89     -91.358  58.430 -59.796  1.00 12.24           C  
ATOM   2985  NH1 ARG B  89     -92.338  57.872 -59.098  1.00 13.69           N  
ATOM   2986  NH2 ARG B  89     -91.616  58.969 -60.978  1.00 11.87           N  
ATOM   2987  N   VAL B  90     -87.066  54.904 -57.405  1.00 12.84           N  
ATOM   2988  CA  VAL B  90     -87.542  53.605 -56.947  1.00 16.71           C  
ATOM   2989  C   VAL B  90     -88.776  53.827 -56.082  1.00 33.20           C  
ATOM   2990  O   VAL B  90     -88.805  54.733 -55.243  1.00 27.65           O  
ATOM   2991  CB  VAL B  90     -86.448  52.832 -56.173  1.00 10.23           C  
ATOM   2992  CG1 VAL B  90     -85.289  52.492 -57.088  1.00  8.82           C  
ATOM   2993  CG2 VAL B  90     -85.946  53.635 -54.983  1.00 22.62           C  
ATOM   2994  N   ASP B  91     -89.805  53.015 -56.303  1.00 51.68           N  
ATOM   2995  CA  ASP B  91     -91.071  53.124 -55.578  1.00 43.26           C  
ATOM   2996  C   ASP B  91     -91.232  51.868 -54.731  1.00 28.39           C  
ATOM   2997  O   ASP B  91     -91.790  50.865 -55.180  1.00 15.86           O  
ATOM   2998  CB  ASP B  91     -92.243  53.302 -56.538  1.00 37.40           C  
ATOM   2999  CG  ASP B  91     -93.563  53.514 -55.820  1.00 38.47           C  
ATOM   3000  OD1 ASP B  91     -93.546  53.749 -54.595  1.00 29.70           O  
ATOM   3001  OD2 ASP B  91     -94.619  53.441 -56.485  1.00 46.14           O  
ATOM   3002  N   LEU B  92     -90.737  51.931 -53.499  1.00 28.70           N  
ATOM   3003  CA  LEU B  92     -90.850  50.802 -52.575  1.00 23.72           C  
ATOM   3004  C   LEU B  92     -92.015  51.016 -51.607  1.00 40.70           C  
ATOM   3005  O   LEU B  92     -91.855  51.017 -50.388  1.00 41.60           O  
ATOM   3006  CB  LEU B  92     -89.531  50.612 -51.823  1.00 15.00           C  
ATOM   3007  CG  LEU B  92     -88.243  50.528 -52.650  1.00 13.39           C  
ATOM   3008  CD1 LEU B  92     -87.034  50.253 -51.757  1.00 12.90           C  
ATOM   3009  CD2 LEU B  92     -88.367  49.475 -53.723  1.00 12.45           C  
ATOM   3010  N   SER B  93     -93.212  51.151 -52.170  1.00 46.09           N  
ATOM   3011  CA  SER B  93     -94.396  51.275 -51.328  1.00 31.82           C  
ATOM   3012  C   SER B  93     -95.527  50.337 -51.718  1.00 26.96           C  
ATOM   3013  O   SER B  93     -96.202  49.801 -50.837  1.00 19.67           O  
ATOM   3014  CB  SER B  93     -94.902  52.727 -51.349  1.00 31.55           C  
ATOM   3015  OG  SER B  93     -96.047  52.868 -50.526  1.00 51.50           O  
ATOM   3016  N   SER B  94     -95.759  50.136 -53.012  1.00 39.37           N  
ATOM   3017  CA  SER B  94     -96.830  49.274 -53.489  1.00 41.52           C  
ATOM   3018  C   SER B  94     -96.404  47.807 -53.433  1.00 23.77           C  
ATOM   3019  O   SER B  94     -95.274  47.475 -53.063  1.00 14.15           O  
ATOM   3020  CB  SER B  94     -97.240  49.685 -54.902  1.00 61.57           C  
ATOM   3021  OG  SER B  94     -96.218  49.396 -55.840  1.00 78.31           O  
ATOM   3022  N   LYS B  95     -97.333  46.909 -53.792  1.00 28.34           N  
ATOM   3023  CA  LYS B  95     -97.019  45.481 -53.810  1.00 29.90           C  
ATOM   3024  C   LYS B  95     -95.842  45.165 -54.726  1.00 15.82           C  
ATOM   3025  O   LYS B  95     -94.864  44.556 -54.257  1.00 15.39           O  
ATOM   3026  CB  LYS B  95     -98.276  44.677 -54.168  1.00 33.84           C  
ATOM   3027  N   PRO B  96     -95.857  45.524 -56.024  1.00 10.31           N  
ATOM   3028  CA  PRO B  96     -94.651  45.322 -56.833  1.00 10.22           C  
ATOM   3029  C   PRO B  96     -93.732  46.537 -56.832  1.00 16.73           C  
ATOM   3030  O   PRO B  96     -94.180  47.669 -57.045  1.00 40.64           O  
ATOM   3031  CB  PRO B  96     -95.216  45.041 -58.229  1.00 10.08           C  
ATOM   3032  CG  PRO B  96     -96.530  45.783 -58.263  1.00 10.83           C  
ATOM   3033  CD  PRO B  96     -96.932  46.124 -56.836  1.00 10.93           C  
ATOM   3034  N   PHE B  97     -92.443  46.314 -56.593  1.00 11.09           N  
ATOM   3035  CA  PHE B  97     -91.478  47.405 -56.631  1.00 11.78           C  
ATOM   3036  C   PHE B  97     -91.347  47.939 -58.053  1.00 12.10           C  
ATOM   3037  O   PHE B  97     -91.149  47.172 -58.999  1.00 13.48           O  
ATOM   3038  CB  PHE B  97     -90.120  46.934 -56.111  1.00 12.81           C  
ATOM   3039  CG  PHE B  97     -90.116  46.581 -54.647  1.00 10.96           C  
ATOM   3040  CD1 PHE B  97     -91.036  47.147 -53.779  1.00 12.31           C  
ATOM   3041  CD2 PHE B  97     -89.185  45.689 -54.139  1.00 27.27           C  
ATOM   3042  CE1 PHE B  97     -91.028  46.829 -52.432  1.00 12.77           C  
ATOM   3043  CE2 PHE B  97     -89.174  45.365 -52.792  1.00 21.94           C  
ATOM   3044  CZ  PHE B  97     -90.097  45.935 -51.939  1.00 11.86           C  
ATOM   3045  N   LYS B  98     -91.462  49.254 -58.204  1.00 13.23           N  
ATOM   3046  CA  LYS B  98     -91.400  49.907 -59.504  1.00 13.72           C  
ATOM   3047  C   LYS B  98     -90.073  50.638 -59.652  1.00 19.37           C  
ATOM   3048  O   LYS B  98     -89.577  51.242 -58.695  1.00 24.91           O  
ATOM   3049  CB  LYS B  98     -92.561  50.888 -59.683  1.00 15.55           C  
ATOM   3050  N   LEU B  99     -89.509  50.588 -60.858  1.00 12.33           N  
ATOM   3051  CA  LEU B  99     -88.223  51.204 -61.149  1.00 11.12           C  
ATOM   3052  C   LEU B  99     -88.337  52.045 -62.411  1.00 11.47           C  
ATOM   3053  O   LEU B  99     -89.073  51.700 -63.340  1.00 12.65           O  
ATOM   3054  CB  LEU B  99     -87.127  50.147 -61.345  1.00 28.87           C  
ATOM   3055  CG  LEU B  99     -86.856  49.144 -60.221  1.00  9.46           C  
ATOM   3056  CD1 LEU B  99     -85.610  48.342 -60.534  1.00  8.47           C  
ATOM   3057  CD2 LEU B  99     -86.723  49.826 -58.877  1.00  9.42           C  
ATOM   3058  N   TRP B 100     -87.592  53.151 -62.444  1.00 21.45           N  
ATOM   3059  CA  TRP B 100     -87.607  54.069 -63.576  1.00 14.44           C  
ATOM   3060  C   TRP B 100     -86.192  54.326 -64.073  1.00  8.67           C  
ATOM   3061  O   TRP B 100     -85.265  54.505 -63.277  1.00  7.51           O  
ATOM   3062  CB  TRP B 100     -88.265  55.405 -63.207  1.00 16.09           C  
ATOM   3063  CG  TRP B 100     -89.753  55.333 -63.062  1.00 12.20           C  
ATOM   3064  CD1 TRP B 100     -90.682  55.479 -64.051  1.00 13.22           C  
ATOM   3065  CD2 TRP B 100     -90.487  55.110 -61.852  1.00 13.17           C  
ATOM   3066  NE1 TRP B 100     -91.949  55.354 -63.533  1.00 14.76           N  
ATOM   3067  CE2 TRP B 100     -91.856  55.128 -62.185  1.00 14.82           C  
ATOM   3068  CE3 TRP B 100     -90.120  54.894 -60.520  1.00 18.15           C  
ATOM   3069  CZ2 TRP B 100     -92.858  54.938 -61.236  1.00 16.13           C  
ATOM   3070  CZ3 TRP B 100     -91.116  54.706 -59.579  1.00 14.21           C  
ATOM   3071  CH2 TRP B 100     -92.468  54.728 -59.941  1.00 15.82           C  
ATOM   3072  N   THR B 101     -86.035  54.343 -65.394  1.00  8.68           N  
ATOM   3073  CA  THR B 101     -84.769  54.687 -66.023  1.00  7.22           C  
ATOM   3074  C   THR B 101     -84.548  56.197 -65.981  1.00  6.76           C  
ATOM   3075  O   THR B 101     -85.488  56.986 -65.865  1.00 16.88           O  
ATOM   3076  CB  THR B 101     -84.739  54.195 -67.474  1.00 24.14           C  
ATOM   3077  OG1 THR B 101     -85.313  52.886 -67.547  1.00 29.75           O  
ATOM   3078  CG2 THR B 101     -83.312  54.137 -68.006  1.00 46.84           C  
ATOM   3079  N   GLU B 102     -83.282  56.595 -66.072  1.00  4.41           N  
ATOM   3080  CA  GLU B 102     -82.959  58.011 -66.144  1.00  4.46           C  
ATOM   3081  C   GLU B 102     -83.399  58.565 -67.494  1.00  5.97           C  
ATOM   3082  O   GLU B 102     -83.346  57.867 -68.511  1.00  3.54           O  
ATOM   3083  CB  GLU B 102     -81.463  58.229 -65.935  1.00 24.52           C  
ATOM   3084  CG  GLU B 102     -81.091  59.643 -65.535  1.00 19.69           C  
ATOM   3085  CD  GLU B 102     -79.640  59.761 -65.117  1.00 31.07           C  
ATOM   3086  OE1 GLU B 102     -78.842  58.871 -65.481  1.00 29.16           O  
ATOM   3087  OE2 GLU B 102     -79.301  60.737 -64.417  1.00 47.84           O  
ATOM   3088  N   TRP B 103     -83.861  59.821 -67.485  1.00  8.57           N  
ATOM   3089  CA  TRP B 103     -84.429  60.514 -68.642  1.00  4.51           C  
ATOM   3090  C   TRP B 103     -85.806  59.960 -68.989  1.00 19.96           C  
ATOM   3091  O   TRP B 103     -86.502  60.503 -69.853  1.00 20.19           O  
ATOM   3092  CB  TRP B 103     -83.505  60.436 -69.860  1.00  1.95           C  
ATOM   3093  CG  TRP B 103     -82.336  61.353 -69.788  1.00  1.95           C  
ATOM   3094  CD1 TRP B 103     -81.090  61.057 -69.322  1.00  1.95           C  
ATOM   3095  CD2 TRP B 103     -82.297  62.723 -70.200  1.00  1.95           C  
ATOM   3096  NE1 TRP B 103     -80.276  62.159 -69.418  1.00  1.95           N  
ATOM   3097  CE2 TRP B 103     -80.994  63.196 -69.955  1.00 13.89           C  
ATOM   3098  CE3 TRP B 103     -83.239  63.597 -70.753  1.00  1.96           C  
ATOM   3099  CZ2 TRP B 103     -80.607  64.502 -70.245  1.00 24.73           C  
ATOM   3100  CZ3 TRP B 103     -82.854  64.893 -71.040  1.00  7.28           C  
ATOM   3101  CH2 TRP B 103     -81.549  65.334 -70.786  1.00 18.08           C  
ATOM   3102  N   ASN B 104     -86.207  58.880 -68.315  1.00 29.79           N  
ATOM   3103  CA  ASN B 104     -87.560  58.342 -68.402  1.00 10.20           C  
ATOM   3104  C   ASN B 104     -88.249  58.399 -67.045  1.00  8.22           C  
ATOM   3105  O   ASN B 104     -89.185  57.637 -66.785  1.00  9.85           O  
ATOM   3106  CB  ASN B 104     -87.542  56.909 -68.937  1.00  9.47           C  
ATOM   3107  CG  ASN B 104     -87.088  56.829 -70.382  1.00 18.55           C  
ATOM   3108  OD1 ASN B 104     -86.746  57.841 -70.995  1.00 13.99           O  
ATOM   3109  ND2 ASN B 104     -87.079  55.621 -70.933  1.00 38.04           N  
ATOM   3110  N   ASP B 105     -87.785  59.295 -66.176  1.00 25.09           N  
ATOM   3111  CA  ASP B 105     -88.330  59.495 -64.842  1.00 29.76           C  
ATOM   3112  C   ASP B 105     -89.599  60.332 -64.954  1.00 47.65           C  
ATOM   3113  O   ASP B 105     -90.152  60.478 -66.049  1.00 56.41           O  
ATOM   3114  CB  ASP B 105     -87.285  60.165 -63.944  1.00 39.10           C  
ATOM   3115  CG  ASP B 105     -87.601  60.030 -62.467  1.00 44.92           C  
ATOM   3116  OD1 ASP B 105     -88.618  59.385 -62.133  1.00 39.90           O  
ATOM   3117  OD2 ASP B 105     -86.831  60.568 -61.642  1.00 44.28           O  
ATOM   3118  N   GLY B 106     -90.075  60.883 -63.843  1.00 45.18           N  
ATOM   3119  CA  GLY B 106     -91.239  61.732 -63.874  1.00 35.10           C  
ATOM   3120  C   GLY B 106     -92.395  61.180 -63.068  1.00 39.77           C  
ATOM   3121  O   GLY B 106     -92.493  59.976 -62.813  1.00 55.70           O  
ATOM   3122  N   PRO B 107     -93.309  62.064 -62.663  1.00 27.19           N  
ATOM   3123  CA  PRO B 107     -94.443  61.622 -61.838  1.00 19.20           C  
ATOM   3124  C   PRO B 107     -95.494  60.837 -62.601  1.00 30.98           C  
ATOM   3125  O   PRO B 107     -96.260  60.099 -61.970  1.00 34.35           O  
ATOM   3126  CB  PRO B 107     -95.014  62.939 -61.298  1.00 19.67           C  
ATOM   3127  CG  PRO B 107     -94.660  63.943 -62.344  1.00 13.96           C  
ATOM   3128  CD  PRO B 107     -93.318  63.521 -62.883  1.00 20.21           C  
ATOM   3129  N   ASP B 108     -95.560  60.956 -63.924  1.00 34.75           N  
ATOM   3130  CA  ASP B 108     -96.613  60.303 -64.693  1.00 25.63           C  
ATOM   3131  C   ASP B 108     -96.031  59.522 -65.861  1.00 29.93           C  
ATOM   3132  O   ASP B 108     -96.586  59.505 -66.962  1.00 24.24           O  
ATOM   3133  CB  ASP B 108     -97.638  61.322 -65.185  1.00 11.37           C  
ATOM   3134  N   LYS B 109     -94.897  58.867 -65.639  1.00 27.54           N  
ATOM   3135  CA  LYS B 109     -94.286  57.998 -66.631  1.00 13.67           C  
ATOM   3136  C   LYS B 109     -94.462  56.544 -66.213  1.00 15.40           C  
ATOM   3137  O   LYS B 109     -94.638  56.232 -65.031  1.00 16.19           O  
ATOM   3138  CB  LYS B 109     -92.799  58.322 -66.811  1.00 12.39           C  
ATOM   3139  N   GLU B 110     -94.409  55.651 -67.197  1.00 25.30           N  
ATOM   3140  CA  GLU B 110     -94.558  54.235 -66.887  1.00 17.52           C  
ATOM   3141  C   GLU B 110     -93.215  53.659 -66.441  1.00 17.24           C  
ATOM   3142  O   GLU B 110     -92.181  53.961 -67.044  1.00 16.73           O  
ATOM   3143  CB  GLU B 110     -95.079  53.467 -68.100  1.00 17.84           C  
ATOM   3144  N   PRO B 111     -93.197  52.844 -65.386  1.00 27.56           N  
ATOM   3145  CA  PRO B 111     -91.928  52.264 -64.934  1.00 20.12           C  
ATOM   3146  C   PRO B 111     -91.317  51.372 -66.003  1.00 17.98           C  
ATOM   3147  O   PRO B 111     -92.019  50.716 -66.775  1.00 25.02           O  
ATOM   3148  CB  PRO B 111     -92.327  51.458 -63.691  1.00 16.89           C  
ATOM   3149  CG  PRO B 111     -93.606  52.077 -63.231  1.00 18.39           C  
ATOM   3150  CD  PRO B 111     -94.311  52.513 -64.482  1.00 29.76           C  
ATOM   3151  N   ALA B 112     -89.984  51.353 -66.037  1.00 15.45           N  
ATOM   3152  CA  ALA B 112     -89.278  50.550 -67.028  1.00 14.94           C  
ATOM   3153  C   ALA B 112     -89.198  49.085 -66.627  1.00 15.26           C  
ATOM   3154  O   ALA B 112     -89.164  48.210 -67.499  1.00 31.03           O  
ATOM   3155  CB  ALA B 112     -87.873  51.104 -67.256  1.00 13.10           C  
ATOM   3156  N   CYS B 113     -89.158  48.799 -65.329  1.00  8.32           N  
ATOM   3157  CA  CYS B 113     -89.109  47.428 -64.849  1.00 11.64           C  
ATOM   3158  C   CYS B 113     -89.727  47.361 -63.463  1.00  1.95           C  
ATOM   3159  O   CYS B 113     -89.532  48.264 -62.644  1.00  1.95           O  
ATOM   3160  CB  CYS B 113     -87.670  46.898 -64.811  1.00 19.37           C  
ATOM   3161  SG  CYS B 113     -87.530  45.116 -64.540  1.00  8.39           S  
ATOM   3162  N   THR B 114     -90.472  46.290 -63.209  1.00  5.85           N  
ATOM   3163  CA  THR B 114     -91.035  46.031 -61.896  1.00 15.59           C  
ATOM   3164  C   THR B 114     -90.679  44.614 -61.473  1.00 15.01           C  
ATOM   3165  O   THR B 114     -90.498  43.725 -62.310  1.00 23.52           O  
ATOM   3166  CB  THR B 114     -92.562  46.229 -61.875  1.00  7.29           C  
ATOM   3167  OG1 THR B 114     -93.068  45.909 -60.573  1.00 21.19           O  
ATOM   3168  CG2 THR B 114     -93.238  45.343 -62.907  1.00  1.95           C  
ATOM   3169  N   ALA B 115     -90.565  44.413 -60.163  1.00  1.95           N  
ATOM   3170  CA  ALA B 115     -90.159  43.121 -59.629  1.00  1.96           C  
ATOM   3171  C   ALA B 115     -90.682  42.985 -58.208  1.00  8.45           C  
ATOM   3172  O   ALA B 115     -91.049  43.971 -57.564  1.00 10.85           O  
ATOM   3173  CB  ALA B 115     -88.637  42.950 -59.665  1.00  1.95           C  
ATOM   3174  N   ASP B 116     -90.700  41.744 -57.727  1.00  7.32           N  
ATOM   3175  CA  ASP B 116     -91.154  41.448 -56.376  1.00  7.66           C  
ATOM   3176  C   ASP B 116     -90.045  41.561 -55.342  1.00  3.43           C  
ATOM   3177  O   ASP B 116     -90.332  41.521 -54.141  1.00 16.31           O  
ATOM   3178  CB  ASP B 116     -91.761  40.042 -56.319  1.00 10.99           C  
ATOM   3179  CG  ASP B 116     -92.951  39.886 -57.242  1.00 30.46           C  
ATOM   3180  OD1 ASP B 116     -93.843  40.760 -57.215  1.00 39.19           O  
ATOM   3181  OD2 ASP B 116     -92.994  38.890 -57.993  1.00 41.38           O  
ATOM   3182  N   ALA B 117     -88.796  41.701 -55.776  1.00  8.25           N  
ATOM   3183  CA  ALA B 117     -87.674  41.877 -54.870  1.00 16.93           C  
ATOM   3184  C   ALA B 117     -86.568  42.614 -55.608  1.00 20.89           C  
ATOM   3185  O   ALA B 117     -86.378  42.429 -56.813  1.00 37.91           O  
ATOM   3186  CB  ALA B 117     -87.162  40.535 -54.335  1.00 16.97           C  
ATOM   3187  N   VAL B 118     -85.843  43.456 -54.878  1.00  9.06           N  
ATOM   3188  CA  VAL B 118     -84.766  44.251 -55.452  1.00 10.60           C  
ATOM   3189  C   VAL B 118     -83.544  44.151 -54.547  1.00  7.22           C  
ATOM   3190  O   VAL B 118     -83.665  44.166 -53.317  1.00  7.45           O  
ATOM   3191  CB  VAL B 118     -85.194  45.722 -55.671  1.00  3.27           C  
ATOM   3192  CG1 VAL B 118     -85.709  46.345 -54.385  1.00  3.74           C  
ATOM   3193  CG2 VAL B 118     -84.051  46.543 -56.255  1.00  5.68           C  
ATOM   3194  N   ILE B 119     -82.369  44.022 -55.161  1.00  6.58           N  
ATOM   3195  CA  ILE B 119     -81.094  43.960 -54.457  1.00  7.98           C  
ATOM   3196  C   ILE B 119     -80.345  45.259 -54.718  1.00 15.47           C  
ATOM   3197  O   ILE B 119     -80.169  45.659 -55.875  1.00 19.80           O  
ATOM   3198  CB  ILE B 119     -80.251  42.754 -54.910  1.00  8.32           C  
ATOM   3199  CG1 ILE B 119     -81.051  41.455 -54.817  1.00 19.77           C  
ATOM   3200  CG2 ILE B 119     -78.996  42.641 -54.064  1.00 13.35           C  
ATOM   3201  CD1 ILE B 119     -81.313  41.004 -53.408  1.00 29.37           C  
ATOM   3202  N   ILE B 120     -79.893  45.907 -53.650  1.00 18.90           N  
ATOM   3203  CA  ILE B 120     -79.154  47.160 -53.748  1.00 11.83           C  
ATOM   3204  C   ILE B 120     -77.681  46.849 -53.521  1.00 12.85           C  
ATOM   3205  O   ILE B 120     -77.258  46.568 -52.394  1.00 19.91           O  
ATOM   3206  CB  ILE B 120     -79.668  48.207 -52.751  1.00  8.58           C  
ATOM   3207  CG1 ILE B 120     -81.105  48.604 -53.094  1.00  7.00           C  
ATOM   3208  CG2 ILE B 120     -78.766  49.432 -52.754  1.00  8.49           C  
ATOM   3209  CD1 ILE B 120     -81.672  49.668 -52.182  1.00  8.04           C  
ATOM   3210  N   ALA B 121     -76.901  46.895 -54.597  1.00 11.22           N  
ATOM   3211  CA  ALA B 121     -75.458  46.686 -54.573  1.00 26.18           C  
ATOM   3212  C   ALA B 121     -74.761  47.808 -55.326  1.00 30.67           C  
ATOM   3213  O   ALA B 121     -73.893  47.586 -56.174  1.00 36.50           O  
ATOM   3214  CB  ALA B 121     -75.093  45.325 -55.158  1.00 46.85           C  
ATOM   3215  N   THR B 122     -75.147  49.044 -55.016  1.00 43.72           N  
ATOM   3216  CA  THR B 122     -74.705  50.229 -55.741  1.00 36.08           C  
ATOM   3217  C   THR B 122     -73.335  50.732 -55.297  1.00  8.93           C  
ATOM   3218  O   THR B 122     -72.920  51.812 -55.730  1.00  8.17           O  
ATOM   3219  CB  THR B 122     -75.739  51.348 -55.581  1.00 19.39           C  
ATOM   3220  OG1 THR B 122     -75.875  51.677 -54.192  1.00  7.79           O  
ATOM   3221  CG2 THR B 122     -77.091  50.907 -56.123  1.00  5.38           C  
ATOM   3222  N   GLY B 123     -72.630  49.983 -54.455  1.00 10.53           N  
ATOM   3223  CA  GLY B 123     -71.273  50.333 -54.079  1.00 46.16           C  
ATOM   3224  C   GLY B 123     -71.192  51.573 -53.203  1.00 29.45           C  
ATOM   3225  O   GLY B 123     -72.182  52.230 -52.885  1.00 15.49           O  
ATOM   3226  N   ALA B 124     -69.958  51.884 -52.804  1.00 34.17           N  
ATOM   3227  CA  ALA B 124     -69.675  53.078 -52.008  1.00 19.89           C  
ATOM   3228  C   ALA B 124     -68.270  53.544 -52.377  1.00 19.49           C  
ATOM   3229  O   ALA B 124     -67.283  53.039 -51.833  1.00 39.09           O  
ATOM   3230  CB  ALA B 124     -69.796  52.792 -50.517  1.00 13.85           C  
ATOM   3231  N   ASN B 125     -68.189  54.499 -53.298  1.00 12.04           N  
ATOM   3232  CA  ASN B 125     -66.903  54.965 -53.788  1.00 29.06           C  
ATOM   3233  C   ASN B 125     -66.222  55.863 -52.762  1.00 21.48           C  
ATOM   3234  O   ASN B 125     -66.874  56.576 -51.994  1.00 12.42           O  
ATOM   3235  CB  ASN B 125     -67.071  55.722 -55.105  1.00 37.99           C  
ATOM   3236  CG  ASN B 125     -67.583  54.838 -56.221  1.00 44.75           C  
ATOM   3237  OD1 ASN B 125     -67.590  53.613 -56.104  1.00 51.54           O  
ATOM   3238  ND2 ASN B 125     -68.011  55.455 -57.316  1.00 39.14           N  
ATOM   3239  N   ALA B 126     -64.892  55.824 -52.761  1.00 18.71           N  
ATOM   3240  CA  ALA B 126     -64.110  56.719 -51.924  1.00 13.84           C  
ATOM   3241  C   ALA B 126     -64.053  58.102 -52.556  1.00 12.67           C  
ATOM   3242  O   ALA B 126     -63.938  58.237 -53.777  1.00 24.64           O  
ATOM   3243  CB  ALA B 126     -62.697  56.172 -51.724  1.00 15.15           C  
ATOM   3244  N   ARG B 127     -64.141  59.132 -51.718  1.00 12.29           N  
ATOM   3245  CA  ARG B 127     -64.163  60.499 -52.221  1.00 10.83           C  
ATOM   3246  C   ARG B 127     -62.781  60.899 -52.725  1.00 17.66           C  
ATOM   3247  O   ARG B 127     -61.771  60.671 -52.051  1.00 12.24           O  
ATOM   3248  CB  ARG B 127     -64.628  61.458 -51.127  1.00 13.59           C  
ATOM   3249  CG  ARG B 127     -66.107  61.354 -50.787  1.00 15.05           C  
ATOM   3250  CD  ARG B 127     -66.453  62.189 -49.562  1.00 19.67           C  
ATOM   3251  NE  ARG B 127     -66.135  63.601 -49.755  1.00 48.58           N  
ATOM   3252  CZ  ARG B 127     -66.996  64.508 -50.203  1.00 53.23           C  
ATOM   3253  NH1 ARG B 127     -68.238  64.155 -50.509  1.00 41.31           N  
ATOM   3254  NH2 ARG B 127     -66.616  65.771 -50.347  1.00 55.46           N  
ATOM   3255  N   ARG B 128     -62.737  61.494 -53.912  1.00 20.83           N  
ATOM   3256  CA  ARG B 128     -61.510  62.023 -54.486  1.00 17.36           C  
ATOM   3257  C   ARG B 128     -61.545  63.546 -54.483  1.00 23.73           C  
ATOM   3258  O   ARG B 128     -62.603  64.166 -54.344  1.00 49.91           O  
ATOM   3259  CB  ARG B 128     -61.302  61.497 -55.911  1.00  9.27           C  
ATOM   3260  CG  ARG B 128     -61.202  59.981 -55.995  1.00 10.47           C  
ATOM   3261  CD  ARG B 128     -60.632  59.522 -57.329  1.00 12.21           C  
ATOM   3262  NE  ARG B 128     -61.447  59.944 -58.464  1.00 47.43           N  
ATOM   3263  CZ  ARG B 128     -61.193  59.614 -59.727  1.00 44.68           C  
ATOM   3264  NH1 ARG B 128     -60.146  58.854 -60.017  1.00 25.43           N  
ATOM   3265  NH2 ARG B 128     -61.987  60.042 -60.700  1.00 46.72           N  
ATOM   3266  N   LEU B 129     -60.366  64.148 -54.641  1.00 10.06           N  
