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Database: PDB
Entry: 5L6I
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Original site: 5L6I 
HEADER    LIGASE                                  30-MAY-16   5L6I              
TITLE     UBA1 IN COMPLEX WITH UB-MLN4924 COVALENT ADDUCT                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-ACTIVATING ENZYME E1 1;                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 6.2.1.45;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: UBIQUITIN-40S RIBOSOMAL PROTEIN S31;                       
COMPND   8 CHAIN: B, D, E;                                                      
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   7 GENE: UBA1, YKL210W;                                                 
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  12 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  13 ORGANISM_TAXID: 4932;                                                
SOURCE  14 GENE: RPS31, RPS37, UBI3, YLR167W, L9470.14;                         
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    E1 ENZYME, UBIQUITIN ACTIVATION, UBA1 INHIBITOR, ADENOSYL SULFAMATE,  
KEYWDS   2 LIGASE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MISRA,H.SCHINDELIN                                                  
REVDAT   4   08-MAY-19 5L6I    1       REMARK LINK                              
REVDAT   3   06-SEP-17 5L6I    1       REMARK                                   
REVDAT   2   19-JUL-17 5L6I    1                                                
REVDAT   1   14-JUN-17 5L6I    0                                                
JRNL        AUTH   M.MISRA,M.KUHN,M.LOBEL,H.AN,A.V.STATSYUK,C.SOTRIFFER,        
JRNL        AUTH 2 H.SCHINDELIN                                                 
JRNL        TITL   DISSECTING THE SPECIFICITY OF ADENOSYL SULFAMATE INHIBITORS  
JRNL        TITL 2 TARGETING THE UBIQUITIN-ACTIVATING ENZYME.                   
JRNL        REF    STRUCTURE                     V.  25  1120 2017              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   28578874                                                     
JRNL        DOI    10.1016/J.STR.2017.05.001                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.76 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 78520                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4093                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.76                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.83                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5315                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2990                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 284                          
REMARK   3   BIN FREE R VALUE                    : 0.3520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17657                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 184                                     
REMARK   3   SOLVENT ATOMS            : 453                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : 2.10000                                              
REMARK   3    B33 (A**2) : -2.16000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.918         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.299         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.238         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.207        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 18193 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 17400 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 24584 ; 1.664 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 40236 ; 1.203 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2236 ; 6.421 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   856 ;37.424 ;25.409       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3227 ;17.232 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;17.373 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2767 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 20459 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3983 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8947 ; 1.147 ; 2.820       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  8946 ; 1.147 ; 2.820       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11173 ; 2.000 ; 4.226       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 11174 ; 2.000 ; 4.226       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9246 ; 1.371 ; 2.975       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  9246 ; 1.370 ; 2.975       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 13409 ; 2.289 ; 4.391       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 19475 ; 3.915 ;21.660       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 19408 ; 3.893 ;21.619       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 4                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    11   1024       C    11   1024  126108  0.07  0.05     
REMARK   3    2     B     1     76       D     1     76    9352  0.07  0.05     
REMARK   3    3     B     1     72       E     1     72    8754  0.11  0.05     
REMARK   3    4     D     1     72       E     1     72    8672  0.12  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 19                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   197                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.7770  27.9977 -41.8283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0989 T22:   0.1788                                     
REMARK   3      T33:   0.1333 T12:   0.0059                                     
REMARK   3      T13:  -0.0376 T23:  -0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0790 L22:   1.5682                                     
REMARK   3      L33:   0.9655 L12:   0.2846                                     
REMARK   3      L13:   0.0395 L23:  -0.0422                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0164 S12:   0.0206 S13:   0.0258                       
REMARK   3      S21:  -0.1209 S22:  -0.0438 S23:   0.4380                       
REMARK   3      S31:   0.0887 S32:  -0.2674 S33:   0.0602                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   198        A   264                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1653  57.0565 -41.8225              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0458 T22:   0.1134                                     
REMARK   3      T33:   0.0450 T12:   0.0283                                     
REMARK   3      T13:   0.0218 T23:   0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6877 L22:   6.9409                                     
REMARK   3      L33:   2.8568 L12:   2.7677                                     
REMARK   3      L13:   1.2166 L23:   1.3332                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0534 S12:   0.1039 S13:  -0.0035                       
REMARK   3      S21:  -0.0748 S22:   0.0843 S23:  -0.3564                       
REMARK   3      S31:  -0.2372 S32:   0.1817 S33:  -0.0309                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   265        A   624                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.1584  18.4237 -31.0587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0523 T22:   0.1115                                     
REMARK   3      T33:   0.0759 T12:  -0.0039                                     
REMARK   3      T13:   0.0095 T23:   0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7458 L22:   1.5776                                     
REMARK   3      L33:   1.0048 L12:  -0.1134                                     
REMARK   3      L13:   0.1246 L23:   0.3337                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0041 S12:   0.0141 S13:  -0.2091                       
REMARK   3      S21:   0.0206 S22:   0.0038 S23:   0.0487                       
REMARK   3      S31:   0.1908 S32:   0.0434 S33:   0.0002                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   625        A   810                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.4177  62.3362  -4.5813              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2693 T22:   0.3019                                     
