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Database: PDB
Entry: 4C9Z
LinkDB: 4C9Z
Original site: 4C9Z 
HEADER    LIGASE                                  04-OCT-13   4C9Z              
TITLE     CRYSTAL STRUCTURE OF SIAH1 AT 1.95 A RESOLUTION                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE SIAH1;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: TWO ZINC FINGERS AND SUBSTRATE BINDING DOMAIN, RESIDUES    
COMPND   5  91-282;                                                             
COMPND   6 SYNONYM: SEVEN IN ABSENTIA HOMOLOG 1, SIAH-1, SIAH-1A;               
COMPND   7 EC: 6.3.2.-;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: GOLD;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET15B                                     
KEYWDS    LIGASE                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.RIMSA,T.C.EADSFORTH,W.N.HUNTER                                      
REVDAT   3   18-DEC-13 4C9Z    1       JRNL                                     
REVDAT   2   11-DEC-13 4C9Z    1       JRNL                                     
REVDAT   1   16-OCT-13 4C9Z    0                                                
JRNL        AUTH   V.RIMSA,T.C.EADSFORTH,W.N.HUNTER                             
JRNL        TITL   TWO HIGH-RESOLUTION STRUCTURES OF THE HUMAN E3 UBIQUITIN     
JRNL        TITL 2 LIGASE SIAH1.                                                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  96  1339 2013              
JRNL        REFN                   ISSN 1744-3091                               
JRNL        PMID   24316825                                                     
JRNL        DOI    10.1107/S1744309113031448                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.27                          
REMARK   3   NUMBER OF REFLECTIONS             : 36417                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.19967                         
REMARK   3   R VALUE            (WORKING SET) : 0.19761                         
REMARK   3   FREE R VALUE                     : 0.23855                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1918                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.950                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.001                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2483                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.284                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 121                          
REMARK   3   BIN FREE R VALUE                    : 0.329                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3057                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 57                                      
REMARK   3   SOLVENT ATOMS            : 217                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.280                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.20                                                
REMARK   3    B22 (A**2) : 0.55                                                 
REMARK   3    B33 (A**2) : -0.34                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.149         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.143         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.872         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3185 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4326 ; 1.302 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   399 ; 5.568 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;39.793 ;24.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   530 ;15.277 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;10.572 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   467 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2420 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1935 ; 2.345 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3130 ; 3.539 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1250 ; 5.572 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1186 ; 7.837 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    90        A   133                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6057  -6.1486  14.1524              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4219 T22:   0.3897                                     
REMARK   3      T33:   0.4974 T12:  -0.0308                                     
REMARK   3      T13:   0.1059 T23:   0.0987                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7898 L22:  13.9127                                     