ATOM   3267  CA  LEU B 129     -60.229  65.598 -54.610  1.00 18.89           C  
ATOM   3268  C   LEU B 129     -60.107  66.223 -55.993  1.00 21.78           C  
ATOM   3269  O   LEU B 129     -60.144  67.454 -56.100  1.00 34.53           O  
ATOM   3270  CB  LEU B 129     -59.018  66.009 -53.759  1.00  7.89           C  
ATOM   3271  CG  LEU B 129     -59.034  65.667 -52.265  1.00  8.93           C  
ATOM   3272  CD1 LEU B 129     -58.597  64.233 -52.001  1.00 10.82           C  
ATOM   3273  CD2 LEU B 129     -58.167  66.645 -51.483  1.00 17.88           C  
ATOM   3274  N   ASN B 130     -59.960  65.412 -57.043  1.00 10.72           N  
ATOM   3275  CA  ASN B 130     -59.882  65.901 -58.421  1.00 32.98           C  
ATOM   3276  C   ASN B 130     -58.755  66.919 -58.594  1.00 41.31           C  
ATOM   3277  O   ASN B 130     -58.917  67.949 -59.251  1.00 41.64           O  
ATOM   3278  CB  ASN B 130     -61.222  66.486 -58.878  1.00 51.14           C  
ATOM   3279  CG  ASN B 130     -61.381  66.469 -60.386  1.00 57.77           C  
ATOM   3280  OD1 ASN B 130     -60.884  65.570 -61.064  1.00 65.05           O  
ATOM   3281  ND2 ASN B 130     -62.075  67.469 -60.920  1.00 45.97           N  
ATOM   3282  N   LEU B 131     -57.604  66.632 -57.988  1.00 37.54           N  
ATOM   3283  CA  LEU B 131     -56.443  67.493 -58.130  1.00 13.26           C  
ATOM   3284  C   LEU B 131     -55.959  67.486 -59.576  1.00 20.12           C  
ATOM   3285  O   LEU B 131     -56.218  66.540 -60.323  1.00 49.41           O  
ATOM   3286  CB  LEU B 131     -55.318  67.029 -57.208  1.00  7.17           C  
ATOM   3287  CG  LEU B 131     -55.547  67.115 -55.700  1.00  8.00           C  
ATOM   3288  CD1 LEU B 131     -54.325  66.606 -54.956  1.00  9.73           C  
ATOM   3289  CD2 LEU B 131     -55.867  68.545 -55.294  1.00  8.54           C  
ATOM   3290  N   PRO B 132     -55.267  68.540 -60.004  1.00 13.14           N  
ATOM   3291  CA  PRO B 132     -54.627  68.500 -61.325  1.00 11.36           C  
ATOM   3292  C   PRO B 132     -53.577  67.399 -61.377  1.00 19.98           C  
ATOM   3293  O   PRO B 132     -52.761  67.248 -60.465  1.00 10.48           O  
ATOM   3294  CB  PRO B 132     -54.007  69.896 -61.466  1.00  1.95           C  
ATOM   3295  CG  PRO B 132     -53.939  70.439 -60.076  1.00  1.95           C  
ATOM   3296  CD  PRO B 132     -55.108  69.851 -59.353  1.00 10.50           C  
ATOM   3297  N   GLY B 133     -53.610  66.622 -62.459  1.00 27.10           N  
ATOM   3298  CA  GLY B 133     -52.769  65.454 -62.587  1.00 19.65           C  
ATOM   3299  C   GLY B 133     -53.309  64.203 -61.929  1.00 12.91           C  
ATOM   3300  O   GLY B 133     -52.719  63.130 -62.104  1.00 14.95           O  
ATOM   3301  N   GLU B 134     -54.409  64.300 -61.178  1.00  7.93           N  
ATOM   3302  CA  GLU B 134     -54.987  63.114 -60.554  1.00  6.91           C  
ATOM   3303  C   GLU B 134     -55.462  62.114 -61.600  1.00  9.83           C  
ATOM   3304  O   GLU B 134     -55.247  60.905 -61.455  1.00 11.39           O  
ATOM   3305  CB  GLU B 134     -56.137  63.515 -59.631  1.00  7.16           C  
ATOM   3306  CG  GLU B 134     -56.934  62.351 -59.076  1.00 18.32           C  
ATOM   3307  CD  GLU B 134     -58.085  62.805 -58.201  1.00 22.34           C  
ATOM   3308  OE1 GLU B 134     -57.842  63.575 -57.247  1.00 10.92           O  
ATOM   3309  OE2 GLU B 134     -59.235  62.402 -58.474  1.00 23.41           O  
ATOM   3310  N   GLU B 135     -56.112  62.599 -62.662  1.00  5.75           N  
ATOM   3311  CA  GLU B 135     -56.565  61.707 -63.724  1.00  6.46           C  
ATOM   3312  C   GLU B 135     -55.401  60.991 -64.397  1.00 16.52           C  
ATOM   3313  O   GLU B 135     -55.560  59.862 -64.875  1.00 32.45           O  
ATOM   3314  CB  GLU B 135     -57.377  62.489 -64.757  1.00  1.95           C  
ATOM   3315  N   THR B 136     -54.228  61.625 -64.444  1.00 30.80           N  
ATOM   3316  CA  THR B 136     -53.079  61.021 -65.109  1.00 29.83           C  
ATOM   3317  C   THR B 136     -52.398  59.968 -64.242  1.00 20.76           C  
ATOM   3318  O   THR B 136     -51.811  59.019 -64.775  1.00 10.49           O  
ATOM   3319  CB  THR B 136     -52.073  62.106 -65.505  1.00 20.55           C  
ATOM   3320  OG1 THR B 136     -52.765  63.196 -66.125  1.00 30.49           O  
ATOM   3321  CG2 THR B 136     -51.036  61.554 -66.476  1.00  9.92           C  
ATOM   3322  N   TYR B 137     -52.482  60.098 -62.918  1.00 12.21           N  
ATOM   3323  CA  TYR B 137     -51.780  59.199 -62.010  1.00  7.43           C  
ATOM   3324  C   TYR B 137     -52.722  58.446 -61.079  1.00  9.29           C  
ATOM   3325  O   TYR B 137     -52.260  57.852 -60.097  1.00  9.46           O  
ATOM   3326  CB  TYR B 137     -50.741  59.975 -61.193  1.00 20.03           C  
ATOM   3327  CG  TYR B 137     -49.748  60.720 -62.055  1.00 13.05           C  
ATOM   3328  CD1 TYR B 137     -48.655  60.072 -62.611  1.00 15.42           C  
ATOM   3329  CD2 TYR B 137     -49.914  62.069 -62.324  1.00  6.98           C  
ATOM   3330  CE1 TYR B 137     -47.752  60.750 -63.408  1.00  6.40           C  
ATOM   3331  CE2 TYR B 137     -49.020  62.755 -63.117  1.00 29.83           C  
ATOM   3332  CZ  TYR B 137     -47.941  62.093 -63.657  1.00 29.56           C  
ATOM   3333  OH  TYR B 137     -47.050  62.782 -64.448  1.00 48.26           O  
ATOM   3334  N   TRP B 138     -54.026  58.457 -61.350  1.00 35.44           N  
ATOM   3335  CA  TRP B 138     -54.946  57.625 -60.587  1.00 30.53           C  
ATOM   3336  C   TRP B 138     -54.678  56.158 -60.890  1.00 25.03           C  
ATOM   3337  O   TRP B 138     -54.611  55.757 -62.057  1.00 18.92           O  
ATOM   3338  CB  TRP B 138     -56.395  57.987 -60.913  1.00 17.02           C  
ATOM   3339  CG  TRP B 138     -57.400  57.138 -60.197  1.00 23.87           C  
ATOM   3340  CD1 TRP B 138     -58.188  56.166 -60.742  1.00 31.73           C  
ATOM   3341  CD2 TRP B 138     -57.709  57.167 -58.798  1.00 25.73           C  
ATOM   3342  NE1 TRP B 138     -58.978  55.598 -59.772  1.00 23.41           N  
ATOM   3343  CE2 TRP B 138     -58.702  56.194 -58.570  1.00 20.55           C  
ATOM   3344  CE3 TRP B 138     -57.245  57.924 -57.718  1.00 26.89           C  
ATOM   3345  CZ2 TRP B 138     -59.241  55.961 -57.307  1.00 15.65           C  
ATOM   3346  CZ3 TRP B 138     -57.780  57.687 -56.463  1.00 12.55           C  
ATOM   3347  CH2 TRP B 138     -58.767  56.714 -56.269  1.00 12.42           C  
ATOM   3348  N   GLN B 139     -54.516  55.360 -59.835  1.00  9.53           N  
ATOM   3349  CA  GLN B 139     -54.095  53.963 -59.906  1.00 20.85           C  
ATOM   3350  C   GLN B 139     -52.726  53.799 -60.559  1.00 25.89           C  
ATOM   3351  O   GLN B 139     -52.321  52.671 -60.868  1.00 41.09           O  
ATOM   3352  CB  GLN B 139     -55.136  53.091 -60.622  1.00 26.55           C  
ATOM   3353  CG  GLN B 139     -56.352  52.772 -59.765  1.00 25.73           C  
ATOM   3354  CD  GLN B 139     -55.996  51.964 -58.529  1.00 32.50           C  
ATOM   3355  OE1 GLN B 139     -55.523  50.831 -58.626  1.00 14.83           O  
ATOM   3356  NE2 GLN B 139     -56.217  52.548 -57.357  1.00 29.47           N  
ATOM   3357  N   ASN B 140     -52.008  54.900 -60.780  1.00 23.81           N  
ATOM   3358  CA  ASN B 140     -50.613  54.889 -61.203  1.00 23.30           C  
ATOM   3359  C   ASN B 140     -49.742  55.624 -60.190  1.00 11.98           C  
ATOM   3360  O   ASN B 140     -48.742  56.249 -60.550  1.00  9.40           O  
ATOM   3361  CB  ASN B 140     -50.459  55.501 -62.595  1.00 14.83           C  
ATOM   3362  CG  ASN B 140     -51.073  54.641 -63.682  1.00 22.39           C  
ATOM   3363  OD1 ASN B 140     -50.911  53.421 -63.691  1.00 33.34           O  
ATOM   3364  ND2 ASN B 140     -51.783  55.275 -64.608  1.00 47.45           N  
ATOM   3365  N   GLY B 141     -50.126  55.562 -58.918  1.00 10.69           N  
ATOM   3366  CA  GLY B 141     -49.436  56.276 -57.863  1.00 11.47           C  
ATOM   3367  C   GLY B 141     -50.397  56.837 -56.836  1.00 12.16           C  
ATOM   3368  O   GLY B 141     -50.031  57.038 -55.674  1.00 12.89           O  
ATOM   3369  N   ILE B 142     -51.634  57.089 -57.254  1.00 11.87           N  
ATOM   3370  CA  ILE B 142     -52.686  57.584 -56.376  1.00 12.49           C  
ATOM   3371  C   ILE B 142     -53.666  56.448 -56.118  1.00 14.70           C  
ATOM   3372  O   ILE B 142     -53.970  55.661 -57.022  1.00 11.95           O  
ATOM   3373  CB  ILE B 142     -53.404  58.809 -56.977  1.00 12.08           C  
ATOM   3374  CG1 ILE B 142     -52.387  59.821 -57.510  1.00 11.67           C  
ATOM   3375  CG2 ILE B 142     -54.297  59.471 -55.941  1.00 12.90           C  
ATOM   3376  CD1 ILE B 142     -53.017  61.055 -58.123  1.00 11.01           C  
ATOM   3377  N   SER B 143     -54.155  56.361 -54.883  1.00 13.45           N  
ATOM   3378  CA  SER B 143     -55.099  55.322 -54.500  1.00 28.96           C  
ATOM   3379  C   SER B 143     -55.926  55.821 -53.323  1.00 22.40           C  
ATOM   3380  O   SER B 143     -55.716  56.924 -52.811  1.00 28.94           O  
ATOM   3381  CB  SER B 143     -54.380  54.014 -54.156  1.00 40.16           C  
ATOM   3382  OG  SER B 143     -55.304  53.022 -53.736  1.00 47.41           O  
ATOM   3383  N   ALA B 144     -56.873  54.990 -52.892  1.00 14.60           N  
ATOM   3384  CA  ALA B 144     -57.738  55.337 -51.774  1.00 17.11           C  
ATOM   3385  C   ALA B 144     -57.915  54.203 -50.778  1.00 25.50           C  
ATOM   3386  O   ALA B 144     -58.621  54.388 -49.781  1.00 23.68           O  
ATOM   3387  CB  ALA B 144     -59.117  55.785 -52.284  1.00 24.57           C  
ATOM   3388  N   CYS B 145     -57.301  53.045 -51.007  1.00 38.69           N  
ATOM   3389  CA  CYS B 145     -57.396  51.901 -50.106  1.00 39.37           C  
ATOM   3390  C   CYS B 145     -55.985  51.463 -49.736  1.00 22.18           C  
ATOM   3391  O   CYS B 145     -55.222  51.020 -50.600  1.00 15.47           O  
ATOM   3392  CB  CYS B 145     -58.171  50.755 -50.754  1.00 28.10           C  
ATOM   3393  SG  CYS B 145     -57.975  49.175 -49.913  1.00 61.67           S  
ATOM   3394  N   ALA B 146     -55.638  51.593 -48.453  1.00 16.56           N  
ATOM   3395  CA  ALA B 146     -54.311  51.187 -48.006  1.00 23.44           C  
ATOM   3396  C   ALA B 146     -54.156  49.672 -47.993  1.00 19.89           C  
ATOM   3397  O   ALA B 146     -53.058  49.162 -48.242  1.00 18.86           O  
ATOM   3398  CB  ALA B 146     -54.026  51.761 -46.619  1.00 48.77           C  
ATOM   3399  N   VAL B 147     -55.233  48.940 -47.705  1.00 29.53           N  
ATOM   3400  CA  VAL B 147     -55.155  47.482 -47.670  1.00 16.04           C  
ATOM   3401  C   VAL B 147     -54.992  46.920 -49.077  1.00 15.52           C  
ATOM   3402  O   VAL B 147     -54.274  45.935 -49.289  1.00 26.00           O  
ATOM   3403  CB  VAL B 147     -56.397  46.900 -46.970  1.00 15.98           C  
ATOM   3404  CG1 VAL B 147     -56.280  45.386 -46.848  1.00 37.41           C  
ATOM   3405  CG2 VAL B 147     -56.589  47.542 -45.605  1.00 16.45           C  
ATOM   3406  N   CYS B 148     -55.646  47.542 -50.059  1.00 15.22           N  
ATOM   3407  CA  CYS B 148     -55.642  47.002 -51.415  1.00 22.17           C  
ATOM   3408  C   CYS B 148     -54.303  47.233 -52.104  1.00 26.99           C  
ATOM   3409  O   CYS B 148     -53.686  46.291 -52.615  1.00 14.35           O  
ATOM   3410  CB  CYS B 148     -56.774  47.630 -52.229  1.00 28.74           C  
ATOM   3411  SG  CYS B 148     -58.348  47.797 -51.356  1.00 70.45           S  
ATOM   3412  N   ASP B 149     -53.840  48.482 -52.134  1.00 20.44           N  
ATOM   3413  CA  ASP B 149     -52.691  48.864 -52.942  1.00 14.32           C  
ATOM   3414  C   ASP B 149     -51.455  49.214 -52.125  1.00 14.78           C  
ATOM   3415  O   ASP B 149     -50.429  49.573 -52.711  1.00 14.55           O  
ATOM   3416  CB  ASP B 149     -53.063  50.049 -53.844  1.00 17.24           C  
ATOM   3417  CG  ASP B 149     -54.265  49.759 -54.728  1.00 27.58           C  
ATOM   3418  OD1 ASP B 149     -54.389  48.615 -55.216  1.00 38.10           O  
ATOM   3419  OD2 ASP B 149     -55.087  50.678 -54.935  1.00 26.73           O  
ATOM   3420  N   GLY B 150     -51.515  49.113 -50.795  1.00 15.39           N  
ATOM   3421  CA  GLY B 150     -50.378  49.508 -49.978  1.00 15.71           C  
ATOM   3422  C   GLY B 150     -49.150  48.640 -50.170  1.00 16.60           C  
ATOM   3423  O   GLY B 150     -48.021  49.114 -50.009  1.00 15.54           O  
ATOM   3424  N   ALA B 151     -49.342  47.371 -50.520  1.00 23.51           N  
ATOM   3425  CA  ALA B 151     -48.230  46.441 -50.658  1.00 24.00           C  
ATOM   3426  C   ALA B 151     -47.616  46.438 -52.051  1.00 23.68           C  
ATOM   3427  O   ALA B 151     -46.611  45.751 -52.262  1.00 18.16           O  
ATOM   3428  CB  ALA B 151     -48.683  45.022 -50.303  1.00 47.20           C  
ATOM   3429  N   VAL B 152     -48.198  47.171 -52.997  1.00 19.14           N  
ATOM   3430  CA  VAL B 152     -47.700  47.250 -54.370  1.00 14.69           C  
ATOM   3431  C   VAL B 152     -46.234  47.668 -54.338  1.00 16.06           C  
ATOM   3432  O   VAL B 152     -45.863  48.559 -53.559  1.00 14.15           O  
ATOM   3433  CB  VAL B 152     -48.554  48.215 -55.209  1.00 13.30           C  
ATOM   3434  CG1 VAL B 152     -47.971  48.391 -56.604  1.00 20.86           C  
ATOM   3435  CG2 VAL B 152     -49.987  47.711 -55.290  1.00 13.23           C  
ATOM   3436  N   PRO B 153     -45.365  47.036 -55.134  1.00 13.22           N  
ATOM   3437  CA  PRO B 153     -43.924  47.330 -55.037  1.00 33.86           C  
ATOM   3438  C   PRO B 153     -43.554  48.775 -55.330  1.00 40.92           C  
ATOM   3439  O   PRO B 153     -42.488  49.222 -54.886  1.00 30.93           O  
ATOM   3440  CB  PRO B 153     -43.305  46.379 -56.072  1.00 20.75           C  
ATOM   3441  CG  PRO B 153     -44.282  45.265 -56.188  1.00 10.87           C  
ATOM   3442  CD  PRO B 153     -45.635  45.890 -56.020  1.00 12.06           C  
ATOM   3443  N   ILE B 154     -44.386  49.523 -56.061  1.00 31.11           N  
ATOM   3444  CA  ILE B 154     -44.047  50.902 -56.397  1.00 12.24           C  
ATOM   3445  C   ILE B 154     -44.065  51.829 -55.191  1.00 13.06           C  
ATOM   3446  O   ILE B 154     -43.587  52.965 -55.289  1.00 26.33           O  
ATOM   3447  CB  ILE B 154     -44.998  51.460 -57.475  1.00 11.51           C  
ATOM   3448  CG1 ILE B 154     -46.386  51.715 -56.883  1.00 12.08           C  
ATOM   3449  CG2 ILE B 154     -45.073  50.506 -58.658  1.00 10.45           C  
ATOM   3450  CD1 ILE B 154     -47.360  52.349 -57.854  1.00 11.45           C  
ATOM   3451  N   PHE B 155     -44.603  51.378 -54.059  1.00 13.75           N  
ATOM   3452  CA  PHE B 155     -44.640  52.168 -52.837  1.00 14.29           C  
ATOM   3453  C   PHE B 155     -43.626  51.710 -51.798  1.00 14.59           C  
ATOM   3454  O   PHE B 155     -43.453  52.394 -50.782  1.00 14.91           O  
ATOM   3455  CB  PHE B 155     -46.044  52.129 -52.218  1.00 14.66           C  
ATOM   3456  CG  PHE B 155     -47.139  52.531 -53.164  1.00 14.27           C  
ATOM   3457  CD1 PHE B 155     -47.173  53.802 -53.710  1.00 13.94           C  
ATOM   3458  CD2 PHE B 155     -48.137  51.636 -53.504  1.00 14.15           C  
ATOM   3459  CE1 PHE B 155     -48.183  54.171 -54.581  1.00 13.50           C  
ATOM   3460  CE2 PHE B 155     -49.148  52.000 -54.372  1.00 13.68           C  
ATOM   3461  CZ  PHE B 155     -49.171  53.268 -54.910  1.00 13.36           C  
ATOM   3462  N   ARG B 156     -42.964  50.577 -52.017  1.00 17.27           N  
ATOM   3463  CA  ARG B 156     -42.053  50.030 -51.020  1.00 18.62           C  
ATOM   3464  C   ARG B 156     -40.775  50.857 -50.948  1.00 15.58           C  
ATOM   3465  O   ARG B 156     -40.158  51.157 -51.976  1.00 20.60           O  
ATOM   3466  CB  ARG B 156     -41.722  48.577 -51.357  1.00 28.16           C  
ATOM   3467  CG  ARG B 156     -41.014  47.815 -50.249  1.00 44.26           C  
ATOM   3468  CD  ARG B 156     -41.977  47.453 -49.133  1.00 30.95           C  
ATOM   3469  NE  ARG B 156     -43.130  46.713 -49.637  1.00 25.13           N  
ATOM   3470  CZ  ARG B 156     -43.166  45.393 -49.779  1.00 29.73           C  
ATOM   3471  NH1 ARG B 156     -42.108  44.661 -49.456  1.00 44.56           N  
ATOM   3472  NH2 ARG B 156     -44.258  44.804 -50.246  1.00 24.55           N  
ATOM   3473  N   ASN B 157     -40.383  51.226 -49.725  1.00 14.13           N  
ATOM   3474  CA  ASN B 157     -39.175  52.018 -49.476  1.00 25.46           C  
ATOM   3475  C   ASN B 157     -39.189  53.325 -50.265  1.00 24.08           C  
ATOM   3476  O   ASN B 157     -38.171  53.752 -50.813  1.00 38.95           O  
ATOM   3477  CB  ASN B 157     -37.910  51.213 -49.781  1.00 33.14           C  
ATOM   3478  CG  ASN B 157     -37.724  50.041 -48.840  1.00 54.83           C  
ATOM   3479  OD1 ASN B 157     -37.671  48.889 -49.270  1.00 55.04           O  
ATOM   3480  ND2 ASN B 157     -37.628  50.328 -47.545  1.00 71.02           N  
ATOM   3481  N   LYS B 158     -40.348  53.966 -50.321  1.00 14.42           N  
ATOM   3482  CA  LYS B 158     -40.525  55.226 -51.022  1.00 14.29           C  
ATOM   3483  C   LYS B 158     -41.322  56.162 -50.132  1.00 14.65           C  
ATOM   3484  O   LYS B 158     -42.044  55.710 -49.235  1.00 26.79           O  
ATOM   3485  CB  LYS B 158     -41.243  55.031 -52.365  1.00 13.96           C  
ATOM   3486  CG  LYS B 158     -40.460  54.205 -53.374  1.00 13.53           C  
ATOM   3487  CD  LYS B 158     -39.135  54.859 -53.730  1.00 13.18           C  
ATOM   3488  CE  LYS B 158     -38.470  54.142 -54.896  1.00 27.74           C  
ATOM   3489  NZ  LYS B 158     -39.353  54.100 -56.097  1.00 62.90           N  
ATOM   3490  N   PRO B 159     -41.200  57.473 -50.338  1.00 14.44           N  
ATOM   3491  CA  PRO B 159     -41.993  58.420 -49.541  1.00 14.66           C  
ATOM   3492  C   PRO B 159     -43.461  58.381 -49.942  1.00 16.70           C  
ATOM   3493  O   PRO B 159     -43.802  58.512 -51.120  1.00 14.54           O  
ATOM   3494  CB  PRO B 159     -41.353  59.775 -49.862  1.00 14.23           C  
ATOM   3495  CG  PRO B 159     -40.736  59.585 -51.210  1.00 13.80           C  
ATOM   3496  CD  PRO B 159     -40.252  58.162 -51.231  1.00 15.08           C  
ATOM   3497  N   LEU B 160     -44.330  58.196 -48.950  1.00 18.35           N  
ATOM   3498  CA  LEU B 160     -45.767  58.117 -49.162  1.00 15.39           C  
ATOM   3499  C   LEU B 160     -46.459  59.271 -48.448  1.00 15.41           C  
ATOM   3500  O   LEU B 160     -46.015  59.721 -47.387  1.00 15.40           O  
ATOM   3501  CB  LEU B 160     -46.330  56.780 -48.664  1.00 15.82           C  
ATOM   3502  CG  LEU B 160     -45.689  55.517 -49.246  1.00 15.69           C  
ATOM   3503  CD1 LEU B 160     -46.352  54.259 -48.693  1.00 16.04           C  
ATOM   3504  CD2 LEU B 160     -45.753  55.541 -50.764  1.00 15.12           C  
ATOM   3505  N   TYR B 161     -47.556  59.744 -49.037  1.00 15.28           N  
ATOM   3506  CA  TYR B 161     -48.310  60.872 -48.507  1.00 22.27           C  
ATOM   3507  C   TYR B 161     -49.776  60.488 -48.358  1.00 18.42           C  
ATOM   3508  O   TYR B 161     -50.337  59.795 -49.212  1.00 15.46           O  
ATOM   3509  CB  TYR B 161     -48.173  62.110 -49.413  1.00 18.28           C  
ATOM   3510  CG  TYR B 161     -46.877  62.869 -49.216  1.00 16.93           C  
ATOM   3511  CD1 TYR B 161     -45.658  62.291 -49.546  1.00 30.98           C  
ATOM   3512  CD2 TYR B 161     -46.872  64.167 -48.718  1.00 17.98           C  
ATOM   3513  CE1 TYR B 161     -44.470  62.971 -49.371  1.00 25.40           C  
ATOM   3514  CE2 TYR B 161     -45.683  64.859 -48.541  1.00 32.63           C  
ATOM   3515  CZ  TYR B 161     -44.485  64.253 -48.870  1.00 27.20           C  
ATOM   3516  OH  TYR B 161     -43.295  64.922 -48.701  1.00 24.17           O  
ATOM   3517  N   VAL B 162     -50.386  60.938 -47.263  1.00 15.35           N  
ATOM   3518  CA  VAL B 162     -51.785  60.663 -46.957  1.00 15.52           C  
ATOM   3519  C   VAL B 162     -52.520  61.988 -46.814  1.00 18.91           C  
ATOM   3520  O   VAL B 162     -51.991  62.942 -46.231  1.00 20.99           O  
ATOM   3521  CB  VAL B 162     -51.929  59.816 -45.675  1.00 15.96           C  
ATOM   3522  CG1 VAL B 162     -53.381  59.431 -45.448  1.00 16.17           C  
ATOM   3523  CG2 VAL B 162     -51.051  58.577 -45.755  1.00 16.47           C  
ATOM   3524  N   ILE B 163     -53.743  62.041 -47.335  1.00 23.20           N  
ATOM   3525  CA  ILE B 163     -54.579  63.236 -47.291  1.00 13.70           C  
ATOM   3526  C   ILE B 163     -55.778  62.944 -46.402  1.00 13.62           C  
ATOM   3527  O   ILE B 163     -56.533  61.999 -46.657  1.00 57.01           O  
ATOM   3528  CB  ILE B 163     -55.037  63.663 -48.694  1.00 13.29           C  
ATOM   3529  CG1 ILE B 163     -53.836  64.032 -49.564  1.00 13.27           C  
ATOM   3530  CG2 ILE B 163     -56.026  64.818 -48.603  1.00 12.00           C  
ATOM   3531  CD1 ILE B 163     -54.210  64.438 -50.971  1.00 12.76           C  
ATOM   3532  N   GLY B 164     -55.955  63.751 -45.371  1.00 12.72           N  
ATOM   3533  CA  GLY B 164     -57.081  63.621 -44.466  1.00 15.94           C  
ATOM   3534  C   GLY B 164     -56.646  63.800 -43.025  1.00 16.81           C  
ATOM   3535  O   GLY B 164     -55.484  63.618 -42.665  1.00 23.37           O  
ATOM   3536  N   GLY B 165     -57.610  64.153 -42.180  1.00 17.59           N  
ATOM   3537  CA  GLY B 165     -57.344  64.360 -40.772  1.00 16.50           C  
ATOM   3538  C   GLY B 165     -58.237  63.529 -39.876  1.00 11.44           C  
ATOM   3539  O   GLY B 165     -58.145  63.609 -38.648  1.00  8.83           O  
ATOM   3540  N   GLY B 166     -59.100  62.722 -40.484  1.00 28.29           N  
ATOM   3541  CA  GLY B 166     -60.033  61.902 -39.746  1.00 43.77           C  
ATOM   3542  C   GLY B 166     -59.403  60.616 -39.244  1.00 29.15           C  
ATOM   3543  O   GLY B 166     -58.187  60.423 -39.263  1.00 13.10           O  
ATOM   3544  N   ASP B 167     -60.272  59.718 -38.775  1.00 28.44           N  
ATOM   3545  CA  ASP B 167     -59.801  58.440 -38.252  1.00 22.20           C  
ATOM   3546  C   ASP B 167     -59.287  57.535 -39.365  1.00 23.95           C  
ATOM   3547  O   ASP B 167     -58.317  56.794 -39.169  1.00 21.14           O  
ATOM   3548  CB  ASP B 167     -60.916  57.753 -37.465  1.00 33.37           C  
ATOM   3549  CG  ASP B 167     -61.274  58.498 -36.194  1.00 39.27           C  
