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Database: PDB
Entry: 6O83
LinkDB: 6O83
Original site: 6O83 
HEADER    LIGASE/PROTEIN BINDING                  08-MAR-19   6O83              
TITLE     S. POMBE UBIQUITIN E1~UBIQUITIN-AMP TETRAHEDRAL INTERMEDIATE MIMIC    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-ACTIVATING ENZYME E1 1;                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 13-1012;                                          
COMPND   5 SYNONYM: POLY(A)+ RNA TRANSPORT PROTEIN 3;                           
COMPND   6 EC: 6.2.1.45;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: UBIQUITIN-60S RIBOSOMAL PROTEIN L40;                       
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: RESIDUES 1-75;                                             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE (STRAIN 972 / ATCC    
SOURCE   3 24843);                                                              
SOURCE   4 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 284812;                                              
SOURCE   6 STRAIN: 972 / ATCC 24843;                                            
SOURCE   7 ATCC: 24843;                                                         
SOURCE   8 GENE: PTR3, SPBC1604.21C, SPBC211.09;                                
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PSMT3;                                    
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE (STRAIN 972 / ATCC    
SOURCE  15 24843);                                                              
SOURCE  16 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE  17 ORGANISM_TAXID: 284812;                                              
SOURCE  18 STRAIN: 972 / ATCC 24843;                                            
SOURCE  19 ATCC: 24843;                                                         
SOURCE  20 GENE: UEP1, UBI2, SPAC1805.12C;                                      
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PTXB1                                     
KEYWDS    THIOESTER, ADENYLATION, INHIBITOR, TETRAHEDRAL INTERMEDIATE, LIGASE,  
KEYWDS   2 NUCLEUS, PHOSPHOPROTEIN, UBL CONJUGATION PATHWAY, ATP-BINDING,       
KEYWDS   3 NUCLEOTIDE-BINDING, ISOPEPTIDE BOND, LIGASE-PROTEIN BINDING COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.S.HANN,C.D.LIMA                                                     
REVDAT   4   20-NOV-19 6O83    1       REMARK                                   
REVDAT   3   14-AUG-19 6O83    1       JRNL                                     
REVDAT   2   10-JUL-19 6O83    1       JRNL                                     
REVDAT   1   19-JUN-19 6O83    0                                                
JRNL        AUTH   Z.S.HANN,C.JI,S.K.OLSEN,X.LU,M.C.LUX,D.S.TAN,C.D.LIMA        
JRNL        TITL   STRUCTURAL BASIS FOR ADENYLATION AND THIOESTER BOND          
JRNL        TITL 2 FORMATION IN THE UBIQUITIN E1.                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 15475 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31235585                                                     
JRNL        DOI    10.1073/PNAS.1905488116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3211                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 113.49                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 53583                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2646                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1113.5665 -  8.4128    0.98     2933   163  0.1753 0.2172        
REMARK   3     2  8.4128 -  6.6777    0.99     2808   164  0.1837 0.2335        
REMARK   3     3  6.6777 -  5.8337    0.97     2745   147  0.1934 0.2600        
REMARK   3     4  5.8337 -  5.3003    0.98     2794   128  0.1830 0.2596        
REMARK   3     5  5.3003 -  4.9204    0.98     2754   145  0.1657 0.2488        
REMARK   3     6  4.9204 -  4.6303    0.99     2759   150  0.1597 0.1932        
REMARK   3     7  4.6303 -  4.3984    0.98     2723   144  0.1526 0.1984        
REMARK   3     8  4.3984 -  4.2069    0.98     2744   140  0.1637 0.2159        
REMARK   3     9  4.2069 -  4.0450    0.95     2644   122  0.1764 0.2258        
REMARK   3    10  4.0450 -  3.9054    0.96     2722   118  0.1973 0.2430        
REMARK   3    11  3.9054 -  3.7832    0.96     2673   128  0.2233 0.2737        
REMARK   3    12  3.7832 -  3.6751    0.96     2659   132  0.2409 0.2605        
REMARK   3    13  3.6751 -  3.5783    0.96     2630   126  0.2408 0.2808        
REMARK   3    14  3.5783 -  3.4910    0.95     2620   148  0.2489 0.2963        
REMARK   3    15  3.4910 -  3.4117    0.95     2574   158  0.2746 0.3152        
REMARK   3    16  3.4117 -  3.3391    0.95     2624   136  0.2803 0.3449        
REMARK   3    17  3.3391 -  3.2723    0.94     2600   123  0.2953 0.3389        
REMARK   3    18  3.2723 -  3.2105    0.94     2590   132  0.3178 0.3491        
REMARK   3    19  3.2105 -  3.1532    0.86     2341   142  0.3434 0.3820        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 89.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 38 THROUGH 538 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -24.3857   2.0593 -26.4859              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3648 T22:   0.4774                                     
REMARK   3      T33:   0.5373 T12:   0.0472                                     
REMARK   3      T13:   0.0440 T23:   0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4803 L22:   1.5623                                     
REMARK   3      L33:   0.6432 L12:  -0.6277                                     
REMARK   3      L13:  -0.4120 L23:   0.1404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1079 S12:  -0.1357 S13:  -0.0705                       
REMARK   3      S21:   0.2301 S22:   0.0824 S23:   0.1279                       
REMARK   3      S31:   0.3032 S32:   0.2338 S33:   0.0358                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 539 THROUGH 898 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.8857  -2.7719 -52.7587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6309 T22:   0.7794                                     
REMARK   3      T33:   0.6721 T12:  -0.0616                                     
REMARK   3      T13:  -0.0740 T23:   0.0675                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4273 L22:   1.9048                                     
REMARK   3      L33:   3.2734 L12:   0.1380                                     
REMARK   3      L13:   0.8625 L23:   1.3117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1031 S12:   0.0583 S13:  -0.0732                       
REMARK   3      S21:  -0.2828 S22:   0.0701 S23:   0.2207                       
REMARK   3      S31:   0.6276 S32:   0.1117 S33:  -0.1757                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 899 THROUGH 1012 )                
REMARK   3    ORIGIN FOR THE GROUP (A): -21.2738  43.2481 -51.2273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5403 T22:   0.4555                                     
REMARK   3      T33:   0.5633 T12:   0.0265                                     
REMARK   3      T13:   0.0256 T23:  -0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1114 L22:   6.7014                                     
REMARK   3      L33:   4.4381 L12:  -0.4328                                     
