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Database: PDB
Entry: 4CA1
LinkDB: 4CA1
Original site: 4CA1 
HEADER    LIGASE                                  04-OCT-13   4CA1              
TITLE     CRYSTAL STRUCTURE OF SIAH1 AT 1.58 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 4CA1    1       JRNL                                     
REVDAT   2   11-DEC-13 4CA1    1       JRNL                                     
REVDAT   1   16-OCT-13 4CA1    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.    1.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.95                          
REMARK   3   NUMBER OF REFLECTIONS             : 69071                          
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) : 0.14315                         
REMARK   3   R VALUE            (WORKING SET) : 0.14075                         
REMARK   3   FREE R VALUE                     : 0.18907                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3666                            
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) : 1.580                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.621                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5081                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.209                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 250                          
REMARK   3   BIN FREE R VALUE                    : 0.260                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3280                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 104                                     
REMARK   3   SOLVENT ATOMS            : 331                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.821                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.23                                                
REMARK   3    B22 (A**2) : -0.73                                                
REMARK   3    B33 (A**2) : 0.97                                                 
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): 0.073         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.071         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.677         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.974                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3472 ; 0.023 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4741 ; 2.335 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   453 ; 6.345 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   157 ;40.065 ;24.204       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   586 ;15.895 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;22.873 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   531 ; 0.171 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2660 ; 0.012 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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):  3471 ;10.043 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   119 ;30.633 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3597 ;22.131 ; 5.000       
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    91        A   134                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2660  -4.9130  14.1300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1637 T22:   0.2806                                     
REMARK   3      T33:   0.0733 T12:  -0.1044                                     
REMARK   3      T13:   0.0126 T23:  -0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9812 L22:   4.6831                                     
REMARK   3      L33:   3.5348 L12:   2.3438                                     
REMARK   3      L13:  -1.1980 L23:  -3.7323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0571 S12:  -0.2979 S13:   0.2548                       
REMARK   3      S21:  -0.5514 S22:   0.2359 S23:   0.3205                       
REMARK   3      S31:   0.6225 S32:  -0.5178 S33:  -0.1788                       
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   135        A   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.6710  17.6700  11.5120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0430 T22:   0.0582                                     
REMARK   3      T33:   0.0171 T12:   0.0035                                     
REMARK   3      T13:  -0.0098 T23:  -0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5443 L22:   1.0591                                     
REMARK   3      L33:   0.9910 L12:   0.4799                                     
REMARK   3      L13:   0.2435 L23:   0.2070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0270 S12:  -0.0123 S13:   0.0594                       
REMARK   3      S21:  -0.1220 S22:  -0.0728 S23:   0.0869                       
REMARK   3      S31:  -0.0844 S32:  -0.0266 S33:   0.0998                       
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    91        B   140                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.8950  55.8820  33.1010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1782 T22:   0.1157                                     
REMARK   3      T33:   0.3327 T12:  -0.0012                                     
REMARK   3      T13:  -0.1644 T23:  -0.0344                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2202 L22:   5.8746                                     
REMARK   3      L33:   0.5491 L12:   2.6493                                     
REMARK   3      L13:  -0.7253 L23:  -1.5693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0774 S12:   0.0148 S13:   0.0906                       
REMARK   3      S21:  -0.3194 S22:   0.0088 S23:   0.3004                       
REMARK   3      S31:   0.0030 S32:   0.0545 S33:   0.0686                       
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   141        B   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.5030  30.5820  33.8200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0293 T22:   0.0934                                     
REMARK   3      T33:   0.0294 T12:   0.0123                                     
REMARK   3      T13:  -0.0168 T23:  -0.0425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7174 L22:   0.8023                                     
REMARK   3      L33:   0.9708 L12:   0.5201                                     
REMARK   3      L13:   0.6252 L23:   0.4505                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0975 S12:  -0.0881 S13:   0.1069                       
REMARK   3      S21:  -0.0347 S22:  -0.0007 S23:   0.0228                       
REMARK   3      S31:  -0.0166 S32:  -0.0876 S33:   0.0983                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   3   RESIDUES 199-201 IN CHAIN A AND RESIDUES 198-199 IN CHAIN          
REMARK   3    B ARE DISORDERED AND WERE NOT MODELED IN.                         
REMARK   4                                                                      
REMARK   4 4CA1 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-58634.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M-F)               
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72738                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.58                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.06                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.9                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.48                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.50                               
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 4C9Z                                       
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 MM HEPES PH7.0, 1.45 LI2SO4).                                  