ATOM   3550  OD1 ASP B 167     -61.870  59.592 -36.291  1.00 39.72           O  
ATOM   3551  OD2 ASP B 167     -60.956  57.992 -35.096  1.00 38.95           O  
ATOM   3552  N   SER B 168     -59.929  57.575 -40.536  1.00 32.28           N  
ATOM   3553  CA  SER B 168     -59.466  56.774 -41.666  1.00 35.81           C  
ATOM   3554  C   SER B 168     -58.046  57.142 -42.074  1.00 44.66           C  
ATOM   3555  O   SER B 168     -57.291  56.281 -42.539  1.00 40.21           O  
ATOM   3556  CB  SER B 168     -60.421  56.936 -42.850  1.00 41.12           C  
ATOM   3557  OG  SER B 168     -60.567  58.302 -43.199  1.00 72.82           O  
ATOM   3558  N   ALA B 169     -57.668  58.413 -41.918  1.00 46.67           N  
ATOM   3559  CA  ALA B 169     -56.314  58.835 -42.261  1.00 22.34           C  
ATOM   3560  C   ALA B 169     -55.284  58.212 -41.327  1.00 22.01           C  
ATOM   3561  O   ALA B 169     -54.305  57.609 -41.782  1.00 41.31           O  
ATOM   3562  CB  ALA B 169     -56.217  60.361 -42.233  1.00 14.87           C  
ATOM   3563  N   ALA B 170     -55.489  58.347 -40.015  1.00 15.65           N  
ATOM   3564  CA  ALA B 170     -54.528  57.815 -39.053  1.00 15.45           C  
ATOM   3565  C   ALA B 170     -54.417  56.298 -39.150  1.00 16.67           C  
ATOM   3566  O   ALA B 170     -53.325  55.738 -38.996  1.00 16.80           O  
ATOM   3567  CB  ALA B 170     -54.919  58.234 -37.636  1.00 13.96           C  
ATOM   3568  N   GLU B 171     -55.537  55.616 -39.403  1.00 24.65           N  
ATOM   3569  CA  GLU B 171     -55.511  54.160 -39.508  1.00 31.38           C  
ATOM   3570  C   GLU B 171     -54.741  53.709 -40.743  1.00 28.23           C  
ATOM   3571  O   GLU B 171     -53.917  52.789 -40.673  1.00 24.52           O  
ATOM   3572  CB  GLU B 171     -56.938  53.608 -39.534  1.00 31.87           C  
ATOM   3573  CG  GLU B 171     -57.023  52.096 -39.385  1.00 47.71           C  
ATOM   3574  CD  GLU B 171     -58.453  51.587 -39.368  1.00 70.69           C  
ATOM   3575  OE1 GLU B 171     -59.376  52.393 -39.613  1.00 77.08           O  
ATOM   3576  OE2 GLU B 171     -58.654  50.381 -39.111  1.00 79.19           O  
ATOM   3577  N   GLU B 172     -54.993  54.348 -41.886  1.00 25.07           N  
ATOM   3578  CA  GLU B 172     -54.308  53.960 -43.113  1.00 22.06           C  
ATOM   3579  C   GLU B 172     -52.862  54.437 -43.139  1.00 23.57           C  
ATOM   3580  O   GLU B 172     -52.018  53.802 -43.782  1.00 26.70           O  
ATOM   3581  CB  GLU B 172     -55.068  54.489 -44.331  1.00 18.07           C  
ATOM   3582  CG  GLU B 172     -56.390  53.774 -44.573  1.00 36.27           C  
ATOM   3583  CD  GLU B 172     -56.920  53.972 -45.979  1.00 41.97           C  
ATOM   3584  OE1 GLU B 172     -56.306  54.746 -46.745  1.00 32.19           O  
ATOM   3585  OE2 GLU B 172     -57.946  53.346 -46.319  1.00 35.30           O  
ATOM   3586  N   ALA B 173     -52.555  55.542 -42.455  1.00 29.90           N  
ATOM   3587  CA  ALA B 173     -51.182  56.038 -42.424  1.00 17.53           C  
ATOM   3588  C   ALA B 173     -50.261  55.059 -41.706  1.00 20.62           C  
ATOM   3589  O   ALA B 173     -49.183  54.722 -42.210  1.00 24.60           O  
ATOM   3590  CB  ALA B 173     -51.134  57.412 -41.757  1.00 16.63           C  
ATOM   3591  N   MET B 174     -50.665  54.602 -40.518  1.00 18.15           N  
ATOM   3592  CA  MET B 174     -49.855  53.634 -39.786  1.00 17.41           C  
ATOM   3593  C   MET B 174     -49.774  52.301 -40.518  1.00 17.78           C  
ATOM   3594  O   MET B 174     -48.790  51.569 -40.362  1.00 25.25           O  
ATOM   3595  CB  MET B 174     -50.418  53.435 -38.379  1.00 21.95           C  
ATOM   3596  CG  MET B 174     -50.392  54.688 -37.520  1.00 15.64           C  
ATOM   3597  SD  MET B 174     -51.012  54.401 -35.852  1.00 29.04           S  
ATOM   3598  CE  MET B 174     -49.828  53.199 -35.251  1.00 30.52           C  
ATOM   3599  N   PHE B 175     -50.795  51.966 -41.311  1.00 18.04           N  
ATOM   3600  CA  PHE B 175     -50.742  50.747 -42.112  1.00 17.82           C  
ATOM   3601  C   PHE B 175     -49.736  50.877 -43.251  1.00 27.78           C  
ATOM   3602  O   PHE B 175     -49.025  49.916 -43.570  1.00 26.62           O  
ATOM   3603  CB  PHE B 175     -52.132  50.413 -42.654  1.00 18.62           C  
ATOM   3604  CG  PHE B 175     -52.214  49.072 -43.327  1.00 21.57           C  
ATOM   3605  CD1 PHE B 175     -52.404  47.920 -42.583  1.00 21.29           C  
ATOM   3606  CD2 PHE B 175     -52.106  48.965 -44.704  1.00 18.36           C  
ATOM   3607  CE1 PHE B 175     -52.481  46.684 -43.200  1.00 20.26           C  
ATOM   3608  CE2 PHE B 175     -52.182  47.733 -45.326  1.00 16.66           C  
ATOM   3609  CZ  PHE B 175     -52.370  46.591 -44.573  1.00 17.52           C  
ATOM   3610  N   LEU B 176     -49.666  52.054 -43.878  1.00 36.84           N  
ATOM   3611  CA  LEU B 176     -48.720  52.278 -44.967  1.00 23.93           C  
ATOM   3612  C   LEU B 176     -47.272  52.293 -44.493  1.00 17.19           C  
ATOM   3613  O   LEU B 176     -46.363  52.162 -45.321  1.00 16.85           O  
ATOM   3614  CB  LEU B 176     -49.045  53.591 -45.684  1.00 17.32           C  
ATOM   3615  CG  LEU B 176     -50.329  53.616 -46.519  1.00 17.25           C  
ATOM   3616  CD1 LEU B 176     -50.698  55.040 -46.904  1.00 17.08           C  
ATOM   3617  CD2 LEU B 176     -50.186  52.745 -47.759  1.00 16.80           C  
ATOM   3618  N   ALA B 177     -47.035  52.456 -43.189  1.00 17.24           N  
ATOM   3619  CA  ALA B 177     -45.675  52.435 -42.663  1.00 16.82           C  
ATOM   3620  C   ALA B 177     -45.014  51.069 -42.804  1.00 17.76           C  
ATOM   3621  O   ALA B 177     -43.788  50.975 -42.684  1.00 18.87           O  
ATOM   3622  CB  ALA B 177     -45.670  52.864 -41.195  1.00 16.58           C  
ATOM   3623  N   LYS B 178     -45.795  50.012 -43.046  1.00 23.01           N  
ATOM   3624  CA  LYS B 178     -45.209  48.690 -43.239  1.00 22.56           C  
ATOM   3625  C   LYS B 178     -44.394  48.613 -44.524  1.00 25.52           C  
ATOM   3626  O   LYS B 178     -43.479  47.788 -44.626  1.00 34.14           O  
ATOM   3627  CB  LYS B 178     -46.301  47.620 -43.253  1.00 16.83           C  
ATOM   3628  CG  LYS B 178     -47.070  47.475 -41.948  1.00 29.15           C  
ATOM   3629  CD  LYS B 178     -48.130  46.386 -42.060  1.00 22.74           C  
ATOM   3630  CE  LYS B 178     -48.854  46.169 -40.740  1.00 15.32           C  
ATOM   3631  NZ  LYS B 178     -49.574  47.391 -40.289  1.00 31.51           N  
ATOM   3632  N   TYR B 179     -44.700  49.458 -45.507  1.00 15.82           N  
ATOM   3633  CA  TYR B 179     -44.077  49.369 -46.822  1.00 15.43           C  
ATOM   3634  C   TYR B 179     -43.249  50.594 -47.170  1.00 25.84           C  
ATOM   3635  O   TYR B 179     -42.089  50.455 -47.576  1.00 36.83           O  
ATOM   3636  CB  TYR B 179     -45.154  49.143 -47.895  1.00 15.54           C  
ATOM   3637  CG  TYR B 179     -46.179  48.101 -47.514  1.00 31.22           C  
ATOM   3638  CD1 TYR B 179     -45.920  46.748 -47.690  1.00 41.01           C  
ATOM   3639  CD2 TYR B 179     -47.405  48.469 -46.974  1.00 30.14           C  
ATOM   3640  CE1 TYR B 179     -46.852  45.791 -47.340  1.00 28.16           C  
ATOM   3641  CE2 TYR B 179     -48.343  47.518 -46.622  1.00 34.45           C  
ATOM   3642  CZ  TYR B 179     -48.062  46.182 -46.808  1.00 28.47           C  
ATOM   3643  OH  TYR B 179     -48.994  45.232 -46.459  1.00 32.16           O  
ATOM   3644  N   GLY B 180     -43.806  51.792 -47.019  1.00 15.86           N  
ATOM   3645  CA  GLY B 180     -43.106  52.983 -47.450  1.00 15.72           C  
ATOM   3646  C   GLY B 180     -41.942  53.335 -46.544  1.00 16.10           C  
ATOM   3647  O   GLY B 180     -41.877  52.950 -45.376  1.00 17.29           O  
ATOM   3648  N   SER B 181     -40.994  54.084 -47.112  1.00 15.21           N  
ATOM   3649  CA  SER B 181     -39.858  54.555 -46.326  1.00 14.90           C  
ATOM   3650  C   SER B 181     -40.295  55.578 -45.285  1.00 15.06           C  
ATOM   3651  O   SER B 181     -39.790  55.579 -44.156  1.00 28.58           O  
ATOM   3652  CB  SER B 181     -38.791  55.146 -47.246  1.00 22.11           C  
ATOM   3653  OG  SER B 181     -39.263  56.318 -47.888  1.00 44.95           O  
ATOM   3654  N   SER B 182     -41.229  56.455 -45.645  1.00 15.31           N  
ATOM   3655  CA  SER B 182     -41.742  57.458 -44.724  1.00 17.34           C  
ATOM   3656  C   SER B 182     -43.158  57.824 -45.138  1.00 15.54           C  
ATOM   3657  O   SER B 182     -43.451  57.946 -46.330  1.00 20.07           O  
ATOM   3658  CB  SER B 182     -40.855  58.709 -44.701  1.00 28.60           C  
ATOM   3659  OG  SER B 182     -40.733  59.276 -45.995  1.00 24.49           O  
ATOM   3660  N   VAL B 183     -44.032  57.989 -44.149  1.00 15.59           N  
ATOM   3661  CA  VAL B 183     -45.426  58.349 -44.373  1.00 15.80           C  
ATOM   3662  C   VAL B 183     -45.677  59.711 -43.743  1.00 15.16           C  
ATOM   3663  O   VAL B 183     -45.383  59.918 -42.560  1.00 37.56           O  
ATOM   3664  CB  VAL B 183     -46.387  57.292 -43.797  1.00 22.13           C  
ATOM   3665  CG1 VAL B 183     -47.831  57.730 -43.984  1.00 27.08           C  
ATOM   3666  CG2 VAL B 183     -46.145  55.942 -44.453  1.00 39.73           C  
ATOM   3667  N   THR B 184     -46.207  60.638 -44.535  1.00 14.97           N  
ATOM   3668  CA  THR B 184     -46.565  61.970 -44.068  1.00 17.72           C  
ATOM   3669  C   THR B 184     -48.049  62.195 -44.318  1.00 30.81           C  
ATOM   3670  O   THR B 184     -48.552  61.887 -45.403  1.00 22.89           O  
ATOM   3671  CB  THR B 184     -45.737  63.051 -44.769  1.00 23.39           C  
ATOM   3672  OG1 THR B 184     -45.857  62.898 -46.187  1.00 50.76           O  
ATOM   3673  CG2 THR B 184     -44.271  62.939 -44.382  1.00 13.47           C  
ATOM   3674  N   VAL B 185     -48.745  62.731 -43.318  1.00 35.66           N  
ATOM   3675  CA  VAL B 185     -50.179  62.984 -43.396  1.00 23.28           C  
ATOM   3676  C   VAL B 185     -50.396  64.484 -43.525  1.00 26.16           C  
ATOM   3677  O   VAL B 185     -49.841  65.268 -42.744  1.00 21.30           O  
ATOM   3678  CB  VAL B 185     -50.916  62.427 -42.166  1.00 13.36           C  
ATOM   3679  CG1 VAL B 185     -52.419  62.565 -42.340  1.00 13.30           C  
ATOM   3680  CG2 VAL B 185     -50.528  60.978 -41.928  1.00 14.34           C  
ATOM   3681  N   LEU B 186     -51.204  64.881 -44.503  1.00 25.25           N  
ATOM   3682  CA  LEU B 186     -51.425  66.288 -44.828  1.00 11.11           C  
ATOM   3683  C   LEU B 186     -52.844  66.660 -44.405  1.00 10.71           C  
ATOM   3684  O   LEU B 186     -53.785  66.586 -45.197  1.00 10.41           O  
ATOM   3685  CB  LEU B 186     -51.209  66.537 -46.317  1.00 11.42           C  
ATOM   3686  CG  LEU B 186     -49.939  65.950 -46.930  1.00 12.26           C  
ATOM   3687  CD1 LEU B 186     -49.895  66.238 -48.420  1.00 12.29           C  
ATOM   3688  CD2 LEU B 186     -48.702  66.493 -46.234  1.00 11.78           C  
ATOM   3689  N   VAL B 187     -52.993  67.057 -43.150  1.00 11.82           N  
ATOM   3690  CA  VAL B 187     -54.268  67.567 -42.664  1.00  7.92           C  
ATOM   3691  C   VAL B 187     -54.382  69.039 -43.041  1.00  8.19           C  
ATOM   3692  O   VAL B 187     -53.419  69.806 -42.918  1.00  5.47           O  
ATOM   3693  CB  VAL B 187     -54.402  67.332 -41.148  1.00  7.13           C  
ATOM   3694  CG1 VAL B 187     -54.159  65.872 -40.845  1.00 10.84           C  
ATOM   3695  CG2 VAL B 187     -53.422  68.170 -40.370  1.00  5.68           C  
ATOM   3696  N   ARG B 188     -55.555  69.441 -43.536  1.00  9.90           N  
ATOM   3697  CA  ARG B 188     -55.696  70.814 -44.010  1.00  3.62           C  
ATOM   3698  C   ARG B 188     -55.751  71.797 -42.846  1.00  4.93           C  
ATOM   3699  O   ARG B 188     -55.097  72.845 -42.882  1.00 14.33           O  
ATOM   3700  CB  ARG B 188     -56.928  70.949 -44.907  1.00  3.12           C  
ATOM   3701  CG  ARG B 188     -58.241  70.464 -44.314  1.00  8.98           C  
ATOM   3702  CD  ARG B 188     -59.357  70.604 -45.340  1.00 24.73           C  
ATOM   3703  NE  ARG B 188     -60.676  70.317 -44.784  1.00 43.42           N  
ATOM   3704  CZ  ARG B 188     -61.805  70.355 -45.486  1.00 42.96           C  
ATOM   3705  NH1 ARG B 188     -61.776  70.670 -46.774  1.00 35.10           N  
ATOM   3706  NH2 ARG B 188     -62.963  70.081 -44.901  1.00 38.13           N  
ATOM   3707  N   ARG B 189     -56.525  71.485 -41.814  1.00 11.80           N  
ATOM   3708  CA  ARG B 189     -56.600  72.326 -40.634  1.00 22.05           C  
ATOM   3709  C   ARG B 189     -55.639  71.802 -39.568  1.00 32.78           C  
ATOM   3710  O   ARG B 189     -54.807  70.926 -39.820  1.00 45.29           O  
ATOM   3711  CB  ARG B 189     -58.041  72.382 -40.122  1.00  8.59           C  
ATOM   3712  N   ASP B 190     -55.745  72.350 -38.364  1.00 17.38           N  
ATOM   3713  CA  ASP B 190     -54.912  71.977 -37.233  1.00  5.96           C  
ATOM   3714  C   ASP B 190     -55.679  70.990 -36.357  1.00 27.60           C  
ATOM   3715  O   ASP B 190     -56.867  70.739 -36.576  1.00 41.29           O  
ATOM   3716  CB  ASP B 190     -54.512  73.226 -36.440  1.00  1.95           C  
ATOM   3717  CG  ASP B 190     -53.327  72.988 -35.526  1.00 11.72           C  
ATOM   3718  OD1 ASP B 190     -52.782  71.865 -35.532  1.00  9.57           O  
ATOM   3719  OD2 ASP B 190     -52.940  73.930 -34.801  1.00 12.74           O  
ATOM   3720  N   LYS B 191     -54.988  70.419 -35.362  1.00 23.54           N  
ATOM   3721  CA  LYS B 191     -55.671  69.599 -34.362  1.00 21.36           C  
ATOM   3722  C   LYS B 191     -56.398  68.395 -34.954  1.00 36.06           C  
ATOM   3723  O   LYS B 191     -57.618  68.455 -35.140  1.00 56.78           O  
ATOM   3724  CB  LYS B 191     -56.654  70.453 -33.551  1.00  1.95           C  
ATOM   3725  N   LEU B 192     -55.660  67.325 -35.271  1.00 23.94           N  
ATOM   3726  CA  LEU B 192     -56.200  66.120 -35.906  1.00 16.22           C  
ATOM   3727  C   LEU B 192     -57.616  65.803 -35.439  1.00 11.20           C  
ATOM   3728  O   LEU B 192     -57.913  65.813 -34.241  1.00 14.98           O  
ATOM   3729  CB  LEU B 192     -55.299  64.919 -35.593  1.00 15.82           C  
ATOM   3730  CG  LEU B 192     -53.942  64.713 -36.257  1.00 22.52           C  
ATOM   3731  CD1 LEU B 192     -53.168  63.636 -35.522  1.00  8.30           C  
ATOM   3732  CD2 LEU B 192     -54.152  64.300 -37.695  1.00 28.50           C  
ATOM   3733  N   ARG B 193     -58.488  65.534 -36.412  1.00 12.36           N  
ATOM   3734  CA  ARG B 193     -59.891  65.198 -36.201  1.00 31.56           C  
ATOM   3735  C   ARG B 193     -60.103  63.769 -35.712  1.00 34.86           C  
ATOM   3736  O   ARG B 193     -61.241  63.402 -35.402  1.00 23.90           O  
ATOM   3737  CB  ARG B 193     -60.652  65.415 -37.515  1.00 39.40           C  
ATOM   3738  CG  ARG B 193     -62.163  65.559 -37.408  1.00 40.91           C  
ATOM   3739  CD  ARG B 193     -62.786  65.565 -38.800  1.00 31.95           C  
ATOM   3740  NE  ARG B 193     -64.223  65.825 -38.776  1.00 37.37           N  
ATOM   3741  CZ  ARG B 193     -64.769  67.015 -39.004  1.00 36.08           C  
ATOM   3742  NH1 ARG B 193     -63.997  68.057 -39.277  1.00 37.02           N  
ATOM   3743  NH2 ARG B 193     -66.086  67.162 -38.961  1.00 27.56           N  
ATOM   3744  N   ALA B 194     -59.049  62.961 -35.630  1.00 46.43           N  
ATOM   3745  CA  ALA B 194     -59.195  61.548 -35.317  1.00 45.38           C  
ATOM   3746  C   ALA B 194     -59.447  61.353 -33.821  1.00 44.15           C  
ATOM   3747  O   ALA B 194     -59.490  62.307 -33.038  1.00 39.13           O  
ATOM   3748  CB  ALA B 194     -57.960  60.775 -35.773  1.00 34.06           C  
ATOM   3749  N   SER B 195     -59.621  60.096 -33.418  1.00 29.02           N  
ATOM   3750  CA  SER B 195     -59.879  59.784 -32.020  1.00  8.87           C  
ATOM   3751  C   SER B 195     -58.642  60.052 -31.169  1.00 18.71           C  
ATOM   3752  O   SER B 195     -57.508  60.024 -31.653  1.00 48.80           O  
ATOM   3753  CB  SER B 195     -60.313  58.327 -31.869  1.00  4.72           C  
ATOM   3754  OG  SER B 195     -60.548  58.005 -30.510  1.00 30.21           O  
ATOM   3755  N   LYS B 196     -58.876  60.307 -29.879  1.00 15.04           N  
ATOM   3756  CA  LYS B 196     -57.781  60.657 -28.979  1.00 25.35           C  
ATOM   3757  C   LYS B 196     -56.849  59.475 -28.732  1.00 36.96           C  
ATOM   3758  O   LYS B 196     -55.632  59.655 -28.610  1.00 33.62           O  
ATOM   3759  CB  LYS B 196     -58.339  61.180 -27.656  1.00  5.38           C  
ATOM   3760  N   ALA B 197     -57.397  58.261 -28.655  1.00 25.73           N  
ATOM   3761  CA  ALA B 197     -56.565  57.097 -28.369  1.00 18.67           C  
ATOM   3762  C   ALA B 197     -55.802  56.622 -29.599  1.00 15.83           C  
ATOM   3763  O   ALA B 197     -54.627  56.255 -29.498  1.00 28.56           O  
ATOM   3764  CB  ALA B 197     -57.423  55.965 -27.809  1.00 10.44           C  
ATOM   3765  N   MET B 198     -56.450  56.618 -30.765  1.00  8.62           N  
ATOM   3766  CA  MET B 198     -55.755  56.220 -31.984  1.00 15.18           C  
ATOM   3767  C   MET B 198     -54.707  57.248 -32.392  1.00 10.65           C  
ATOM   3768  O   MET B 198     -53.679  56.886 -32.975  1.00  7.90           O  
ATOM   3769  CB  MET B 198     -56.756  55.995 -33.113  1.00 11.48           C  
ATOM   3770  CG  MET B 198     -56.142  55.396 -34.362  1.00 28.60           C  
ATOM   3771  SD  MET B 198     -57.326  55.389 -35.710  1.00 51.35           S  
ATOM   3772  CE  MET B 198     -57.797  57.112 -35.682  1.00 45.07           C  
ATOM   3773  N   ALA B 199     -54.951  58.530 -32.109  1.00 10.56           N  
ATOM   3774  CA  ALA B 199     -53.942  59.549 -32.379  1.00 20.06           C  
ATOM   3775  C   ALA B 199     -52.731  59.394 -31.469  1.00 18.75           C  
ATOM   3776  O   ALA B 199     -51.624  59.797 -31.842  1.00 13.34           O  
ATOM   3777  CB  ALA B 199     -54.542  60.947 -32.228  1.00 17.97           C  
ATOM   3778  N   LYS B 200     -52.919  58.828 -30.273  1.00 15.96           N  
ATOM   3779  CA  LYS B 200     -51.792  58.614 -29.370  1.00 17.71           C  
ATOM   3780  C   LYS B 200     -50.744  57.709 -30.008  1.00 27.25           C  
ATOM   3781  O   LYS B 200     -49.549  58.029 -30.012  1.00  1.96           O  
ATOM   3782  CB  LYS B 200     -52.284  58.024 -28.048  1.00  1.95           C  
ATOM   3783  N   ARG B 201     -51.174  56.568 -30.552  1.00 41.90           N  
ATOM   3784  CA  ARG B 201     -50.245  55.675 -31.235  1.00 33.84           C  
ATOM   3785  C   ARG B 201     -49.785  56.233 -32.577  1.00 33.98           C  
ATOM   3786  O   ARG B 201     -48.745  55.803 -33.086  1.00 32.04           O  
ATOM   3787  CB  ARG B 201     -50.867  54.287 -31.423  1.00  5.82           C  
ATOM   3788  CG  ARG B 201     -52.066  54.235 -32.354  1.00  7.82           C  
ATOM   3789  CD  ARG B 201     -52.487  52.794 -32.617  1.00 25.81           C  
ATOM   3790  NE  ARG B 201     -53.656  52.704 -33.488  1.00 36.40           N  
ATOM   3791  CZ  ARG B 201     -54.166  51.563 -33.941  1.00 20.64           C  
ATOM   3792  NH1 ARG B 201     -53.606  50.407 -33.611  1.00 16.62           N  
ATOM   3793  NH2 ARG B 201     -55.233  51.575 -34.729  1.00 13.20           N  
ATOM   3794  N   LEU B 202     -50.532  57.174 -33.160  1.00 26.90           N  
ATOM   3795  CA  LEU B 202     -50.129  57.760 -34.436  1.00 13.35           C  
ATOM   3796  C   LEU B 202     -48.888  58.630 -34.271  1.00 19.00           C  
ATOM   3797  O   LEU B 202     -47.855  58.386 -34.905  1.00 23.97           O  
ATOM   3798  CB  LEU B 202     -51.279  58.576 -35.030  1.00  9.79           C  
ATOM   3799  CG  LEU B 202     -50.957  59.312 -36.335  1.00 10.96           C  
ATOM   3800  CD1 LEU B 202     -50.660  58.333 -37.463  1.00 13.05           C  
ATOM   3801  CD2 LEU B 202     -52.077  60.265 -36.721  1.00 10.75           C  
ATOM   3802  N   LEU B 203     -48.971  59.655 -33.420  1.00 13.67           N  
ATOM   3803  CA  LEU B 203     -47.823  60.526 -33.191  1.00 18.01           C  
ATOM   3804  C   LEU B 203     -46.660  59.803 -32.526  1.00 36.81           C  
ATOM   3805  O   LEU B 203     -45.544  60.335 -32.523  1.00 40.77           O  
ATOM   3806  CB  LEU B 203     -48.226  61.743 -32.352  1.00 21.70           C  
ATOM   3807  CG  LEU B 203     -49.085  62.833 -33.006  1.00 11.39           C  
ATOM   3808  CD1 LEU B 203     -50.547  62.435 -33.145  1.00  2.99           C  
ATOM   3809  CD2 LEU B 203     -48.956  64.141 -32.236  1.00  7.01           C  
ATOM   3810  N   ALA B 204     -46.888  58.614 -31.968  1.00 41.63           N  
ATOM   3811  CA  ALA B 204     -45.817  57.832 -31.369  1.00 34.38           C  
ATOM   3812  C   ALA B 204     -45.139  56.901 -32.365  1.00 38.83           C  
ATOM   3813  O   ALA B 204     -44.002  56.481 -32.121  1.00 32.48           O  
ATOM   3814  CB  ALA B 204     -46.352  57.014 -30.189  1.00 19.95           C  
ATOM   3815  N   HIS B 205     -45.805  56.569 -33.467  1.00 39.09           N  
ATOM   3816  CA  HIS B 205     -45.207  55.696 -34.471  1.00 31.63           C  
ATOM   3817  C   HIS B 205     -44.025  56.404 -35.125  1.00 24.87           C  
ATOM   3818  O   HIS B 205     -44.150  57.568 -35.523  1.00 20.79           O  
ATOM   3819  CB  HIS B 205     -46.244  55.301 -35.522  1.00 36.05           C  
ATOM   3820  CG  HIS B 205     -45.880  54.079 -36.307  1.00 42.00           C  
ATOM   3821  ND1 HIS B 205     -44.881  54.072 -37.257  1.00 44.32           N  
ATOM   3822  CD2 HIS B 205     -46.388  52.824 -36.289  1.00 38.27           C  
ATOM   3823  CE1 HIS B 205     -44.786  52.865 -37.786  1.00 44.08           C  
ATOM   3824  NE2 HIS B 205     -45.690  52.089 -37.216  1.00 41.52           N  
ATOM   3825  N   PRO B 206     -42.871  55.745 -35.256  1.00 30.53           N  
ATOM   3826  CA  PRO B 206     -41.677  56.469 -35.724  1.00 30.57           C  
ATOM   3827  C   PRO B 206     -41.716  56.829 -37.198  1.00 33.27           C  
ATOM   3828  O   PRO B 206     -41.276  57.923 -37.574  1.00 36.83           O  
ATOM   3829  CB  PRO B 206     -40.537  55.492 -35.405  1.00 19.03           C  
ATOM   3830  CG  PRO B 206     -41.183  54.147 -35.448  1.00 23.67           C  
ATOM   3831  CD  PRO B 206     -42.573  54.345 -34.909  1.00 29.88           C  
ATOM   3832  N   LYS B 207     -42.228  55.942 -38.048  1.00 28.10           N  
ATOM   3833  CA  LYS B 207     -42.133  56.119 -39.491  1.00 38.26           C  