REMARK   3      L13:  -0.4650 L23:  -3.9228                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1733 S12:   0.5982 S13:  -0.0031                       
REMARK   3      S21:  -0.7829 S22:  -0.0744 S23:  -0.4033                       
REMARK   3      S31:   0.0993 S32:   0.3097 S33:  -0.0927                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 75 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8361  15.9616 -32.9859              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2651 T22:   0.9819                                     
REMARK   3      T33:   0.7170 T12:  -0.0071                                     
REMARK   3      T13:  -0.0297 T23:  -0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3328 L22:   0.6884                                     
REMARK   3      L33:   0.4967 L12:  -1.2669                                     
REMARK   3      L13:  -0.1051 L23:   0.0522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1544 S12:   0.2986 S13:   0.7115                       
REMARK   3      S21:   0.0956 S22:   0.4186 S23:  -0.6303                       
REMARK   3      S31:  -0.3319 S32:   0.9834 S33:   0.0788                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 37 THROUGH 304 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -83.7670  14.0308  -7.4365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3911 T22:   0.5864                                     
REMARK   3      T33:   0.7116 T12:   0.0895                                     
REMARK   3      T13:  -0.0139 T23:  -0.1880                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8629 L22:   2.5338                                     
REMARK   3      L33:   1.4029 L12:   0.5178                                     
REMARK   3      L13:  -0.3155 L23:   0.2313                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1693 S12:   0.0177 S13:   0.3008                       
REMARK   3      S21:   0.1529 S22:  -0.2963 S23:   0.2770                       
REMARK   3      S31:  -0.2552 S32:  -0.0639 S33:   0.1498                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 305 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -84.2429  -9.8539  -9.1231              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3233 T22:   0.5919                                     
REMARK   3      T33:   0.5432 T12:  -0.0492                                     
REMARK   3      T13:   0.0073 T23:  -0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6788 L22:   3.8460                                     
REMARK   3      L33:   3.1129 L12:   0.0121                                     
REMARK   3      L13:   0.8085 L23:  -0.4703                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2030 S12:  -0.1050 S13:  -0.0984                       
REMARK   3      S21:   0.2105 S22:  -0.3490 S23:   0.2580                       
REMARK   3      S31:   0.1964 S32:  -0.0775 S33:   0.1193                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 563 THROUGH 637 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -89.5447   2.4044  10.7442              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6880 T22:   1.3152                                     
REMARK   3      T33:   0.5911 T12:  -0.0853                                     
REMARK   3      T13:  -0.0012 T23:   0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0480 L22:   1.2236                                     
REMARK   3      L33:   2.7756 L12:  -0.1243                                     
REMARK   3      L13:   0.3322 L23:   0.1692                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0806 S12:   0.0996 S13:  -0.3159                       
REMARK   3      S21:   0.2731 S22:   0.0318 S23:   0.2227                       
REMARK   3      S31:  -0.1719 S32:  -0.9064 S33:  -0.1047                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 638 THROUGH 753 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):-102.3330   3.5100  27.4310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5402 T22:   1.2606                                     
REMARK   3      T33:   0.6888 T12:  -0.0538                                     
REMARK   3      T13:   0.1189 T23:   0.1138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8406 L22:   4.1047                                     
REMARK   3      L33:   3.3378 L12:  -1.3061                                     
REMARK   3      L13:  -0.2877 L23:   0.4992                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3858 S12:  -0.1117 S13:  -0.2827                       
REMARK   3      S21:   0.4119 S22:   0.2902 S23:   0.6334                       
REMARK   3      S31:   0.4102 S32:  -1.1166 S33:   0.1349                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 754 THROUGH 898 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -90.9035   4.0038  11.5038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2780 T22:   0.7418                                     
REMARK   3      T33:   0.5896 T12:  -0.0751                                     
REMARK   3      T13:   0.0467 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0668 L22:   0.9757                                     
REMARK   3      L33:   1.6832 L12:  -0.1679                                     
REMARK   3      L13:  -0.1210 L23:  -0.2204                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0112 S12:  -0.0839 S13:  -0.0019                       
REMARK   3      S21:   0.1011 S22:   0.1318 S23:   0.0742                       
REMARK   3      S31:  -0.0798 S32:   0.1659 S33:  -0.0268                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 899 THROUGH 1012 )                
REMARK   3    ORIGIN FOR THE GROUP (A): -57.3748 -29.7691  14.0840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7333 T22:   0.9914                                     
REMARK   3      T33:   0.9991 T12:   0.0597                                     
REMARK   3      T13:  -0.2245 T23:   0.2456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6623 L22:   4.1135                                     
REMARK   3      L33:   3.0259 L12:  -2.3477                                     
REMARK   3      L13:   2.2237 L23:  -2.9051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0236 S12:   0.2550 S13:  -0.0036                       
REMARK   3      S21:   0.3752 S22:  -0.1522 S23:  -0.6313                       
REMARK   3      S31:   0.1651 S32:   0.4954 S33:   0.0350                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 75 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -58.5162   5.2633  -1.1012              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3825 T22:   0.8821                                     
REMARK   3      T33:   0.8930 T12:  -0.2887                                     
REMARK   3      T13:  -0.0960 T23:   0.0839                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3834 L22:   1.4447                                     
REMARK   3      L33:   0.4897 L12:   1.3594                                     
REMARK   3      L13:   0.5692 L23:   0.4007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3592 S12:  -0.7602 S13:   0.2425                       
REMARK   3      S21:   0.5855 S22:  -0.4236 S23:  -0.5105                       