REMARK   3      T33:   0.0961 T12:   0.0501                                     
REMARK   3      T13:  -0.0093 T23:  -0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0747 L22:   3.0513                                     
REMARK   3      L33:   4.8345 L12:   0.4460                                     
REMARK   3      L13:  -1.5125 L23:  -1.2024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0122 S12:  -0.5231 S13:   0.0374                       
REMARK   3      S21:   0.3690 S22:  -0.1009 S23:  -0.2767                       
REMARK   3      S31:  -0.3548 S32:   0.3835 S33:   0.1132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   811        A   925                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3194  33.1862 -21.9300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0916 T22:   0.1057                                     
REMARK   3      T33:   0.0701 T12:   0.0056                                     
REMARK   3      T13:   0.0431 T23:   0.0238                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2000 L22:   0.9146                                     
REMARK   3      L33:   0.7755 L12:  -0.1056                                     
REMARK   3      L13:   0.2792 L23:   0.3739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0190 S12:  -0.0303 S13:  -0.0789                       
REMARK   3      S21:   0.1214 S22:   0.0045 S23:   0.1839                       
REMARK   3      S31:   0.0360 S32:  -0.0401 S33:   0.0145                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   926        A  1024                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0114  15.2066   3.4424              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3956 T22:   0.1793                                     
REMARK   3      T33:   0.1907 T12:   0.1304                                     
REMARK   3      T13:  -0.0031 T23:   0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5573 L22:   1.4718                                     
REMARK   3      L33:   4.5711 L12:   0.3022                                     
REMARK   3      L13:   1.4172 L23:  -0.1059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0468 S12:  -0.4123 S13:   0.2346                       
REMARK   3      S21:   0.4245 S22:   0.1888 S23:   0.1270                       
REMARK   3      S31:  -0.4159 S32:  -0.4094 S33:  -0.1420                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    65                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2529  31.7746 -37.1660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1245 T22:   0.2099                                     
REMARK   3      T33:   0.1787 T12:   0.0007                                     
REMARK   3      T13:   0.0161 T23:   0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8145 L22:   7.5112                                     
REMARK   3      L33:   2.4607 L12:   0.8495                                     
REMARK   3      L13:   0.1230 L23:  -0.5363                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0295 S12:   0.2785 S13:   0.0184                       
REMARK   3      S21:  -0.4506 S22:   0.0708 S23:  -0.8249                       
REMARK   3      S31:   0.0653 S32:   0.3974 S33:  -0.0412                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    66        B    76                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3029  30.9354 -30.5605              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1608 T22:   0.0481                                     
REMARK   3      T33:   0.1618 T12:   0.0223                                     
REMARK   3      T13:  -0.0279 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1054 L22:   1.5929                                     
REMARK   3      L33:  10.9570 L12:   2.9391                                     
REMARK   3      L13:  -5.4489 L23:  -3.2107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0824 S12:   0.0077 S13:   0.2933                       
REMARK   3      S21:  -0.0071 S22:   0.0130 S23:  -0.0405                       
REMARK   3      S31:  -0.2273 S32:   0.1971 S33:  -0.0955                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    11        C   166                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.1473  64.5556 -39.4898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0873 T22:   0.1476                                     
REMARK   3      T33:   0.0469 T12:   0.0430                                     
REMARK   3      T13:   0.0429 T23:   0.0549                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8075 L22:   1.0645                                     
REMARK   3      L33:   1.7133 L12:   0.0615                                     
REMARK   3      L13:   0.3327 L23:  -0.1340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0960 S12:  -0.2510 S13:  -0.0485                       
REMARK   3      S21:   0.2081 S22:   0.1477 S23:   0.2090                       
REMARK   3      S31:   0.1641 S32:  -0.1746 S33:  -0.0517                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   167        C   264                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1895  51.8299 -59.9526              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1087 T22:   0.2408                                     
REMARK   3      T33:   0.1398 T12:   0.0414                                     
REMARK   3      T13:  -0.0243 T23:  -0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2614 L22:   4.3167                                     
REMARK   3      L33:   4.1413 L12:  -1.5887                                     
REMARK   3      L13:  -3.4795 L23:   1.6463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0018 S12:   0.1383 S13:  -0.2145                       
REMARK   3      S21:  -0.3454 S22:  -0.0161 S23:  -0.3805                       
REMARK   3      S31:   0.1906 S32:   0.3799 S33:   0.0179                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   265        C   545                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.1427  79.1335 -50.9371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0777 T22:   0.1434                                     
REMARK   3      T33:   0.0618 T12:   0.0469                                     
REMARK   3      T13:   0.0213 T23:   0.0641                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1845 L22:   1.6809                                     
REMARK   3      L33:   1.7921 L12:  -0.5057                                     
REMARK   3      L13:   0.3888 L23:  -0.2694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0966 S12:  -0.0186 S13:   0.1589                       
REMARK   3      S21:   0.0856 S22:   0.1180 S23:   0.0694                       
REMARK   3      S31:  -0.3298 S32:  -0.0542 S33:  -0.0215                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   546        C   624                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.4248  63.9473 -74.8438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4212 T22:   0.3856                                     
REMARK   3      T33:   0.0869 T12:   0.1260                                     
REMARK   3      T13:   0.1037 T23:   0.0732                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1492 L22:   3.0639                                     
REMARK   3      L33:   0.2936 L12:  -0.2855                                     
REMARK   3      L13:   0.0317 L23:   0.7759                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2132 S12:   0.1864 S13:   0.0501                       
REMARK   3      S21:  -0.8476 S22:  -0.0983 S23:  -0.4609                       
REMARK   3      S31:  -0.0852 S32:   0.0892 S33:  -0.1149                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   625        C   844                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.6471  33.4605 -82.5734              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4317 T22:   0.3510                                     
REMARK   3      T33:   0.1472 T12:  -0.0191                                     
REMARK   3      T13:  -0.0898 T23:  -0.0726                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6555 L22:   2.1758                                     
REMARK   3      L33:   1.8387 L12:  -1.1401                                     