ATOM   3834  C   LYS B 207     -43.235  57.001 -40.072  1.00 28.87           C  
ATOM   3835  O   LYS B 207     -43.322  57.119 -41.299  1.00 14.80           O  
ATOM   3836  CB  LYS B 207     -42.147  54.751 -40.179  1.00 41.29           C  
ATOM   3837  CG  LYS B 207     -40.875  53.943 -39.964  1.00 38.99           C  
ATOM   3838  CD  LYS B 207     -40.828  52.713 -40.855  1.00 25.54           C  
ATOM   3839  CE  LYS B 207     -40.769  53.093 -42.323  1.00 17.11           C  
ATOM   3840  NZ  LYS B 207     -40.675  51.895 -43.202  1.00 19.28           N  
ATOM   3841  N   VAL B 208     -44.068  57.626 -39.241  1.00 26.29           N  
ATOM   3842  CA  VAL B 208     -45.110  58.532 -39.711  1.00 13.67           C  
ATOM   3843  C   VAL B 208     -44.897  59.903 -39.080  1.00 12.27           C  
ATOM   3844  O   VAL B 208     -44.454  60.008 -37.931  1.00 36.74           O  
ATOM   3845  CB  VAL B 208     -46.522  57.986 -39.398  1.00 14.12           C  
ATOM   3846  CG1 VAL B 208     -46.766  57.934 -37.900  1.00 12.88           C  
ATOM   3847  CG2 VAL B 208     -47.593  58.813 -40.098  1.00 14.92           C  
ATOM   3848  N   THR B 209     -45.196  60.953 -39.845  1.00 12.32           N  
ATOM   3849  CA  THR B 209     -45.115  62.328 -39.367  1.00 18.12           C  
ATOM   3850  C   THR B 209     -46.324  63.096 -39.879  1.00 19.86           C  
ATOM   3851  O   THR B 209     -46.613  63.072 -41.078  1.00 12.91           O  
ATOM   3852  CB  THR B 209     -43.819  63.016 -39.825  1.00 17.77           C  
ATOM   3853  OG1 THR B 209     -43.686  62.901 -41.247  1.00 13.44           O  
ATOM   3854  CG2 THR B 209     -42.600  62.397 -39.149  1.00 12.52           C  
ATOM   3855  N   VAL B 210     -47.026  63.772 -38.974  1.00 23.35           N  
ATOM   3856  CA  VAL B 210     -48.219  64.537 -39.323  1.00 21.79           C  
ATOM   3857  C   VAL B 210     -47.822  65.984 -39.578  1.00 16.60           C  
ATOM   3858  O   VAL B 210     -47.198  66.627 -38.725  1.00 24.46           O  
ATOM   3859  CB  VAL B 210     -49.281  64.443 -38.214  1.00 23.71           C  
ATOM   3860  CG1 VAL B 210     -50.543  65.188 -38.627  1.00 23.32           C  
ATOM   3861  CG2 VAL B 210     -49.593  62.988 -37.899  1.00 19.72           C  
ATOM   3862  N   ARG B 211     -48.189  66.501 -40.748  1.00 13.24           N  
ATOM   3863  CA  ARG B 211     -47.894  67.877 -41.143  1.00  9.73           C  
ATOM   3864  C   ARG B 211     -49.195  68.671 -41.120  1.00 12.16           C  
ATOM   3865  O   ARG B 211     -49.984  68.619 -42.069  1.00  8.66           O  
ATOM   3866  CB  ARG B 211     -47.239  67.926 -42.520  1.00  8.77           C  
ATOM   3867  CG  ARG B 211     -45.847  67.326 -42.568  1.00 12.00           C  
ATOM   3868  CD  ARG B 211     -45.119  67.759 -43.827  1.00 12.18           C  
ATOM   3869  NE  ARG B 211     -45.153  69.209 -43.994  1.00  8.68           N  
ATOM   3870  CZ  ARG B 211     -44.478  69.869 -44.929  1.00 21.40           C  
ATOM   3871  NH1 ARG B 211     -43.708  69.207 -45.782  1.00 32.70           N  
ATOM   3872  NH2 ARG B 211     -44.568  71.190 -45.009  1.00 17.60           N  
ATOM   3873  N   PHE B 212     -49.415  69.402 -40.031  1.00 18.23           N  
ATOM   3874  CA  PHE B 212     -50.619  70.207 -39.899  1.00 12.87           C  
ATOM   3875  C   PHE B 212     -50.580  71.400 -40.847  1.00 19.96           C  
ATOM   3876  O   PHE B 212     -49.511  71.889 -41.224  1.00 41.64           O  
ATOM   3877  CB  PHE B 212     -50.778  70.692 -38.459  1.00 14.51           C  
ATOM   3878  CG  PHE B 212     -50.852  69.582 -37.448  1.00 27.95           C  
ATOM   3879  CD1 PHE B 212     -52.047  68.926 -37.203  1.00 28.14           C  
ATOM   3880  CD2 PHE B 212     -49.724  69.195 -36.744  1.00 29.11           C  
ATOM   3881  CE1 PHE B 212     -52.115  67.903 -36.274  1.00 18.30           C  
ATOM   3882  CE2 PHE B 212     -49.785  68.174 -35.814  1.00 35.25           C  
ATOM   3883  CZ  PHE B 212     -50.983  67.527 -35.578  1.00 31.02           C  
ATOM   3884  N   ASN B 213     -51.771  71.869 -41.228  1.00  9.56           N  
ATOM   3885  CA  ASN B 213     -51.936  73.035 -42.096  1.00 10.78           C  
ATOM   3886  C   ASN B 213     -51.186  72.855 -43.419  1.00  2.46           C  
ATOM   3887  O   ASN B 213     -50.339  73.663 -43.804  1.00 18.58           O  
ATOM   3888  CB  ASN B 213     -51.496  74.316 -41.378  1.00 11.85           C  
ATOM   3889  CG  ASN B 213     -52.463  74.733 -40.290  1.00  1.95           C  
ATOM   3890  OD1 ASN B 213     -53.680  74.664 -40.466  1.00  1.95           O  
ATOM   3891  ND2 ASN B 213     -51.927  75.174 -39.158  1.00  1.95           N  
ATOM   3892  N   THR B 214     -51.518  71.771 -44.116  1.00  4.31           N  
ATOM   3893  CA  THR B 214     -50.868  71.434 -45.376  1.00  5.72           C  
ATOM   3894  C   THR B 214     -51.888  70.809 -46.315  1.00  7.35           C  
ATOM   3895  O   THR B 214     -52.665  69.942 -45.904  1.00 22.62           O  
ATOM   3896  CB  THR B 214     -49.691  70.474 -45.153  1.00 13.91           C  
ATOM   3897  OG1 THR B 214     -48.789  71.038 -44.192  1.00 15.78           O  
ATOM   3898  CG2 THR B 214     -48.944  70.227 -46.455  1.00 19.00           C  
ATOM   3899  N   VAL B 215     -51.884  71.251 -47.572  1.00  6.38           N  
ATOM   3900  CA  VAL B 215     -52.827  70.790 -48.584  1.00  6.74           C  
ATOM   3901  C   VAL B 215     -52.057  70.444 -49.851  1.00  7.70           C  
ATOM   3902  O   VAL B 215     -51.147  71.176 -50.257  1.00  7.28           O  
ATOM   3903  CB  VAL B 215     -53.910  71.852 -48.881  1.00  4.76           C  
ATOM   3904  CG1 VAL B 215     -54.849  71.374 -49.979  1.00  4.91           C  
ATOM   3905  CG2 VAL B 215     -54.692  72.192 -47.619  1.00  8.89           C  
ATOM   3906  N   ALA B 216     -52.421  69.325 -50.474  1.00  9.17           N  
ATOM   3907  CA  ALA B 216     -51.829  68.927 -51.744  1.00  9.49           C  
ATOM   3908  C   ALA B 216     -52.461  69.720 -52.881  1.00  8.74           C  
ATOM   3909  O   ALA B 216     -53.688  69.840 -52.956  1.00 24.20           O  
ATOM   3910  CB  ALA B 216     -52.016  67.428 -51.972  1.00 10.86           C  
ATOM   3911  N   THR B 217     -51.626  70.259 -53.769  1.00  7.80           N  
ATOM   3912  CA  THR B 217     -52.096  71.133 -54.839  1.00  6.13           C  
ATOM   3913  C   THR B 217     -52.090  70.478 -56.210  1.00  6.28           C  
ATOM   3914  O   THR B 217     -53.020  70.692 -56.990  1.00 18.25           O  
ATOM   3915  CB  THR B 217     -51.240  72.405 -54.894  1.00  5.08           C  
ATOM   3916  OG1 THR B 217     -51.204  73.015 -53.599  1.00 18.42           O  
ATOM   3917  CG2 THR B 217     -51.814  73.396 -55.898  1.00  9.42           C  
ATOM   3918  N   GLU B 218     -51.071  69.684 -56.531  1.00  7.65           N  
ATOM   3919  CA  GLU B 218     -51.019  69.014 -57.823  1.00  7.53           C  
ATOM   3920  C   GLU B 218     -50.092  67.813 -57.714  1.00  9.25           C  
ATOM   3921  O   GLU B 218     -49.171  67.795 -56.894  1.00 10.29           O  
ATOM   3922  CB  GLU B 218     -50.568  69.953 -58.951  1.00  5.97           C  
ATOM   3923  CG  GLU B 218     -49.120  70.384 -58.907  1.00 10.39           C  
ATOM   3924  CD  GLU B 218     -48.729  71.199 -60.125  1.00 39.03           C  
ATOM   3925  OE1 GLU B 218     -49.429  71.097 -61.155  1.00 28.68           O  
ATOM   3926  OE2 GLU B 218     -47.728  71.944 -60.054  1.00 52.25           O  
ATOM   3927  N   VAL B 219     -50.362  66.805 -58.538  1.00 12.41           N  
ATOM   3928  CA  VAL B 219     -49.600  65.562 -58.558  1.00 10.16           C  
ATOM   3929  C   VAL B 219     -48.708  65.564 -59.792  1.00 10.88           C  
ATOM   3930  O   VAL B 219     -49.191  65.752 -60.916  1.00  7.68           O  
ATOM   3931  CB  VAL B 219     -50.527  64.335 -58.547  1.00 10.37           C  
ATOM   3932  CG1 VAL B 219     -49.728  63.058 -58.753  1.00 10.52           C  
ATOM   3933  CG2 VAL B 219     -51.307  64.277 -57.243  1.00 11.54           C  
ATOM   3934  N   LEU B 220     -47.408  65.361 -59.582  1.00 13.71           N  
ATOM   3935  CA  LEU B 220     -46.425  65.337 -60.654  1.00 10.35           C  
ATOM   3936  C   LEU B 220     -45.819  63.945 -60.758  1.00  8.87           C  
ATOM   3937  O   LEU B 220     -45.764  63.198 -59.776  1.00  9.76           O  
ATOM   3938  CB  LEU B 220     -45.301  66.368 -60.432  1.00  8.85           C  
ATOM   3939  CG  LEU B 220     -45.613  67.866 -60.347  1.00  8.47           C  
ATOM   3940  CD1 LEU B 220     -46.608  68.280 -61.424  1.00  6.86           C  
ATOM   3941  CD2 LEU B 220     -46.100  68.266 -58.960  1.00  9.53           C  
ATOM   3942  N   GLY B 221     -45.380  63.595 -61.959  1.00  7.82           N  
ATOM   3943  CA  GLY B 221     -44.762  62.301 -62.161  1.00  7.78           C  
ATOM   3944  C   GLY B 221     -44.266  62.138 -63.577  1.00  6.40           C  
ATOM   3945  O   GLY B 221     -44.137  63.109 -64.327  1.00  9.61           O  
ATOM   3946  N   GLU B 222     -43.980  60.887 -63.929  1.00  6.10           N  
ATOM   3947  CA  GLU B 222     -43.549  60.560 -65.280  1.00  4.60           C  
ATOM   3948  C   GLU B 222     -44.678  60.799 -66.276  1.00  3.31           C  
ATOM   3949  O   GLU B 222     -45.860  60.726 -65.936  1.00  6.55           O  
ATOM   3950  CB  GLU B 222     -43.103  59.098 -65.355  1.00  4.47           C  
ATOM   3951  CG  GLU B 222     -42.185  58.654 -64.226  1.00 26.97           C  
ATOM   3952  CD  GLU B 222     -41.957  57.153 -64.218  1.00 31.71           C  
ATOM   3953  OE1 GLU B 222     -40.793  56.722 -64.080  1.00 42.90           O  
ATOM   3954  OE2 GLU B 222     -42.946  56.403 -64.362  1.00 26.33           O  
ATOM   3955  N   LYS B 223     -44.306  61.083 -67.520  1.00  1.95           N  
ATOM   3956  CA  LYS B 223     -45.263  61.162 -68.621  1.00  1.95           C  
ATOM   3957  C   LYS B 223     -44.843  60.126 -69.650  1.00  8.74           C  
ATOM   3958  O   LYS B 223     -44.171  60.433 -70.636  1.00  1.95           O  
ATOM   3959  CB  LYS B 223     -45.323  62.573 -69.203  1.00  1.95           C  
ATOM   3960  CG  LYS B 223     -45.829  63.608 -68.212  1.00 23.52           C  
ATOM   3961  CD  LYS B 223     -46.644  64.699 -68.888  1.00 41.05           C  
ATOM   3962  CE  LYS B 223     -47.306  65.611 -67.860  1.00 47.80           C  
ATOM   3963  NZ  LYS B 223     -48.233  66.592 -68.492  1.00 41.01           N  
ATOM   3964  N   LYS B 224     -45.256  58.889 -69.414  1.00 39.44           N  
ATOM   3965  CA  LYS B 224     -45.001  57.793 -70.336  1.00 34.54           C  
ATOM   3966  C   LYS B 224     -46.187  56.851 -70.270  1.00 34.87           C  
ATOM   3967  O   LYS B 224     -47.099  57.044 -69.452  1.00  4.86           O  
ATOM   3968  CB  LYS B 224     -43.699  57.057 -69.988  1.00 11.78           C  
ATOM   3969  CG  LYS B 224     -43.757  56.291 -68.678  1.00  1.95           C  
ATOM   3970  CD  LYS B 224     -42.459  55.539 -68.439  1.00  2.99           C  
ATOM   3971  CE  LYS B 224     -42.517  54.746 -67.142  1.00 21.15           C  
ATOM   3972  NZ  LYS B 224     -41.239  54.029 -66.870  1.00 21.19           N  
ATOM   3973  N   PRO B 225     -46.223  55.827 -71.125  1.00 44.93           N  
ATOM   3974  CA  PRO B 225     -47.264  54.802 -70.988  1.00 32.96           C  
ATOM   3975  C   PRO B 225     -47.237  54.217 -69.585  1.00 21.52           C  
ATOM   3976  O   PRO B 225     -46.256  53.596 -69.168  1.00 28.99           O  
ATOM   3977  CB  PRO B 225     -46.876  53.778 -72.054  1.00 20.04           C  
ATOM   3978  CG  PRO B 225     -46.269  54.597 -73.130  1.00  7.59           C  
ATOM   3979  CD  PRO B 225     -45.525  55.717 -72.426  1.00 27.32           C  
ATOM   3980  N   ASN B 226     -48.326  54.442 -68.853  1.00 15.38           N  
ATOM   3981  CA  ASN B 226     -48.481  53.984 -67.476  1.00 28.35           C  
ATOM   3982  C   ASN B 226     -47.407  54.623 -66.587  1.00 36.81           C  
ATOM   3983  O   ASN B 226     -46.571  53.948 -65.980  1.00 32.16           O  
ATOM   3984  CB  ASN B 226     -48.420  52.452 -67.414  1.00 32.49           C  
ATOM   3985  CG  ASN B 226     -49.788  51.804 -67.541  1.00 40.33           C  
ATOM   3986  OD1 ASN B 226     -50.804  52.370 -67.137  1.00 54.43           O  
ATOM   3987  ND2 ASN B 226     -49.818  50.605 -68.117  1.00 36.92           N  
ATOM   3988  N   GLY B 227     -47.449  55.953 -66.520  1.00 33.09           N  
ATOM   3989  CA  GLY B 227     -46.441  56.701 -65.779  1.00  3.92           C  
ATOM   3990  C   GLY B 227     -46.750  56.738 -64.290  1.00 10.73           C  
ATOM   3991  O   GLY B 227     -47.883  56.975 -63.872  1.00  6.89           O  
ATOM   3992  N   LEU B 228     -45.716  56.513 -63.487  1.00 33.46           N  
ATOM   3993  CA  LEU B 228     -45.858  56.493 -62.040  1.00 23.55           C  
ATOM   3994  C   LEU B 228     -45.761  57.901 -61.455  1.00 12.25           C  
ATOM   3995  O   LEU B 228     -45.365  58.860 -62.121  1.00  7.96           O  
ATOM   3996  CB  LEU B 228     -44.801  55.585 -61.408  1.00 23.76           C  
ATOM   3997  CG  LEU B 228     -44.993  54.065 -61.469  1.00 26.52           C  
ATOM   3998  CD1 LEU B 228     -44.885  53.518 -62.889  1.00 16.09           C  
ATOM   3999  CD2 LEU B 228     -43.989  53.383 -60.556  1.00 66.59           C  
ATOM   4000  N   MET B 229     -46.124  58.009 -60.180  1.00  9.66           N  
ATOM   4001  CA  MET B 229     -46.062  59.268 -59.452  1.00 15.62           C  
ATOM   4002  C   MET B 229     -44.669  59.449 -58.863  1.00 37.24           C  
ATOM   4003  O   MET B 229     -44.133  58.532 -58.233  1.00 62.36           O  
ATOM   4004  CB  MET B 229     -47.113  59.287 -58.342  1.00 11.02           C  
ATOM   4005  CG  MET B 229     -47.162  60.573 -57.545  1.00 11.52           C  
ATOM   4006  SD  MET B 229     -48.318  60.466 -56.166  1.00 12.44           S  
ATOM   4007  CE  MET B 229     -48.128  62.094 -55.442  1.00 17.50           C  
ATOM   4008  N   THR B 230     -44.084  60.629 -59.068  1.00 10.30           N  
ATOM   4009  CA  THR B 230     -42.739  60.915 -58.583  1.00 10.47           C  
ATOM   4010  C   THR B 230     -42.663  62.089 -57.620  1.00 21.39           C  
ATOM   4011  O   THR B 230     -41.807  62.082 -56.733  1.00 32.88           O  
ATOM   4012  CB  THR B 230     -41.776  61.185 -59.753  1.00 13.90           C  
ATOM   4013  OG1 THR B 230     -42.124  62.419 -60.394  1.00 34.74           O  
ATOM   4014  CG2 THR B 230     -41.830  60.054 -60.768  1.00 15.42           C  
ATOM   4015  N   HIS B 231     -43.518  63.098 -57.771  1.00 16.46           N  
ATOM   4016  CA  HIS B 231     -43.456  64.288 -56.937  1.00 11.33           C  
ATOM   4017  C   HIS B 231     -44.863  64.756 -56.602  1.00 11.65           C  
ATOM   4018  O   HIS B 231     -45.812  64.515 -57.351  1.00 12.42           O  
ATOM   4019  CB  HIS B 231     -42.684  65.423 -57.623  1.00 10.81           C  
ATOM   4020  CG  HIS B 231     -41.232  65.128 -57.833  1.00 10.51           C  
ATOM   4021  ND1 HIS B 231     -40.738  64.636 -59.022  1.00  9.80           N  
ATOM   4022  CD2 HIS B 231     -40.165  65.260 -57.009  1.00 10.72           C  
ATOM   4023  CE1 HIS B 231     -39.431  64.474 -58.920  1.00  9.67           C  
ATOM   4024  NE2 HIS B 231     -39.058  64.846 -57.709  1.00 10.23           N  
ATOM   4025  N   LEU B 232     -44.984  65.425 -55.459  1.00 12.06           N  
ATOM   4026  CA  LEU B 232     -46.242  66.006 -55.014  1.00 12.24           C  
ATOM   4027  C   LEU B 232     -46.000  67.456 -54.631  1.00 11.80           C  
ATOM   4028  O   LEU B 232     -45.050  67.756 -53.902  1.00 11.74           O  
ATOM   4029  CB  LEU B 232     -46.823  65.233 -53.827  1.00 12.73           C  
ATOM   4030  CG  LEU B 232     -48.149  65.752 -53.272  1.00 12.67           C  
ATOM   4031  CD1 LEU B 232     -49.269  65.535 -54.278  1.00 13.87           C  
ATOM   4032  CD2 LEU B 232     -48.473  65.083 -51.946  1.00 13.11           C  
ATOM   4033  N   ARG B 233     -46.853  68.350 -55.119  1.00 11.17           N  
ATOM   4034  CA  ARG B 233     -46.769  69.768 -54.793  1.00 12.83           C  
ATOM   4035  C   ARG B 233     -47.714  70.037 -53.628  1.00 18.83           C  
ATOM   4036  O   ARG B 233     -48.937  69.943 -53.776  1.00 32.81           O  
ATOM   4037  CB  ARG B 233     -47.123  70.638 -55.996  1.00  8.94           C  
ATOM   4038  CG  ARG B 233     -47.101  72.132 -55.702  1.00  7.52           C  
ATOM   4039  CD  ARG B 233     -47.502  72.959 -56.917  1.00  5.92           C  
ATOM   4040  NE  ARG B 233     -46.479  72.979 -57.958  1.00  5.96           N  
ATOM   4041  CZ  ARG B 233     -45.515  73.890 -58.040  1.00 31.75           C  
ATOM   4042  NH1 ARG B 233     -45.439  74.861 -57.140  1.00 42.70           N  
ATOM   4043  NH2 ARG B 233     -44.628  73.834 -59.024  1.00 55.54           N  
ATOM   4044  N   ILE B 234     -47.145  70.363 -52.474  1.00  9.76           N  
ATOM   4045  CA  ILE B 234     -47.920  70.653 -51.278  1.00  9.18           C  
ATOM   4046  C   ILE B 234     -47.856  72.150 -51.011  1.00  7.61           C  
ATOM   4047  O   ILE B 234     -46.942  72.853 -51.452  1.00  7.21           O  
ATOM   4048  CB  ILE B 234     -47.427  69.846 -50.060  1.00  9.94           C  
ATOM   4049  CG1 ILE B 234     -45.976  70.197 -49.734  1.00  9.86           C  
ATOM   4050  CG2 ILE B 234     -47.563  68.355 -50.321  1.00 11.19           C  
ATOM   4051  CD1 ILE B 234     -45.387  69.358 -48.625  1.00 10.41           C  
ATOM   4052  N   LYS B 235     -48.852  72.641 -50.278  1.00  6.56           N  
ATOM   4053  CA  LYS B 235     -49.008  74.071 -50.045  1.00  4.64           C  
ATOM   4054  C   LYS B 235     -49.372  74.304 -48.589  1.00  3.81           C  
ATOM   4055  O   LYS B 235     -50.390  73.792 -48.113  1.00  3.86           O  
ATOM   4056  CB  LYS B 235     -50.082  74.662 -50.964  1.00  3.34           C  
ATOM   4057  CG  LYS B 235     -50.508  76.077 -50.604  1.00  1.95           C  
ATOM   4058  CD  LYS B 235     -51.609  76.566 -51.534  1.00  1.95           C  
ATOM   4059  CE  LYS B 235     -52.072  77.966 -51.162  1.00 11.78           C  
ATOM   4060  NZ  LYS B 235     -53.167  78.441 -52.053  1.00 13.00           N  
ATOM   4061  N   ASN B 236     -48.539  75.067 -47.887  1.00  2.94           N  
ATOM   4062  CA  ASN B 236     -48.893  75.517 -46.549  1.00  5.77           C  
ATOM   4063  C   ASN B 236     -50.117  76.422 -46.624  1.00  8.57           C  
ATOM   4064  O   ASN B 236     -50.177  77.334 -47.453  1.00  1.95           O  
ATOM   4065  CB  ASN B 236     -47.709  76.246 -45.916  1.00  1.95           C  
ATOM   4066  CG  ASN B 236     -48.043  76.831 -44.567  1.00  7.79           C  
ATOM   4067  OD1 ASN B 236     -48.551  77.945 -44.478  1.00 30.72           O  
ATOM   4068  ND2 ASN B 236     -47.767  76.081 -43.506  1.00  5.39           N  
ATOM   4069  N   THR B 237     -51.100  76.166 -45.759  1.00 20.42           N  
ATOM   4070  CA  THR B 237     -52.395  76.823 -45.878  1.00  9.88           C  
ATOM   4071  C   THR B 237     -52.491  78.145 -45.125  1.00  1.96           C  
ATOM   4072  O   THR B 237     -53.492  78.852 -45.284  1.00  1.95           O  
ATOM   4073  CB  THR B 237     -53.511  75.889 -45.393  1.00 15.64           C  
ATOM   4074  OG1 THR B 237     -54.772  76.343 -45.901  1.00 29.56           O  
ATOM   4075  CG2 THR B 237     -53.569  75.870 -43.875  1.00 16.99           C  
ATOM   4076  N   VAL B 238     -51.496  78.501 -44.319  1.00  7.33           N  
ATOM   4077  CA  VAL B 238     -51.481  79.786 -43.623  1.00  9.67           C  
ATOM   4078  C   VAL B 238     -50.513  80.765 -44.277  1.00  3.99           C  
ATOM   4079  O   VAL B 238     -50.849  81.930 -44.490  1.00  1.95           O  
ATOM   4080  CB  VAL B 238     -51.174  79.598 -42.119  1.00 13.07           C  
ATOM   4081  CG1 VAL B 238     -52.420  79.125 -41.384  1.00 14.49           C  
ATOM   4082  CG2 VAL B 238     -50.036  78.619 -41.904  1.00 15.76           C  
ATOM   4083  N   THR B 239     -49.302  80.309 -44.606  1.00 16.02           N  
ATOM   4084  CA  THR B 239     -48.336  81.182 -45.266  1.00  7.74           C  
ATOM   4085  C   THR B 239     -48.587  81.265 -46.769  1.00  6.35           C  
ATOM   4086  O   THR B 239     -48.470  82.344 -47.359  1.00 34.30           O  
ATOM   4087  CB  THR B 239     -46.910  80.698 -44.991  1.00  1.95           C  
ATOM   4088  OG1 THR B 239     -46.693  79.444 -45.648  1.00  1.95           O  
ATOM   4089  CG2 THR B 239     -46.682  80.528 -43.496  1.00  1.95           C  
ATOM   4090  N   GLY B 240     -48.928  80.144 -47.402  1.00  1.95           N  
ATOM   4091  CA  GLY B 240     -49.177  80.109 -48.828  1.00  1.95           C  
ATOM   4092  C   GLY B 240     -48.014  79.673 -49.692  1.00 14.66           C  
ATOM   4093  O   GLY B 240     -48.160  79.644 -50.920  1.00 19.25           O  
ATOM   4094  N   GLU B 241     -46.868  79.338 -49.103  1.00 19.85           N  
ATOM   4095  CA  GLU B 241     -45.702  78.939 -49.883  1.00 27.66           C  
ATOM   4096  C   GLU B 241     -45.864  77.498 -50.360  1.00 29.55           C  
ATOM   4097  O   GLU B 241     -46.006  76.577 -49.548  1.00  2.61           O  
ATOM   4098  CB  GLU B 241     -44.426  79.105 -49.058  1.00 38.72           C  
ATOM   4099  CG  GLU B 241     -44.474  78.465 -47.677  1.00 48.15           C  
ATOM   4100  CD  GLU B 241     -43.199  78.676 -46.883  1.00 49.66           C  
ATOM   4101  OE1 GLU B 241     -42.277  79.345 -47.396  1.00 36.13           O  
ATOM   4102  OE2 GLU B 241     -43.122  78.172 -45.742  1.00 54.02           O  
ATOM   4103  N   GLU B 242     -45.861  77.306 -51.675  1.00 32.82           N  
ATOM   4104  CA  GLU B 242     -45.951  75.974 -52.252  1.00  3.90           C  
ATOM   4105  C   GLU B 242     -44.559  75.432 -52.553  1.00  5.84           C  
ATOM   4106  O   GLU B 242     -43.627  76.183 -52.851  1.00 30.82           O  
ATOM   4107  CB  GLU B 242     -46.798  75.987 -53.525  1.00  3.43           C  
ATOM   4108  CG  GLU B 242     -48.178  76.594 -53.333  1.00 12.71           C  
ATOM   4109  CD  GLU B 242     -49.129  76.271 -54.470  1.00 38.42           C  
ATOM   4110  OE1 GLU B 242     -50.092  77.039 -54.676  1.00 50.84           O  
ATOM   4111  OE2 GLU B 242     -48.912  75.253 -55.159  1.00 43.15           O  
ATOM   4112  N   GLU B 243     -44.430  74.110 -52.473  1.00  6.77           N  
ATOM   4113  CA  GLU B 243     -43.149  73.449 -52.664  1.00  7.82           C  
ATOM   4114  C   GLU B 243     -43.392  72.089 -53.300  1.00 14.28           C  
ATOM   4115  O   GLU B 243     -44.488  71.529 -53.216  1.00 29.36           O  
ATOM   4116  CB  GLU B 243     -42.382  73.300 -51.344  1.00  7.97           C  