REMARK   3      S31:  -0.0275 S32:   0.1866 S33:  -0.1568                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6O83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000239327.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97920                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53605                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 113.500                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4II3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27.3% MPD, 6.6% PEG 8000, 100 MM BIS     
REMARK 280  -TRIS PROPANE PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       61.28750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.38800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.26100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       86.38800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       61.28750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.26100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 5200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     SER A    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     ILE A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     TYR A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     ARG A    22                                                      
REMARK 465     GLN A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     TYR A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     HIS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     MET A    32                                                      
REMARK 465     LYS A    33                                                      
REMARK 465     GLN A    34                                                      
REMARK 465     MET A    35                                                      
REMARK 465     SER A    36                                                      
REMARK 465     GLN A    37                                                      
REMARK 465     LYS A   762                                                      
REMARK 465     SER A   763                                                      
REMARK 465     GLY A   764                                                      
REMARK 465     ILE A   765                                                      
REMARK 465     LYS A   766                                                      
REMARK 465     ILE A   767                                                      
REMARK 465     GLN A   768                                                      
REMARK 465     VAL A   769                                                      
REMARK 465     ASN A   770                                                      
REMARK 465     GLU A   771                                                      
REMARK 465     ASN A   772                                                      
REMARK 465     GLU A   773                                                      
REMARK 465     GLU A   774                                                      
REMARK 465     ALA A   775                                                      
REMARK 465     PRO A   776                                                      
REMARK 465     GLU A   777                                                      
REMARK 465     THR A   778                                                      
REMARK 465     ALA A   779                                                      
REMARK 465     ALA A   780                                                      
REMARK 465     ASN A   781                                                      
REMARK 465     LYS A   782                                                      
REMARK 465     SER C    12                                                      
REMARK 465     ASN C    13                                                      
REMARK 465     THR C    14                                                      
REMARK 465     ILE C    15                                                      
REMARK 465     ASP C    16                                                      
REMARK 465     GLU C    17                                                      
REMARK 465     GLY C    18                                                      
REMARK 465     LEU C    19                                                      
REMARK 465     TYR C    20                                                      
REMARK 465     SER C    21                                                      
REMARK 465     ARG C    22                                                      
REMARK 465     GLN C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     TYR C    25                                                      
REMARK 465     VAL C    26                                                      
REMARK 465     LEU C    27                                                      
REMARK 465     GLY C    28                                                      
REMARK 465     HIS C    29                                                      
REMARK 465     GLU C    30                                                      
REMARK 465     ALA C    31                                                      
REMARK 465     MET C    32                                                      
REMARK 465     LYS C    33                                                      
REMARK 465     GLN C    34                                                      
REMARK 465     MET C    35                                                      
REMARK 465     SER C    36                                                      
REMARK 465     LYS C   762                                                      
REMARK 465     SER C   763                                                      
REMARK 465     GLY C   764                                                      
REMARK 465     ILE C   765                                                      
REMARK 465     LYS C   766                                                      
REMARK 465     ILE C   767                                                      
REMARK 465     GLN C   768                                                      
REMARK 465     VAL C   769                                                      
REMARK 465     ASN C   770                                                      
REMARK 465     GLU C   771                                                      
REMARK 465     ASN C   772                                                      
REMARK 465     GLU C   773                                                      
REMARK 465     GLU C   774                                                      
REMARK 465     ALA C   775                                                      
REMARK 465     PRO C   776                                                      
REMARK 465     GLU C   777                                                      
REMARK 465     THR C   778                                                      
REMARK 465     ALA C   779                                                      
REMARK 465     ALA C   780                                                      
REMARK 465     ASN C   781                                                      
REMARK 465     LYS C   782                                                      
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   OH   TYR C   106     OE1  GLN C   619              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A   250     OD2  ASP C   840     2454     1.98            