REMARK   3      L13:   1.5334 L23:   0.3293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1445 S12:   0.6294 S13:  -0.1535                       
REMARK   3      S21:  -0.4526 S22:  -0.0099 S23:  -0.0460                       
REMARK   3      S31:   0.2562 S32:   0.0457 S33:  -0.1345                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   845        C   925                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.7198  72.6098 -65.0866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0397 T22:   0.1811                                     
REMARK   3      T33:   0.0164 T12:   0.0094                                     
REMARK   3      T13:   0.0011 T23:   0.0355                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3329 L22:   0.5055                                     
REMARK   3      L33:   1.7316 L12:  -0.0794                                     
REMARK   3      L13:   0.0528 L23:   0.2531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0229 S12:   0.1202 S13:   0.0023                       
REMARK   3      S21:   0.0648 S22:   0.0703 S23:  -0.0312                       
REMARK   3      S31:  -0.1920 S32:   0.0397 S33:  -0.0473                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   926        C  1024                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.4116  87.2579 -98.1705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1643 T22:   0.2199                                     
REMARK   3      T33:   0.1098 T12:  -0.0024                                     
REMARK   3      T13:  -0.0320 T23:   0.0938                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7852 L22:   2.0592                                     
REMARK   3      L33:   5.5453 L12:   0.3438                                     
REMARK   3      L13:  -0.9589 L23:  -0.7190                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0891 S12:   0.1547 S13:  -0.1445                       
REMARK   3      S21:  -0.1055 S22:  -0.0202 S23:   0.2435                       
REMARK   3      S31:   0.3830 S32:  -0.5441 S33:  -0.0688                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D    65                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7853  77.4342 -66.6140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1582 T22:   0.2925                                     
REMARK   3      T33:   0.1896 T12:  -0.0268                                     
REMARK   3      T13:   0.0692 T23:   0.0602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3405 L22:   5.8358                                     
REMARK   3      L33:   3.9710 L12:  -2.3031                                     
REMARK   3      L13:  -0.4331 L23:  -0.4483                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1003 S12:   0.1018 S13:   0.5801                       
REMARK   3      S21:  -0.2557 S22:  -0.0283 S23:  -0.8913                       
REMARK   3      S31:  -0.3496 S32:   0.4662 S33:  -0.0720                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    66        D    76                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.7594  70.9645 -65.2324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1286 T22:   0.1367                                     
REMARK   3      T33:   0.1454 T12:   0.0125                                     
REMARK   3      T13:   0.0562 T23:   0.0428                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7876 L22:   0.4393                                     
REMARK   3      L33:   1.7390 L12:  -0.8371                                     
REMARK   3      L13:   1.0388 L23:  -0.8382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0270 S12:   0.0177 S13:  -0.2550                       
REMARK   3      S21:  -0.0558 S22:  -0.0582 S23:  -0.0557                       
REMARK   3      S31:   0.0453 S32:   0.0998 S33:   0.0312                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E    65                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9063  58.8716 -81.6376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4715 T22:   0.6152                                     
REMARK   3      T33:   0.5157 T12:  -0.0235                                     
REMARK   3      T13:   0.0082 T23:  -0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0695 L22:  11.6235                                     
REMARK   3      L33:   5.3254 L12:   3.1074                                     
REMARK   3      L13:  -0.5337 L23:   0.7524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2553 S12:   0.3399 S13:  -0.2831                       
REMARK   3      S21:  -0.5572 S22:   0.3606 S23:   0.3631                       
REMARK   3      S31:  -0.0224 S32:  -0.1851 S33:  -0.1054                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    66        E    72                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6918  55.6887 -79.7430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4434 T22:   0.3998                                     
REMARK   3      T33:   0.3542 T12:   0.0260                                     
REMARK   3      T13:  -0.0033 T23:  -0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6582 L22:   6.3871                                     
REMARK   3      L33:   0.4416 L12:  -1.5438                                     
REMARK   3      L13:  -1.4596 L23:  -0.1396                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0072 S12:   0.5439 S13:  -0.1938                       
REMARK   3      S21:  -0.0274 S22:  -0.0141 S23:   0.6490                       
REMARK   3      S31:  -0.0821 S32:  -0.1412 S33:   0.0069                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5L6I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000147.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9184                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82916                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.82800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4NNJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULFATE, 0.1M BIS-TRIS,     
REMARK 280  15% PEG 3350, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       95.94500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.09850            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       95.94500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      115.09850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 7360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 49640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ASN A   788                                                      
REMARK 465     ALA A   789                                                      
REMARK 465     ASN A   790                                                      
REMARK 465     ALA A   791                                                      
REMARK 465     ALA A   792                                                      
REMARK 465     ASN A   793                                                      
REMARK 465     GLY A   794                                                      
REMARK 465     SER A   795                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     ASN C     4                                                      
REMARK 465     ASN C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     LEU C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     ASP C   786                                                      
REMARK 465     PRO C   787                                                      
REMARK 465     ASN C   788                                                      
REMARK 465     ALA C   789                                                      
REMARK 465     ASN C   790                                                      
REMARK 465     ALA C   791                                                      
REMARK 465     ALA C   792                                                      
REMARK 465     ASN C   793                                                      
REMARK 465     GLY C   794                                                      
REMARK 465     SER C   795                                                      
REMARK 465     LEU E    73                                                      
REMARK 465     ARG E    74                                                      