ATOM   4117  CG  GLU B 243     -42.909  72.203 -50.436  1.00 19.59           C  
ATOM   4118  CD  GLU B 243     -42.214  72.175 -49.088  1.00 34.83           C  
ATOM   4119  OE1 GLU B 243     -42.546  73.019 -48.229  1.00 50.52           O  
ATOM   4120  OE2 GLU B 243     -41.329  71.317 -48.891  1.00 34.43           O  
ATOM   4121  N   ILE B 244     -42.354  71.561 -53.943  1.00  9.61           N  
ATOM   4122  CA  ILE B 244     -42.412  70.261 -54.599  1.00 10.44           C  
ATOM   4123  C   ILE B 244     -41.521  69.308 -53.817  1.00 10.92           C  
ATOM   4124  O   ILE B 244     -40.324  69.569 -53.637  1.00 10.71           O  
ATOM   4125  CB  ILE B 244     -41.978  70.339 -56.070  1.00 10.31           C  
ATOM   4126  CG1 ILE B 244     -42.855  71.330 -56.837  1.00  9.47           C  
ATOM   4127  CG2 ILE B 244     -42.049  68.964 -56.715  1.00 10.73           C  
ATOM   4128  CD1 ILE B 244     -42.598  71.332 -58.327  1.00  9.05           C  
ATOM   4129  N   VAL B 245     -42.106  68.208 -53.348  1.00 11.44           N  
ATOM   4130  CA  VAL B 245     -41.404  67.214 -52.551  1.00 11.80           C  
ATOM   4131  C   VAL B 245     -41.525  65.859 -53.234  1.00 12.09           C  
ATOM   4132  O   VAL B 245     -42.454  65.601 -54.005  1.00 13.98           O  
ATOM   4133  CB  VAL B 245     -41.941  67.144 -51.108  1.00 11.98           C  
ATOM   4134  CG1 VAL B 245     -41.550  68.391 -50.338  1.00 28.66           C  
ATOM   4135  CG2 VAL B 245     -43.451  66.984 -51.122  1.00 12.17           C  
ATOM   4136  N   ASP B 246     -40.566  64.986 -52.937  1.00 12.21           N  
ATOM   4137  CA  ASP B 246     -40.588  63.636 -53.484  1.00 12.32           C  
ATOM   4138  C   ASP B 246     -41.749  62.849 -52.889  1.00 12.83           C  
ATOM   4139  O   ASP B 246     -41.954  62.850 -51.671  1.00 13.20           O  
ATOM   4140  CB  ASP B 246     -39.265  62.927 -53.197  1.00 12.34           C  
ATOM   4141  CG  ASP B 246     -38.065  63.697 -53.714  1.00 19.09           C  
ATOM   4142  OD1 ASP B 246     -38.138  64.236 -54.838  1.00 37.61           O  
ATOM   4143  OD2 ASP B 246     -37.047  63.764 -52.992  1.00 32.05           O  
ATOM   4144  N   ALA B 247     -42.508  62.177 -53.753  1.00 25.61           N  
ATOM   4145  CA  ALA B 247     -43.666  61.401 -53.315  1.00 22.06           C  
ATOM   4146  C   ALA B 247     -43.998  60.382 -54.391  1.00 12.89           C  
ATOM   4147  O   ALA B 247     -44.356  60.762 -55.510  1.00 23.79           O  
ATOM   4148  CB  ALA B 247     -44.865  62.309 -53.044  1.00 18.46           C  
ATOM   4149  N   ASN B 248     -43.894  59.097 -54.054  1.00 13.15           N  
ATOM   4150  CA  ASN B 248     -44.254  58.038 -54.987  1.00 14.10           C  
ATOM   4151  C   ASN B 248     -45.684  57.554 -54.812  1.00 13.07           C  
ATOM   4152  O   ASN B 248     -46.221  56.910 -55.721  1.00 12.66           O  
ATOM   4153  CB  ASN B 248     -43.298  56.849 -54.839  1.00 12.89           C  
ATOM   4154  CG  ASN B 248     -41.887  57.178 -55.278  1.00 15.35           C  
ATOM   4155  OD1 ASN B 248     -41.088  57.705 -54.503  1.00 39.11           O  
ATOM   4156  ND2 ASN B 248     -41.571  56.868 -56.530  1.00 11.74           N  
ATOM   4157  N   GLY B 249     -46.311  57.850 -53.677  1.00 13.68           N  
ATOM   4158  CA  GLY B 249     -47.665  57.403 -53.426  1.00 13.95           C  
ATOM   4159  C   GLY B 249     -48.512  58.407 -52.675  1.00 14.31           C  
ATOM   4160  O   GLY B 249     -48.084  58.961 -51.658  1.00 14.64           O  
ATOM   4161  N   LEU B 250     -49.722  58.649 -53.171  1.00 22.00           N  
ATOM   4162  CA  LEU B 250     -50.675  59.553 -52.541  1.00 19.19           C  
ATOM   4163  C   LEU B 250     -51.967  58.789 -52.295  1.00 14.69           C  
ATOM   4164  O   LEU B 250     -52.612  58.333 -53.245  1.00 14.33           O  
ATOM   4165  CB  LEU B 250     -50.929  60.783 -53.414  1.00 13.98           C  
ATOM   4166  CG  LEU B 250     -51.841  61.845 -52.803  1.00 14.04           C  
ATOM   4167  CD1 LEU B 250     -51.230  62.368 -51.516  1.00 14.20           C  
ATOM   4168  CD2 LEU B 250     -52.080  62.980 -53.786  1.00 13.48           C  
ATOM   4169  N   PHE B 251     -52.342  58.649 -51.026  1.00 15.23           N  
ATOM   4170  CA  PHE B 251     -53.510  57.871 -50.628  1.00 15.53           C  
ATOM   4171  C   PHE B 251     -54.566  58.813 -50.068  1.00 15.56           C  
ATOM   4172  O   PHE B 251     -54.356  59.441 -49.024  1.00 15.67           O  
ATOM   4173  CB  PHE B 251     -53.135  56.804 -49.603  1.00 17.43           C  
ATOM   4174  CG  PHE B 251     -52.416  55.625 -50.190  1.00 15.87           C  
ATOM   4175  CD1 PHE B 251     -51.040  55.638 -50.337  1.00 18.12           C  
ATOM   4176  CD2 PHE B 251     -53.118  54.504 -50.597  1.00 15.71           C  
ATOM   4177  CE1 PHE B 251     -50.376  54.552 -50.877  1.00 15.48           C  
ATOM   4178  CE2 PHE B 251     -52.462  53.416 -51.138  1.00 15.41           C  
ATOM   4179  CZ  PHE B 251     -51.089  53.441 -51.278  1.00 15.31           C  
ATOM   4180  N   TYR B 252     -55.695  58.911 -50.763  1.00 22.92           N  
ATOM   4181  CA  TYR B 252     -56.819  59.684 -50.255  1.00 17.28           C  
ATOM   4182  C   TYR B 252     -57.428  58.968 -49.057  1.00 22.84           C  
ATOM   4183  O   TYR B 252     -57.720  57.770 -49.119  1.00 25.46           O  
ATOM   4184  CB  TYR B 252     -57.869  59.884 -51.347  1.00 14.52           C  
ATOM   4185  CG  TYR B 252     -57.381  60.674 -52.543  1.00 13.93           C  
ATOM   4186  CD1 TYR B 252     -56.341  61.587 -52.425  1.00 25.05           C  
ATOM   4187  CD2 TYR B 252     -57.962  60.503 -53.793  1.00 20.97           C  
ATOM   4188  CE1 TYR B 252     -55.895  62.308 -53.520  1.00 29.18           C  
ATOM   4189  CE2 TYR B 252     -57.522  61.219 -54.892  1.00 12.64           C  
ATOM   4190  CZ  TYR B 252     -56.490  62.119 -54.750  1.00 15.00           C  
ATOM   4191  OH  TYR B 252     -56.052  62.832 -55.843  1.00 24.20           O  
ATOM   4192  N   ALA B 253     -57.623  59.705 -47.964  1.00 20.76           N  
ATOM   4193  CA  ALA B 253     -58.158  59.128 -46.738  1.00 15.82           C  
ATOM   4194  C   ALA B 253     -59.292  59.976 -46.174  1.00 15.08           C  
ATOM   4195  O   ALA B 253     -59.475  60.052 -44.955  1.00 14.99           O  
ATOM   4196  CB  ALA B 253     -57.057  58.940 -45.699  1.00 16.19           C  
ATOM   4197  N   VAL B 254     -60.050  60.631 -47.050  1.00 26.43           N  
ATOM   4198  CA  VAL B 254     -61.325  61.228 -46.672  1.00 26.29           C  
ATOM   4199  C   VAL B 254     -62.365  60.116 -46.700  1.00 44.65           C  
ATOM   4200  O   VAL B 254     -62.087  59.011 -47.181  1.00 49.63           O  
ATOM   4201  CB  VAL B 254     -61.708  62.392 -47.604  1.00 11.94           C  
ATOM   4202  CG1 VAL B 254     -60.727  63.544 -47.444  1.00 11.24           C  
ATOM   4203  CG2 VAL B 254     -61.742  61.921 -49.044  1.00 12.15           C  
ATOM   4204  N   GLY B 255     -63.559  60.384 -46.175  1.00 43.09           N  
ATOM   4205  CA  GLY B 255     -64.576  59.352 -46.080  1.00 53.64           C  
ATOM   4206  C   GLY B 255     -65.068  58.830 -47.418  1.00 50.10           C  
ATOM   4207  O   GLY B 255     -64.543  59.206 -48.470  1.00 58.08           O  
ATOM   4208  N   HIS B 256     -66.088  57.977 -47.396  1.00 24.27           N  
ATOM   4209  CA  HIS B 256     -66.636  57.384 -48.606  1.00 13.60           C  
ATOM   4210  C   HIS B 256     -68.081  57.835 -48.782  1.00 13.97           C  
ATOM   4211  O   HIS B 256     -68.725  58.312 -47.844  1.00 30.06           O  
ATOM   4212  CB  HIS B 256     -66.562  55.850 -48.568  1.00 14.67           C  
ATOM   4213  CG  HIS B 256     -65.176  55.312 -48.377  1.00 29.73           C  
ATOM   4214  ND1 HIS B 256     -64.424  55.570 -47.251  1.00 39.38           N  
ATOM   4215  CD2 HIS B 256     -64.409  54.525 -49.169  1.00 37.46           C  
ATOM   4216  CE1 HIS B 256     -63.252  54.969 -47.359  1.00 48.81           C  
ATOM   4217  NE2 HIS B 256     -63.217  54.328 -48.514  1.00 39.98           N  
ATOM   4218  N   ASP B 257     -68.587  57.674 -50.001  1.00 11.58           N  
ATOM   4219  CA  ASP B 257     -69.940  58.108 -50.348  1.00 10.02           C  
ATOM   4220  C   ASP B 257     -70.768  56.910 -50.785  1.00 14.64           C  
ATOM   4221  O   ASP B 257     -70.691  56.489 -51.954  1.00 28.24           O  
ATOM   4222  CB  ASP B 257     -69.905  59.168 -51.447  1.00 14.35           C  
ATOM   4223  CG  ASP B 257     -69.486  60.531 -50.927  1.00 38.82           C  
ATOM   4224  OD1 ASP B 257     -69.371  60.690 -49.693  1.00 44.46           O  
ATOM   4225  OD2 ASP B 257     -69.271  61.443 -51.751  1.00 49.19           O  
ATOM   4226  N   PRO B 258     -71.571  56.328 -49.895  1.00 12.73           N  
ATOM   4227  CA  PRO B 258     -72.477  55.254 -50.316  1.00 10.75           C  
ATOM   4228  C   PRO B 258     -73.542  55.772 -51.272  1.00  8.83           C  
ATOM   4229  O   PRO B 258     -74.102  56.854 -51.083  1.00 31.85           O  
ATOM   4230  CB  PRO B 258     -73.092  54.768 -48.998  1.00 11.49           C  
ATOM   4231  CG  PRO B 258     -72.954  55.927 -48.067  1.00 11.04           C  
ATOM   4232  CD  PRO B 258     -71.674  56.609 -48.452  1.00 11.16           C  
ATOM   4233  N   ALA B 259     -73.816  54.983 -52.309  1.00  8.53           N  
ATOM   4234  CA  ALA B 259     -74.790  55.366 -53.324  1.00  6.50           C  
ATOM   4235  C   ALA B 259     -76.213  55.055 -52.874  1.00 14.77           C  
ATOM   4236  O   ALA B 259     -76.967  54.386 -53.589  1.00 17.01           O  
ATOM   4237  CB  ALA B 259     -74.485  54.664 -54.649  1.00  6.14           C  
ATOM   4238  N   THR B 260     -76.587  55.537 -51.687  1.00  8.15           N  
ATOM   4239  CA  THR B 260     -77.921  55.341 -51.134  1.00  5.52           C  
ATOM   4240  C   THR B 260     -78.886  56.453 -51.529  1.00 13.78           C  
ATOM   4241  O   THR B 260     -79.859  56.713 -50.807  1.00 13.70           O  
ATOM   4242  CB  THR B 260     -77.844  55.222 -49.612  1.00  6.81           C  
ATOM   4243  OG1 THR B 260     -77.338  56.444 -49.062  1.00  8.25           O  
ATOM   4244  CG2 THR B 260     -76.918  54.088 -49.223  1.00 14.16           C  
ATOM   4245  N   ALA B 261     -78.638  57.121 -52.657  1.00 24.01           N  
ATOM   4246  CA  ALA B 261     -79.471  58.251 -53.052  1.00 14.67           C  
ATOM   4247  C   ALA B 261     -80.878  57.819 -53.446  1.00 14.23           C  
ATOM   4248  O   ALA B 261     -81.836  58.569 -53.227  1.00  7.07           O  
ATOM   4249  CB  ALA B 261     -78.811  59.013 -54.201  1.00  1.95           C  
ATOM   4250  N   LEU B 262     -81.027  56.624 -54.026  1.00 14.91           N  
ATOM   4251  CA  LEU B 262     -82.328  56.222 -54.552  1.00  1.95           C  
ATOM   4252  C   LEU B 262     -83.351  55.984 -53.448  1.00  1.95           C  
ATOM   4253  O   LEU B 262     -84.545  56.231 -53.654  1.00  8.98           O  
ATOM   4254  CB  LEU B 262     -82.188  54.965 -55.411  1.00  1.95           C  
ATOM   4255  CG  LEU B 262     -81.108  54.966 -56.491  1.00  1.95           C  
ATOM   4256  CD1 LEU B 262     -81.201  53.698 -57.323  1.00  1.95           C  
ATOM   4257  CD2 LEU B 262     -81.241  56.195 -57.372  1.00 27.07           C  
ATOM   4258  N   VAL B 263     -82.920  55.510 -52.280  1.00  1.95           N  
ATOM   4259  CA  VAL B 263     -83.865  55.208 -51.210  1.00  1.95           C  
ATOM   4260  C   VAL B 263     -84.230  56.489 -50.468  1.00 36.11           C  
ATOM   4261  O   VAL B 263     -85.379  56.941 -50.531  1.00 54.68           O  
ATOM   4262  CB  VAL B 263     -83.306  54.135 -50.254  1.00  2.18           C  
ATOM   4263  CG1 VAL B 263     -83.536  52.756 -50.838  1.00  3.12           C  
ATOM   4264  CG2 VAL B 263     -81.819  54.341 -50.008  1.00  3.67           C  
ATOM   4265  N   LYS B 264     -83.253  57.094 -49.796  1.00 29.22           N  
ATOM   4266  CA  LYS B 264     -83.402  58.376 -49.105  1.00 10.76           C  
ATOM   4267  C   LYS B 264     -84.703  58.434 -48.303  1.00 17.01           C  
ATOM   4268  O   LYS B 264     -85.574  59.274 -48.530  1.00 32.48           O  
ATOM   4269  CB  LYS B 264     -83.318  59.537 -50.095  1.00  6.40           C  
ATOM   4270  N   GLY B 265     -84.825  57.509 -47.348  1.00  6.00           N  
ATOM   4271  CA  GLY B 265     -85.954  57.457 -46.433  1.00 16.58           C  
ATOM   4272  C   GLY B 265     -86.777  56.188 -46.546  1.00 38.18           C  
ATOM   4273  O   GLY B 265     -87.380  55.758 -45.558  1.00 49.79           O  
ATOM   4274  N   GLN B 266     -86.826  55.588 -47.738  1.00 32.04           N  
ATOM   4275  CA  GLN B 266     -87.597  54.361 -47.918  1.00  6.91           C  
ATOM   4276  C   GLN B 266     -87.008  53.220 -47.097  1.00  7.56           C  
ATOM   4277  O   GLN B 266     -87.740  52.471 -46.439  1.00 30.02           O  
ATOM   4278  CB  GLN B 266     -87.654  53.986 -49.398  1.00  1.95           C  
ATOM   4279  CG  GLN B 266     -87.928  55.157 -50.320  1.00  1.95           C  
ATOM   4280  CD  GLN B 266     -88.514  54.724 -51.646  1.00  1.95           C  
ATOM   4281  OE1 GLN B 266     -89.318  53.795 -51.708  1.00  1.95           O  
ATOM   4282  NE2 GLN B 266     -88.110  55.395 -52.719  1.00  1.95           N  
ATOM   4283  N   ILE B 267     -85.688  53.069 -47.131  1.00  4.23           N  
ATOM   4284  CA  ILE B 267     -84.972  52.088 -46.326  1.00  5.38           C  
ATOM   4285  C   ILE B 267     -84.207  52.831 -45.241  1.00  5.78           C  
ATOM   4286  O   ILE B 267     -83.700  53.935 -45.473  1.00 25.72           O  
ATOM   4287  CB  ILE B 267     -84.018  51.247 -47.197  1.00  6.75           C  
ATOM   4288  CG1 ILE B 267     -84.810  50.444 -48.224  1.00 22.58           C  
ATOM   4289  CG2 ILE B 267     -83.173  50.310 -46.343  1.00  8.83           C  
ATOM   4290  CD1 ILE B 267     -83.937  49.623 -49.128  1.00 47.01           C  
ATOM   4291  N   ASP B 268     -84.120  52.225 -44.058  1.00  6.96           N  
ATOM   4292  CA  ASP B 268     -83.417  52.861 -42.954  1.00  7.20           C  
ATOM   4293  C   ASP B 268     -81.933  52.984 -43.273  1.00 12.88           C  
ATOM   4294  O   ASP B 268     -81.310  52.050 -43.787  1.00 14.06           O  
ATOM   4295  CB  ASP B 268     -83.613  52.065 -41.664  1.00 11.23           C  
ATOM   4296  CG  ASP B 268     -85.068  51.981 -41.244  1.00 43.15           C  
ATOM   4297  OD1 ASP B 268     -85.924  52.574 -41.933  1.00 57.55           O  
ATOM   4298  OD2 ASP B 268     -85.354  51.323 -40.221  1.00 50.08           O  
ATOM   4299  N   LEU B 269     -81.369  54.147 -42.965  1.00 22.86           N  
ATOM   4300  CA  LEU B 269     -79.954  54.419 -43.153  1.00 10.53           C  
ATOM   4301  C   LEU B 269     -79.304  54.684 -41.801  1.00 17.56           C  
ATOM   4302  O   LEU B 269     -79.981  54.848 -40.782  1.00 31.91           O  
ATOM   4303  CB  LEU B 269     -79.754  55.615 -44.092  1.00  7.18           C  
ATOM   4304  CG  LEU B 269     -80.176  55.397 -45.547  1.00  6.55           C  
ATOM   4305  CD1 LEU B 269     -80.029  56.678 -46.351  1.00  8.09           C  
ATOM   4306  CD2 LEU B 269     -79.378  54.275 -46.178  1.00  8.35           C  
ATOM   4307  N   ASP B 270     -77.976  54.745 -41.801  1.00 10.16           N  
ATOM   4308  CA  ASP B 270     -77.219  54.994 -40.587  1.00 14.64           C  
ATOM   4309  C   ASP B 270     -76.746  56.448 -40.557  1.00 25.71           C  
ATOM   4310  O   ASP B 270     -77.120  57.267 -41.403  1.00 16.90           O  
ATOM   4311  CB  ASP B 270     -76.054  54.005 -40.479  1.00 13.21           C  
ATOM   4312  CG  ASP B 270     -74.971  54.257 -41.512  1.00 30.84           C  
ATOM   4313  OD1 ASP B 270     -75.275  54.853 -42.566  1.00 47.26           O  
ATOM   4314  OD2 ASP B 270     -73.812  53.858 -41.267  1.00 30.34           O  
ATOM   4315  N   GLU B 271     -75.913  56.776 -39.566  1.00 38.64           N  
ATOM   4316  CA  GLU B 271     -75.450  58.151 -39.410  1.00 32.15           C  
ATOM   4317  C   GLU B 271     -74.570  58.582 -40.578  1.00 23.35           C  
ATOM   4318  O   GLU B 271     -74.618  59.743 -41.001  1.00 26.54           O  
ATOM   4319  CB  GLU B 271     -74.706  58.312 -38.081  1.00 45.36           C  
ATOM   4320  CG  GLU B 271     -73.568  57.321 -37.850  1.00 57.46           C  
ATOM   4321  CD  GLU B 271     -74.027  56.030 -37.193  1.00 55.51           C  
ATOM   4322  OE1 GLU B 271     -75.219  55.931 -36.834  1.00 52.64           O  
ATOM   4323  OE2 GLU B 271     -73.191  55.114 -37.034  1.00 43.34           O  
ATOM   4324  N   ASP B 272     -73.765  57.666 -41.115  1.00 32.75           N  
ATOM   4325  CA  ASP B 272     -72.832  57.995 -42.185  1.00 33.05           C  
ATOM   4326  C   ASP B 272     -73.433  57.849 -43.579  1.00 17.48           C  
ATOM   4327  O   ASP B 272     -72.797  58.264 -44.554  1.00  9.83           O  
ATOM   4328  CB  ASP B 272     -71.576  57.123 -42.073  1.00 31.19           C  
ATOM   4329  CG  ASP B 272     -70.770  57.419 -40.819  1.00 43.17           C  
ATOM   4330  OD1 ASP B 272     -70.628  58.610 -40.465  1.00 32.97           O  
ATOM   4331  OD2 ASP B 272     -70.280  56.460 -40.186  1.00 53.76           O  
ATOM   4332  N   GLY B 273     -74.626  57.271 -43.702  1.00 13.12           N  
ATOM   4333  CA  GLY B 273     -75.314  57.172 -44.975  1.00  9.00           C  
ATOM   4334  C   GLY B 273     -75.444  55.770 -45.530  1.00 12.26           C  
ATOM   4335  O   GLY B 273     -76.152  55.584 -46.526  1.00  9.57           O  
ATOM   4336  N   TYR B 274     -74.785  54.783 -44.931  1.00 23.28           N  
ATOM   4337  CA  TYR B 274     -74.860  53.417 -45.424  1.00 12.94           C  
ATOM   4338  C   TYR B 274     -76.218  52.794 -45.099  1.00 26.16           C  
ATOM   4339  O   TYR B 274     -76.928  53.216 -44.182  1.00 31.96           O  
ATOM   4340  CB  TYR B 274     -73.736  52.570 -44.825  1.00 14.37           C  
ATOM   4341  CG  TYR B 274     -72.348  52.982 -45.268  1.00 15.81           C  
ATOM   4342  CD1 TYR B 274     -71.781  52.454 -46.420  1.00 41.73           C  
ATOM   4343  CD2 TYR B 274     -71.603  53.895 -44.533  1.00 15.42           C  
ATOM   4344  CE1 TYR B 274     -70.513  52.823 -46.830  1.00 32.31           C  
ATOM   4345  CE2 TYR B 274     -70.333  54.271 -44.936  1.00 15.05           C  
ATOM   4346  CZ  TYR B 274     -69.794  53.731 -46.085  1.00 15.31           C  
ATOM   4347  OH  TYR B 274     -68.532  54.099 -46.491  1.00 23.28           O  
ATOM   4348  N   ILE B 275     -76.576  51.772 -45.872  1.00 22.35           N  
ATOM   4349  CA  ILE B 275     -77.821  51.049 -45.646  1.00 12.62           C  
ATOM   4350  C   ILE B 275     -77.646  50.125 -44.450  1.00 13.61           C  
ATOM   4351  O   ILE B 275     -76.714  49.313 -44.406  1.00 14.46           O  
ATOM   4352  CB  ILE B 275     -78.232  50.259 -46.898  1.00 12.33           C  
ATOM   4353  CG1 ILE B 275     -78.717  51.206 -47.994  1.00 10.80           C  
ATOM   4354  CG2 ILE B 275     -79.317  49.250 -46.553  1.00 12.37           C  
ATOM   4355  CD1 ILE B 275     -79.235  50.498 -49.224  1.00 10.18           C  
ATOM   4356  N   ILE B 276     -78.542  50.245 -43.478  1.00 21.61           N  
ATOM   4357  CA  ILE B 276     -78.498  49.388 -42.300  1.00 16.64           C  
ATOM   4358  C   ILE B 276     -79.071  48.025 -42.659  1.00 23.30           C  
ATOM   4359  O   ILE B 276     -80.152  47.926 -43.252  1.00 13.28           O  
ATOM   4360  CB  ILE B 276     -79.268  50.024 -41.132  1.00 12.74           C  
ATOM   4361  CG1 ILE B 276     -78.633  51.354 -40.728  1.00 12.38           C  
ATOM   4362  CG2 ILE B 276     -79.314  49.073 -39.943  1.00 14.53           C  
ATOM   4363  CD1 ILE B 276     -79.251  51.970 -39.492  1.00 11.20           C  
ATOM   4364  N   THR B 277     -78.338  46.971 -42.307  1.00 40.81           N  
ATOM   4365  CA  THR B 277     -78.762  45.599 -42.539  1.00 29.62           C  
ATOM   4366  C   THR B 277     -78.453  44.772 -41.301  1.00 29.72           C  
ATOM   4367  O   THR B 277     -77.544  45.098 -40.532  1.00 39.06           O  
ATOM   4368  CB  THR B 277     -78.066  44.976 -43.757  1.00 14.52           C  
ATOM   4369  OG1 THR B 277     -76.647  45.126 -43.624  1.00 14.87           O  
ATOM   4370  CG2 THR B 277     -78.531  45.641 -45.044  1.00 16.65           C  
ATOM   4371  N   LYS B 278     -79.224  43.707 -41.112  1.00 14.09           N  
ATOM   4372  CA  LYS B 278     -78.956  42.781 -40.022  1.00 12.59           C  
ATOM   4373  C   LYS B 278     -77.540  42.230 -40.162  1.00 19.91           C  
ATOM   4374  O   LYS B 278     -77.160  41.790 -41.256  1.00 52.23           O  
ATOM   4375  CB  LYS B 278     -79.972  41.640 -40.021  1.00 12.12           C  
ATOM   4376  N   PRO B 279     -76.728  42.262 -39.105  1.00 11.97           N  
ATOM   4377  CA  PRO B 279     -75.322  41.863 -39.244  1.00 33.68           C  
ATOM   4378  C   PRO B 279     -75.200  40.425 -39.726  1.00 31.93           C  
ATOM   4379  O   PRO B 279     -75.956  39.544 -39.310  1.00 10.94           O  
ATOM   4380  CB  PRO B 279     -74.764  42.035 -37.826  1.00 37.78           C  
ATOM   4381  CG  PRO B 279     -75.682  43.023 -37.175  1.00 25.84           C  
ATOM   4382  CD  PRO B 279     -77.039  42.743 -37.748  1.00 10.90           C  
ATOM   4383  N   GLY B 280     -74.233  40.193 -40.613  1.00 44.63           N  
ATOM   4384  CA  GLY B 280     -74.079  38.896 -41.236  1.00 36.96           C  
ATOM   4385  C   GLY B 280     -75.172  38.528 -42.213  1.00 18.23           C  
ATOM   4386  O   GLY B 280     -75.160  37.408 -42.737  1.00 13.14           O  
ATOM   4387  N   THR B 281     -76.110  39.436 -42.479  1.00 12.56           N  
ATOM   4388  CA  THR B 281     -77.255  39.190 -43.339  1.00 12.73           C  
ATOM   4389  C   THR B 281     -77.396  40.350 -44.317  1.00 13.37           C  
ATOM   4390  O   THR B 281     -76.777  41.405 -44.156  1.00 29.46           O  
ATOM   4391  CB  THR B 281     -78.535  39.039 -42.500  1.00 15.93           C  
ATOM   4392  OG1 THR B 281     -78.228  38.349 -41.282  1.00 25.07           O  
ATOM   4393  CG2 THR B 281     -79.596  38.262 -43.246  1.00 27.92           C  
ATOM   4394  N   SER B 282     -78.218  40.149 -45.346  1.00 13.28           N  
ATOM   4395  CA  SER B 282     -78.566  41.210 -46.280  1.00 18.06           C  
ATOM   4396  C   SER B 282     -79.967  41.761 -46.041  1.00 18.24           C  
ATOM   4397  O   SER B 282     -80.469  42.528 -46.868  1.00 13.24           O  
ATOM   4398  CB  SER B 282     -78.434  40.714 -47.722  1.00 13.08           C  
ATOM   4399  OG  SER B 282     -79.401  39.721 -48.011  1.00 12.62           O  