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    ASP A  68       81.65   -161.80                                   
REMARK 500    HIS A 147       74.76     50.80                                   
REMARK 500    GLU A 198     -107.13     57.32                                   
REMARK 500    ASN A 251       71.71     39.74                                   
REMARK 500    LYS A 284       60.96   -115.96                                   
REMARK 500    HIS A 305       47.78   -142.10                                   
REMARK 500    PHE A 377      144.13     76.42                                   
REMARK 500    SER A 388       50.59   -119.54                                   
REMARK 500    ILE A 398       78.65   -110.47                                   
REMARK 500    HIS A 458      145.50   -171.01                                   
REMARK 500    ASP A 463      118.21   -174.55                                   
REMARK 500    SER A 470      109.25   -172.22                                   
REMARK 500    LEU A 562       90.67   -170.74                                   
REMARK 500    LEU A 575      -63.68   -131.27                                   
REMARK 500    LYS A 618      -68.05   -143.91                                   
REMARK 500    ASN A 632       55.99   -105.69                                   
REMARK 500    ASN A 643       73.63   -152.50                                   
REMARK 500    VAL A 656      -60.36   -140.99                                   
REMARK 500    ASN A 679      -67.60   -128.75                                   
REMARK 500    THR A 695     -169.91   -104.42                                   
REMARK 500    ARG A 707     -168.89    -66.36                                   
REMARK 500    SER A 799       38.46    -81.26                                   
REMARK 500    THR A 806      108.64    -59.25                                   
REMARK 500    ASP A 997     -157.55    -74.19                                   
REMARK 500    PRO A1006     -170.37    -66.98                                   
REMARK 500    ASP C  68       82.06   -157.71                                   
REMARK 500    LEU C  77        4.22    -69.91                                   
REMARK 500    SER C  79       -2.06   -147.28                                   
REMARK 500    SER C 187      148.53   -173.52                                   
REMARK 500    TYR C 235       -4.51   -141.32                                   
REMARK 500    PHE C 237      144.00   -172.32                                   
REMARK 500    LYS C 284       50.91   -116.21                                   
REMARK 500    HIS C 305       46.51   -140.50                                   
REMARK 500    PHE C 377      147.86     66.86                                   
REMARK 500    ILE C 398       79.25   -115.46                                   
REMARK 500    SER C 427       59.46   -101.96                                   
REMARK 500    ASP C 463      105.48   -172.95                                   
REMARK 500    LEU C 472       42.39   -157.12                                   
REMARK 500    ASN C 473      114.04   -164.37                                   
REMARK 500    GLU C 553       61.49     61.95                                   
REMARK 500    LEU C 562       93.39   -172.62                                   
REMARK 500    LEU C 575      -59.74   -144.50                                   
REMARK 500    THR C 594      140.89   -172.71                                   
REMARK 500    LYS C 618      -52.40   -134.68                                   
REMARK 500    ASN C 632       44.88    -88.78                                   
REMARK 500    VAL C 656      -68.60   -139.41                                   
REMARK 500    GLU C 658       49.91   -103.95                                   
REMARK 500    ASN C 679      -66.08   -127.85                                   
REMARK 500    VAL C 694     -168.17   -111.57                                   
REMARK 500    SER C 793       33.88    -83.88                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 320   OE1                                                    
REMARK 620 2 GLU A 320   OE2  54.0                                              
REMARK 620 3 ASP A 715   OD1  78.1 119.8                                        
REMARK 620 4 ASP A 715   OD2  79.3 120.3   1.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 320   OE1                                                    
REMARK 620 2 GLU C 320   OE2  57.5                                              
REMARK 620 3 ASP C 715   OD1  78.1 105.0                                        
REMARK 620 4 ASP C 715   OD2  76.7 103.9   1.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VMX A 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS C 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 1108                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4II3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6O82   RELATED DB: PDB                                   
DBREF  6O83 A   13  1012  UNP    O94609   UBA1_SCHPO      13   1012             
DBREF  6O83 B    1    75  UNP    P0CH07   RL402_SCHPO      1     75             
DBREF  6O83 C   13  1012  UNP    O94609   UBA1_SCHPO      13   1012             
DBREF  6O83 D    1    75  UNP    P0CH07   RL402_SCHPO      1     75             
SEQADV 6O83 SER A   12  UNP  O94609              EXPRESSION TAG                 
SEQADV 6O83 SER C   12  UNP  O94609              EXPRESSION TAG                 
SEQRES   1 A 1001  SER ASN THR ILE ASP GLU GLY LEU TYR SER ARG GLN LEU          
SEQRES   2 A 1001  TYR VAL LEU GLY HIS GLU ALA MET LYS GLN MET SER GLN          
SEQRES   3 A 1001  SER ASN VAL LEU ILE ILE GLY CYS LYS GLY LEU GLY VAL          
SEQRES   4 A 1001  GLU ILE ALA LYS ASN VAL CYS LEU ALA GLY VAL LYS SER          
SEQRES   5 A 1001  VAL THR LEU TYR ASP PRO GLN PRO THR ARG ILE GLU ASP          
SEQRES   6 A 1001  LEU SER SER GLN TYR PHE LEU THR GLU ASP ASP ILE GLY          
SEQRES   7 A 1001  VAL PRO ARG ALA LYS VAL THR VAL SER LYS LEU ALA GLU          
SEQRES   8 A 1001  LEU ASN GLN TYR VAL PRO VAL SER VAL VAL ASP GLU LEU          
SEQRES   9 A 1001  SER THR GLU TYR LEU LYS ASN PHE LYS CYS VAL VAL VAL          
SEQRES  10 A 1001  THR GLU THR SER LEU THR LYS GLN LEU GLU ILE ASN ASP          
SEQRES  11 A 1001  PHE THR HIS LYS ASN HIS ILE ALA TYR ILE ALA ALA ASP          
SEQRES  12 A 1001  SER ARG GLY LEU PHE GLY SER ILE PHE CYS ASP PHE GLY          
SEQRES  13 A 1001  GLU ASN PHE ILE CYS THR ASP THR ASP GLY ASN GLU PRO          
SEQRES  14 A 1001  LEU THR GLY MET ILE ALA SER ILE THR ASP ASP GLY VAL          
SEQRES  15 A 1001  VAL THR MET LEU GLU GLU THR ARG HIS GLY LEU GLU ASN          
SEQRES  16 A 1001  GLY ASP PHE VAL LYS PHE THR GLU VAL LYS GLY MET PRO          
SEQRES  17 A 1001  GLY LEU ASN ASP GLY THR PRO ARG LYS VAL GLU VAL LYS          
SEQRES  18 A 1001  GLY PRO TYR THR PHE SER ILE GLY SER VAL LYS ASP LEU          
SEQRES  19 A 1001  GLY SER ALA GLY TYR ASN GLY VAL PHE THR GLN VAL LYS          
SEQRES  20 A 1001  VAL PRO THR LYS ILE SER PHE LYS SER LEU ARG GLU SER          
SEQRES  21 A 1001  LEU LYS ASP PRO GLU TYR VAL TYR PRO ASP PHE GLY LYS          
SEQRES  22 A 1001  MET MET ARG PRO PRO GLN TYR HIS ILE ALA PHE GLN ALA          
SEQRES  23 A 1001  LEU SER ALA PHE ALA ASP ALA HIS GLU GLY SER LEU PRO          
SEQRES  24 A 1001  ARG PRO ARG ASN ASP ILE ASP ALA ALA GLU PHE PHE GLU          