REMARK   3      L33:   5.3807 L12:   9.9341                                     
REMARK   3      L13:  -5.3188 L23:  -8.3993                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4688 S12:   0.1471 S13:   0.4224                       
REMARK   3      S21:  -0.8270 S22:   0.6563 S23:   0.3922                       
REMARK   3      S31:   0.6847 S32:  -0.5695 S33:  -0.1875                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   134        A   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4334  18.0240  11.6512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1037 T22:   0.0474                                     
REMARK   3      T33:   0.0671 T12:   0.0376                                     
REMARK   3      T13:  -0.0055 T23:  -0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1781 L22:   3.4785                                     
REMARK   3      L33:   2.7085 L12:  -0.0706                                     
REMARK   3      L13:  -0.0223 L23:   1.0544                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0125 S12:   0.0333 S13:   0.0824                       
REMARK   3      S21:  -0.3124 S22:  -0.1291 S23:   0.2332                       
REMARK   3      S31:  -0.2000 S32:  -0.1989 S33:   0.1166                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    95        B   138                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1731  52.9178  29.1869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9724 T22:   0.5293                                     
REMARK   3      T33:   1.0422 T12:   0.2328                                     
REMARK   3      T13:  -0.1241 T23:   0.1980                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4433 L22:  13.8213                                     
REMARK   3      L33:   8.3378 L12:  -3.4409                                     
REMARK   3      L13:   1.5497 L23: -12.9901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0758 S12:  -0.1089 S13:  -0.1889                       
REMARK   3      S21:  -0.8138 S22:   0.5358 S23:   0.3262                       
REMARK   3      S31:   0.1660 S32:  -0.5517 S33:  -0.4600                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   139        B   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.6930  31.0691  33.7028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0861 T22:   0.0923                                     
REMARK   3      T33:   0.1283 T12:   0.0414                                     
REMARK   3      T13:  -0.0415 T23:  -0.0775                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5365 L22:   2.3427                                     
REMARK   3      L33:   3.4301 L12:   1.1048                                     
REMARK   3      L13:   1.6042 L23:   2.0844                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0524 S12:  -0.1825 S13:   0.1856                       
REMARK   3      S21:   0.1655 S22:   0.0341 S23:  -0.1084                       
REMARK   3      S31:  -0.0700 S32:  -0.0556 S33:   0.0183                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   3   CHAIN A CONTAINS METHIONINE AT THE N-TERMINAL END, WHICH           
REMARK   3    WAS LEFT FROM THE HISTIDINE TAG. RESIDUES 91-94 IN CHAIN          
REMARK   3    B ARE DISORDERED.                                                 
REMARK   4                                                                      
REMARK   4 4C9Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-58626.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU  MICROMAX-007               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE (RAXIS IV)             
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38340                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.95                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.99                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.18                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.50                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2A25                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS GREW FROM EQUAL                 
REMARK 280  VOLUMES OF  PROTEIN SOLUTION (15 MG ML-1 IN 15 MM TRIS-HCL          
REMARK 280  PH7.5, 30 MM NACL AND 10 MM  DTT) AND RESERVOIR SOLUTION            