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       38.03000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.06000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       66.79500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       38.03000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.06000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       66.79500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       38.03000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       52.06000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       66.79500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       38.03000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       52.06000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       66.79500            
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: 5870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.7 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 A2036   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A2042   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A2060   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A2124   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A2187   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     MET A    90                                                      
REMARK 465     TYR A   199                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     GLY A   201                                                      
REMARK 465     GLY B    88                                                      
REMARK 465     HIS B    89                                                      
REMARK 465     MET B    90                                                      
REMARK 465     LYS B   198                                                      
REMARK 465     TYR B   199                                                      
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   OG B SER A   242     O    HOH A  2114              2.11            
REMARK 500   O    CYS B   282     O    HOH B  2085              2.13            
REMARK 500   O2   SO4 B  1283     O    HOH B  2127              2.20            
REMARK 500   O3   GOL B  1286     O    HOH B  2132              2.09            
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   CE B MET A   281     CE B MET A   281     2655     1.90            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 130   CB B  CYS A 130   SG B   -0.115                       
REMARK 500    ARG B 232   CZ A  ARG B 232   NH1A    0.119                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A 145   CG  -  SD  -  CE  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    ASP A 177   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    LEU A 191   CB  -  CG  -  CD1 ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ARG A 215   CG  -  CD  -  NE  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    MET B 145   CG  -  SD  -  CE  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    LEU B 191   CB  -  CG  -  CD1 ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG B 231   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG B 231   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG B 232   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG B 232   NE  -  CZ  -  NH2 ANGL. DEV. = -10.4 DEGREES          
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    CYS A 256     -179.94   -176.66                                   
REMARK 500    CYS B 256     -178.33   -176.85                                   
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    ILE A 107        22.4      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 105   SG                                                     
REMARK 620 2 CYS A  98   SG  108.2                                              
REMARK 620 3 CYS A 121   SG  112.3 115.3                                        
REMARK 620 4 HIS A 117   NE2 108.3 105.1 107.2                                  
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  98   SG                                                     
REMARK 620 2 CYS B 121   SG  115.7                                              
REMARK 620 3 CYS B 105   SG  110.0 111.1                                        
REMARK 620 4 HIS B 117   NE2 109.5 103.7 106.3                                  
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 135   SG                                                     
REMARK 620 2 CYS A 128   SG  114.2                                              
REMARK 620 3 HIS A 147   NE2 108.4 107.8                                        
REMARK 620 4 HIS A 152   NE2 120.7 106.7  97.1                                  
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 152   NE2                                                    
REMARK 620 2 CYS B 128   SG  105.0                                              
REMARK 620 3 CYS B 135   SG  120.9 114.5                                        
REMARK 620 4 HIS B 147   NE2  97.6 106.3 110.5                                  
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 SO4 A1283                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1284                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1283                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1284                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1285                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1293                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1285                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1287                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1288                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1287                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1288                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1289                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1289                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1291                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1291                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1292                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C9Z   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SIAH1 AT 1.95 A RESOLUTION                     