SEQRES  25 A 1001  PHE CYS LYS LYS ILE ALA SER THR LEU GLN PHE ASP VAL          
SEQRES  26 A 1001  GLU LEU ASP GLU LYS LEU ILE LYS GLU ILE SER TYR GLN          
SEQRES  27 A 1001  ALA ARG GLY ASP LEU VAL ALA MET SER ALA PHE LEU GLY          
SEQRES  28 A 1001  GLY ALA VAL ALA GLN GLU VAL LEU LYS ALA THR THR SER          
SEQRES  29 A 1001  LYS PHE TYR PRO LEU LYS GLN TYR PHE TYR PHE ASP SER          
SEQRES  30 A 1001  LEU GLU SER LEU PRO SER SER VAL THR ILE SER GLU GLU          
SEQRES  31 A 1001  THR CYS LYS PRO ARG GLY CYS ARG TYR ASP GLY GLN ILE          
SEQRES  32 A 1001  ALA VAL PHE GLY SER GLU PHE GLN GLU LYS ILE ALA SER          
SEQRES  33 A 1001  LEU SER THR PHE LEU VAL GLY ALA GLY ALA ILE GLY CYS          
SEQRES  34 A 1001  GLU MET LEU LYS ASN TRP ALA MET MET GLY VAL ALA THR          
SEQRES  35 A 1001  GLY GLU SER GLY HIS ILE SER VAL THR ASP MET ASP SER          
SEQRES  36 A 1001  ILE GLU LYS SER ASN LEU ASN ARG GLN PHE LEU PHE ARG          
SEQRES  37 A 1001  PRO ARG ASP VAL GLY LYS LEU LYS SER GLU CYS ALA SER          
SEQRES  38 A 1001  THR ALA VAL SER ILE MET ASN PRO SER LEU THR GLY LYS          
SEQRES  39 A 1001  ILE THR SER TYR GLN GLU ARG VAL GLY PRO GLU SER GLU          
SEQRES  40 A 1001  GLY ILE PHE GLY ASP GLU PHE PHE GLU LYS LEU SER LEU          
SEQRES  41 A 1001  VAL THR ASN ALA LEU ASP ASN VAL GLU ALA ARG MET TYR          
SEQRES  42 A 1001  VAL ASP ARG ARG CYS VAL PHE PHE GLU LYS PRO LEU LEU          
SEQRES  43 A 1001  GLU SER GLY THR LEU GLY THR LYS GLY ASN THR GLN VAL          
SEQRES  44 A 1001  VAL VAL PRO HIS LEU THR GLU SER TYR GLY SER SER GLN          
SEQRES  45 A 1001  ASP PRO PRO GLU LYS SER PHE PRO ILE CYS THR LEU LYS          
SEQRES  46 A 1001  ASN PHE PRO ASN ARG ILE GLU HIS THR ILE ALA TRP ALA          
SEQRES  47 A 1001  ARG ASP LEU PHE GLU GLY LEU PHE LYS GLN PRO ILE ASP          
SEQRES  48 A 1001  ASN VAL ASN MET TYR LEU SER SER PRO ASN PHE LEU GLU          
SEQRES  49 A 1001  THR SER LEU LYS THR SER SER ASN PRO ARG GLU VAL LEU          
SEQRES  50 A 1001  GLU ASN ILE ARG ASP TYR LEU VAL THR GLU LYS PRO LEU          
SEQRES  51 A 1001  SER PHE GLU GLU CYS ILE MET TRP ALA ARG LEU GLN PHE          
SEQRES  52 A 1001  ASP LYS PHE PHE ASN ASN ASN ILE GLN GLN LEU LEU PHE          
SEQRES  53 A 1001  ASN PHE PRO LYS ASP SER VAL THR SER THR GLY GLN PRO          
SEQRES  54 A 1001  PHE TRP SER GLY PRO LYS ARG ALA PRO THR PRO LEU SER          
SEQRES  55 A 1001  PHE ASP ILE HIS ASN ARG GLU HIS PHE ASP PHE ILE VAL          
SEQRES  56 A 1001  ALA ALA ALA SER LEU TYR ALA PHE ASN TYR GLY LEU LYS          
SEQRES  57 A 1001  SER GLU THR ASP PRO ALA ILE TYR GLU ARG VAL LEU ALA          
SEQRES  58 A 1001  GLY TYR ASN PRO PRO PRO PHE ALA PRO LYS SER GLY ILE          
SEQRES  59 A 1001  LYS ILE GLN VAL ASN GLU ASN GLU GLU ALA PRO GLU THR          
SEQRES  60 A 1001  ALA ALA ASN LYS ASP LYS GLN GLU LEU LYS SER ILE ALA          
SEQRES  61 A 1001  ASP SER LEU PRO PRO PRO SER SER LEU VAL GLY PHE ARG          
SEQRES  62 A 1001  LEU THR PRO ALA GLU PHE GLU LYS ASP ASP ASP SER ASN          
SEQRES  63 A 1001  HIS HIS ILE ASP PHE ILE THR ALA ALA SER ASN LEU ARG          
SEQRES  64 A 1001  ALA MET ASN TYR ASP ILE THR PRO ALA ASP ARG PHE LYS          
SEQRES  65 A 1001  THR LYS PHE VAL ALA GLY LYS ILE VAL PRO ALA MET CYS          
SEQRES  66 A 1001  THR SER THR ALA VAL VAL SER GLY LEU VAL CYS LEU GLU          
SEQRES  67 A 1001  LEU VAL LYS LEU VAL ASP GLY LYS LYS LYS ILE GLU GLU          
SEQRES  68 A 1001  TYR LYS ASN GLY PHE PHE ASN LEU ALA ILE GLY LEU PHE          
SEQRES  69 A 1001  THR PHE SER ASP PRO ILE ALA SER PRO LYS MET LYS VAL          
SEQRES  70 A 1001  ASN GLY LYS GLU ILE ASP LYS ILE TRP ASP ARG TYR ASN          
SEQRES  71 A 1001  LEU PRO ASP CYS THR LEU GLN GLU LEU ILE ASP TYR PHE          
SEQRES  72 A 1001  GLN LYS GLU GLU GLY LEU GLU VAL THR MET LEU SER SER          
SEQRES  73 A 1001  GLY VAL SER LEU LEU TYR ALA ASN PHE GLN PRO PRO LYS          
SEQRES  74 A 1001  LYS LEU ALA GLU ARG LEU PRO LEU LYS ILE SER GLU LEU          
SEQRES  75 A 1001  VAL GLU GLN ILE THR LYS LYS LYS LEU GLU PRO PHE ARG          
SEQRES  76 A 1001  LYS HIS LEU VAL LEU GLU ILE CYS CYS ASP ASP ALA ASN          
SEQRES  77 A 1001  GLY GLU ASP VAL GLU VAL PRO PHE ILE CYS ILE LYS LEU          
SEQRES   1 B   75  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 B   75  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 B   75  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 B   75  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 B   75  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 B   75  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY                      
SEQRES   1 C 1001  SER ASN THR ILE ASP GLU GLY LEU TYR SER ARG GLN LEU          
SEQRES   2 C 1001  TYR VAL LEU GLY HIS GLU ALA MET LYS GLN MET SER GLN          
SEQRES   3 C 1001  SER ASN VAL LEU ILE ILE GLY CYS LYS GLY LEU GLY VAL          
SEQRES   4 C 1001  GLU ILE ALA LYS ASN VAL CYS LEU ALA GLY VAL LYS SER          
SEQRES   5 C 1001  VAL THR LEU TYR ASP PRO GLN PRO THR ARG ILE GLU ASP          
SEQRES   6 C 1001  LEU SER SER GLN TYR PHE LEU THR GLU ASP ASP ILE GLY          
SEQRES   7 C 1001  VAL PRO ARG ALA LYS VAL THR VAL SER LYS LEU ALA GLU          
SEQRES   8 C 1001  LEU ASN GLN TYR VAL PRO VAL SER VAL VAL ASP GLU LEU          
SEQRES   9 C 1001  SER THR GLU TYR LEU LYS ASN PHE LYS CYS VAL VAL VAL          
SEQRES  10 C 1001  THR GLU THR SER LEU THR LYS GLN LEU GLU ILE ASN ASP          
SEQRES  11 C 1001  PHE THR HIS LYS ASN HIS ILE ALA TYR ILE ALA ALA ASP          
SEQRES  12 C 1001  SER ARG GLY LEU PHE GLY SER ILE PHE CYS ASP PHE GLY          
SEQRES  13 C 1001  GLU ASN PHE ILE CYS THR ASP THR ASP GLY ASN GLU PRO          
SEQRES  14 C 1001  LEU THR GLY MET ILE ALA SER ILE THR ASP ASP GLY VAL          
SEQRES  15 C 1001  VAL THR MET LEU GLU GLU THR ARG HIS GLY LEU GLU ASN          
SEQRES  16 C 1001  GLY ASP PHE VAL LYS PHE THR GLU VAL LYS GLY MET PRO          
SEQRES  17 C 1001  GLY LEU ASN ASP GLY THR PRO ARG LYS VAL GLU VAL LYS          
SEQRES  18 C 1001  GLY PRO TYR THR PHE SER ILE GLY SER VAL LYS ASP LEU          
SEQRES  19 C 1001  GLY SER ALA GLY TYR ASN GLY VAL PHE THR GLN VAL LYS          
SEQRES  20 C 1001  VAL PRO THR LYS ILE SER PHE LYS SER LEU ARG GLU SER          
SEQRES  21 C 1001  LEU LYS ASP PRO GLU TYR VAL TYR PRO ASP PHE GLY LYS          
SEQRES  22 C 1001  MET MET ARG PRO PRO GLN TYR HIS ILE ALA PHE GLN ALA          
SEQRES  23 C 1001  LEU SER ALA PHE ALA ASP ALA HIS GLU GLY SER LEU PRO          
SEQRES  24 C 1001  ARG PRO ARG ASN ASP ILE ASP ALA ALA GLU PHE PHE GLU          
SEQRES  25 C 1001  PHE CYS LYS LYS ILE ALA SER THR LEU GLN PHE ASP VAL          
SEQRES  26 C 1001  GLU LEU ASP GLU LYS LEU ILE LYS GLU ILE SER TYR GLN          
SEQRES  27 C 1001  ALA ARG GLY ASP LEU VAL ALA MET SER ALA PHE LEU GLY          
SEQRES  28 C 1001  GLY ALA VAL ALA GLN GLU VAL LEU LYS ALA THR THR SER          
SEQRES  29 C 1001  LYS PHE TYR PRO LEU LYS GLN TYR PHE TYR PHE ASP SER          
SEQRES  30 C 1001  LEU GLU SER LEU PRO SER SER VAL THR ILE SER GLU GLU          
SEQRES  31 C 1001  THR CYS LYS PRO ARG GLY CYS ARG TYR ASP GLY GLN ILE          
SEQRES  32 C 1001  ALA VAL PHE GLY SER GLU PHE GLN GLU LYS ILE ALA SER          
SEQRES  33 C 1001  LEU SER THR PHE LEU VAL GLY ALA GLY ALA ILE GLY CYS          
SEQRES  34 C 1001  GLU MET LEU LYS ASN TRP ALA MET MET GLY VAL ALA THR          