REMARK 280  (100 MES PH6.5, 1.5 M MGSO4).                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       37.57000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.29500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       66.58000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.57000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.29500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       66.58000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.57000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       52.29500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       66.58000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.57000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       52.29500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       66.58000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2029   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A2085   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A2135   LIES ON A SPECIAL POSITION.                         
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    88                                                      
REMARK 465     HIS A    89                                                      
REMARK 465     GLY B    88                                                      
REMARK 465     HIS B    89                                                      
REMARK 465     MET B    90                                                      
REMARK 465     ALA B    91                                                      
REMARK 465     ASN B    92                                                      
REMARK 465     SER B    93                                                      
REMARK 465     VAL B    94                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 120      -15.67   -140.75                                   
REMARK 500    HIS A 230       99.25    -61.03                                   
REMARK 500    CYS A 256     -179.58   -175.70                                   
REMARK 500    CYS B 256     -177.82   -175.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A 165        18.1      L          L   OUTSIDE RANGE           
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                              ZN A 283  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 135   SG                                                     
REMARK 620 2 CYS A 128   SG  116.7                                              
REMARK 620 3 HIS A 147   NE2 109.3 116.1                                        
REMARK 620 4 HIS A 152   NE2 113.7 112.8  84.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 283  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 128   SG                                                     
REMARK 620 2 HIS B 152   NE2 113.0                                              
REMARK 620 3 CYS B 135   SG  118.3 104.3                                        
REMARK 620 4 HIS B 147   NE2 104.8 103.1 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 284  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 105   SG                                                     
REMARK 620 2 CYS A  98   SG  112.1                                              
REMARK 620 3 CYS A 121   SG  109.2 110.1                                        
REMARK 620 4 HIS A 117   NE2 110.6 106.0 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 284  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 117   NE2                                                    
REMARK 620 2 CYS B  98   SG  111.5                                              
REMARK 620 3 CYS B 121   SG  110.6 116.3                                        
REMARK 620 4 CYS B 105   SG  107.6 110.7  99.2                                  
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  ZN A 283                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 284                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 283                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 284                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1283                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1285                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B1283                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1287                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1284                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1285                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1288                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1289                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A1290                 