REMARK 465     GLY E    75                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS C   600     C    GLY E    76              1.64            
REMARK 500   O    GLY B    76     N31  B39 B   101              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  20      -60.57    -26.60                                   
REMARK 500    THR A 177      -30.14   -131.98                                   
REMARK 500    ASP A 199     -137.02     55.00                                   
REMARK 500    ASP A 200       57.78   -104.75                                   
REMARK 500    ASP A 220      -77.04      4.79                                   
REMARK 500    LYS A 250      -65.55   -102.91                                   
REMARK 500    ASN A 275       70.37   -157.13                                   
REMARK 500    ASP A 282      114.82   -160.01                                   
REMARK 500    PRO A 334       29.06    -74.12                                   
REMARK 500    PHE A 382      164.24     78.98                                   
REMARK 500    GLN A 482       78.65   -107.53                                   
REMARK 500    LEU A 582      -59.59   -130.39                                   
REMARK 500    GLN A 647       31.67   -145.99                                   
REMARK 500    PHE A 821      109.66    -45.54                                   
REMARK 500    ASN A 920     -130.60     55.11                                   
REMARK 500    SER C  20      -60.00    -26.39                                   
REMARK 500    ASN C 103      103.01   -160.04                                   
REMARK 500    THR C 177      -30.94   -132.56                                   
REMARK 500    LEU C 198      -77.69    -51.61                                   
REMARK 500    ASP C 199     -140.02    -99.25                                   
REMARK 500    ASP C 220      -77.54      3.94                                   
REMARK 500    LYS C 250      -64.67   -103.57                                   
REMARK 500    ASN C 275       68.99   -157.52                                   
REMARK 500    ASP C 282      115.73   -160.41                                   
REMARK 500    PRO C 334       29.48    -71.17                                   
REMARK 500    PHE C 382      163.51     78.23                                   
REMARK 500    GLN C 482       79.30   -108.63                                   
REMARK 500    LEU C 569       99.82   -160.36                                   
REMARK 500    LEU C 582      -57.79   -132.09                                   
REMARK 500    GLN C 647       32.94   -145.97                                   
REMARK 500    ASN C 750       41.77   -145.10                                   
REMARK 500    ASN C 921       19.05     58.44                                   
REMARK 500    ASP E  52      -70.85    -36.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1111                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1112                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1113                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1114                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1116                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1117                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B39 B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 1103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 1106                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1111                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1112                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1113                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1114                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1116                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide B39 D 101 and GLY D    
REMARK 800  76                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY E 76 and CYS C     
REMARK 800  600                                                                 
DBREF  5L6I A    1  1024  UNP    P22515   UBA1_YEAST       1   1024             
DBREF  5L6I B    1    76  UNP    P05759   RS27A_YEAST      1     76             
DBREF  5L6I C    1  1024  UNP    P22515   UBA1_YEAST       1   1024             
DBREF  5L6I D    1    76  UNP    P05759   RS27A_YEAST      1     76             
DBREF  5L6I E    1    76  UNP    P05759   RS27A_YEAST      1     76             
SEQRES   1 A 1024  MET SER SER ASN ASN SER GLY LEU SER ALA ALA GLY GLU          
SEQRES   2 A 1024  ILE ASP GLU SER LEU TYR SER ARG GLN LEU TYR VAL LEU          
SEQRES   3 A 1024  GLY LYS GLU ALA MET LEU LYS MET GLN THR SER ASN VAL          
SEQRES   4 A 1024  LEU ILE LEU GLY LEU LYS GLY LEU GLY VAL GLU ILE ALA          
SEQRES   5 A 1024  LYS ASN VAL VAL LEU ALA GLY VAL LYS SER MET THR VAL          
SEQRES   6 A 1024  PHE ASP PRO GLU PRO VAL GLN LEU ALA ASP LEU SER THR          
SEQRES   7 A 1024  GLN PHE PHE LEU THR GLU LYS ASP ILE GLY GLN LYS ARG          
SEQRES   8 A 1024  GLY ASP VAL THR ARG ALA LYS LEU ALA GLU LEU ASN ALA          
SEQRES   9 A 1024  TYR VAL PRO VAL ASN VAL LEU ASP SER LEU ASP ASP VAL          
SEQRES  10 A 1024  THR GLN LEU SER GLN PHE GLN VAL VAL VAL ALA THR ASP          
SEQRES  11 A 1024  THR VAL SER LEU GLU ASP LYS VAL LYS ILE ASN GLU PHE          
SEQRES  12 A 1024  CYS HIS SER SER GLY ILE ARG PHE ILE SER SER GLU THR          
SEQRES  13 A 1024  ARG GLY LEU PHE GLY ASN THR PHE VAL ASP LEU GLY ASP          
SEQRES  14 A 1024  GLU PHE THR VAL LEU ASP PRO THR GLY GLU GLU PRO ARG          
SEQRES  15 A 1024  THR GLY MET VAL SER ASP ILE GLU PRO ASP GLY THR VAL          
SEQRES  16 A 1024  THR MET LEU ASP ASP ASN ARG HIS GLY LEU GLU ASP GLY          
SEQRES  17 A 1024  ASN PHE VAL ARG PHE SER GLU VAL GLU GLY LEU ASP LYS          
SEQRES  18 A 1024  LEU ASN ASP GLY THR LEU PHE LYS VAL GLU VAL LEU GLY          
SEQRES  19 A 1024  PRO PHE ALA PHE ARG ILE GLY SER VAL LYS GLU TYR GLY          
SEQRES  20 A 1024  GLU TYR LYS LYS GLY GLY ILE PHE THR GLU VAL LYS VAL          
SEQRES  21 A 1024  PRO ARG LYS ILE SER PHE LYS SER LEU LYS GLN GLN LEU          
SEQRES  22 A 1024  SER ASN PRO GLU PHE VAL PHE SER ASP PHE ALA LYS PHE          
SEQRES  23 A 1024  ASP ARG ALA ALA GLN LEU HIS LEU GLY PHE GLN ALA LEU          
SEQRES  24 A 1024  HIS GLN PHE ALA VAL ARG HIS ASN GLY GLU LEU PRO ARG          
SEQRES  25 A 1024  THR MET ASN ASP GLU ASP ALA ASN GLU LEU ILE LYS LEU          
SEQRES  26 A 1024  VAL THR ASP LEU SER VAL GLN GLN PRO GLU VAL LEU GLY          
SEQRES  27 A 1024  GLU GLY VAL ASP VAL ASN GLU ASP LEU ILE LYS GLU LEU          
SEQRES  28 A 1024  SER TYR GLN ALA ARG GLY ASP ILE PRO GLY VAL VAL ALA          
SEQRES  29 A 1024  PHE PHE GLY GLY LEU VAL ALA GLN GLU VAL LEU LYS ALA          
SEQRES  30 A 1024  CYS SER GLY LYS PHE THR PRO LEU LYS GLN PHE MET TYR          
SEQRES  31 A 1024  PHE ASP SER LEU GLU SER LEU PRO ASP PRO LYS ASN PHE          
SEQRES  32 A 1024  PRO ARG ASN GLU LYS THR THR GLN PRO VAL ASN SER ARG          
SEQRES  33 A 1024  TYR ASP ASN GLN ILE ALA VAL PHE GLY LEU ASP PHE GLN          
SEQRES  34 A 1024  LYS LYS ILE ALA ASN SER LYS VAL PHE LEU VAL GLY SER          
SEQRES  35 A 1024  GLY ALA ILE GLY CYS GLU MET LEU LYS ASN TRP ALA LEU          
SEQRES  36 A 1024  LEU GLY LEU GLY SER GLY SER ASP GLY TYR ILE VAL VAL          
SEQRES  37 A 1024  THR ASP ASN ASP SER ILE GLU LYS SER ASN LEU ASN ARG          
SEQRES  38 A 1024  GLN PHE LEU PHE ARG PRO LYS ASP VAL GLY LYS ASN LYS          
SEQRES  39 A 1024  SER GLU VAL ALA ALA GLU ALA VAL CYS ALA MET ASN PRO          
SEQRES  40 A 1024  ASP LEU LYS GLY LYS ILE ASN ALA LYS ILE ASP LYS VAL          
SEQRES  41 A 1024  GLY PRO GLU THR GLU GLU ILE PHE ASN ASP SER PHE TRP          
SEQRES  42 A 1024  GLU SER LEU ASP PHE VAL THR ASN ALA LEU ASP ASN VAL          
SEQRES  43 A 1024  ASP ALA ARG THR TYR VAL ASP ARG ARG CYS VAL PHE TYR          
SEQRES  44 A 1024  ARG LYS PRO LEU LEU GLU SER GLY THR LEU GLY THR LYS          
SEQRES  45 A 1024  GLY ASN THR GLN VAL ILE ILE PRO ARG LEU THR GLU SER          
SEQRES  46 A 1024  TYR SER SER SER ARG ASP PRO PRO GLU LYS SER ILE PRO          
SEQRES  47 A 1024  LEU CYS THR LEU ARG SER PHE PRO ASN LYS ILE ASP HIS          
SEQRES  48 A 1024  THR ILE ALA TRP ALA LYS SER LEU PHE GLN GLY TYR PHE          
SEQRES  49 A 1024  THR ASP SER ALA GLU ASN VAL ASN MET TYR LEU THR GLN          