SEQRES  35 C 1001  GLY GLU SER GLY HIS ILE SER VAL THR ASP MET ASP SER          
SEQRES  36 C 1001  ILE GLU LYS SER ASN LEU ASN ARG GLN PHE LEU PHE ARG          
SEQRES  37 C 1001  PRO ARG ASP VAL GLY LYS LEU LYS SER GLU CYS ALA SER          
SEQRES  38 C 1001  THR ALA VAL SER ILE MET ASN PRO SER LEU THR GLY LYS          
SEQRES  39 C 1001  ILE THR SER TYR GLN GLU ARG VAL GLY PRO GLU SER GLU          
SEQRES  40 C 1001  GLY ILE PHE GLY ASP GLU PHE PHE GLU LYS LEU SER LEU          
SEQRES  41 C 1001  VAL THR ASN ALA LEU ASP ASN VAL GLU ALA ARG MET TYR          
SEQRES  42 C 1001  VAL ASP ARG ARG CYS VAL PHE PHE GLU LYS PRO LEU LEU          
SEQRES  43 C 1001  GLU SER GLY THR LEU GLY THR LYS GLY ASN THR GLN VAL          
SEQRES  44 C 1001  VAL VAL PRO HIS LEU THR GLU SER TYR GLY SER SER GLN          
SEQRES  45 C 1001  ASP PRO PRO GLU LYS SER PHE PRO ILE CYS THR LEU LYS          
SEQRES  46 C 1001  ASN PHE PRO ASN ARG ILE GLU HIS THR ILE ALA TRP ALA          
SEQRES  47 C 1001  ARG ASP LEU PHE GLU GLY LEU PHE LYS GLN PRO ILE ASP          
SEQRES  48 C 1001  ASN VAL ASN MET TYR LEU SER SER PRO ASN PHE LEU GLU          
SEQRES  49 C 1001  THR SER LEU LYS THR SER SER ASN PRO ARG GLU VAL LEU          
SEQRES  50 C 1001  GLU ASN ILE ARG ASP TYR LEU VAL THR GLU LYS PRO LEU          
SEQRES  51 C 1001  SER PHE GLU GLU CYS ILE MET TRP ALA ARG LEU GLN PHE          
SEQRES  52 C 1001  ASP LYS PHE PHE ASN ASN ASN ILE GLN GLN LEU LEU PHE          
SEQRES  53 C 1001  ASN PHE PRO LYS ASP SER VAL THR SER THR GLY GLN PRO          
SEQRES  54 C 1001  PHE TRP SER GLY PRO LYS ARG ALA PRO THR PRO LEU SER          
SEQRES  55 C 1001  PHE ASP ILE HIS ASN ARG GLU HIS PHE ASP PHE ILE VAL          
SEQRES  56 C 1001  ALA ALA ALA SER LEU TYR ALA PHE ASN TYR GLY LEU LYS          
SEQRES  57 C 1001  SER GLU THR ASP PRO ALA ILE TYR GLU ARG VAL LEU ALA          
SEQRES  58 C 1001  GLY TYR ASN PRO PRO PRO PHE ALA PRO LYS SER GLY ILE          
SEQRES  59 C 1001  LYS ILE GLN VAL ASN GLU ASN GLU GLU ALA PRO GLU THR          
SEQRES  60 C 1001  ALA ALA ASN LYS ASP LYS GLN GLU LEU LYS SER ILE ALA          
SEQRES  61 C 1001  ASP SER LEU PRO PRO PRO SER SER LEU VAL GLY PHE ARG          
SEQRES  62 C 1001  LEU THR PRO ALA GLU PHE GLU LYS ASP ASP ASP SER ASN          
SEQRES  63 C 1001  HIS HIS ILE ASP PHE ILE THR ALA ALA SER ASN LEU ARG          
SEQRES  64 C 1001  ALA MET ASN TYR ASP ILE THR PRO ALA ASP ARG PHE LYS          
SEQRES  65 C 1001  THR LYS PHE VAL ALA GLY LYS ILE VAL PRO ALA MET CYS          
SEQRES  66 C 1001  THR SER THR ALA VAL VAL SER GLY LEU VAL CYS LEU GLU          
SEQRES  67 C 1001  LEU VAL LYS LEU VAL ASP GLY LYS LYS LYS ILE GLU GLU          
SEQRES  68 C 1001  TYR LYS ASN GLY PHE PHE ASN LEU ALA ILE GLY LEU PHE          
SEQRES  69 C 1001  THR PHE SER ASP PRO ILE ALA SER PRO LYS MET LYS VAL          
SEQRES  70 C 1001  ASN GLY LYS GLU ILE ASP LYS ILE TRP ASP ARG TYR ASN          
SEQRES  71 C 1001  LEU PRO ASP CYS THR LEU GLN GLU LEU ILE ASP TYR PHE          
SEQRES  72 C 1001  GLN LYS GLU GLU GLY LEU GLU VAL THR MET LEU SER SER          
SEQRES  73 C 1001  GLY VAL SER LEU LEU TYR ALA ASN PHE GLN PRO PRO LYS          
SEQRES  74 C 1001  LYS LEU ALA GLU ARG LEU PRO LEU LYS ILE SER GLU LEU          
SEQRES  75 C 1001  VAL GLU GLN ILE THR LYS LYS LYS LEU GLU PRO PHE ARG          
SEQRES  76 C 1001  LYS HIS LEU VAL LEU GLU ILE CYS CYS ASP ASP ALA ASN          
SEQRES  77 C 1001  GLY GLU ASP VAL GLU VAL PRO PHE ILE CYS ILE LYS LEU          
SEQRES   1 D   75  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 D   75  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 D   75  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 D   75  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 D   75  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 D   75  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY                      
HET     CA  A1101       1                                                       
HET    TRS  A1102       8                                                       
HET    MPD  A1103       8                                                       
HET    MPD  A1104       8                                                       
HET    MPD  A1105       8                                                       
HET    MPD  A1106       8                                                       
HET    MPD  A1107       8                                                       
HET    VMX  A1108      26                                                       
HET     CA  C1101       1                                                       
HET    TRS  C1102       8                                                       
HET    MPD  C1103       8                                                       
HET    MPD  C1104       8                                                       
HET    MPD  C1105       8                                                       
HET    MPD  C1106       8                                                       
HET    MPD  C1107       8                                                       
HET    MPD  C1108       8                                                       
HET    VMX  C1109      26                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     VMX 5'-{[(3-AMINOPROPYL)SULFONYL]AMINO}-5'-DEOXYADENOSINE            
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   5   CA    2(CA 2+)                                                     
FORMUL   6  TRS    2(C4 H12 N O3 1+)                                            
FORMUL   7  MPD    11(C6 H14 O2)                                                
FORMUL  12  VMX    2(C13 H21 N7 O5 S)                                           
FORMUL  22  HOH   *37(H2 O)                                                     
HELIX    1 AA1 LYS A   46  GLY A   60  1                                  15    
HELIX    2 AA2 ARG A   73  SER A   79  5                                   7    
HELIX    3 AA3 PRO A   91  GLU A  102  1                                  12    
HELIX    4 AA4 THR A  117  PHE A  123  5                                   7    
HELIX    5 AA5 SER A  132  ASN A  146  1                                  15    
HELIX    6 AA6 MET A  218  ASN A  222  5                                   5    
HELIX    7 AA7 ASP A  281  MET A  285  5                                   5    
HELIX    8 AA8 MET A  286  ALA A  304  1                                  19    
HELIX    9 AA9 ASN A  314  LEU A  332  1                                  19    
HELIX   10 AB1 ASP A  339  GLN A  349  1                                  11    
HELIX   11 AB2 LEU A  354  SER A  375  1                                  22    
HELIX   12 AB3 LEU A  389  LEU A  392  5                                   4    
HELIX   13 AB4 TYR A  410  GLY A  418  1                                   9    
HELIX   14 AB5 GLY A  418  SER A  427  1                                  10    
HELIX   15 AB6 GLY A  436  GLY A  450  1                                  15    
HELIX   16 AB7 ARG A  479  VAL A  483  5                                   5    
HELIX   17 AB8 LEU A  486  ASN A  499  1                                  14    
HELIX   18 AB9 PRO A  500  THR A  503  5                                   4    
HELIX   19 AC1 PRO A  515  ILE A  520  5                                   6    
HELIX   20 AC2 GLY A  522  LYS A  528  1                                   7    