DBREF  4C9Z A   91   282  UNP    Q8IUQ4   SIAH1_HUMAN     91    282             
DBREF  4C9Z B   91   282  UNP    Q8IUQ4   SIAH1_HUMAN     91    282             
SEQADV 4C9Z GLY A   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4C9Z HIS A   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4C9Z MET A   90  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4C9Z GLY B   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4C9Z HIS B   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4C9Z MET B   90  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQRES   1 A  195  GLY HIS MET ALA ASN SER VAL LEU PHE PRO CYS LYS TYR          
SEQRES   2 A  195  ALA SER SER GLY CYS GLU ILE THR LEU PRO HIS THR GLU          
SEQRES   3 A  195  LYS ALA ASP HIS GLU GLU LEU CYS GLU PHE ARG PRO TYR          
SEQRES   4 A  195  SER CYS PRO CYS PRO GLY ALA SER CYS LYS TRP GLN GLY          
SEQRES   5 A  195  SER LEU ASP ALA VAL MET PRO HIS LEU MET HIS GLN HIS          
SEQRES   6 A  195  LYS SER ILE THR THR LEU GLN GLY GLU ASP ILE VAL PHE          
SEQRES   7 A  195  LEU ALA THR ASP ILE ASN LEU PRO GLY ALA VAL ASP TRP          
SEQRES   8 A  195  VAL MET MET GLN SER CYS PHE GLY PHE HIS PHE MET LEU          
SEQRES   9 A  195  VAL LEU GLU LYS GLN GLU LYS TYR ASP GLY HIS GLN GLN          
SEQRES  10 A  195  PHE PHE ALA ILE VAL GLN LEU ILE GLY THR ARG LYS GLN          
SEQRES  11 A  195  ALA GLU ASN PHE ALA TYR ARG LEU GLU LEU ASN GLY HIS          
SEQRES  12 A  195  ARG ARG ARG LEU THR TRP GLU ALA THR PRO ARG SER ILE          
SEQRES  13 A  195  HIS GLU GLY ILE ALA THR ALA ILE MET ASN SER ASP CYS          
SEQRES  14 A  195  LEU VAL PHE ASP THR SER ILE ALA GLN LEU PHE ALA GLU          
SEQRES  15 A  195  ASN GLY ASN LEU GLY ILE ASN VAL THR ILE SER MET CYS          
SEQRES   1 B  195  GLY HIS MET ALA ASN SER VAL LEU PHE PRO CYS LYS TYR          
SEQRES   2 B  195  ALA SER SER GLY CYS GLU ILE THR LEU PRO HIS THR GLU          
SEQRES   3 B  195  LYS ALA ASP HIS GLU GLU LEU CYS GLU PHE ARG PRO TYR          
SEQRES   4 B  195  SER CYS PRO CYS PRO GLY ALA SER CYS LYS TRP GLN GLY          
SEQRES   5 B  195  SER LEU ASP ALA VAL MET PRO HIS LEU MET HIS GLN HIS          
SEQRES   6 B  195  LYS SER ILE THR THR LEU GLN GLY GLU ASP ILE VAL PHE          
SEQRES   7 B  195  LEU ALA THR ASP ILE ASN LEU PRO GLY ALA VAL ASP TRP          
SEQRES   8 B  195  VAL MET MET GLN SER CYS PHE GLY PHE HIS PHE MET LEU          
SEQRES   9 B  195  VAL LEU GLU LYS GLN GLU LYS TYR ASP GLY HIS GLN GLN          
SEQRES  10 B  195  PHE PHE ALA ILE VAL GLN LEU ILE GLY THR ARG LYS GLN          
SEQRES  11 B  195  ALA GLU ASN PHE ALA TYR ARG LEU GLU LEU ASN GLY HIS          
SEQRES  12 B  195  ARG ARG ARG LEU THR TRP GLU ALA THR PRO ARG SER ILE          
SEQRES  13 B  195  HIS GLU GLY ILE ALA THR ALA ILE MET ASN SER ASP CYS          
SEQRES  14 B  195  LEU VAL PHE ASP THR SER ILE ALA GLN LEU PHE ALA GLU          
SEQRES  15 B  195  ASN GLY ASN LEU GLY ILE ASN VAL THR ILE SER MET CYS          
HET     ZN  A 283       1                                                       
HET     ZN  A 284       1                                                       
HET     ZN  B 283       1                                                       
HET     ZN  B 284       1                                                       
HET     CL  A1283       1                                                       
HET     CL  B1286       1                                                       
HET     CL  A1284       1                                                       
HET     CL  A1285       1                                                       
HET    TRS  B1283       8                                                       
HET    GOL  A1286       6                                                       
HET    GOL  A1287       6                                                       
HET    SO4  B1284       5                                                       
HET    SO4  B1285       5                                                       
HET    GOL  A1288       6                                                       
HET    SO4  A1289       5                                                       
HET    TRS  A1290       8                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2  SO4    3(O4 S 2-)                                                   
FORMUL   3  GOL    3(C3 H8 O3)                                                  
FORMUL   4   CL    4(CL 1-)                                                     