ATOM   4400  N   TYR B 283     -80.606  41.393 -44.932  1.00 14.35           N  
ATOM   4401  CA  TYR B 283     -81.961  41.854 -44.650  1.00 13.16           C  
ATOM   4402  C   TYR B 283     -81.949  43.334 -44.283  1.00 15.56           C  
ATOM   4403  O   TYR B 283     -81.355  43.727 -43.274  1.00 23.42           O  
ATOM   4404  CB  TYR B 283     -82.584  41.030 -43.524  1.00 16.28           C  
ATOM   4405  CG  TYR B 283     -82.873  39.590 -43.889  1.00 12.54           C  
ATOM   4406  CD1 TYR B 283     -83.042  39.211 -45.212  1.00 14.83           C  
ATOM   4407  CD2 TYR B 283     -83.001  38.615 -42.907  1.00 28.81           C  
ATOM   4408  CE1 TYR B 283     -83.311  37.899 -45.551  1.00 16.05           C  
ATOM   4409  CE2 TYR B 283     -83.270  37.297 -43.238  1.00 32.10           C  
ATOM   4410  CZ  TYR B 283     -83.426  36.947 -44.563  1.00 17.31           C  
ATOM   4411  OH  TYR B 283     -83.696  35.642 -44.904  1.00 20.08           O  
ATOM   4412  N   THR B 284     -82.602  44.155 -45.102  1.00 16.49           N  
ATOM   4413  CA  THR B 284     -82.736  45.579 -44.821  1.00 16.67           C  
ATOM   4414  C   THR B 284     -83.905  45.796 -43.864  1.00 11.84           C  
ATOM   4415  O   THR B 284     -84.428  44.855 -43.261  1.00 11.84           O  
ATOM   4416  CB  THR B 284     -82.916  46.371 -46.112  1.00 11.70           C  
ATOM   4417  OG1 THR B 284     -84.111  45.944 -46.778  1.00 24.33           O  
ATOM   4418  CG2 THR B 284     -81.730  46.157 -47.036  1.00 13.46           C  
ATOM   4419  N   SER B 285     -84.338  47.050 -43.719  1.00 11.01           N  
ATOM   4420  CA  SER B 285     -85.461  47.355 -42.844  1.00 10.04           C  
ATOM   4421  C   SER B 285     -86.804  47.114 -43.517  1.00  9.10           C  
ATOM   4422  O   SER B 285     -87.807  46.925 -42.821  1.00  8.41           O  
ATOM   4423  CB  SER B 285     -85.381  48.805 -42.366  1.00 25.11           C  
ATOM   4424  OG  SER B 285     -85.466  49.706 -43.457  1.00 35.67           O  
ATOM   4425  N   ARG B 286     -86.843  47.117 -44.846  1.00  8.82           N  
ATOM   4426  CA  ARG B 286     -88.046  46.807 -45.606  1.00 14.50           C  
ATOM   4427  C   ARG B 286     -87.948  45.368 -46.099  1.00  8.65           C  
ATOM   4428  O   ARG B 286     -87.004  45.019 -46.815  1.00  9.28           O  
ATOM   4429  CB  ARG B 286     -88.194  47.773 -46.782  1.00 18.76           C  
ATOM   4430  CG  ARG B 286     -89.243  47.389 -47.812  1.00 22.02           C  
ATOM   4431  CD  ARG B 286     -90.619  47.929 -47.470  1.00 39.25           C  
ATOM   4432  NE  ARG B 286     -91.616  47.477 -48.436  1.00 47.48           N  
ATOM   4433  CZ  ARG B 286     -92.742  48.126 -48.712  1.00 40.45           C  
ATOM   4434  NH1 ARG B 286     -93.017  49.271 -48.102  1.00 52.61           N  
ATOM   4435  NH2 ARG B 286     -93.588  47.637 -49.607  1.00 19.55           N  
ATOM   4436  N   GLU B 287     -88.916  44.539 -45.719  1.00 19.49           N  
ATOM   4437  CA  GLU B 287     -88.913  43.148 -46.155  1.00 23.38           C  
ATOM   4438  C   GLU B 287     -89.215  43.076 -47.647  1.00 19.25           C  
ATOM   4439  O   GLU B 287     -90.253  43.563 -48.105  1.00 22.93           O  
ATOM   4440  CB  GLU B 287     -89.914  42.322 -45.348  1.00 21.06           C  
ATOM   4441  CG  GLU B 287     -91.298  42.928 -45.204  1.00 35.09           C  
ATOM   4442  CD  GLU B 287     -92.224  42.045 -44.389  1.00 39.38           C  
ATOM   4443  OE1 GLU B 287     -91.762  40.994 -43.895  1.00 27.16           O  
ATOM   4444  OE2 GLU B 287     -93.413  42.400 -44.244  1.00 36.92           O  
ATOM   4445  N   GLY B 288     -88.295  42.487 -48.405  1.00  8.78           N  
ATOM   4446  CA  GLY B 288     -88.403  42.383 -49.847  1.00  7.87           C  
ATOM   4447  C   GLY B 288     -87.250  43.005 -50.601  1.00  7.84           C  
ATOM   4448  O   GLY B 288     -87.024  42.654 -51.768  1.00  7.26           O  
ATOM   4449  N   VAL B 289     -86.511  43.919 -49.977  1.00  8.35           N  
ATOM   4450  CA  VAL B 289     -85.339  44.541 -50.580  1.00  8.42           C  
ATOM   4451  C   VAL B 289     -84.134  44.201 -49.715  1.00  9.94           C  
ATOM   4452  O   VAL B 289     -84.195  44.310 -48.484  1.00 10.61           O  
ATOM   4453  CB  VAL B 289     -85.510  46.065 -50.731  1.00  9.34           C  
ATOM   4454  CG1 VAL B 289     -86.039  46.678 -49.448  1.00  7.45           C  
ATOM   4455  CG2 VAL B 289     -84.194  46.710 -51.133  1.00 16.09           C  
ATOM   4456  N   PHE B 290     -83.053  43.769 -50.355  1.00 10.27           N  
ATOM   4457  CA  PHE B 290     -81.833  43.382 -49.669  1.00 11.42           C  
ATOM   4458  C   PHE B 290     -80.686  44.264 -50.145  1.00 14.54           C  
ATOM   4459  O   PHE B 290     -80.738  44.853 -51.228  1.00 42.90           O  
ATOM   4460  CB  PHE B 290     -81.517  41.895 -49.904  1.00 11.57           C  
ATOM   4461  CG  PHE B 290     -82.715  40.989 -49.752  1.00 12.24           C  
ATOM   4462  CD1 PHE B 290     -83.578  40.773 -50.816  1.00 10.29           C  
ATOM   4463  CD2 PHE B 290     -82.984  40.366 -48.545  1.00 12.73           C  
ATOM   4464  CE1 PHE B 290     -84.681  39.951 -50.682  1.00  9.99           C  
ATOM   4465  CE2 PHE B 290     -84.088  39.540 -48.408  1.00 11.38           C  
ATOM   4466  CZ  PHE B 290     -84.935  39.333 -49.478  1.00 10.59           C  
ATOM   4467  N   ALA B 291     -79.643  44.357 -49.321  1.00 12.43           N  
ATOM   4468  CA  ALA B 291     -78.497  45.211 -49.612  1.00 12.63           C  
ATOM   4469  C   ALA B 291     -77.217  44.433 -49.357  1.00 13.29           C  
ATOM   4470  O   ALA B 291     -77.001  43.931 -48.249  1.00 44.53           O  
ATOM   4471  CB  ALA B 291     -78.524  46.486 -48.766  1.00 15.05           C  
ATOM   4472  N   CYS B 292     -76.375  44.337 -50.381  1.00 13.04           N  
ATOM   4473  CA  CYS B 292     -75.093  43.658 -50.293  1.00 13.34           C  
ATOM   4474  C   CYS B 292     -73.992  44.572 -50.813  1.00 32.78           C  
ATOM   4475  O   CYS B 292     -74.241  45.511 -51.574  1.00 50.14           O  
ATOM   4476  CB  CYS B 292     -75.106  42.347 -51.085  1.00 12.82           C  
ATOM   4477  SG  CYS B 292     -75.608  42.551 -52.809  1.00 11.86           S  
ATOM   4478  N   GLY B 293     -72.764  44.285 -50.393  1.00 13.71           N  
ATOM   4479  CA  GLY B 293     -71.615  45.015 -50.890  1.00 13.76           C  
ATOM   4480  C   GLY B 293     -71.222  46.204 -50.041  1.00 26.47           C  
ATOM   4481  O   GLY B 293     -71.474  46.224 -48.832  1.00 47.68           O  
ATOM   4482  N   ASP B 294     -70.603  47.206 -50.669  1.00 25.00           N  
ATOM   4483  CA  ASP B 294     -70.124  48.377 -49.944  1.00 18.74           C  
ATOM   4484  C   ASP B 294     -71.246  49.307 -49.502  1.00 18.93           C  
ATOM   4485  O   ASP B 294     -70.990  50.214 -48.703  1.00 45.77           O  
ATOM   4486  CB  ASP B 294     -69.122  49.153 -50.803  1.00 48.40           C  
ATOM   4487  CG  ASP B 294     -67.750  48.501 -50.840  1.00 47.51           C  
ATOM   4488  OD1 ASP B 294     -67.632  47.329 -50.423  1.00 42.94           O  
ATOM   4489  OD2 ASP B 294     -66.788  49.164 -51.283  1.00 36.37           O  
ATOM   4490  N   VAL B 295     -72.471  49.115 -49.999  1.00 16.81           N  
ATOM   4491  CA  VAL B 295     -73.584  49.947 -49.553  1.00 13.70           C  
ATOM   4492  C   VAL B 295     -73.891  49.684 -48.085  1.00 14.39           C  
ATOM   4493  O   VAL B 295     -74.381  50.570 -47.375  1.00 14.17           O  
ATOM   4494  CB  VAL B 295     -74.820  49.707 -50.436  1.00 12.65           C  
ATOM   4495  CG1 VAL B 295     -75.787  50.871 -50.323  1.00 11.58           C  
ATOM   4496  CG2 VAL B 295     -74.406  49.485 -51.871  1.00 17.49           C  
ATOM   4497  N   GLN B 296     -73.618  48.467 -47.610  1.00 14.95           N  
ATOM   4498  CA  GLN B 296     -73.805  48.109 -46.213  1.00 15.41           C  
ATOM   4499  C   GLN B 296     -72.500  47.950 -45.452  1.00 15.91           C  
ATOM   4500  O   GLN B 296     -72.511  48.019 -44.219  1.00 16.09           O  
ATOM   4501  CB  GLN B 296     -74.592  46.796 -46.102  1.00 15.25           C  
ATOM   4502  CG  GLN B 296     -73.872  45.607 -46.717  1.00 15.08           C  
ATOM   4503  CD  GLN B 296     -74.437  44.285 -46.256  1.00 41.80           C  
ATOM   4504  OE1 GLN B 296     -75.472  44.240 -45.595  1.00 67.67           O  
ATOM   4505  NE2 GLN B 296     -73.759  43.197 -46.603  1.00 69.89           N  
ATOM   4506  N   ASP B 297     -71.388  47.734 -46.150  1.00 17.68           N  
ATOM   4507  CA  ASP B 297     -70.100  47.471 -45.524  1.00 20.70           C  
ATOM   4508  C   ASP B 297     -69.241  48.729 -45.553  1.00 31.93           C  
ATOM   4509  O   ASP B 297     -68.944  49.259 -46.630  1.00 30.56           O  
ATOM   4510  CB  ASP B 297     -69.381  46.320 -46.225  1.00 31.50           C  
ATOM   4511  CG  ASP B 297     -67.933  46.200 -45.801  1.00 47.57           C  
ATOM   4512  OD1 ASP B 297     -67.667  46.262 -44.583  1.00 47.91           O  
ATOM   4513  OD2 ASP B 297     -67.063  46.045 -46.684  1.00 52.90           O  
ATOM   4514  N   LYS B 298     -68.847  49.201 -44.371  1.00 31.78           N  
ATOM   4515  CA  LYS B 298     -67.911  50.305 -44.242  1.00 18.11           C  
ATOM   4516  C   LYS B 298     -66.637  49.927 -43.500  1.00 43.37           C  
ATOM   4517  O   LYS B 298     -65.704  50.738 -43.457  1.00 60.38           O  
ATOM   4518  CB  LYS B 298     -68.574  51.501 -43.538  1.00 17.02           C  
ATOM   4519  CG  LYS B 298     -69.172  51.188 -42.177  1.00 16.92           C  
ATOM   4520  CD  LYS B 298     -69.840  52.421 -41.582  1.00 17.56           C  
ATOM   4521  CE  LYS B 298     -70.486  52.117 -40.239  1.00 30.01           C  
ATOM   4522  NZ  LYS B 298     -71.138  53.322 -39.652  1.00 25.18           N  
ATOM   4523  N   ARG B 299     -66.570  48.726 -42.918  1.00 37.01           N  
ATOM   4524  CA  ARG B 299     -65.439  48.303 -42.102  1.00 30.00           C  
ATOM   4525  C   ARG B 299     -64.401  47.495 -42.871  1.00 23.07           C  
ATOM   4526  O   ARG B 299     -63.250  47.415 -42.425  1.00 16.27           O  
ATOM   4527  CB  ARG B 299     -65.933  47.480 -40.904  1.00 15.85           C  
ATOM   4528  CG  ARG B 299     -66.808  48.272 -39.942  1.00 27.49           C  
ATOM   4529  CD  ARG B 299     -67.327  47.427 -38.783  1.00 36.38           C  
ATOM   4530  NE  ARG B 299     -68.287  46.413 -39.212  1.00 42.90           N  
ATOM   4531  CZ  ARG B 299     -68.078  45.104 -39.130  1.00 39.91           C  
ATOM   4532  NH1 ARG B 299     -66.941  44.644 -38.624  1.00 46.42           N  
ATOM   4533  NH2 ARG B 299     -69.008  44.253 -39.544  1.00 13.26           N  
ATOM   4534  N   TYR B 300     -64.774  46.889 -43.996  1.00 24.09           N  
ATOM   4535  CA  TYR B 300     -63.868  46.046 -44.768  1.00 15.66           C  
ATOM   4536  C   TYR B 300     -63.604  46.592 -46.161  1.00 15.72           C  
ATOM   4537  O   TYR B 300     -62.438  46.757 -46.543  1.00 22.17           O  
ATOM   4538  CB  TYR B 300     -64.434  44.621 -44.849  1.00 14.95           C  
ATOM   4539  CG  TYR B 300     -64.896  44.086 -43.512  1.00 14.60           C  
ATOM   4540  CD1 TYR B 300     -63.979  43.744 -42.526  1.00 16.57           C  
ATOM   4541  CD2 TYR B 300     -66.246  43.929 -43.231  1.00 14.50           C  
ATOM   4542  CE1 TYR B 300     -64.393  43.254 -41.302  1.00 16.92           C  
ATOM   4543  CE2 TYR B 300     -66.671  43.440 -42.009  1.00 25.88           C  
ATOM   4544  CZ  TYR B 300     -65.739  43.104 -41.049  1.00 18.08           C  
ATOM   4545  OH  TYR B 300     -66.156  42.620 -39.831  1.00 14.06           O  
ATOM   4546  N   ARG B 301     -64.656  46.875 -46.935  1.00 15.66           N  
ATOM   4547  CA  ARG B 301     -64.535  47.511 -48.250  1.00 17.80           C  
ATOM   4548  C   ARG B 301     -63.602  46.729 -49.178  1.00 14.82           C  
ATOM   4549  O   ARG B 301     -62.674  47.280 -49.773  1.00 14.76           O  
ATOM   4550  CB  ARG B 301     -64.074  48.964 -48.104  1.00 33.82           C  
ATOM   4551  CG  ARG B 301     -65.083  49.874 -47.412  1.00 22.44           C  
ATOM   4552  CD  ARG B 301     -64.445  51.183 -46.967  1.00 35.90           C  
ATOM   4553  NE  ARG B 301     -63.527  50.987 -45.846  1.00 56.75           N  
ATOM   4554  CZ  ARG B 301     -62.203  50.928 -45.958  1.00 60.76           C  
ATOM   4555  NH1 ARG B 301     -61.627  51.054 -47.146  1.00 59.34           N  
ATOM   4556  NH2 ARG B 301     -61.454  50.744 -44.879  1.00 52.72           N  
ATOM   4557  N   GLN B 302     -63.855  45.429 -49.296  1.00 21.66           N  
ATOM   4558  CA  GLN B 302     -63.080  44.552 -50.161  1.00 13.82           C  
ATOM   4559  C   GLN B 302     -63.991  43.906 -51.197  1.00 32.07           C  
ATOM   4560  O   GLN B 302     -65.199  43.762 -50.990  1.00 75.46           O  
ATOM   4561  CB  GLN B 302     -62.358  43.468 -49.352  1.00 13.89           C  
ATOM   4562  CG  GLN B 302     -61.302  44.009 -48.407  1.00 16.78           C  
ATOM   4563  CD  GLN B 302     -60.141  44.643 -49.143  1.00 18.65           C  
ATOM   4564  OE1 GLN B 302     -59.788  44.228 -50.248  1.00 20.08           O  
ATOM   4565  NE2 GLN B 302     -59.545  45.663 -48.537  1.00 14.95           N  
ATOM   4566  N   ALA B 303     -63.394  43.512 -52.325  1.00 15.48           N  
ATOM   4567  CA  ALA B 303     -64.173  42.859 -53.373  1.00 12.18           C  
ATOM   4568  C   ALA B 303     -64.551  41.437 -52.979  1.00 13.71           C  
ATOM   4569  O   ALA B 303     -65.668  40.987 -53.260  1.00 26.69           O  
ATOM   4570  CB  ALA B 303     -63.399  42.857 -54.689  1.00 11.72           C  
ATOM   4571  N   ILE B 304     -63.633  40.714 -52.334  1.00 31.45           N  
ATOM   4572  CA  ILE B 304     -63.933  39.352 -51.905  1.00 13.62           C  
ATOM   4573  C   ILE B 304     -65.022  39.347 -50.838  1.00 20.50           C  
ATOM   4574  O   ILE B 304     -65.813  38.400 -50.755  1.00 49.66           O  
ATOM   4575  CB  ILE B 304     -62.649  38.649 -51.420  1.00 13.09           C  
ATOM   4576  CG1 ILE B 304     -62.918  37.170 -51.136  1.00 13.15           C  
ATOM   4577  CG2 ILE B 304     -62.079  39.344 -50.190  1.00 13.36           C  
ATOM   4578  CD1 ILE B 304     -63.516  36.427 -52.306  1.00 12.90           C  
ATOM   4579  N   THR B 305     -65.095  40.397 -50.017  1.00 12.82           N  
ATOM   4580  CA  THR B 305     -66.155  40.482 -49.019  1.00 12.88           C  
ATOM   4581  C   THR B 305     -67.467  40.939 -49.643  1.00 18.95           C  
ATOM   4582  O   THR B 305     -68.541  40.468 -49.251  1.00 36.03           O  
ATOM   4583  CB  THR B 305     -65.749  41.428 -47.888  1.00 13.32           C  
ATOM   4584  OG1 THR B 305     -65.554  42.748 -48.411  1.00 13.65           O  
ATOM   4585  CG2 THR B 305     -64.464  40.949 -47.233  1.00 13.37           C  
ATOM   4586  N   SER B 306     -67.400  41.855 -50.611  1.00 12.71           N  
ATOM   4587  CA  SER B 306     -68.607  42.274 -51.313  1.00 12.56           C  
ATOM   4588  C   SER B 306     -69.176  41.136 -52.150  1.00 11.95           C  
ATOM   4589  O   SER B 306     -70.398  40.967 -52.229  1.00 41.10           O  
ATOM   4590  CB  SER B 306     -68.312  43.492 -52.185  1.00 12.56           C  
ATOM   4591  OG  SER B 306     -67.890  44.593 -51.398  1.00 13.25           O  
ATOM   4592  N   ALA B 307     -68.304  40.348 -52.783  1.00 15.49           N  
ATOM   4593  CA  ALA B 307     -68.764  39.176 -53.521  1.00 11.19           C  
ATOM   4594  C   ALA B 307     -69.458  38.184 -52.597  1.00 11.35           C  
ATOM   4595  O   ALA B 307     -70.479  37.591 -52.965  1.00 11.06           O  
ATOM   4596  CB  ALA B 307     -67.588  38.511 -54.236  1.00 11.11           C  
ATOM   4597  N   GLY B 308     -68.918  37.993 -51.392  1.00 11.73           N  
ATOM   4598  CA  GLY B 308     -69.559  37.105 -50.434  1.00 11.75           C  
ATOM   4599  C   GLY B 308     -70.936  37.585 -50.017  1.00 11.74           C  
ATOM   4600  O   GLY B 308     -71.902  36.817 -50.020  1.00 24.49           O  
ATOM   4601  N   SER B 309     -71.044  38.864 -49.645  1.00 20.41           N  
ATOM   4602  CA  SER B 309     -72.343  39.403 -49.256  1.00 12.43           C  
ATOM   4603  C   SER B 309     -73.318  39.402 -50.424  1.00 12.13           C  
ATOM   4604  O   SER B 309     -74.535  39.327 -50.216  1.00 17.18           O  
ATOM   4605  CB  SER B 309     -72.184  40.816 -48.692  1.00 12.98           C  
ATOM   4606  OG  SER B 309     -71.698  41.713 -49.674  1.00 21.30           O  
ATOM   4607  N   GLY B 310     -72.808  39.475 -51.656  1.00 11.77           N  
ATOM   4608  CA  GLY B 310     -73.680  39.377 -52.815  1.00 11.35           C  
ATOM   4609  C   GLY B 310     -74.298  37.999 -52.958  1.00 10.96           C  
ATOM   4610  O   GLY B 310     -75.454  37.867 -53.369  1.00 10.75           O  
ATOM   4611  N   CYS B 311     -73.531  36.955 -52.635  1.00 31.84           N  
ATOM   4612  CA  CYS B 311     -74.086  35.607 -52.605  1.00 16.94           C  
ATOM   4613  C   CYS B 311     -75.143  35.473 -51.515  1.00 10.94           C  
ATOM   4614  O   CYS B 311     -76.143  34.769 -51.692  1.00 34.31           O  
ATOM   4615  CB  CYS B 311     -72.965  34.589 -52.396  1.00 10.81           C  
ATOM   4616  SG  CYS B 311     -73.520  32.883 -52.264  1.00 10.77           S  
ATOM   4617  N   ILE B 312     -74.935  36.143 -50.379  1.00 11.28           N  
ATOM   4618  CA  ILE B 312     -75.927  36.133 -49.308  1.00 11.43           C  
ATOM   4619  C   ILE B 312     -77.222  36.788 -49.769  1.00 11.53           C  
ATOM   4620  O   ILE B 312     -78.320  36.279 -49.509  1.00 11.37           O  
ATOM   4621  CB  ILE B 312     -75.363  36.816 -48.049  1.00 11.77           C  
ATOM   4622  CG1 ILE B 312     -74.103  36.092 -47.568  1.00 11.57           C  
ATOM   4623  CG2 ILE B 312     -76.422  36.907 -46.963  1.00 11.91           C  
ATOM   4624  CD1 ILE B 312     -73.567  36.609 -46.253  1.00 11.74           C  
ATOM   4625  N   ALA B 313     -77.117  37.929 -50.454  1.00 12.84           N  
ATOM   4626  CA  ALA B 313     -78.313  38.596 -50.955  1.00 11.61           C  
ATOM   4627  C   ALA B 313     -79.047  37.743 -51.980  1.00 32.34           C  
ATOM   4628  O   ALA B 313     -80.269  37.859 -52.121  1.00 60.35           O  
ATOM   4629  CB  ALA B 313     -77.944  39.953 -51.556  1.00 11.68           C  
ATOM   4630  N   ALA B 314     -78.327  36.880 -52.699  1.00 17.92           N  
ATOM   4631  CA  ALA B 314     -78.973  36.026 -53.691  1.00  9.92           C  
ATOM   4632  C   ALA B 314     -79.759  34.907 -53.021  1.00 10.49           C  
ATOM   4633  O   ALA B 314     -80.927  34.668 -53.351  1.00 15.65           O  
ATOM   4634  CB  ALA B 314     -77.932  35.454 -54.652  1.00  9.51           C  
ATOM   4635  N   LEU B 315     -79.131  34.210 -52.071  1.00 10.37           N  
ATOM   4636  CA  LEU B 315     -79.787  33.083 -51.414  1.00 10.17           C  
ATOM   4637  C   LEU B 315     -80.987  33.539 -50.595  1.00 26.71           C  
ATOM   4638  O   LEU B 315     -82.047  32.903 -50.627  1.00 60.85           O  
ATOM   4639  CB  LEU B 315     -78.786  32.344 -50.525  1.00 10.28           C  
ATOM   4640  CG  LEU B 315     -77.523  31.808 -51.205  1.00 10.38           C  
ATOM   4641  CD1 LEU B 315     -76.655  31.052 -50.208  1.00 10.46           C  
ATOM   4642  CD2 LEU B 315     -77.873  30.928 -52.398  1.00 10.18           C  
ATOM   4643  N   GLU B 316     -80.838  34.638 -49.854  1.00 10.59           N  
ATOM   4644  CA  GLU B 316     -81.925  35.127 -49.015  1.00 10.75           C  
ATOM   4645  C   GLU B 316     -83.040  35.772 -49.826  1.00 10.52           C  
ATOM   4646  O   GLU B 316     -84.162  35.897 -49.322  1.00 13.82           O  
ATOM   4647  CB  GLU B 316     -81.369  36.096 -47.977  1.00 11.32           C  
ATOM   4648  CG  GLU B 316     -80.559  35.378 -46.915  1.00 23.66           C  
ATOM   4649  CD  GLU B 316     -79.711  36.310 -46.086  1.00 27.58           C  
ATOM   4650  OE1 GLU B 316     -79.082  35.826 -45.122  1.00 33.71           O  
ATOM   4651  OE2 GLU B 316     -79.662  37.517 -46.403  1.00 16.24           O  
ATOM   4652  N   ALA B 317     -82.761  36.183 -51.064  1.00 10.22           N  
ATOM   4653  CA  ALA B 317     -83.830  36.632 -51.948  1.00  9.59           C  
ATOM   4654  C   ALA B 317     -84.629  35.452 -52.484  1.00 22.75           C  
ATOM   4655  O   ALA B 317     -85.855  35.535 -52.612  1.00 18.04           O  
ATOM   4656  CB  ALA B 317     -83.258  37.458 -53.100  1.00 10.66           C  
ATOM   4657  N   GLU B 318     -83.950  34.346 -52.802  1.00 35.82           N  
ATOM   4658  CA  GLU B 318     -84.652  33.159 -53.274  1.00 25.68           C  
ATOM   4659  C   GLU B 318     -85.510  32.543 -52.175  1.00  8.74           C  
ATOM   4660  O   GLU B 318     -86.597  32.026 -52.459  1.00  8.34           O  
ATOM   4661  CB  GLU B 318     -83.653  32.133 -53.809  1.00 31.94           C  
ATOM   4662  CG  GLU B 318     -84.298  30.891 -54.402  1.00 57.49           C  
ATOM   4663  CD  GLU B 318     -83.282  29.878 -54.893  1.00 70.26           C  
ATOM   4664  OE1 GLU B 318     -82.066  30.134 -54.757  1.00 67.02           O  
ATOM   4665  OE2 GLU B 318     -83.703  28.826 -55.417  1.00 81.32           O  
ATOM   4666  N   LYS B 319     -85.055  32.599 -50.920  1.00  9.19           N  
ATOM   4667  CA  LYS B 319     -85.904  32.148 -49.822  1.00 10.63           C  
ATOM   4668  C   LYS B 319     -87.112  33.061 -49.667  1.00  9.20           C  
ATOM   4669  O   LYS B 319     -88.217  32.596 -49.362  1.00  8.96           O  
ATOM   4670  CB  LYS B 319     -85.101  32.088 -48.521  1.00 30.02           C  
ATOM   4671  CG  LYS B 319     -85.956  31.912 -47.273  1.00 27.90           C  
ATOM   4672  CD  LYS B 319     -85.110  31.631 -46.044  1.00 27.23           C  
ATOM   4673  CE  LYS B 319     -84.603  30.198 -46.046  1.00 42.42           C  
ATOM   4674  NZ  LYS B 319     -85.729  29.220 -46.040  1.00 55.71           N  
ATOM   4675  N   PHE B 320     -86.922  34.361 -49.889  1.00 18.79           N  
ATOM   4676  CA  PHE B 320     -88.045  35.289 -49.837  1.00 25.92           C  
ATOM   4677  C   PHE B 320     -89.023  35.030 -50.975  1.00 22.05           C  
ATOM   4678  O   PHE B 320     -90.242  35.075 -50.775  1.00 13.66           O  
ATOM   4679  CB  PHE B 320     -87.534  36.728 -49.885  1.00 15.36           C  
ATOM   4680  CG  PHE B 320     -88.608  37.743 -50.151  1.00 16.63           C  
ATOM   4681  CD1 PHE B 320     -89.479  38.131 -49.147  1.00  8.89           C  
ATOM   4682  CD2 PHE B 320     -88.743  38.313 -51.407  1.00 21.06           C  