SEQRES  50 A 1024  PRO ASN PHE VAL GLU GLN THR LEU LYS GLN SER GLY ASP          
SEQRES  51 A 1024  VAL LYS GLY VAL LEU GLU SER ILE SER ASP SER LEU SER          
SEQRES  52 A 1024  SER LYS PRO HIS ASN PHE GLU ASP CYS ILE LYS TRP ALA          
SEQRES  53 A 1024  ARG LEU GLU PHE GLU LYS LYS PHE ASN HIS ASP ILE LYS          
SEQRES  54 A 1024  GLN LEU LEU PHE ASN PHE PRO LYS ASP ALA LYS THR SER          
SEQRES  55 A 1024  ASN GLY GLU PRO PHE TRP SER GLY ALA LYS ARG ALA PRO          
SEQRES  56 A 1024  THR PRO LEU GLU PHE ASP ILE TYR ASN ASN ASP HIS PHE          
SEQRES  57 A 1024  HIS PHE VAL VAL ALA GLY ALA SER LEU ARG ALA TYR ASN          
SEQRES  58 A 1024  TYR GLY ILE LYS SER ASP ASP SER ASN SER LYS PRO ASN          
SEQRES  59 A 1024  VAL ASP GLU TYR LYS SER VAL ILE ASP HIS MET ILE ILE          
SEQRES  60 A 1024  PRO GLU PHE THR PRO ASN ALA ASN LEU LYS ILE GLN VAL          
SEQRES  61 A 1024  ASN ASP ASP ASP PRO ASP PRO ASN ALA ASN ALA ALA ASN          
SEQRES  62 A 1024  GLY SER ASP GLU ILE ASP GLN LEU VAL SER SER LEU PRO          
SEQRES  63 A 1024  ASP PRO SER THR LEU ALA GLY PHE LYS LEU GLU PRO VAL          
SEQRES  64 A 1024  ASP PHE GLU LYS ASP ASP ASP THR ASN HIS HIS ILE GLU          
SEQRES  65 A 1024  PHE ILE THR ALA CYS SER ASN CYS ARG ALA GLN ASN TYR          
SEQRES  66 A 1024  PHE ILE GLU THR ALA ASP ARG GLN LYS THR LYS PHE ILE          
SEQRES  67 A 1024  ALA GLY ARG ILE ILE PRO ALA ILE ALA THR THR THR SER          
SEQRES  68 A 1024  LEU VAL THR GLY LEU VAL ASN LEU GLU LEU TYR LYS LEU          
SEQRES  69 A 1024  ILE ASP ASN LYS THR ASP ILE GLU GLN TYR LYS ASN GLY          
SEQRES  70 A 1024  PHE VAL ASN LEU ALA LEU PRO PHE PHE GLY PHE SER GLU          
SEQRES  71 A 1024  PRO ILE ALA SER PRO LYS GLY GLU TYR ASN ASN LYS LYS          
SEQRES  72 A 1024  TYR ASP LYS ILE TRP ASP ARG PHE ASP ILE LYS GLY ASP          
SEQRES  73 A 1024  ILE LYS LEU SER ASP LEU ILE GLU HIS PHE GLU LYS ASP          
SEQRES  74 A 1024  GLU GLY LEU GLU ILE THR MET LEU SER TYR GLY VAL SER          
SEQRES  75 A 1024  LEU LEU TYR ALA SER PHE PHE PRO PRO LYS LYS LEU LYS          
SEQRES  76 A 1024  GLU ARG LEU ASN LEU PRO ILE THR GLN LEU VAL LYS LEU          
SEQRES  77 A 1024  VAL THR LYS LYS ASP ILE PRO ALA HIS VAL SER THR MET          
SEQRES  78 A 1024  ILE LEU GLU ILE CSO ALA ASP ASP LYS GLU GLY GLU ASP          
SEQRES  79 A 1024  VAL GLU VAL PRO PHE ILE THR ILE HIS LEU                      
SEQRES   1 B   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 B   76  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 B   76  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 B   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 B   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 B   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 C 1024  MET SER SER ASN ASN SER GLY LEU SER ALA ALA GLY GLU          
SEQRES   2 C 1024  ILE ASP GLU SER LEU TYR SER ARG GLN LEU TYR VAL LEU          
SEQRES   3 C 1024  GLY LYS GLU ALA MET LEU LYS MET GLN THR SER ASN VAL          
SEQRES   4 C 1024  LEU ILE LEU GLY LEU LYS GLY LEU GLY VAL GLU ILE ALA          
SEQRES   5 C 1024  LYS ASN VAL VAL LEU ALA GLY VAL LYS SER MET THR VAL          
SEQRES   6 C 1024  PHE ASP PRO GLU PRO VAL GLN LEU ALA ASP LEU SER THR          
SEQRES   7 C 1024  GLN PHE PHE LEU THR GLU LYS ASP ILE GLY GLN LYS ARG          
SEQRES   8 C 1024  GLY ASP VAL THR ARG ALA LYS LEU ALA GLU LEU ASN ALA          
SEQRES   9 C 1024  TYR VAL PRO VAL ASN VAL LEU ASP SER LEU ASP ASP VAL          
SEQRES  10 C 1024  THR GLN LEU SER GLN PHE GLN VAL VAL VAL ALA THR ASP          
SEQRES  11 C 1024  THR VAL SER LEU GLU ASP LYS VAL LYS ILE ASN GLU PHE          
SEQRES  12 C 1024  CYS HIS SER SER GLY ILE ARG PHE ILE SER SER GLU THR          
SEQRES  13 C 1024  ARG GLY LEU PHE GLY ASN THR PHE VAL ASP LEU GLY ASP          
SEQRES  14 C 1024  GLU PHE THR VAL LEU ASP PRO THR GLY GLU GLU PRO ARG          
SEQRES  15 C 1024  THR GLY MET VAL SER ASP ILE GLU PRO ASP GLY THR VAL          
SEQRES  16 C 1024  THR MET LEU ASP ASP ASN ARG HIS GLY LEU GLU ASP GLY          
SEQRES  17 C 1024  ASN PHE VAL ARG PHE SER GLU VAL GLU GLY LEU ASP LYS          
SEQRES  18 C 1024  LEU ASN ASP GLY THR LEU PHE LYS VAL GLU VAL LEU GLY          
SEQRES  19 C 1024  PRO PHE ALA PHE ARG ILE GLY SER VAL LYS GLU TYR GLY          
SEQRES  20 C 1024  GLU TYR LYS LYS GLY GLY ILE PHE THR GLU VAL LYS VAL          
SEQRES  21 C 1024  PRO ARG LYS ILE SER PHE LYS SER LEU LYS GLN GLN LEU          
SEQRES  22 C 1024  SER ASN PRO GLU PHE VAL PHE SER ASP PHE ALA LYS PHE          
SEQRES  23 C 1024  ASP ARG ALA ALA GLN LEU HIS LEU GLY PHE GLN ALA LEU          
SEQRES  24 C 1024  HIS GLN PHE ALA VAL ARG HIS ASN GLY GLU LEU PRO ARG          
SEQRES  25 C 1024  THR MET ASN ASP GLU ASP ALA ASN GLU LEU ILE LYS LEU          
SEQRES  26 C 1024  VAL THR ASP LEU SER VAL GLN GLN PRO GLU VAL LEU GLY          
SEQRES  27 C 1024  GLU GLY VAL ASP VAL ASN GLU ASP LEU ILE LYS GLU LEU          
SEQRES  28 C 1024  SER TYR GLN ALA ARG GLY ASP ILE PRO GLY VAL VAL ALA          
SEQRES  29 C 1024  PHE PHE GLY GLY LEU VAL ALA GLN GLU VAL LEU LYS ALA          
SEQRES  30 C 1024  CYS SER GLY LYS PHE THR PRO LEU LYS GLN PHE MET TYR          
SEQRES  31 C 1024  PHE ASP SER LEU GLU SER LEU PRO ASP PRO LYS ASN PHE          
SEQRES  32 C 1024  PRO ARG ASN GLU LYS THR THR GLN PRO VAL ASN SER ARG          
SEQRES  33 C 1024  TYR ASP ASN GLN ILE ALA VAL PHE GLY LEU ASP PHE GLN          
SEQRES  34 C 1024  LYS LYS ILE ALA ASN SER LYS VAL PHE LEU VAL GLY SER          
SEQRES  35 C 1024  GLY ALA ILE GLY CYS GLU MET LEU LYS ASN TRP ALA LEU          
SEQRES  36 C 1024  LEU GLY LEU GLY SER GLY SER ASP GLY TYR ILE VAL VAL          
SEQRES  37 C 1024  THR ASP ASN ASP SER ILE GLU LYS SER ASN LEU ASN ARG          
SEQRES  38 C 1024  GLN PHE LEU PHE ARG PRO LYS ASP VAL GLY LYS ASN LYS          
SEQRES  39 C 1024  SER GLU VAL ALA ALA GLU ALA VAL CYS ALA MET ASN PRO          
SEQRES  40 C 1024  ASP LEU LYS GLY LYS ILE ASN ALA LYS ILE ASP LYS VAL          
SEQRES  41 C 1024  GLY PRO GLU THR GLU GLU ILE PHE ASN ASP SER PHE TRP          
SEQRES  42 C 1024  GLU SER LEU ASP PHE VAL THR ASN ALA LEU ASP ASN VAL          
SEQRES  43 C 1024  ASP ALA ARG THR TYR VAL ASP ARG ARG CYS VAL PHE TYR          
SEQRES  44 C 1024  ARG LYS PRO LEU LEU GLU SER GLY THR LEU GLY THR LYS          
SEQRES  45 C 1024  GLY ASN THR GLN VAL ILE ILE PRO ARG LEU THR GLU SER          
SEQRES  46 C 1024  TYR SER SER SER ARG ASP PRO PRO GLU LYS SER ILE PRO          
SEQRES  47 C 1024  LEU CYS THR LEU ARG SER PHE PRO ASN LYS ILE ASP HIS          
SEQRES  48 C 1024  THR ILE ALA TRP ALA LYS SER LEU PHE GLN GLY TYR PHE          
SEQRES  49 C 1024  THR ASP SER ALA GLU ASN VAL ASN MET TYR LEU THR GLN          
SEQRES  50 C 1024  PRO ASN PHE VAL GLU GLN THR LEU LYS GLN SER GLY ASP          
SEQRES  51 C 1024  VAL LYS GLY VAL LEU GLU SER ILE SER ASP SER LEU SER          
SEQRES  52 C 1024  SER LYS PRO HIS ASN PHE GLU ASP CYS ILE LYS TRP ALA          
SEQRES  53 C 1024  ARG LEU GLU PHE GLU LYS LYS PHE ASN HIS ASP ILE LYS          
SEQRES  54 C 1024  GLN LEU LEU PHE ASN PHE PRO LYS ASP ALA LYS THR SER          
SEQRES  55 C 1024  ASN GLY GLU PRO PHE TRP SER GLY ALA LYS ARG ALA PRO          
SEQRES  56 C 1024  THR PRO LEU GLU PHE ASP ILE TYR ASN ASN ASP HIS PHE          
SEQRES  57 C 1024  HIS PHE VAL VAL ALA GLY ALA SER LEU ARG ALA TYR ASN          
SEQRES  58 C 1024  TYR GLY ILE LYS SER ASP ASP SER ASN SER LYS PRO ASN          
SEQRES  59 C 1024  VAL ASP GLU TYR LYS SER VAL ILE ASP HIS MET ILE ILE          
SEQRES  60 C 1024  PRO GLU PHE THR PRO ASN ALA ASN LEU LYS ILE GLN VAL          
SEQRES  61 C 1024  ASN ASP ASP ASP PRO ASP PRO ASN ALA ASN ALA ALA ASN          
SEQRES  62 C 1024  GLY SER ASP GLU ILE ASP GLN LEU VAL SER SER LEU PRO          
SEQRES  63 C 1024  ASP PRO SER THR LEU ALA GLY PHE LYS LEU GLU PRO VAL          
SEQRES  64 C 1024  ASP PHE GLU LYS ASP ASP ASP THR ASN HIS HIS ILE GLU          
SEQRES  65 C 1024  PHE ILE THR ALA CYS SER ASN CYS ARG ALA GLN ASN TYR          
SEQRES  66 C 1024  PHE ILE GLU THR ALA ASP ARG GLN LYS THR LYS PHE ILE          
SEQRES  67 C 1024  ALA GLY ARG ILE ILE PRO ALA ILE ALA THR THR THR SER          
SEQRES  68 C 1024  LEU VAL THR GLY LEU VAL ASN LEU GLU LEU TYR LYS LEU          
SEQRES  69 C 1024  ILE ASP ASN LYS THR ASP ILE GLU GLN TYR LYS ASN GLY          
SEQRES  70 C 1024  PHE VAL ASN LEU ALA LEU PRO PHE PHE GLY PHE SER GLU          