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  TRS    2(C4 H12 N O3 1+)                                            
FORMUL   7  HOH   *217(H2 O)                                                    
HELIX    1   1 PRO A  110  GLU A  119  1                                  10    
HELIX    2   2 SER A  140  ASP A  142  5                                   3    
HELIX    3   3 ALA A  143  HIS A  152  1                                  10    
HELIX    4   4 THR A  214  GLU A  219  1                                   6    
HELIX    5   5 ILE A  247  ASN A  253  1                                   7    
HELIX    6   6 THR A  261  PHE A  267  1                                   7    
HELIX    7   7 TYR B  100  GLY B  104  5                                   5    
HELIX    8   8 PRO B  110  CYS B  121  1                                  12    
HELIX    9   9 SER B  140  ASP B  142  5                                   3    
HELIX   10  10 ALA B  143  HIS B  152  1                                  10    
HELIX   11  11 THR B  214  GLU B  219  1                                   6    
HELIX   12  12 ILE B  247  ASN B  253  1                                   7    
HELIX   13  13 THR B  261  ALA B  268  1                                   8    
SHEET    1  AA 2 PHE A  96  PRO A  97  0                                        
SHEET    2  AA 2 THR A 108  LEU A 109 -1  O  LEU A 109   N  PHE A  96           
SHEET    1  AB 2 TYR A 126  SER A 127  0                                        
SHEET    2  AB 2 GLN A 138  GLY A 139 -1  O  GLY A 139   N  TYR A 126           
SHEET    1  AC 5 THR A 156  GLN A 159  0                                        
SHEET    2  AC 5 ASP A 177  CYS A 184  1  O  VAL A 179   N  THR A 156           
SHEET    3  AC 5 PHE A 187  TYR A 199 -1  O  PHE A 187   N  CYS A 184           
SHEET    4  AC 5 HIS A 202  LEU A 211 -1  O  HIS A 202   N  TYR A 199           
SHEET    5  AC 5 ARG A 241  SER A 242 -1  O  ARG A 241   N  LEU A 211           
SHEET    1  AD 5 THR A 156  GLN A 159  0                                        
SHEET    2  AD 5 ASP A 177  CYS A 184  1  O  VAL A 179   N  THR A 156           
SHEET    3  AD 5 PHE A 187  TYR A 199 -1  O  PHE A 187   N  CYS A 184           
SHEET    4  AD 5 HIS A 202  LEU A 211 -1  O  HIS A 202   N  TYR A 199           
SHEET    5  AD 5 LEU A 257  ASP A 260 -1  O  LEU A 257   N  ALA A 207           
SHEET    1  AE 2 ARG A 241  SER A 242  0                                        
SHEET    2  AE 2 HIS A 202  LEU A 211 -1  O  VAL A 209   N  ARG A 241           
SHEET    1  AF 2 ASP A 162  ALA A 167  0                                        
SHEET    2  AF 2 ASN A 272  MET A 281 -1  O  LEU A 273   N  ALA A 167           
SHEET    1  AG 2 ALA A 268  GLU A 269  0                                        
SHEET    2  AG 2 ASN A 272  MET A 281 -1  O  ASN A 272   N  GLU A 269           
SHEET    1  BA 8 ASP B 162  ALA B 167  0                                        
SHEET    2  BA 8 LEU B 273  MET B 281 -1  O  LEU B 273   N  ALA B 167           
SHEET    3  BA 8 PHE B 221  GLY B 229 -1  O  ALA B 222   N  SER B 280           
SHEET    4  BA 8 ARG B 232  ALA B 238 -1  O  ARG B 232   N  GLY B 229           
SHEET    5  BA 8 ARG A 232  ALA A 238 -1  O  ARG A 233   N  GLU B 237           
SHEET    6  BA 8 PHE A 221  GLY A 229 -1  O  TYR A 223   N  ALA A 238           
SHEET    7  BA 8 ASN A 272  MET A 281 -1  O  ASN A 276   N  GLU A 226           
SHEET    8  BA 8 ALA A 268  GLU A 269 -1  O  GLU A 269   N  ASN A 272           
SHEET    1  BB 8 ASP B 162  ALA B 167  0                                        
SHEET    2  BB 8 LEU B 273  MET B 281 -1  O  LEU B 273   N  ALA B 167           
SHEET    3  BB 8 PHE B 221  GLY B 229 -1  O  ALA B 222   N  SER B 280           
SHEET    4  BB 8 ARG B 232  ALA B 238 -1  O  ARG B 232   N  GLY B 229           
SHEET    5  BB 8 ARG A 232  ALA A 238 -1  O  ARG A 233   N  GLU B 237           
SHEET    6  BB 8 PHE A 221  GLY A 229 -1  O  TYR A 223   N  ALA A 238           
SHEET    7  BB 8 ASN A 272  MET A 281 -1  O  ASN A 276   N  GLU A 226           
SHEET    8  BB 8 ASP A 162  ALA A 167 -1  O  ILE A 163   N  VAL A 277           
SHEET    1  BC 2 PHE B  96  PRO B  97  0                                        
SHEET    2  BC 2 THR B 108  LEU B 109 -1  O  LEU B 109   N  PHE B  96           
SHEET    1  BD 2 TYR B 126  SER B 127  0                                        
SHEET    2  BD 2 GLN B 138  GLY B 139 -1  O  GLY B 139   N  TYR B 126           
SHEET    1  BE 5 THR B 157  GLN B 159  0                                        