ATOM   4683  CE1 PHE B 320     -90.466  39.066 -49.391  1.00  8.04           C  
ATOM   4684  CE2 PHE B 320     -89.728  39.249 -51.658  1.00  6.97           C  
ATOM   4685  CZ  PHE B 320     -90.591  39.626 -50.649  1.00  7.01           C  
ATOM   4686  N   ILE B 321     -88.505  34.755 -52.174  1.00  7.96           N  
ATOM   4687  CA  ILE B 321     -89.371  34.526 -53.327  1.00  7.02           C  
ATOM   4688  C   ILE B 321     -90.091  33.187 -53.207  1.00 14.74           C  
ATOM   4689  O   ILE B 321     -91.278  33.075 -53.538  1.00 20.80           O  
ATOM   4690  CB  ILE B 321     -88.552  34.622 -54.627  1.00  6.55           C  
ATOM   4691  CG1 ILE B 321     -88.111  36.066 -54.867  1.00  6.30           C  
ATOM   4692  CG2 ILE B 321     -89.356  34.115 -55.813  1.00  5.54           C  
ATOM   4693  CD1 ILE B 321     -87.367  36.266 -56.165  1.00 38.05           C  
ATOM   4694  N   ALA B 322     -89.390  32.153 -52.736  1.00 19.42           N  
ATOM   4695  CA  ALA B 322     -90.005  30.834 -52.603  1.00 15.66           C  
ATOM   4696  C   ALA B 322     -91.171  30.861 -51.621  1.00  9.22           C  
ATOM   4697  O   ALA B 322     -92.261  30.360 -51.919  1.00 21.91           O  
ATOM   4698  CB  ALA B 322     -88.957  29.808 -52.170  1.00 33.70           C  
ATOM   4699  N   GLU B 323     -90.957  31.443 -50.440  1.00 10.01           N  
ATOM   4700  CA  GLU B 323     -91.990  31.527 -49.413  1.00 35.96           C  
ATOM   4701  C   GLU B 323     -93.064  32.566 -49.722  1.00 30.81           C  
ATOM   4702  O   GLU B 323     -93.974  32.745 -48.905  1.00 24.56           O  
ATOM   4703  CB  GLU B 323     -91.348  31.828 -48.055  1.00 56.19           C  
ATOM   4704  CG  GLU B 323     -90.298  30.810 -47.625  1.00 58.15           C  
ATOM   4705  CD  GLU B 323     -89.696  31.122 -46.266  1.00 65.55           C  
ATOM   4706  OE1 GLU B 323     -89.867  32.263 -45.785  1.00 64.51           O  
ATOM   4707  OE2 GLU B 323     -89.048  30.227 -45.681  1.00 71.65           O  
ATOM   4708  N   ALA B 324     -92.990  33.247 -50.864  1.00 29.02           N  
ATOM   4709  CA  ALA B 324     -93.952  34.281 -51.227  1.00 31.36           C  
ATOM   4710  C   ALA B 324     -95.000  33.811 -52.226  1.00 47.44           C  
ATOM   4711  O   ALA B 324     -96.159  34.227 -52.137  1.00 59.05           O  
ATOM   4712  CB  ALA B 324     -93.229  35.505 -51.799  1.00 19.30           C  
ATOM   4713  N   GLU B 325     -94.630  32.952 -53.171  1.00 43.42           N  
ATOM   4714  CA  GLU B 325     -95.552  32.501 -54.201  1.00 41.33           C  
ATOM   4715  C   GLU B 325     -96.343  31.282 -53.737  1.00 39.17           C  
ATOM   4716  O   GLU B 325     -95.987  30.605 -52.769  1.00 35.32           O  
ATOM   4717  CB  GLU B 325     -94.796  32.174 -55.491  1.00 34.81           C  
ATOM   4718  N   SER B 326     -97.436  31.013 -54.447  1.00 43.23           N  
ATOM   4719  CA  SER B 326     -98.314  29.893 -54.125  1.00 44.95           C  
ATOM   4720  C   SER B 326     -98.128  28.743 -55.110  1.00 55.94           C  
ATOM   4721  O   SER B 326     -97.379  27.802 -54.847  1.00 55.13           O  
ATOM   4722  CB  SER B 326     -99.776  30.345 -54.118  1.00 25.94           C  
TER    4723      SER B 326                                                      
HETATM 4724  PA  FAD A 401     -62.905  23.661 -45.566  0.93156.31           P  
HETATM 4725  O1A FAD A 401     -62.316  23.763 -46.939  0.93150.62           O  
HETATM 4726  O2A FAD A 401     -64.246  22.999 -45.657  0.93160.18           O1-
HETATM 4727  O5B FAD A 401     -61.945  22.771 -44.615  0.93161.82           O  
HETATM 4728  C5B FAD A 401     -60.638  23.297 -44.255  0.93163.72           C  
HETATM 4729  C4B FAD A 401     -59.576  22.170 -44.266  0.93163.60           C  
HETATM 4730  O4B FAD A 401     -58.774  22.295 -43.255  0.93156.85           O  
HETATM 4731  C3B FAD A 401     -60.201  20.785 -44.056  0.93170.58           C  
HETATM 4732  O3B FAD A 401     -60.601  20.275 -45.212  0.93173.08           O  
HETATM 4733  C2B FAD A 401     -59.038  19.957 -43.467  0.93169.35           C  
HETATM 4734  O2B FAD A 401     -58.334  19.198 -44.556  0.93173.32           O  
HETATM 4735  C1B FAD A 401     -58.218  20.807 -42.927  0.93160.94           C  
HETATM 4736  N9A FAD A 401     -58.143  20.597 -41.512  0.93155.45           N  
HETATM 4737  C8A FAD A 401     -59.183  20.290 -40.716  0.93155.12           C  
HETATM 4738  N7A FAD A 401     -58.720  20.169 -39.445  0.93150.97           N  
HETATM 4739  C5A FAD A 401     -57.388  20.403 -39.461  0.93148.14           C  
HETATM 4740  C6A FAD A 401     -56.429  20.408 -38.437  0.93139.33           C  
HETATM 4741  N6A FAD A 401     -56.421  20.185 -37.018  0.93132.73           N  
HETATM 4742  N1A FAD A 401     -55.136  20.676 -38.723  0.93138.97           N  
HETATM 4743  C2A FAD A 401     -54.764  20.945 -40.019  0.93140.96           C  
HETATM 4744  N3A FAD A 401     -55.699  20.942 -41.020  0.93149.16           N  
HETATM 4745  C4A FAD A 401     -57.023  20.667 -40.731  0.93152.96           C  
HETATM 4746  N1  FAD A 401     -68.853  25.888 -52.684  0.93144.95           N  
HETATM 4747  C2  FAD A 401     -68.845  26.801 -53.836  0.93142.33           C  
HETATM 4748  O2  FAD A 401     -68.697  28.002 -53.673  0.93143.66           O  
HETATM 4749  N3  FAD A 401     -69.023  26.264 -55.209  0.93145.47           N  
HETATM 4750  C4  FAD A 401     -69.201  24.851 -55.404  0.93151.91           C  
HETATM 4751  O4  FAD A 401     -69.348  24.394 -56.532  0.93153.61           O  
HETATM 4752  C4X FAD A 401     -69.203  23.937 -54.220  0.93153.68           C  
HETATM 4753  N5  FAD A 401     -69.382  22.530 -54.424  0.93157.78           N  
HETATM 4754  C5X FAD A 401     -69.392  21.619 -53.277  0.93158.73           C  
HETATM 4755  C6  FAD A 401     -69.572  20.222 -53.503  0.93152.83           C  
HETATM 4756  C7  FAD A 401     -69.582  19.334 -52.419  0.93146.20           C  
HETATM 4757  C7M FAD A 401     -69.792  17.914 -52.962  0.93143.50           C  
HETATM 4758  C8  FAD A 401     -69.416  19.823 -51.112  0.93141.64           C  
HETATM 4759  C8M FAD A 401     -69.421  18.902 -49.894  0.93128.88           C  
HETATM 4760  C9  FAD A 401     -69.240  21.207 -50.885  0.93149.45           C  
HETATM 4761  C9A FAD A 401     -69.226  22.115 -51.976  0.93152.15           C  
HETATM 4762  N10 FAD A 401     -69.036  23.583 -51.756  0.93148.74           N  
HETATM 4763  C10 FAD A 401     -69.032  24.464 -52.876  0.93148.86           C  
HETATM 4764  C1' FAD A 401     -68.858  24.138 -50.387  0.93150.86           C  
HETATM 4765  C2' FAD A 401     -67.433  23.868 -49.862  0.93153.15           C  
HETATM 4766  O2' FAD A 401     -67.502  23.021 -48.776  0.93166.12           O  
HETATM 4767  C3' FAD A 401     -66.720  25.159 -49.457  0.93142.70           C  
HETATM 4768  O3' FAD A 401     -65.334  25.005 -49.682  0.93143.37           O  
HETATM 4769  C4' FAD A 401     -66.936  25.456 -47.992  0.93132.85           C  
HETATM 4770  O4' FAD A 401     -68.194  26.085 -47.828  0.93112.61           O  
HETATM 4771  C5' FAD A 401     -65.844  26.374 -47.478  0.93133.07           C  
HETATM 4772  O5' FAD A 401     -64.810  25.624 -46.801  0.93125.45           O  
HETATM 4773  P   FAD A 401     -64.002  26.265 -45.604  0.93106.01           P  
HETATM 4774  O1P FAD A 401     -63.120  27.398 -46.101  0.93111.08           O  
HETATM 4775  O2P FAD A 401     -64.943  26.812 -44.553  0.93 66.12           O1-
HETATM 4776  O3P FAD A 401     -63.078  25.125 -44.948  0.93137.80           O  
HETATM 4777  C1  MLI A 402     -71.345  16.526 -61.389  1.00120.65           C  
HETATM 4778  C2  MLI A 402     -71.471  16.296 -59.883  1.00112.24           C  
HETATM 4779  C3  MLI A 402     -70.039  17.242 -61.732  1.00130.69           C  
HETATM 4780  O6  MLI A 402     -71.631  15.127 -59.441  1.00107.64           O  
HETATM 4781  O7  MLI A 402     -71.419  17.267 -59.083  1.00109.15           O  
HETATM 4782  O8  MLI A 402     -69.464  16.996 -62.825  1.00133.18           O  
HETATM 4783  O9  MLI A 402     -69.532  18.074 -60.934  1.00134.15           O  
HETATM 4784  C1  MLI A 403     -80.418  27.624 -50.344  1.00159.63           C  
HETATM 4785  C2  MLI A 403     -80.699  26.122 -50.393  1.00161.36           C  
HETATM 4786  C3  MLI A 403     -81.698  28.427 -50.583  1.00155.14           C  
HETATM 4787  O6  MLI A 403     -81.201  25.601 -51.425  1.00158.62           O  
HETATM 4788  O7  MLI A 403     -80.424  25.399 -49.399  1.00159.41           O  
HETATM 4789  O8  MLI A 403     -82.762  27.848 -50.925  1.00154.96           O  
HETATM 4790  O9  MLI A 403     -81.687  29.677 -50.439  1.00149.10           O  
HETATM 4791  C1  MLI A 404     -57.950  48.170 -42.124  1.00153.49           C  
HETATM 4792  C2  MLI A 404     -57.227  47.406 -41.015  1.00152.15           C  
HETATM 4793  C3  MLI A 404     -57.118  49.372 -42.570  1.00155.54           C  
HETATM 4794  O6  MLI A 404     -57.561  46.221 -40.749  1.00152.34           O  
HETATM 4795  O7  MLI A 404     -56.304  47.958 -40.361  1.00152.34           O  
HETATM 4796  O8  MLI A 404     -55.897  49.234 -42.842  1.00154.66           O  
HETATM 4797  O9  MLI A 404     -57.658  50.505 -42.672  1.00153.68           O  
HETATM 4798  C   FMT A 405     -66.746   1.252 -53.730  1.00118.11           C  
HETATM 4799  O1  FMT A 405     -67.499   1.917 -53.020  1.00115.73           O  
HETATM 4800  O2  FMT A 405     -66.837   1.184 -54.955  1.00117.78           O  
HETATM 4801  C   FMT A 406     -80.603  31.099 -46.722  1.00 99.59           C  
HETATM 4802  O1  FMT A 406     -81.712  31.589 -46.927  1.00 98.22           O  
HETATM 4803  O2  FMT A 406     -80.306  29.936 -46.989  1.00 97.58           O  
HETATM 4804  PA  NAP A 407     -80.400  17.183 -38.927  0.96184.25           P  
HETATM 4805  O1A NAP A 407     -78.953  16.831 -38.622  0.96180.63           O  
HETATM 4806  O2A NAP A 407     -81.233  16.956 -37.702  0.96184.64           O  
HETATM 4807  O5B NAP A 407     -80.969  16.197 -40.191  0.96181.21           O  
HETATM 4808  C5B NAP A 407     -80.906  14.778 -40.024  0.96169.55           C  
HETATM 4809  C4B NAP A 407     -81.915  14.087 -40.957  0.96150.71           C  
HETATM 4810  O4B NAP A 407     -81.286  13.280 -41.781  0.96147.01           O  
HETATM 4811  C3B NAP A 407     -82.849  13.192 -40.121  0.96139.52           C  
HETATM 4812  O3B NAP A 407     -84.081  13.111 -40.705  0.96126.81           O  
HETATM 4813  C2B NAP A 407     -82.146  11.819 -40.160  0.96148.88           C  
HETATM 4814  O2B NAP A 407     -83.122  10.720 -39.902  0.96161.09           O  
HETATM 4815  C1B NAP A 407     -81.677  11.758 -41.375  0.96142.81           C  
HETATM 4816  N9A NAP A 407     -80.508  10.898 -41.418  0.96130.95           N  
HETATM 4817  C8A NAP A 407     -79.373  10.889 -40.682  0.96128.38           C  
HETATM 4818  N7A NAP A 407     -78.607   9.886 -41.116  0.96126.58           N  
HETATM 4819  C5A NAP A 407     -79.266   9.265 -42.128  0.96125.21           C  
HETATM 4820  C6A NAP A 407     -78.942   8.186 -42.922  0.96113.52           C  
HETATM 4821  N6A NAP A 407     -77.748   7.315 -42.951  0.96104.06           N  
HETATM 4822  N1A NAP A 407     -79.793   7.768 -43.868  0.96113.07           N  
HETATM 4823  C2A NAP A 407     -80.980   8.409 -44.045  0.96117.22           C  
HETATM 4824  N3A NAP A 407     -81.300   9.468 -43.268  0.96109.95           N  
HETATM 4825  C4A NAP A 407     -80.438   9.893 -42.307  0.96122.91           C  
HETATM 4826  O3  NAP A 407     -80.504  18.790 -39.367  0.96181.64           O  
HETATM 4827  PN  NAP A 407     -80.873  19.330 -40.930  0.96174.06           P  
HETATM 4828  O1N NAP A 407     -80.286  18.388 -41.941  0.96177.82           O  
HETATM 4829  O2N NAP A 407     -82.382  19.384 -41.109  0.96170.99           O  
HETATM 4830  O5D NAP A 407     -80.238  20.826 -41.151  0.96173.27           O  
HETATM 4831  P2B NAP A 407     -83.930  10.727 -38.494  0.96165.01           P  
HETATM 4832  O1X NAP A 407     -85.175  11.563 -38.632  0.96160.38           O  
HETATM 4833  O2X NAP A 407     -83.041  11.313 -37.397  0.96159.75           O  
HETATM 4834  O3X NAP A 407     -84.310   9.314 -38.126  0.96174.77           O  
HETATM 4835  C   ACT A 408     -89.415  10.644 -64.511  1.00118.14           C  
HETATM 4836  O   ACT A 408     -88.448  11.010 -65.238  1.00119.27           O  
HETATM 4837  OXT ACT A 408     -89.392  10.220 -63.321  1.00124.68           O  
HETATM 4838  CH3 ACT A 408     -90.823  10.734 -65.189  1.00107.23           C  
HETATM 4839  PA  FAD B 401     -69.168  48.311 -56.690  0.85175.01           P  
HETATM 4840  O1A FAD B 401     -67.837  47.749 -57.092  0.85175.14           O  
HETATM 4841  O2A FAD B 401     -68.960  49.472 -55.766  0.85189.64           O1-
HETATM 4842  O5B FAD B 401     -69.964  48.786 -58.013  0.85179.81           O  
HETATM 4843  C5B FAD B 401     -70.754  50.006 -57.971  0.85185.89           C  
HETATM 4844  C4B FAD B 401     -71.787  49.964 -59.124  0.85191.16           C  
HETATM 4845  O4B FAD B 401     -72.943  50.390 -58.719  0.85191.33           O  
HETATM 4846  C3B FAD B 401     -71.386  50.925 -60.258  0.85193.80           C  
HETATM 4847  O3B FAD B 401     -70.941  50.244 -61.303  0.85197.87           O  
HETATM 4848  C2B FAD B 401     -72.682  51.668 -60.643  0.85185.57           C  
HETATM 4849  O2B FAD B 401     -72.878  51.612 -62.132  0.85182.65           O  
HETATM 4850  C1B FAD B 401     -73.631  51.028 -60.038  0.85176.72           C  
HETATM 4851  N9A FAD B 401     -74.687  51.923 -59.677  0.85141.20           N  
HETATM 4852  C8A FAD B 401     -74.662  52.792 -58.651  0.85132.57           C  
HETATM 4853  N7A FAD B 401     -75.846  53.459 -58.641  0.85128.77           N  
HETATM 4854  C5A FAD B 401     -76.598  52.995 -59.666  0.85121.27           C  
HETATM 4855  C6A FAD B 401     -77.886  53.327 -60.111  0.85 90.95           C  
HETATM 4856  N6A FAD B 401     -78.916  54.244 -59.712  0.85 85.49           N  
HETATM 4857  N1A FAD B 401     -78.415  52.699 -61.186  0.85 78.52           N  
HETATM 4858  C2A FAD B 401     -77.691  51.731 -61.843  0.85 72.61           C  
HETATM 4859  N3A FAD B 401     -76.434  51.405 -61.409  0.85 91.29           N  
HETATM 4860  C4A FAD B 401     -75.890  52.047 -60.311  0.85125.03           C  
HETATM 4861  N1  FAD B 401     -61.109  45.485 -53.531  0.85161.84           N  
HETATM 4862  C2  FAD B 401     -60.257  44.288 -53.590  0.85159.25           C  
HETATM 4863  O2  FAD B 401     -60.679  43.207 -53.206  0.85150.19           O  
HETATM 4864  N3  FAD B 401     -58.872  44.390 -54.117  0.85164.01           N  
HETATM 4865  C4  FAD B 401     -58.373  45.662 -54.567  0.85160.01           C  
HETATM 4866  O4  FAD B 401     -57.231  45.756 -55.003  0.85156.06           O  
HETATM 4867  C4X FAD B 401     -59.254  46.870 -54.501  0.85165.97           C  
HETATM 4868  N5  FAD B 401     -58.752  48.138 -54.949  0.85171.93           N  
HETATM 4869  C5X FAD B 401     -59.606  49.329 -54.889  0.85171.47           C  
HETATM 4870  C6  FAD B 401     -59.094  50.583 -55.339  0.85160.21           C  
HETATM 4871  C7  FAD B 401     -59.901  51.729 -55.286  0.85141.22           C  
HETATM 4872  C7M FAD B 401     -59.080  52.903 -55.831  0.85126.38           C  
HETATM 4873  C8  FAD B 401     -61.214  51.649 -54.791  0.85142.57           C  
HETATM 4874  C8M FAD B 401     -62.144  52.859 -54.707  0.85131.13           C  
HETATM 4875  C9  FAD B 401     -61.719  50.409 -54.343  0.85155.15           C  
HETATM 4876  C9A FAD B 401     -60.912  49.241 -54.394  0.85166.76           C  
HETATM 4877  N10 FAD B 401     -61.441  47.924 -53.926  0.85162.56           N  
HETATM 4878  C10 FAD B 401     -60.610  46.767 -53.983  0.85163.40           C  
HETATM 4879  C1' FAD B 401     -62.824  47.810 -53.399  0.85157.95           C  
HETATM 4880  C2' FAD B 401     -63.832  47.831 -54.562  0.85154.60           C  
HETATM 4881  O2' FAD B 401     -64.570  48.996 -54.508  0.85158.09           O  
HETATM 4882  C3' FAD B 401     -64.772  46.633 -54.494  0.85148.14           C  
HETATM 4883  O3' FAD B 401     -65.207  46.318 -55.802  0.85144.38           O  
HETATM 4884  C4' FAD B 401     -65.965  46.978 -53.636  0.85141.42           C  
HETATM 4885  O4' FAD B 401     -65.721  46.570 -52.303  0.85144.65           O  
HETATM 4886  C5' FAD B 401     -67.187  46.268 -54.168  0.85121.61           C  
HETATM 4887  O5' FAD B 401     -68.354  47.097 -53.994  0.85104.40           O  
HETATM 4888  P   FAD B 401     -69.734  46.561 -54.524  0.85 93.10           P  
HETATM 4889  O1P FAD B 401     -69.674  45.047 -54.639  0.85109.51           O  
HETATM 4890  O2P FAD B 401     -70.840  46.949 -53.568  0.85 76.19           O1-
HETATM 4891  O3P FAD B 401     -70.037  47.179 -55.974  0.85137.83           O  
HETATM 4892  C1  MLI B 402     -84.647  41.749 -39.189  1.00164.49           C  
HETATM 4893  C2  MLI B 402     -85.699  41.931 -40.283  1.00154.72           C  
HETATM 4894  C3  MLI B 402     -84.901  42.716 -38.032  1.00170.25           C  
HETATM 4895  O6  MLI B 402     -85.674  41.192 -41.303  1.00146.16           O  
HETATM 4896  O7  MLI B 402     -86.587  42.818 -40.173  1.00149.62           O  
HETATM 4897  O8  MLI B 402     -84.007  43.533 -37.687  1.00170.90           O  
HETATM 4898  O9  MLI B 402     -86.001  42.693 -37.418  1.00172.59           O  
HETATM 4899  C1  MLI B 403     -50.603  50.464 -58.010  1.00129.89           C  
HETATM 4900  C2  MLI B 403     -51.620  51.526 -57.593  1.00126.25           C  
HETATM 4901  C3  MLI B 403     -51.235  49.474 -58.988  1.00136.40           C  
HETATM 4902  O6  MLI B 403     -51.474  52.721 -57.961  1.00121.92           O  
HETATM 4903  O7  MLI B 403     -52.606  51.207 -56.878  1.00126.49           O  
HETATM 4904  O8  MLI B 403     -50.503  48.806 -59.766  1.00139.93           O  
HETATM 4905  O9  MLI B 403     -52.485  49.322 -59.020  1.00135.04           O  
HETATM 4906  C   FMT B 404     -55.891  65.888 -65.265  1.00127.86           C  
HETATM 4907  O1  FMT B 404     -56.012  66.824 -64.476  1.00129.79           O  
HETATM 4908  O2  FMT B 404     -54.850  65.251 -65.423  1.00125.72           O  
HETATM 4909  C   FMT B 405     -36.870  58.701 -48.228  1.00123.99           C  
HETATM 4910  O1  FMT B 405     -37.949  59.031 -47.737  1.00121.29           O  
HETATM 4911  O2  FMT B 405     -36.098  57.890 -47.717  1.00124.37           O  
HETATM 4912  C   FMT B 406     -61.873  46.644 -39.497  1.00118.80           C  
HETATM 4913  O1  FMT B 406     -60.957  45.837 -39.350  1.00117.45           O  
HETATM 4914  O2  FMT B 406     -62.648  46.975 -38.601  1.00118.01           O  
HETATM 4915  C   FMT B 407     -47.849  42.799 -53.653  1.00102.76           C  
HETATM 4916  O1  FMT B 407     -47.121  42.507 -52.706  1.00101.94           O  
HETATM 4917  O2  FMT B 407     -48.979  43.273 -53.536  1.00101.80           O  
HETATM 4918  C   FMT B 408     -73.713  24.361 -64.939  1.00 95.17           C  
HETATM 4919  O1  FMT B 408     -72.796  23.751 -64.390  1.00 91.35           O  
HETATM 4920  O2  FMT B 408     -74.539  25.052 -64.343  1.00 89.05           O  
HETATM 4921  PA  NAP B 409     -65.450  62.898 -42.742  0.89203.50           P  
HETATM 4922  O1A NAP B 409     -65.804  62.989 -44.218  0.89201.50           O  
HETATM 4923  O2A NAP B 409     -66.386  63.763 -41.951  0.89198.50           O  
HETATM 4924  O5B NAP B 409     -63.850  63.418 -42.501  0.89197.39           O  
HETATM 4925  C5B NAP B 409     -63.075  63.817 -43.633  0.89184.95           C  
HETATM 4926  C4B NAP B 409     -61.614  64.002 -43.192  0.89168.60           C  
HETATM 4927  O4B NAP B 409     -60.863  64.271 -44.231  0.89161.51           O  
HETATM 4928  C3B NAP B 409     -61.511  65.244 -42.293  0.89163.80           C  
HETATM 4929  O3B NAP B 409     -60.392  65.179 -41.511  0.89159.90           O  
HETATM 4930  C2B NAP B 409     -61.382  66.390 -43.317  0.89164.89           C  
HETATM 4931  O2B NAP B 409     -60.689  67.560 -42.705  0.89177.68           O  
HETATM 4932  C1B NAP B 409     -60.668  65.882 -44.285  0.89155.95           C  
HETATM 4933  N9A NAP B 409     -61.127  66.402 -45.560  0.89140.46           N  
HETATM 4934  C8A NAP B 409     -62.360  66.456 -46.112  0.89136.70           C  
HETATM 4935  N7A NAP B 409     -62.251  67.037 -47.309  0.89136.39           N  
HETATM 4936  C5A NAP B 409     -60.944  67.348 -47.505  0.89140.23           C  
HETATM 4937  C6A NAP B 409     -60.281  67.951 -48.552  0.89142.84           C  
HETATM 4938  N6A NAP B 409     -60.766  68.478 -49.846  0.89144.89           N  
HETATM 4939  N1A NAP B 409     -58.955  68.142 -48.487  0.89136.39           N  
HETATM 4940  C2A NAP B 409     -58.263  67.741 -47.387  0.89131.03           C  
HETATM 4941  N3A NAP B 409     -58.912  67.149 -46.359  0.89131.18           N  
HETATM 4942  C4A NAP B 409     -60.256  66.954 -46.423  0.89138.26           C  
HETATM 4943  O3  NAP B 409     -65.567  61.317 -42.219  0.89207.86           O  
HETATM 4944  PN  NAP B 409     -64.259  60.464 -41.561  0.89199.14           P  
HETATM 4945  O1N NAP B 409     -63.064  60.605 -42.459  0.89200.43           O  
HETATM 4946  O2N NAP B 409     -64.620  58.992 -41.426  0.89195.68           O  
HETATM 4947  O5D NAP B 409     -63.896  61.071 -40.081  0.89192.28           O  
HETATM 4948  P2B NAP B 409     -61.606  68.712 -42.027  0.89186.16           P  
HETATM 4949  O1X NAP B 409     -62.872  68.902 -42.862  0.89179.14           O  
HETATM 4950  O2X NAP B 409     -61.983  68.302 -40.628  0.89190.63           O  
HETATM 4951  O3X NAP B 409     -60.833  70.007 -41.980  0.89193.48           O  
HETATM 4952  C1  MLT B 410     -70.096  37.565 -43.463  1.00115.65           C  
HETATM 4953  O1  MLT B 410     -70.969  36.748 -43.828  1.00121.21           O  
HETATM 4954  O2  MLT B 410     -69.230  37.210 -42.633  1.00117.94           O  
HETATM 4955  C2  MLT B 410     -70.080  38.960 -44.018  1.00105.47           C  
HETATM 4956  O3  MLT B 410     -71.345  39.292 -44.547  1.00101.79           O  
HETATM 4957  C3  MLT B 410     -69.019  39.090 -45.107  1.00 96.85           C  
HETATM 4958  C4  MLT B 410     -69.146  37.975 -46.119  1.00 86.18           C  
HETATM 4959  O4  MLT B 410     -69.773  38.160 -47.183  1.00 84.08           O  
HETATM 4960  O5  MLT B 410     -68.616  36.859 -45.918  1.00 78.50           O  
HETATM 4961  O   HOH A 501     -85.890   9.594 -34.038  1.00 56.92           O  
HETATM 4962  O   HOH A 502     -85.215  24.988 -65.603  1.00 71.94           O  
HETATM 4963  O   HOH A 503     -89.641  23.167 -64.214  1.00 71.50           O  
HETATM 4964  O   HOH A 504     -84.383  12.039 -32.525  1.00 85.17           O  
HETATM 4965  O   HOH A 505     -46.949  50.840 -27.316  1.00 66.76           O  