SEQRES  71 C 1024  PRO ILE ALA SER PRO LYS GLY GLU TYR ASN ASN LYS LYS          
SEQRES  72 C 1024  TYR ASP LYS ILE TRP ASP ARG PHE ASP ILE LYS GLY ASP          
SEQRES  73 C 1024  ILE LYS LEU SER ASP LEU ILE GLU HIS PHE GLU LYS ASP          
SEQRES  74 C 1024  GLU GLY LEU GLU ILE THR MET LEU SER TYR GLY VAL SER          
SEQRES  75 C 1024  LEU LEU TYR ALA SER PHE PHE PRO PRO LYS LYS LEU LYS          
SEQRES  76 C 1024  GLU ARG LEU ASN LEU PRO ILE THR GLN LEU VAL LYS LEU          
SEQRES  77 C 1024  VAL THR LYS LYS ASP ILE PRO ALA HIS VAL SER THR MET          
SEQRES  78 C 1024  ILE LEU GLU ILE CSO ALA ASP ASP LYS GLU GLY GLU ASP          
SEQRES  79 C 1024  VAL GLU VAL PRO PHE ILE THR ILE HIS LEU                      
SEQRES   1 D   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 D   76  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 D   76  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 D   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 D   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 D   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 E   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 E   76  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 E   76  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 E   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 E   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 E   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
MODRES 5L6I CSO A 1006  CYS  MODIFIED RESIDUE                                   
MODRES 5L6I CSO C 1006  CYS  MODIFIED RESIDUE                                   
HET    CSO  A1006       7                                                       
HET    CSO  C1006       7                                                       
HET    SO4  A1101       5                                                       
HET     CL  A1102       1                                                       
HET     CL  A1103       1                                                       
HET     CL  A1104       1                                                       
HET     CL  A1105       1                                                       
HET     CL  A1106       1                                                       
HET     CL  A1107       1                                                       
HET     CL  A1108       1                                                       
HET    GOL  A1109       6                                                       
HET    GOL  A1110       6                                                       
HET    GOL  A1111       6                                                       
HET    GOL  A1112       6                                                       
HET    GOL  A1113       6                                                       
HET    GOL  A1114       6                                                       
HET    GOL  A1115       6                                                       
HET    GOL  A1116       6                                                       
HET    GOL  A1117       6                                                       
HET    B39  B 101      31                                                       
HET     CL  B 102       1                                                       
HET    SO4  C1101       5                                                       
HET     CL  C1102       1                                                       
HET     CL  C1103       1                                                       
HET     CL  C1104       1                                                       
HET     CL  C1105       1                                                       
HET     CL  C1106       1                                                       
HET     CL  C1107       1                                                       
HET     CL  C1108       1                                                       
HET     CL  C1109       1                                                       
HET    GOL  C1110       6                                                       
HET    GOL  C1111       6                                                       
HET    GOL  C1112       6                                                       
HET    GOL  C1113       6                                                       
HET    GOL  C1114       6                                                       
HET    GOL  C1115       6                                                       
HET    GOL  C1116       6                                                       
HET    B39  D 101      31                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     B39 [(1S,2S,4R)-4-{4-[(1S)-2,3-DIHYDRO-1H-INDEN-1-YLAMINO]-          
HETNAM   2 B39  7H-PYRROLO[2,3-D]PYRIMIDIN-7-YL}-2-                             
HETNAM   3 B39  HYDROXYCYCLOPENTYL]METHYL SULFAMATE                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  CSO    2(C3 H7 N O3 S)                                              
FORMUL   6  SO4    2(O4 S 2-)                                                   
FORMUL   7   CL    16(CL 1-)                                                    
FORMUL  14  GOL    16(C3 H8 O3)                                                 
FORMUL  23  B39    2(C21 H25 N5 O4 S)                                           
FORMUL  42  HOH   *453(H2 O)                                                    
HELIX    1 AA1 ASP A   15  GLY A   27  1                                  13    
HELIX    2 AA2 GLY A   27  GLN A   35  1                                   9    
HELIX    3 AA3 LYS A   45  GLY A   59  1                                  15    
HELIX    4 AA4 GLN A   72  THR A   78  5                                   7    
HELIX    5 AA5 THR A   83  ILE A   87  5                                   5    
HELIX    6 AA6 LYS A   90  GLU A  101  1                                  12    
HELIX    7 AA7 ASP A  116  PHE A  123  5                                   8    
HELIX    8 AA8 SER A  133  SER A  147  1                                  15    
HELIX    9 AA9 LEU A  219  ASP A  224  5                                   6    
HELIX   10 AB1 VAL A  243  GLY A  247  5                                   5    
HELIX   11 AB2 SER A  268  ASN A  275  1                                   8    
HELIX   12 AB3 ASP A  282  PHE A  286  5                                   5    
HELIX   13 AB4 ASP A  287  HIS A  306  1                                  20    
HELIX   14 AB5 ASN A  315  GLN A  333  1                                  19    
HELIX   15 AB6 ASN A  344  GLN A  354  1                                  11    
HELIX   16 AB7 ILE A  359  GLY A  380  1                                  22    
HELIX   17 AB8 LEU A  394  LEU A  397  5                                   4    
HELIX   18 AB9 TYR A  417  GLY A  425  1                                   9    
HELIX   19 AC1 GLY A  425  ASN A  434  1                                  10    
HELIX   20 AC2 GLY A  443  GLY A  457  1                                  15    
HELIX   21 AC3 GLU A  475  ARG A  481  5                                   7    
HELIX   22 AC4 ARG A  486  VAL A  490  5                                   5    
HELIX   23 AC5 ASN A  493  ASN A  506  1                                  14    
HELIX   24 AC6 PRO A  507  LYS A  510  5                                   4    
HELIX   25 AC7 GLY A  521  GLU A  525  5                                   5    
HELIX   26 AC8 ASN A  529  SER A  535  1                                   7    
HELIX   27 AC9 ASN A  545  ARG A  560  1                                  16    
HELIX   28 AD1 SER A  585  SER A  589  5                                   5    
HELIX   29 AD2 PRO A  598  SER A  604  1                                   7    
HELIX   30 AD3 LYS A  608  THR A  625  1                                  18    
HELIX   31 AD4 THR A  625  GLN A  637  1                                  13    
HELIX   32 AD5 ASN A  639  SER A  648  1                                  10    
HELIX   33 AD6 ASP A  650  SER A  664  1                                  15    
HELIX   34 AD7 ASN A  668  ASN A  685  1                                  18    
HELIX   35 AD8 ASN A  685  PHE A  695  1                                  11    
HELIX   36 AD9 ASN A  724  GLY A  743  1                                  20    
HELIX   37 AE1 ASN A  754  ASP A  763  1                                  10    