SHEET    2  BE 5 VAL B 176  CYS B 184  1  O  MET B 181   N  LEU B 158           
SHEET    3  BE 5 PHE B 187  TYR B 199 -1  O  PHE B 187   N  CYS B 184           
SHEET    4  BE 5 HIS B 202  LEU B 211 -1  O  HIS B 202   N  TYR B 199           
SHEET    5  BE 5 ARG B 241  SER B 242 -1  O  ARG B 241   N  LEU B 211           
SHEET    1  BF 5 THR B 157  GLN B 159  0                                        
SHEET    2  BF 5 VAL B 176  CYS B 184  1  O  MET B 181   N  LEU B 158           
SHEET    3  BF 5 PHE B 187  TYR B 199 -1  O  PHE B 187   N  CYS B 184           
SHEET    4  BF 5 HIS B 202  LEU B 211 -1  O  HIS B 202   N  TYR B 199           
SHEET    5  BF 5 LEU B 257  ASP B 260 -1  O  LEU B 257   N  ALA B 207           
SHEET    1  BG 2 ARG B 241  SER B 242  0                                        
SHEET    2  BG 2 HIS B 202  LEU B 211 -1  O  VAL B 209   N  ARG B 241           
LINK        ZN    ZN A 283                 SG  CYS A 135     1555   1555  2.40  
LINK        ZN    ZN A 283                 SG  CYS A 128     1555   1555  2.21  
LINK        ZN    ZN A 283                 NE2 HIS A 147     1555   1555  1.93  
LINK        ZN    ZN A 283                 NE2 HIS A 152     1555   1555  2.08  
LINK        ZN    ZN A 284                 SG  CYS A 105     1555   1555  2.06  
LINK        ZN    ZN A 284                 NE2 HIS A 117     1555   1555  2.03  
LINK        ZN    ZN A 284                 SG  CYS A 121     1555   1555  2.50  
LINK        ZN    ZN A 284                 SG  CYS A  98     1555   1555  2.35  
LINK        ZN    ZN B 283                 NE2 HIS B 147     1555   1555  1.97  
LINK        ZN    ZN B 283                 SG  CYS B 135     1555   1555  2.24  
LINK        ZN    ZN B 283                 NE2 HIS B 152     1555   1555  1.96  
LINK        ZN    ZN B 283                 SG  CYS B 128     1555   1555  2.13  
LINK        ZN    ZN B 284                 SG  CYS B  98     1555   1555  2.44  
LINK        ZN    ZN B 284                 SG  CYS B 121     1555   1555  2.49  
LINK        ZN    ZN B 284                 SG  CYS B 105     1555   1555  2.49  
LINK        ZN    ZN B 284                 NE2 HIS B 117     1555   1555  2.20  
CISPEP   1 PRO A  131    GLY A  132          0        -1.46                     
CISPEP   2 PRO B  131    GLY B  132          0        -8.50                     
CISPEP   3 ALA B  133    SER B  134          0       -10.16                     
SITE     1 AC1  4 CYS A 128  CYS A 135  HIS A 147  HIS A 152                    
SITE     1 AC2  4 CYS A  98  CYS A 105  HIS A 117  CYS A 121                    
SITE     1 AC3  4 CYS B 128  CYS B 135  HIS B 147  HIS B 152                    
SITE     1 AC4  4 CYS B  98  CYS B 105  HIS B 117  CYS B 121                    
SITE     1 AC5  1 ARG A 224                                                     
SITE     1 AC6  1 ARG B 224                                                     
SITE     1 AC7  2 HIS A 230  ARG A 232                                          
SITE     1 AC8  8 GLU A 237  ALA A 238  HOH A2106  HOH A2142                    
SITE     2 AC8  8 ARG B 231  ARG B 232  ARG B 233  HOH B2057                    
SITE     1 AC9  5 ARG A 231  ARG A 232  ARG A 233  HOH A2143                    
SITE     2 AC9  5 ALA B 222                                                     
SITE     1 BC1  7 GLU A 161  CYS A 184  PHE A 185  GLY A 186                    
SITE     2 BC1  7 PHE A 187  HOH A2144  HOH A2145                               
SITE     1 BC2  5 THR A 239  ARG A 241  HOH A2080  ARG B 231                    
SITE     2 BC2  5 ARG B 232                                                     
SITE     1 BC3  6 HIS A 244  PRO B 146  HIS B 147  HIS B 150                    
SITE     2 BC3  6 GLN B 151  HOH B2013                                          
SITE     1 BC4  4 CYS A 130  HIS A 152  LYS A 153  SER A 154                    
SITE     1 BC5  8 GLU A 119  ARG A 124  THR A 214  ARG A 215                    
SITE     2 BC5  8 HIS A 244  HOH A2076  HOH A2078  HOH A2110                    
SITE     1 BC6  6 GLU A 219  ASN A 220  CYS A 282  HOH A2083                    
SITE     2 BC6  6 HOH A2140  HOH A2146                                          
CRYST1   75.140  104.590  133.160  90.00  90.00  90.00 I 2 2 2      16          
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      0.013308  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009561  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007510        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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