HETATM 4966  O   HOH A 506     -76.416  28.357 -57.837  1.00 55.68           O  
HETATM 4967  O   HOH A 507     -69.442  33.040 -42.989  1.00 72.52           O  
HETATM 4968  O   HOH A 508     -53.277  15.772 -47.800  1.00 92.10           O  
HETATM 4969  O   HOH A 509     -80.508  23.192 -38.703  1.00 71.64           O  
HETATM 4970  O   HOH A 510     -85.416  -4.120 -42.022  1.00 60.37           O  
HETATM 4971  O   HOH A 511     -77.143  21.960 -39.755  1.00 62.19           O  
HETATM 4972  O   HOH A 512     -77.152   8.859 -37.758  1.00 84.38           O  
HETATM 4973  O   HOH A 513     -75.179  10.988 -40.370  1.00 70.56           O  
HETATM 4974  O   HOH A 514     -42.426  36.101 -33.219  1.00 69.94           O  
HETATM 4975  O   HOH A 515     -57.650  38.768 -23.563  1.00 70.29           O  
HETATM 4976  O   HOH A 516     -42.860  26.287 -36.630  1.00 74.22           O  
HETATM 4977  O   HOH A 517     -87.213  22.799 -66.759  1.00 77.50           O  
HETATM 4978  O   HOH A 518     -55.265  27.015 -67.619  1.00 93.19           O  
HETATM 4979  O   HOH A 519     -50.780  28.170 -17.929  1.00 77.57           O  
HETATM 4980  O   HOH A 520     -65.425  12.806 -37.915  1.00 78.30           O  
HETATM 4981  O   HOH A 521     -82.877  23.951 -37.337  1.00 79.68           O  
HETATM 4982  O   HOH A 522     -73.303  33.039 -21.247  1.00 73.32           O  
HETATM 4983  O   HOH B 501     -49.550  80.054 -53.031  1.00 92.69           O  
HETATM 4984  O   HOH B 502     -89.754  39.745 -68.373  1.00 96.97           O  
HETATM 4985  O   HOH B 503     -89.264  43.580 -39.571  1.00 79.45           O  
HETATM 4986  O   HOH B 504     -52.613  50.314 -65.972  1.00 73.05           O  
HETATM 4987  O   HOH B 505     -79.343  58.570 -68.404  1.00 89.58           O  
HETATM 4988  O   HOH B 506     -84.459  61.468 -65.068  1.00 89.35           O  
HETATM 4989  O   HOH B 507     -67.347  45.210 -35.590  1.00 67.30           O  
HETATM 4990  O   HOH B 508     -37.468  66.346 -51.149  1.00 84.44           O  
HETATM 4991  O   HOH B 509     -91.679  37.056 -65.397  1.00 75.12           O  
HETATM 4992  O   HOH B 510     -73.916  43.282 -42.803  1.00 78.85           O  
HETATM 4993  O   HOH B 511     -56.614  48.635 -65.490  1.00 84.91           O  
HETATM 4994  O   HOH B 512     -70.869  52.814 -35.215  1.00 80.41           O  
HETATM 4995  O   HOH B 513     -73.705  55.035 -63.543  1.00 54.92           O  
HETATM 4996  O   HOH B 514     -85.594  49.619 -36.780  1.00 90.46           O  
HETATM 4997  O   HOH B 515     -75.736  58.261 -55.239  1.00 75.45           O  
HETATM 4998  O   HOH B 516     -64.543  55.140 -40.124  1.00 75.38           O  
HETATM 4999  O   HOH B 517     -54.667  65.926 -69.469  1.00 77.84           O  
HETATM 5000  O   HOH B 518     -41.036  63.597 -45.314  1.00 72.70           O  
HETATM 5001  O   HOH B 519     -85.621  36.359 -41.144  1.00 82.63           O  
HETATM 5002  O   HOH B 520     -86.875  51.214 -73.426  1.00 80.73           O  
HETATM 5003  O   HOH B 521     -82.252  39.111 -38.263  1.00 63.24           O  
HETATM 5004  O   HOH B 522     -92.388  55.334 -45.455  1.00 74.56           O  
HETATM 5005  O   HOH B 523     -91.918  47.200 -72.147  1.00 71.62           O  
CONECT 1026 1044                                                                
CONECT 1044 1026                                                                
CONECT 3393 3411                                                                
CONECT 3411 3393                                                                
CONECT 4724 4725 4726 4727 4776                                                 
CONECT 4725 4724                                                                
CONECT 4726 4724                                                                
CONECT 4727 4724 4728                                                           
CONECT 4728 4727 4729                                                           
CONECT 4729 4728 4730 4731                                                      
CONECT 4730 4729 4735                                                           
CONECT 4731 4729 4732 4733                                                      
CONECT 4732 4731                                                                
CONECT 4733 4731 4734 4735                                                      
CONECT 4734 4733                                                                
CONECT 4735 4730 4733 4736                                                      
CONECT 4736 4735 4737 4745                                                      
CONECT 4737 4736 4738                                                           
CONECT 4738 4737 4739                                                           
CONECT 4739 4738 4740 4745                                                      
CONECT 4740 4739 4741 4742                                                      
CONECT 4741 4740                                                                
CONECT 4742 4740 4743                                                           
CONECT 4743 4742 4744                                                           
CONECT 4744 4743 4745                                                           
CONECT 4745 4736 4739 4744                                                      
CONECT 4746 4747 4763                                                           
CONECT 4747 4746 4748 4749                                                      
CONECT 4748 4747                                                                
CONECT 4749 4747 4750                                                           
CONECT 4750 4749 4751 4752                                                      
CONECT 4751 4750                                                                
CONECT 4752 4750 4753 4763                                                      
CONECT 4753 4752 4754                                                           
CONECT 4754 4753 4755 4761                                                      
CONECT 4755 4754 4756                                                           
CONECT 4756 4755 4757 4758                                                      
CONECT 4757 4756                                                                
CONECT 4758 4756 4759 4760                                                      
CONECT 4759 4758                                                                
CONECT 4760 4758 4761                                                           
CONECT 4761 4754 4760 4762                                                      
CONECT 4762 4761 4763 4764                                                      
CONECT 4763 4746 4752 4762                                                      
CONECT 4764 4762 4765                                                           
CONECT 4765 4764 4766 4767                                                      
CONECT 4766 4765                                                                
CONECT 4767 4765 4768 4769                                                      
CONECT 4768 4767                                                                
CONECT 4769 4767 4770 4771                                                      
CONECT 4770 4769                                                                
CONECT 4771 4769 4772                                                           
CONECT 4772 4771 4773                                                           
CONECT 4773 4772 4774 4775 4776                                                 
CONECT 4774 4773                                                                
CONECT 4775 4773                                                                
CONECT 4776 4724 4773                                                           
CONECT 4777 4778 4779                                                           
CONECT 4778 4777 4780 4781                                                      
CONECT 4779 4777 4782 4783                                                      
CONECT 4780 4778                                                                
CONECT 4781 4778                                                                
CONECT 4782 4779                                                                
CONECT 4783 4779                                                                
CONECT 4784 4785 4786                                                           
CONECT 4785 4784 4787 4788                                                      
CONECT 4786 4784 4789 4790                                                      
CONECT 4787 4785                                                                
CONECT 4788 4785                                                                
CONECT 4789 4786                                                                
CONECT 4790 4786                                                                
CONECT 4791 4792 4793                                                           
CONECT 4792 4791 4794 4795                                                      
CONECT 4793 4791 4796 4797                                                      
CONECT 4794 4792                                                                
CONECT 4795 4792                                                                
CONECT 4796 4793                                                                
CONECT 4797 4793                                                                
CONECT 4798 4799 4800                                                           
CONECT 4799 4798                                                                
CONECT 4800 4798                                                                
CONECT 4801 4802 4803                                                           
CONECT 4802 4801                                                                
CONECT 4803 4801                                                                
CONECT 4804 4805 4806 4807 4826                                                 
CONECT 4805 4804                                                                
CONECT 4806 4804                                                                
CONECT 4807 4804 4808                                                           
CONECT 4808 4807 4809                                                           
CONECT 4809 4808 4810 4811                                                      
CONECT 4810 4809 4815                                                           
CONECT 4811 4809 4812 4813                                                      
CONECT 4812 4811                                                                
CONECT 4813 4811 4814 4815                                                      
CONECT 4814 4813 4831                                                           
CONECT 4815 4810 4813 4816                                                      
CONECT 4816 4815 4817 4825                                                      
CONECT 4817 4816 4818                                                           
CONECT 4818 4817 4819                                                           
CONECT 4819 4818 4820 4825                                                      
CONECT 4820 4819 4821 4822                                                      
CONECT 4821 4820                                                                
CONECT 4822 4820 4823                                                           
CONECT 4823 4822 4824                                                           
CONECT 4824 4823 4825                                                           
CONECT 4825 4816 4819 4824                                                      
CONECT 4826 4804 4827                                                           
CONECT 4827 4826 4828 4829 4830                                                 
CONECT 4828 4827                                                                
CONECT 4829 4827                                                                
CONECT 4830 4827                                                                
CONECT 4831 4814 4832 4833 4834                                                 
CONECT 4832 4831                                                                
CONECT 4833 4831                                                                
CONECT 4834 4831                                                                
CONECT 4835 4836 4837 4838                                                      
CONECT 4836 4835                                                                
CONECT 4837 4835                                                                
CONECT 4838 4835                                                                
CONECT 4839 4840 4841 4842 4891                                                 
CONECT 4840 4839                                                                
CONECT 4841 4839                                                                
CONECT 4842 4839 4843                                                           
CONECT 4843 4842 4844                                                           
CONECT 4844 4843 4845 4846                                                      
CONECT 4845 4844 4850                                                           
CONECT 4846 4844 4847 4848                                                      
CONECT 4847 4846                                                                
CONECT 4848 4846 4849 4850                                                      
CONECT 4849 4848                                                                
CONECT 4850 4845 4848 4851                                                      
CONECT 4851 4850 4852 4860                                                      
CONECT 4852 4851 4853                                                           
CONECT 4853 4852 4854                                                           
CONECT 4854 4853 4855 4860                                                      
CONECT 4855 4854 4856 4857                                                      
CONECT 4856 4855                                                                
CONECT 4857 4855 4858                                                           
CONECT 4858 4857 4859                                                           
CONECT 4859 4858 4860                                                           
CONECT 4860 4851 4854 4859                                                      
CONECT 4861 4862 4878                                                           
CONECT 4862 4861 4863 4864                                                      
CONECT 4863 4862                                                                
CONECT 4864 4862 4865                                                           
CONECT 4865 4864 4866 4867                                                      
CONECT 4866 4865                                                                
CONECT 4867 4865 4868 4878                                                      
CONECT 4868 4867 4869                                                           
CONECT 4869 4868 4870 4876                                                      
CONECT 4870 4869 4871                                                           
CONECT 4871 4870 4872 4873                                                      
CONECT 4872 4871                                                                
CONECT 4873 4871 4874 4875                                                      
CONECT 4874 4873                                                                
CONECT 4875 4873 4876                                                           
CONECT 4876 4869 4875 4877                                                      
CONECT 4877 4876 4878 4879                                                      
CONECT 4878 4861 4867 4877                                                      
CONECT 4879 4877 4880                                                           
CONECT 4880 4879 4881 4882                                                      
CONECT 4881 4880                                                                
CONECT 4882 4880 4883 4884                                                      
CONECT 4883 4882                                                                
CONECT 4884 4882 4885 4886                                                      
CONECT 4885 4884                                                                
CONECT 4886 4884 4887                                                           
CONECT 4887 4886 4888                                                           
CONECT 4888 4887 4889 4890 4891                                                 
CONECT 4889 4888                                                                
CONECT 4890 4888                                                                
CONECT 4891 4839 4888                                                           
CONECT 4892 4893 4894                                                           
CONECT 4893 4892 4895 4896                                                      
CONECT 4894 4892 4897 4898                                                      
CONECT 4895 4893                                                                
CONECT 4896 4893                                                                
CONECT 4897 4894                                                                
CONECT 4898 4894                                                                
CONECT 4899 4900 4901                                                           
CONECT 4900 4899 4902 4903                                                      
CONECT 4901 4899 4904 4905                                                      
CONECT 4902 4900                                                                
CONECT 4903 4900                                                                
CONECT 4904 4901                                                                
CONECT 4905 4901                                                                
CONECT 4906 4907 4908                                                           
CONECT 4907 4906                                                                
CONECT 4908 4906                                                                
CONECT 4909 4910 4911                                                           
CONECT 4910 4909                                                                
CONECT 4911 4909                                                                
CONECT 4912 4913 4914                                                           
CONECT 4913 4912                                                                
CONECT 4914 4912                                                                
CONECT 4915 4916 4917                                                           
CONECT 4916 4915                                                                
CONECT 4917 4915                                                                
CONECT 4918 4919 4920                                                           
CONECT 4919 4918                                                                
CONECT 4920 4918                                                                
CONECT 4921 4922 4923 4924 4943                                                 
CONECT 4922 4921                                                                
CONECT 4923 4921                                                                
CONECT 4924 4921 4925                                                           
CONECT 4925 4924 4926                                                           
CONECT 4926 4925 4927 4928                                                      
CONECT 4927 4926 4932                                                           
CONECT 4928 4926 4929 4930                                                      
CONECT 4929 4928                                                                
CONECT 4930 4928 4931 4932                                                      
CONECT 4931 4930 4948                                                           
CONECT 4932 4927 4930 4933                                                      
CONECT 4933 4932 4934 4942                                                      
CONECT 4934 4933 4935                                                           
CONECT 4935 4934 4936                                                           
CONECT 4936 4935 4937 4942                                                      
CONECT 4937 4936 4938 4939                                                      
CONECT 4938 4937                                                                
CONECT 4939 4937 4940                                                           
CONECT 4940 4939 4941                                                           
CONECT 4941 4940 4942                                                           
CONECT 4942 4933 4936 4941                                                      
CONECT 4943 4921 4944                                                           
CONECT 4944 4943 4945 4946 4947                                                 
CONECT 4945 4944                                                                
CONECT 4946 4944                                                                
CONECT 4947 4944                                                                
CONECT 4948 4931 4949 4950 4951                                                 
CONECT 4949 4948                                                                
CONECT 4950 4948                                                                
CONECT 4951 4948                                                                
CONECT 4952 4953 4954 4955                                                      
CONECT 4953 4952                                                                
CONECT 4954 4952                                                                
CONECT 4955 4952 4956 4957                                                      
CONECT 4956 4955                                                                
CONECT 4957 4955 4958                                                           
CONECT 4958 4957 4959 4960                                                      
CONECT 4959 4958                                                                
CONECT 4960 4958                                                                
MASTER      651    0   18   20   42    0   39    6 5003    2  241   58          
END                                                                             