HELIX   38 AE2 GLU A  797  LEU A  805  1                                   9    
HELIX   39 AE3 ASP A  807  ALA A  812  5                                   6    
HELIX   40 AE4 HIS A  829  TYR A  845  1                                  17    
HELIX   41 AE5 ASP A  851  GLY A  860  1                                  10    
HELIX   42 AE6 ILE A  866  ASP A  886  1                                  21    
HELIX   43 AE7 ASP A  890  TYR A  894  5                                   5    
HELIX   44 AE8 LYS A  938  GLY A  951  1                                  14    
HELIX   45 AE9 PRO A  970  LEU A  978  1                                   9    
HELIX   46 AF1 PRO A  981  LYS A  991  1                                  11    
HELIX   47 AF2 THR B   22  GLY B   35  1                                  14    
HELIX   48 AF3 PRO B   37  GLN B   41  5                                   5    
HELIX   49 AF4 LEU B   56  ASN B   60  5                                   5    
HELIX   50 AF5 ASP C   15  GLY C   27  1                                  13    
HELIX   51 AF6 GLY C   27  GLN C   35  1                                   9    
HELIX   52 AF7 LYS C   45  GLY C   59  1                                  15    
HELIX   53 AF8 GLN C   72  THR C   78  5                                   7    
HELIX   54 AF9 THR C   83  ILE C   87  5                                   5    
HELIX   55 AG1 LYS C   90  GLU C  101  1                                  12    
HELIX   56 AG2 ASP C  116  PHE C  123  5                                   8    
HELIX   57 AG3 SER C  133  SER C  147  1                                  15    
HELIX   58 AG4 LEU C  219  ASP C  224  5                                   6    
HELIX   59 AG5 VAL C  243  GLY C  247  5                                   5    
HELIX   60 AG6 SER C  268  ASN C  275  1                                   8    
HELIX   61 AG7 ASP C  282  PHE C  286  5                                   5    
HELIX   62 AG8 ASP C  287  HIS C  306  1                                  20    
HELIX   63 AG9 ASN C  315  GLN C  333  1                                  19    
HELIX   64 AH1 ASN C  344  GLN C  354  1                                  11    
HELIX   65 AH2 ILE C  359  GLY C  380  1                                  22    
HELIX   66 AH3 LEU C  394  LEU C  397  5                                   4    
HELIX   67 AH4 TYR C  417  GLY C  425  1                                   9    
HELIX   68 AH5 GLY C  425  ASN C  434  1                                  10    
HELIX   69 AH6 GLY C  443  GLY C  457  1                                  15    
HELIX   70 AH7 GLU C  475  ARG C  481  5                                   7    
HELIX   71 AH8 ARG C  486  VAL C  490  5                                   5    
HELIX   72 AH9 ASN C  493  ASN C  506  1                                  14    
HELIX   73 AI1 PRO C  507  LYS C  510  5                                   4    
HELIX   74 AI2 GLY C  521  GLU C  525  5                                   5    
HELIX   75 AI3 ASN C  529  SER C  535  1                                   7    
HELIX   76 AI4 ASN C  545  ARG C  560  1                                  16    
HELIX   77 AI5 SER C  585  SER C  589  5                                   5    
HELIX   78 AI6 PRO C  598  PHE C  605  1                                   8    
HELIX   79 AI7 LYS C  608  THR C  625  1                                  18    
HELIX   80 AI8 THR C  625  GLN C  637  1                                  13    
HELIX   81 AI9 ASN C  639  SER C  648  1                                  10    
HELIX   82 AJ1 ASP C  650  SER C  664  1                                  15    
HELIX   83 AJ2 ASN C  668  ASN C  685  1                                  18    
HELIX   84 AJ3 ASN C  685  PHE C  695  1                                  11    
HELIX   85 AJ4 ASN C  724  GLY C  743  1                                  20    
HELIX   86 AJ5 ASN C  754  ASP C  763  1                                  10    
HELIX   87 AJ6 GLU C  797  LEU C  805  1                                   9    
HELIX   88 AJ7 ASP C  807  ALA C  812  5                                   6    
HELIX   89 AJ8 HIS C  829  TYR C  845  1                                  17    
HELIX   90 AJ9 ASP C  851  GLY C  860  1                                  10    
HELIX   91 AK1 ILE C  866  ASP C  886  1                                  21    
HELIX   92 AK2 ASP C  890  TYR C  894  5                                   5    
HELIX   93 AK3 LYS C  938  GLY C  951  1                                  14    
HELIX   94 AK4 PRO C  970  LEU C  978  1                                   9    
HELIX   95 AK5 PRO C  981  LYS C  991  1                                  11    
HELIX   96 AK6 THR D   22  GLY D   35  1                                  14    
HELIX   97 AK7 PRO D   37  GLN D   41  5                                   5    
HELIX   98 AK8 LEU D   56  ASN D   60  5                                   5    
HELIX   99 AK9 THR E   22  GLY E   35  1                                  14    
HELIX  100 AL1 PRO E   37  GLN E   41  5                                   5    
HELIX  101 AL2 LEU E   56  ASN E   60  5                                   5    
SHEET    1 AA1 7 VAL A 108  VAL A 110  0                                        
SHEET    2 AA1 7 SER A  62  PHE A  66  1  N  MET A  63   O  ASN A 109           
SHEET    3 AA1 7 ASN A  38  LEU A  42  1  N  ILE A  41   O  THR A  64           
SHEET    4 AA1 7 VAL A 125  ALA A 128  1  O  VAL A 127   N  LEU A  42           
SHEET    5 AA1 7 ARG A 150  ARG A 157  1  O  ARG A 150   N  VAL A 126           
SHEET    6 AA1 7 PHE A 160  ASP A 166 -1  O  PHE A 164   N  SER A 153           
SHEET    7 AA1 7 PHE A 388  ASP A 392 -1  O  MET A 389   N  THR A 163           
SHEET    1 AA2 2 PHE A 171  VAL A 173  0                                        
SHEET    2 AA2 2 ARG A 262  ILE A 264 -1  O  ILE A 264   N  PHE A 171           
SHEET    1 AA3 7 PHE A 228  LYS A 229  0                                        
SHEET    2 AA3 7 PHE A 210  SER A 214 -1  N  VAL A 211   O  PHE A 228           
SHEET    3 AA3 7 ILE A 254  VAL A 258 -1  O  THR A 256   N  ARG A 212           
SHEET    4 AA3 7 THR A 183  ILE A 189 -1  N  GLY A 184   O  PHE A 255           
SHEET    5 AA3 7 THR A 194  MET A 197 -1  O  THR A 196   N  SER A 187           
SHEET    6 AA3 7 ALA A 237  ARG A 239 -1  O  PHE A 238   N  VAL A 195           
SHEET    7 AA3 7 GLU A 231  VAL A 232 -1  N  GLU A 231   O  ARG A 239           
SHEET    1 AA4 8 ILE A 513  LYS A 516  0                                        
SHEET    2 AA4 8 TYR A 465  THR A 469  1  N  VAL A 468   O  LYS A 516           
SHEET    3 AA4 8 LYS A 436  VAL A 440  1  N  LEU A 439   O  VAL A 467           
SHEET    4 AA4 8 PHE A 538  ASN A 541  1  O  THR A 540   N  PHE A 438           
SHEET    5 AA4 8 LEU A 563  LEU A 569  1  O  LEU A 564   N  ASN A 541           
SHEET    6 AA4 8 LYS A 572  ILE A 578 -1  O  GLN A 576   N  GLU A 565           
SHEET    7 AA4 8 ASN A 896  ASN A 900 -1  O  VAL A 899   N  GLY A 573           
SHEET    8 AA4 8 PHE A 905  SER A 909 -1  O  SER A 909   N  ASN A 896           
SHEET    1 AA5 2 LYS A 916  TYR A 919  0                                        
SHEET    2 AA5 2 LYS A 922  ASP A 925 -1  O  TYR A 924   N  GLY A 917           
SHEET    1 AA6 5 ARG A 930  LYS A 934  0                                        
SHEET    2 AA6 5 PHE A1019  HIS A1023  1  O  PHE A1019   N  PHE A 931           
SHEET    3 AA6 5 THR A1000  ASP A1008 -1  N  MET A1001   O  ILE A1022           
SHEET    4 AA6 5 GLU A 953  TYR A 959 -1  N  THR A 955   O  CSO A1006           
SHEET    5 AA6 5 SER A 962  ALA A 966 -1  O  LEU A 964   N  LEU A 957           
SHEET    1 AA7 4 ARG A 930  LYS A 934  0                                        
SHEET    2 AA7 4 PHE A1019  HIS A1023  1  O  PHE A1019   N  PHE A 931           
SHEET    3 AA7 4 THR A1000  ASP A1008 -1  N  MET A1001   O  ILE A1022           
SHEET    4 AA7 4 ASP A1014  VAL A1015 -1  O  VAL A1015   N  ALA A1007           
SHEET    1 AA8 5 THR B  12  GLU B  16  0                                        
SHEET    2 AA8 5 GLN B   2  THR B   7 -1  N  VAL B   5   O  ILE B  13           
SHEET    3 AA8 5 THR B  66  VAL B  70  1  O  LEU B  67   N  PHE B   4           
SHEET    4 AA8 5 ARG B  42  PHE B  45 -1  N  ILE B  44   O  HIS B  68           
SHEET    5 AA8 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
SHEET    1 AA9 7 VAL C 108  VAL C 110  0                                        