HELIX   21 AC3 ASN A  538  GLU A  553  1                                  16    
HELIX   22 AC4 SER A  578  SER A  582  5                                   5    
HELIX   23 AC5 ARG A  601  LYS A  618  1                                  18    
HELIX   24 AC6 LYS A  618  LEU A  628  1                                  11    
HELIX   25 AC7 ASN A  632  LEU A  638  1                                   7    
HELIX   26 AC8 ASN A  643  VAL A  656  1                                  14    
HELIX   27 AC9 SER A  662  ASN A  679  1                                  18    
HELIX   28 AD1 ASN A  679  PHE A  689  1                                  11    
HELIX   29 AD2 ASN A  718  TYR A  736  1                                  19    
HELIX   30 AD3 ASP A  743  ALA A  752  1                                  10    
HELIX   31 AD4 LYS A  784  SER A  793  1                                  10    
HELIX   32 AD5 HIS A  818  TYR A  834  1                                  17    
HELIX   33 AD6 ASP A  840  LYS A  850  1                                  11    
HELIX   34 AD7 MET A  855  GLY A  876  1                                  22    
HELIX   35 AD8 LYS A  879  TYR A  883  5                                   5    
HELIX   36 AD9 ALA A  891  GLY A  893  5                                   3    
HELIX   37 AE1 THR A  926  GLU A  937  1                                  12    
HELIX   38 AE2 PRO A  958  GLU A  964  1                                   7    
HELIX   39 AE3 LYS A  969  LYS A  979  1                                  11    
HELIX   40 AE4 THR B   22  GLY B   35  1                                  14    
HELIX   41 AE5 PRO B   37  GLN B   41  5                                   5    
HELIX   42 AE6 LYS C   46  GLY C   60  1                                  15    
HELIX   43 AE7 ARG C   73  SER C   79  5                                   7    
HELIX   44 AE8 PRO C   91  ALA C  101  1                                  11    
HELIX   45 AE9 THR C  117  PHE C  123  5                                   7    
HELIX   46 AF1 SER C  132  HIS C  147  1                                  16    
HELIX   47 AF2 LEU C  268  LEU C  272  5                                   5    
HELIX   48 AF3 ASP C  281  MET C  285  5                                   5    
HELIX   49 AF4 ARG C  287  ALA C  304  1                                  18    
HELIX   50 AF5 ASN C  314  LEU C  332  1                                  19    
HELIX   51 AF6 ASP C  339  GLN C  349  1                                  11    
HELIX   52 AF7 LEU C  354  SER C  375  1                                  22    
HELIX   53 AF8 LEU C  389  LEU C  392  5                                   4    
HELIX   54 AF9 TYR C  410  SER C  427  1                                  18    
HELIX   55 AG1 GLY C  436  GLY C  450  1                                  15    
HELIX   56 AG2 ARG C  479  VAL C  483  5                                   5    
HELIX   57 AG3 LEU C  486  ASN C  499  1                                  14    
HELIX   58 AG4 PRO C  500  THR C  503  5                                   4    
HELIX   59 AG5 GLY C  514  ILE C  520  5                                   7    
HELIX   60 AG6 GLY C  522  LYS C  528  1                                   7    
HELIX   61 AG7 ASN C  538  GLU C  553  1                                  16    
HELIX   62 AG8 SER C  578  SER C  582  5                                   5    
HELIX   63 AG9 ARG C  601  LYS C  618  1                                  18    
HELIX   64 AH1 LYS C  618  LEU C  628  1                                  11    
HELIX   65 AH2 ASN C  632  LEU C  638  1                                   7    
HELIX   66 AH3 ASN C  643  TYR C  654  1                                  12    
HELIX   67 AH4 SER C  662  ASN C  679  1                                  18    
HELIX   68 AH5 ASN C  679  PHE C  689  1                                  11    
HELIX   69 AH6 ASN C  718  TYR C  736  1                                  19    
HELIX   70 AH7 ASP C  743  GLY C  753  1                                  11    
HELIX   71 AH8 LYS C  784  SER C  793  1                                  10    
HELIX   72 AH9 HIS C  818  ASP C  835  1                                  18    
HELIX   73 AI1 ASP C  840  LYS C  850  1                                  11    
HELIX   74 AI2 MET C  855  GLY C  876  1                                  22    
HELIX   75 AI3 LYS C  879  TYR C  883  5                                   5    
HELIX   76 AI4 ALA C  891  GLY C  893  5                                   3    
HELIX   77 AI5 THR C  926  GLU C  937  1                                  12    
HELIX   78 AI6 PRO C  959  GLU C  964  1                                   6    
HELIX   79 AI7 LYS C  969  LYS C  979  1                                  11    
HELIX   80 AI8 THR D   22  GLY D   35  1                                  14    
HELIX   81 AI9 PRO D   37  GLN D   41  5                                   5    
HELIX   82 AJ1 THR D   55  TYR D   59  5                                   5    
SHEET    1 AA1 7 VAL A 109  VAL A 111  0                                        
SHEET    2 AA1 7 SER A  63  TYR A  67  1  N  VAL A  64   O  SER A 110           
SHEET    3 AA1 7 ASN A  39  ILE A  43  1  N  ILE A  42   O  THR A  65           
SHEET    4 AA1 7 CYS A 125  VAL A 128  1  O  VAL A 127   N  ILE A  43           
SHEET    5 AA1 7 ALA A 149  ARG A 156  1  O  ALA A 153   N  VAL A 128           
SHEET    6 AA1 7 PHE A 159  ASP A 165 -1  O  SER A 161   N  ASP A 154           
SHEET    7 AA1 7 TYR A 383  ASP A 387 -1  O  PHE A 386   N  GLY A 160           
SHEET    1 AA2 2 PHE A 170  CYS A 172  0                                        
SHEET    2 AA2 2 THR A 261  ILE A 263 -1  O  ILE A 263   N  PHE A 170           
SHEET    1 AA3 7 ARG A 227  LYS A 228  0                                        
SHEET    2 AA3 7 PHE A 209  THR A 213 -1  N  VAL A 210   O  ARG A 227           
SHEET    3 AA3 7 GLY A 249  VAL A 257 -1  O  VAL A 257   N  PHE A 209           
SHEET    4 AA3 7 THR A 182  ILE A 188 -1  N  GLY A 183   O  PHE A 254           
SHEET    5 AA3 7 VAL A 193  MET A 196 -1  O  THR A 195   N  SER A 187           
SHEET    6 AA3 7 THR A 236  SER A 238 -1  O  PHE A 237   N  VAL A 194           
SHEET    7 AA3 7 GLU A 230  VAL A 231 -1  N  GLU A 230   O  SER A 238           
SHEET    1 AA4 8 ILE A 506  TYR A 509  0                                        
SHEET    2 AA4 8 HIS A 458  THR A 462  1  N  VAL A 461   O  TYR A 509           
SHEET    3 AA4 8 SER A 429  VAL A 433  1  N  LEU A 432   O  SER A 460           
SHEET    4 AA4 8 LEU A 531  ASN A 534  1  O  THR A 533   N  VAL A 433           
SHEET    5 AA4 8 LEU A 556  LEU A 562  1  O  LEU A 557   N  ASN A 534           
SHEET    6 AA4 8 LYS A 565  VAL A 571 -1  O  GLN A 569   N  GLU A 558           
SHEET    7 AA4 8 ASN A 885  ASN A 889 -1  O  GLY A 886   N  THR A 568           
SHEET    8 AA4 8 LEU A 894  SER A 898 -1  O  SER A 898   N  ASN A 885           
SHEET    1 AA5 2 PHE A 590  ILE A 592  0                                        
SHEET    2 AA5 2 ILE A 851  PRO A 853  1  O  VAL A 852   N  PHE A 590           
SHEET    1 AA6 2 LYS A 905  VAL A 908  0                                        
SHEET    2 AA6 2 LYS A 911  ASP A 914 -1  O  LYS A 911   N  VAL A 908           
SHEET    1 AA7 5 TYR A 920  PRO A 923  0                                        
SHEET    2 AA7 5 ILE A1008  LYS A1011  1  O  CYS A1009   N  TYR A 920           
SHEET    3 AA7 5 HIS A 988  ASP A 996 -1  N  LEU A 991   O  ILE A1008           