DBREF  4CA1 A   91   282  UNP    Q8IUQ4   SIAH1_HUMAN     91    282             
DBREF  4CA1 B   91   282  UNP    Q8IUQ4   SIAH1_HUMAN     91    282             
SEQADV 4CA1 GLY A   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4CA1 HIS A   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4CA1 MET A   90  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4CA1 GLY B   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4CA1 HIS B   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4CA1 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    SO4  A1283       5                                                       
HET    SO4  A1284       5                                                       
HET    SO4  B1283       5                                                       
HET    SO4  B1284       5                                                       
HET    SO4  A1285       5                                                       
HET     CL  A1293       1                                                       
HET     CL  B1285       1                                                       
HET     CL  A1286       1                                                       
HET    GOL  B1286       6                                                       
HET    GOL  A1287       6                                                       
HET    GOL  A1288       6                                                       
HET    GOL  B1287       6                                                       
HET    GOL  B1288       6                                                       
HET    GOL  A1289       6                                                       
HET    GOL  B1289       6                                                       
HET    GOL  B1290       6                                                       
HET    GOL  B1291       6                                                       
HET    GOL  A1290       6                                                       
HET    GOL  A1291       6                                                       
HET    GOL  A1292       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   4  GOL    12(C3 H8 O3)                                                 
FORMUL   5   CL    3(CL 1-)                                                     
FORMUL   6   ZN    4(ZN 2+)                                                     
FORMUL   7  HOH   *331(H2 O)                                                    
HELIX    1   1 TYR A  100  GLY A  104  5                                   5    
HELIX    2   2 PRO A  110  CYS A  121  1                                  12    
HELIX    3   3 SER A  140  ASP A  142  5                                   3    
HELIX    4   4 ALA A  143  HIS A  152  1                                  10    
HELIX    5   5 THR A  214  GLU A  219  1                                   6    
HELIX    6   6 ILE A  247  ASN A  253  1                                   7    
HELIX    7   7 THR A  261  ALA A  268  1                                   8    
HELIX    8   8 TYR B  100  GLY B  104  5                                   5    
HELIX    9   9 HIS B  111  CYS B  121  1                                  11    
HELIX   10  10 SER B  140  ASP B  142  5                                   3    
HELIX   11  11 ALA B  143  HIS B  152  1                                  10    
HELIX   12  12 THR B  214  GLU B  219  1                                   6    
HELIX   13  13 ILE B  247  ASN B  253  1                                   7    
HELIX   14  14 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 VAL A 176  CYS A 184  1  O  VAL A 179   N  THR A 156           
SHEET    3  AC 5 PHE A 187  GLU A 197 -1  O  PHE A 187   N  CYS A 184           
SHEET    4  AC 5 GLN A 203  LEU A 211 -1  O  GLN A 204   N  GLN A 196           
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 VAL A 176  CYS A 184  1  O  VAL A 179   N  THR A 156           
SHEET    3  AD 5 PHE A 187  GLU A 197 -1  O  PHE A 187   N  CYS A 184           
SHEET    4  AD 5 GLN A 203  LEU A 211 -1  O  GLN A 204   N  GLN A 196           
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 GLN A 203  LEU A 211 -1  O  VAL A 209   N  ARG A 241           
SHEET    1  AF 8 ASP A 162  ALA A 167  0                                        
SHEET    2  AF 8 LEU A 273  MET A 281 -1  O  LEU A 273   N  ALA A 167           
SHEET    3  AF 8 PHE A 221  GLY A 229 -1  O  ALA A 222   N  SER A 280           
SHEET    4  AF 8 ARG A 232  ALA A 238 -1  O  ARG A 232   N  GLY A 229           
SHEET    5  AF 8 ARG B 232  ALA B 238 -1  O  ARG B 233   N  GLU A 237           
SHEET    6  AF 8 PHE B 221  GLY B 229 -1  O  TYR B 223   N  ALA B 238           
SHEET    7  AF 8 LEU B 273  MET B 281 -1  O  ASN B 276   N  GLU B 226           
SHEET    8  AF 8 ASP B 162  ALA B 167 -1  O  ILE B 163   N  VAL B 277           
SHEET    1  BA 2 LEU B  95  PRO B  97  0                                        
SHEET    2  BA 2 THR B 108  PRO B 110 -1  O  LEU B 109   N  PHE B  96           
SHEET    1  BB 2 TYR B 126  SER B 127  0                                        
SHEET    2  BB 2 GLN B 138  GLY B 139 -1  O  GLY B 139   N  TYR B 126           