SHEET    2 AA9 7 SER C  62  PHE C  66  1  N  MET C  63   O  ASN C 109           
SHEET    3 AA9 7 ASN C  38  LEU C  42  1  N  ILE C  41   O  THR C  64           
SHEET    4 AA9 7 VAL C 125  ALA C 128  1  O  VAL C 127   N  LEU C  40           
SHEET    5 AA9 7 ARG C 150  ARG C 157  1  O  ARG C 150   N  VAL C 126           
SHEET    6 AA9 7 PHE C 160  ASP C 166 -1  O  PHE C 164   N  SER C 153           
SHEET    7 AA9 7 PHE C 388  ASP C 392 -1  O  MET C 389   N  THR C 163           
SHEET    1 AB1 2 PHE C 171  VAL C 173  0                                        
SHEET    2 AB1 2 ARG C 262  ILE C 264 -1  O  ILE C 264   N  PHE C 171           
SHEET    1 AB2 7 PHE C 228  LYS C 229  0                                        
SHEET    2 AB2 7 PHE C 210  SER C 214 -1  N  VAL C 211   O  PHE C 228           
SHEET    3 AB2 7 ILE C 254  VAL C 258 -1  O  ILE C 254   N  SER C 214           
SHEET    4 AB2 7 THR C 183  ILE C 189 -1  N  GLY C 184   O  PHE C 255           
SHEET    5 AB2 7 THR C 194  MET C 197 -1  O  THR C 196   N  SER C 187           
SHEET    6 AB2 7 ALA C 237  ARG C 239 -1  O  PHE C 238   N  VAL C 195           
SHEET    7 AB2 7 GLU C 231  VAL C 232 -1  N  GLU C 231   O  ARG C 239           
SHEET    1 AB3 8 ILE C 513  LYS C 516  0                                        
SHEET    2 AB3 8 TYR C 465  THR C 469  1  N  VAL C 468   O  LYS C 516           
SHEET    3 AB3 8 LYS C 436  VAL C 440  1  N  LEU C 439   O  VAL C 467           
SHEET    4 AB3 8 PHE C 538  ASN C 541  1  O  THR C 540   N  PHE C 438           
SHEET    5 AB3 8 LEU C 563  LEU C 569  1  O  LEU C 564   N  ASN C 541           
SHEET    6 AB3 8 LYS C 572  ILE C 578 -1  O  GLN C 576   N  GLU C 565           
SHEET    7 AB3 8 ASN C 896  ASN C 900 -1  O  VAL C 899   N  GLY C 573           
SHEET    8 AB3 8 PHE C 905  SER C 909 -1  O  SER C 909   N  ASN C 896           
SHEET    1 AB4 2 LYS C 916  TYR C 919  0                                        
SHEET    2 AB4 2 LYS C 922  ASP C 925 -1  O  TYR C 924   N  GLY C 917           
SHEET    1 AB5 5 ARG C 930  LYS C 934  0                                        
SHEET    2 AB5 5 PHE C1019  HIS C1023  1  O  PHE C1019   N  PHE C 931           
SHEET    3 AB5 5 THR C1000  ASP C1008 -1  N  MET C1001   O  ILE C1022           
SHEET    4 AB5 5 GLU C 953  TYR C 959 -1  N  THR C 955   O  CSO C1006           
SHEET    5 AB5 5 SER C 962  ALA C 966 -1  O  TYR C 965   N  LEU C 957           
SHEET    1 AB6 4 ARG C 930  LYS C 934  0                                        
SHEET    2 AB6 4 PHE C1019  HIS C1023  1  O  PHE C1019   N  PHE C 931           
SHEET    3 AB6 4 THR C1000  ASP C1008 -1  N  MET C1001   O  ILE C1022           
SHEET    4 AB6 4 ASP C1014  VAL C1015 -1  O  VAL C1015   N  ALA C1007           
SHEET    1 AB7 5 THR D  12  GLU D  16  0                                        
SHEET    2 AB7 5 GLN D   2  THR D   7 -1  N  VAL D   5   O  ILE D  13           
SHEET    3 AB7 5 THR D  66  VAL D  70  1  O  LEU D  67   N  PHE D   4           
SHEET    4 AB7 5 ARG D  42  PHE D  45 -1  N  ILE D  44   O  HIS D  68           
SHEET    5 AB7 5 LYS D  48  GLN D  49 -1  O  LYS D  48   N  PHE D  45           
SHEET    1 AB8 5 THR E  12  GLU E  16  0                                        
SHEET    2 AB8 5 GLN E   2  THR E   7 -1  N  VAL E   5   O  ILE E  13           
SHEET    3 AB8 5 THR E  66  VAL E  70  1  O  LEU E  67   N  PHE E   4           
SHEET    4 AB8 5 ARG E  42  PHE E  45 -1  N  ILE E  44   O  HIS E  68           
SHEET    5 AB8 5 LYS E  48  GLN E  49 -1  O  LYS E  48   N  PHE E  45           
LINK         C   ILE A1005                 N   CSO A1006     1555   1555  1.32  
LINK         C   CSO A1006                 N   ALA A1007     1555   1555  1.33  
LINK         C   GLY B  76                 N31 B39 B 101     1555   1555  1.29  
LINK         C   ILE C1005                 N   CSO C1006     1555   1555  1.32  
LINK         C   CSO C1006                 N   ALA C1007     1555   1555  1.32  
LINK         C   GLY D  76                 N31 B39 D 101     1555   1555  1.28  
CISPEP   1 LYS A  386    GLN A  387          0        -1.34                     
CISPEP   2 LEU A  903    PRO A  904          0       -11.96                     
CISPEP   3 LYS C  386    GLN C  387          0        -1.32                     
CISPEP   4 LEU C  903    PRO C  904          0       -13.11                     
SITE     1 AC1  8 ARG A  21  ASN A 478  ARG A 481  HOH A1216                    
SITE     2 AC1  8 HOH A1225  HOH A1252  HOH A1277  B39 B 101                    
SITE     1 AC2  1 ARG A  96                                                     
SITE     1 AC3  1 HOH A1377                                                     
SITE     1 AC4  9 ASP A 282  LYS A 285  PHE A 391  ASP A 392                    
SITE     2 AC4  9 SER A 393  GLU A 395  LYS A 895  HOH A1229                    
SITE     3 AC4  9 HOH A1288                                                     
SITE     1 AC5  4 TYR A 740  ASN A 828  HIS A 830  HOH A1358                    
SITE     1 AC6  7 SER A 153  GLU A 155  ASN A 162  HIS A 293                    
SITE     2 AC6  7 PHE A 296  TYR A 390  HOH A1213                               
SITE     1 AC7  2 ASN A 344  HOH A1357                                          
SITE     1 AC8  3 LEU A 134  GLU A 135  HOH A1204                               
SITE     1 AC9  4 LEU A 114  VAL A 117  ASP A 136  LYS A 139                    
SITE     1 AD1  3 THR A 172  CYS A 378  SER A 379                               
SITE     1 AD2  2 ASP A 851  ARG A 852                                          
SITE     1 AD3  3 ARG A 554  VAL A 557  GLU A1004                               
SITE     1 AD4 18 GLY A 441  GLY A 443  ALA A 444  ASP A 470                    
SITE     2 AD4 18 ASN A 471  ASP A 472  ARG A 481  GLN A 482                    
SITE     3 AD4 18 LYS A 494  LYS A 519  VAL A 520  ALA A 542                    
SITE     4 AD4 18 ASP A 544  ALA A 548  TYR A 551  SO4 A1101                    
SITE     5 AD4 18 HOH A1252  GLY B  76                                          
SITE     1 AD5  2 HOH A1375  ARG B  74                                          
SITE     1 AD6  6 ARG C  21  ASN C 478  ARG C 481  HOH C1205                    
SITE     2 AD6  6 HOH C1252  B39 D 101                                          
SITE     1 AD7  2 ARG C 861  ARG D  74                                          
SITE     1 AD8  3 ARG C 202  ARG E  42  ARG E  72                               
SITE     1 AD9  3 ARG C 288  GOL C1114  HOH C1384                               
SITE     1 AE1  8 ASP C 282  LYS C 285  ASP C 392  SER C 393                    
SITE     2 AE1  8 GLU C 395  HOH C1238  HOH C1243  HOH C1285                    
SITE     1 AE2  3 ASP C 851  ARG C 852  GLN C 853                               
SITE     1 AE3  6 SER C 153  GLU C 155  ASN C 162  PHE C 296                    
SITE     2 AE3  6 GLN C 297  HIS C 300                                          
SITE     1 AE4  1 GLU C 180                                                     
SITE     1 AE5  4 ARG C 288  ASN C 344  ASP C 346   CL C1106                    
SITE     1 AE6  5 LYS C  33  ARG C 150  THR C 172  SER C 379                    
SITE     2 AE6  5 GLY C 380                                                     
SITE     1 AE7  2 ASN C 828  HIS C 830                                          
SITE     1 AE8 20 GLY C 441  GLY C 443  ALA C 444  ILE C 445                    
SITE     2 AE8 20 ASP C 470  ASN C 471  ASP C 472  ARG C 481                    
SITE     3 AE8 20 GLN C 482  LYS C 494  LYS C 519  VAL C 520                    
SITE     4 AE8 20 ALA C 542  LEU C 543  ASP C 544  ALA C 548                    
SITE     5 AE8 20 SO4 C1101  HOH C1289  GLY D  75  HOH D 202                    
SITE     1 AE9 15 LEU C  73  ALA C  74  ASP C  75  SER C  77                    
SITE     2 AE9 15 THR C  78  LEU C  82  ARG C 416  PRO C 598                    
SITE     3 AE9 15 LEU C 599  THR C 601  LEU C 602  ARG C 603                    
SITE     4 AE9 15 SER C 604  PHE C 605  VAL C 780                               
CRYST1   72.500  191.890  230.197  90.00  90.00  90.00 P 2 21 21    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      0.013793  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005211  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004344        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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