SHEET    4 AA7 5 GLU A 941  SER A 947 -1  N  GLU A 941   O  ASP A 996           
SHEET    5 AA7 5 SER A 950  ALA A 954 -1  O  SER A 950   N  SER A 947           
SHEET    1 AA8 4 TYR A 920  PRO A 923  0                                        
SHEET    2 AA8 4 ILE A1008  LYS A1011  1  O  CYS A1009   N  TYR A 920           
SHEET    3 AA8 4 HIS A 988  ASP A 996 -1  N  LEU A 991   O  ILE A1008           
SHEET    4 AA8 4 ASP A1002  VAL A1003 -1  O  VAL A1003   N  CYS A 995           
SHEET    1 AA9 5 THR B  12  GLU B  16  0                                        
SHEET    2 AA9 5 GLN B   2  THR B   7 -1  N  ILE B   3   O  LEU B  15           
SHEET    3 AA9 5 THR B  66  VAL B  70  1  O  LEU B  67   N  PHE B   4           
SHEET    4 AA9 5 ARG B  42  PHE B  45 -1  N  ARG B  42   O  VAL B  70           
SHEET    5 AA9 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
SHEET    1 AB1 7 VAL C 109  VAL C 111  0                                        
SHEET    2 AB1 7 SER C  63  TYR C  67  1  N  VAL C  64   O  SER C 110           
SHEET    3 AB1 7 ASN C  39  ILE C  43  1  N  ILE C  42   O  THR C  65           
SHEET    4 AB1 7 CYS C 125  VAL C 128  1  O  VAL C 127   N  ILE C  43           
SHEET    5 AB1 7 ALA C 149  ARG C 156  1  O  ALA C 153   N  VAL C 128           
SHEET    6 AB1 7 PHE C 159  ASP C 165 -1  O  PHE C 159   N  ARG C 156           
SHEET    7 AB1 7 TYR C 383  ASP C 387 -1  O  PHE C 384   N  ILE C 162           
SHEET    1 AB2 2 PHE C 170  CYS C 172  0                                        
SHEET    2 AB2 2 THR C 261  ILE C 263 -1  O  THR C 261   N  CYS C 172           
SHEET    1 AB3 6 PHE C 209  PHE C 212  0                                        
SHEET    2 AB3 6 ALA C 248  VAL C 257 -1  O  THR C 255   N  LYS C 211           
SHEET    3 AB3 6 THR C 182  THR C 189 -1  N  ILE C 185   O  GLY C 252           
SHEET    4 AB3 6 VAL C 194  MET C 196 -1  O  THR C 195   N  ALA C 186           
SHEET    5 AB3 6 THR C 236  SER C 238 -1  N  PHE C 237   O  VAL C 194           
SHEET    6 AB3 6 GLU C 230  VAL C 231 -1  N  GLU C 230   O  SER C 238           
SHEET    1 AB4 8 ILE C 506  TYR C 509  0                                        
SHEET    2 AB4 8 HIS C 458  THR C 462  1  N  VAL C 461   O  TYR C 509           
SHEET    3 AB4 8 SER C 429  VAL C 433  1  N  LEU C 432   O  SER C 460           
SHEET    4 AB4 8 LEU C 531  ASN C 534  1  O  THR C 533   N  PHE C 431           
SHEET    5 AB4 8 LEU C 556  LEU C 562  1  O  LEU C 557   N  ASN C 534           
SHEET    6 AB4 8 LYS C 565  VAL C 571 -1  O  GLN C 569   N  GLU C 558           
SHEET    7 AB4 8 ASN C 885  ASN C 889 -1  O  PHE C 888   N  GLY C 566           
SHEET    8 AB4 8 LEU C 894  SER C 898 -1  O  SER C 898   N  ASN C 885           
SHEET    1 AB5 2 PHE C 590  ILE C 592  0                                        
SHEET    2 AB5 2 ILE C 851  PRO C 853  1  O  VAL C 852   N  PHE C 590           
SHEET    1 AB6 2 LYS C 905  VAL C 908  0                                        
SHEET    2 AB6 2 LYS C 911  ASP C 914 -1  O  ILE C 913   N  MET C 906           
SHEET    1 AB7 5 TYR C 920  LEU C 922  0                                        
SHEET    2 AB7 5 ILE C1008  LYS C1011  1  O  CYS C1009   N  TYR C 920           
SHEET    3 AB7 5 HIS C 988  ASP C 996 -1  N  LEU C 991   O  ILE C1008           
SHEET    4 AB7 5 GLU C 941  SER C 947 -1  N  GLU C 941   O  ASP C 996           
SHEET    5 AB7 5 SER C 950  ALA C 954 -1  O  TYR C 953   N  LEU C 945           
SHEET    1 AB8 4 TYR C 920  LEU C 922  0                                        
SHEET    2 AB8 4 ILE C1008  LYS C1011  1  O  CYS C1009   N  TYR C 920           
SHEET    3 AB8 4 HIS C 988  ASP C 996 -1  N  LEU C 991   O  ILE C1008           
SHEET    4 AB8 4 ASP C1002  VAL C1003 -1  O  VAL C1003   N  CYS C 995           
SHEET    1 AB9 5 THR D  12  GLU D  16  0                                        
SHEET    2 AB9 5 GLN D   2  THR D   7 -1  N  ILE D   3   O  LEU D  15           
SHEET    3 AB9 5 THR D  66  VAL D  70  1  O  LEU D  67   N  LYS D   6           
SHEET    4 AB9 5 ARG D  42  PHE D  45 -1  N  ARG D  42   O  VAL D  70           
SHEET    5 AB9 5 LYS D  48  GLN D  49 -1  O  LYS D  48   N  PHE D  45           
LINK         OE1 GLU A 320                CA    CA A1101     1555   1555  2.45  
LINK         OE2 GLU A 320                CA    CA A1101     1555   1555  2.38  
LINK         SG  CYS A 593                 C10 VMX A1108     1555   1555  1.68  
LINK         C   GLY B  75                 N12 VMX A1108     1555   1555  1.33  
LINK         OE1 GLU C 320                CA    CA C1101     1555   1555  2.30  
LINK         OE2 GLU C 320                CA    CA C1101     1555   1555  2.25  
LINK         SG  CYS C 593                 C10 VMX C1109     1555   1555  1.68  
LINK         C   GLY D  75                 N12 VMX C1109     1555   1555  1.34  
LINK         OD1 ASP A 715                CA    CA A1101     1555   2454  2.25  
LINK         OD2 ASP A 715                CA    CA A1101     1555   2454  2.84  
LINK         OD1 ASP C 715                CA    CA C1101     1555   2355  2.47  
LINK         OD2 ASP C 715                CA    CA C1101     1555   2355  2.24  
CISPEP   1 LYS A  381    GLN A  382          0        -1.21                     
CISPEP   2 LYS C  381    GLN C  382          0        -0.83                     
SITE     1 AC1  4 HIS A 305  GLU A 320  ASP A 715  HIS A 717                    
SITE     1 AC2  4 GLU A 553  ARG A 919  ASN A 921  CYS A1009                    
SITE     1 AC3  2 THR A 175  TYR A 378                                          
SITE     1 AC4  4 GLN A 136  SER A 161  PHE A 295  TYR A 385                    
SITE     1 AC5  3 GLU A 658  GLU A 665  MET A 668                               
SITE     1 AC6  4 ARG A 547  VAL A 990  GLU A 992  PHE A1007                    
SITE     1 AC7  3 ILE A 716  HIS A 717  GLU A 748                               
SITE     1 AC8 13 ALA A 437  ILE A 438  ASP A 463  MET A 464                    
SITE     2 AC8 13 ASP A 465  LYS A 487  VAL A 513  ALA A 535                    
SITE     3 AC8 13 ASP A 537  ASN A 538  THR A 561  CYS A 593                    
SITE     4 AC8 13 GLY B  75                                                     
SITE     1 AC9  4 HIS C 305  GLU C 320  ASP C 715  HIS C 717                    
SITE     1 AD1  6 GLU C 553  ARG C 919  ASN C 921  HIS C 988                    
SITE     2 AD1  6 CYS C1009  LYS C1011                                          
SITE     1 AD2  3 GLU C 658  GLU C 665  LEU C 672                               
SITE     1 AD3  5 ASP C  68  PRO C  69  GLN C  70  GLU C 130                    
SITE     2 AD3  5 THR C 131                                                     
SITE     1 AD4  2 GLU C 577  SER C 582                                          
SITE     1 AD5  3 ILE C 716  PHE C 722  GLU C 748                               
SITE     1 AD6  5 LEU C 133  GLN C 136  SER C 161  PHE C 295                    
SITE     2 AD6  5 TYR C 385                                                     
SITE     1 AD7  3 VAL C 990  GLU C 992  PHE C1007                               
CRYST1  122.575  150.522  172.776  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008158  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006644  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005788        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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