SHEET    1  BC 5 THR B 157  GLN B 159  0                                        
SHEET    2  BC 5 VAL B 176  CYS B 184  1  O  MET B 181   N  LEU B 158           
SHEET    3  BC 5 PHE B 187  GLN B 196 -1  O  PHE B 187   N  CYS B 184           
SHEET    4  BC 5 GLN B 204  LEU B 211 -1  O  GLN B 204   N  GLN B 196           
SHEET    5  BC 5 ARG B 241  SER B 242 -1  O  ARG B 241   N  LEU B 211           
SHEET    1  BD 5 THR B 157  GLN B 159  0                                        
SHEET    2  BD 5 VAL B 176  CYS B 184  1  O  MET B 181   N  LEU B 158           
SHEET    3  BD 5 PHE B 187  GLN B 196 -1  O  PHE B 187   N  CYS B 184           
SHEET    4  BD 5 GLN B 204  LEU B 211 -1  O  GLN B 204   N  GLN B 196           
SHEET    5  BD 5 LEU B 257  ASP B 260 -1  O  LEU B 257   N  ALA B 207           
SHEET    1  BE 2 ARG B 241  SER B 242  0                                        
SHEET    2  BE 2 GLN B 204  LEU B 211 -1  O  VAL B 209   N  ARG B 241           
LINK        ZN    ZN A 283                 SG  CYS A 105     1555   1555  2.24  
LINK        ZN    ZN A 283                 SG  CYS A  98     1555   1555  2.25  
LINK        ZN    ZN A 283                 SG  CYS A 121     1555   1555  2.28  
LINK        ZN    ZN A 283                 NE2 HIS A 117     1555   1555  2.13  
LINK        ZN    ZN A 284                 SG  CYS A 135     1555   1555  2.25  
LINK        ZN    ZN A 284                 NE2 HIS A 152     1555   1555  2.04  
LINK        ZN    ZN A 284                 NE2 HIS A 147     1555   1555  2.01  
LINK        ZN    ZN A 284                 SG  CYS A 128     1555   1555  2.23  
LINK        ZN    ZN B 283                 NE2 HIS B 117     1555   1555  1.97  
LINK        ZN    ZN B 283                 SG  CYS B 105     1555   1555  2.36  
LINK        ZN    ZN B 283                 SG  CYS B 121     1555   1555  2.32  
LINK        ZN    ZN B 283                 SG  CYS B  98     1555   1555  2.28  
LINK        ZN    ZN B 284                 SG  CYS B 128     1555   1555  2.25  
LINK        ZN    ZN B 284                 SG  CYS B 135     1555   1555  2.25  
LINK        ZN    ZN B 284                 NE2 HIS B 147     1555   1555  1.98  
LINK        ZN    ZN B 284                 NE2 HIS B 152     1555   1555  1.85  
CISPEP   1 PRO A  131    GLY A  132          0        -7.85                     
CISPEP   2 PRO B  131    GLY B  132          0       -10.94                     
SITE     1 AC1  5 CYS A  98  CYS A 105  HIS A 117  CYS A 121                    
SITE     2 AC1  5 HOH A2010                                                     
SITE     1 AC2  4 CYS A 128  CYS A 135  HIS A 147  HIS A 152                    
SITE     1 AC3  4 CYS B  98  CYS B 105  HIS B 117  CYS B 121                    
SITE     1 AC4  4 CYS B 128  CYS B 135  HIS B 147  HIS B 152                    
SITE     1 AC5  9 ARG A 124  TYR A 126  THR A 214  ARG A 215                    
SITE     2 AC5  9 HOH A2114  HOH A2116  HOH A2162  HOH A2192                    
SITE     3 AC5  9 HOH A2193                                                     
SITE     1 AC6  7 HIS A 244  HOH A2194  TRP B 137  HIS B 147                    
SITE     2 AC6  7 HIS B 150  GLN B 151  HOH B2027                               
SITE     1 AC7  4 ASN B 220  ASN B 270  HOH B2086  HOH B2127                    
SITE     1 AC8  7 ARG B 124  TYR B 126  THR B 214  ARG B 215                    
SITE     2 AC8  7 HIS B 244  HOH B2082  HOH B2084                               
SITE     1 AC9  6 GLN A 151  HIS A 152  LYS A 153  SER A 154                    
SITE     2 AC9  6 HOH A2029  HOH A2058                                          
SITE     1 BC1  1 HOH A2152                                                     
SITE     1 BC2  3 TYR B 100  HIS B 244  HOH B2015                               
SITE     1 BC3  1 ARG A 232                                                     
SITE     1 BC4  4 HOH A2127  ARG B 231  HOH B2132  HOH B2133                    
SITE     1 BC5  9 GLY A 246  ILE A 247  ALA A 248  HOH A2028                    
SITE     2 BC5  9 HOH A2163  HOH A2164  HOH A2166  HOH A2195                    
SITE     3 BC5  9 MET B 149                                                     
SITE     1 BC6  7 ASN A 228  GLY A 229  HIS A 230  LEU A 266                    
SITE     2 BC6  7 PHE A 267  ALA A 268  GLU A 269                               
SITE     1 BC7  8 ASN B 228  HIS B 230  LEU B 266  PHE B 267                    
SITE     2 BC7  8 ALA B 268  GLU B 269  HOH B2098  HOH B2103                    
SITE     1 BC8  4 PRO B 129  GLY B 246  ILE B 247  ALA B 248                    
SITE     1 BC9  3 ARG A 231  GLU B 237  ALA B 238                               
SITE     1 CC1  8 PHE B 187  GLN B 217  ASN B 220  PHE B 221                    
SITE     2 CC1  8 GLN B 265  HOH B2057  HOH B2086  HOH B2134                    
SITE     1 CC2  3 HIS B 152  LYS B 153  SER B 154                               
SITE     1 CC3  7 SER B  93  VAL B  94  PHE B  96  PRO B 110                    
SITE     2 CC3  7 HIS B 111  HOH B2009  HOH B2135                               
SITE     1 CC4  2 ARG A 224  HOH A2196                                          
SITE     1 CC5  5 GLU A 161  PHE A 185  GLY A 186  PHE A 187                    
SITE     2 CC5  5 HOH A2099                                                     
SITE     1 CC6  6 THR A 168  VAL A 176  ASP A 177  TRP A 178                    
SITE     2 CC6  6 HOH A2091  HOH A2093                                          
CRYST1   76.060  104.120  133.590  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      0.013148  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009604  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007486        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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