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Database: PDB
Entry: 4X3G
LinkDB: 4X3G
Original site: 4X3G 
HEADER    LIGASE                                  28-NOV-14   4X3G              
TITLE     CRYSTAL STRUCTURE OF SIAH1 SINA DOMAIN IN COMPLEX WITH A USP19 PEPTIDE
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE SIAH1;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SINA DOMAIN, RESIDUES 91-282;                              
COMPND   5 SYNONYM: SEVEN IN ABSENTIA HOMOLOG 1,SIAH-1,SIAH-1A;                 
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 19;                  
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 FRAGMENT: SIAH1 BINDING MOTIF (SBM), RESIDUES 461-474;               
COMPND  12 SYNONYM: DEUBIQUITINATING ENZYME 19,UBIQUITIN THIOESTERASE 19,       
COMPND  13 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE 19,ZINC FINGER MYND DOMAIN-   
COMPND  14 CONTAINING PROTEIN 9;                                                
COMPND  15 EC: 3.4.19.12;                                                       
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SIAH1, HUMSIAH;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: V2R-PRARE2;                               
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28-MHL;                                
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606                                                 
KEYWDS    LIGASE, UBIQUITIN-PROTEIN LIGASE, HYDROLASE, UBIQUITIN SPECIFIC       
KEYWDS   2 PROTEASE, PROTEIN-PEPTIDE COMPLEX, SGC                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.WALKER,A.DONG,Q.ZHANG,X.HUANG,Y.LI,C.BOUNTRA,A.M.EDWARDS,         
AUTHOR   2 C.H.ARROWSMITH,Y.TONG,STRUCTURAL GENOMICS CONSORTIUM (SGC)           
REVDAT   3   24-JAN-18 4X3G    1       JRNL   REMARK                            
REVDAT   2   27-APR-16 4X3G    1       REMARK DBREF1 SHEET  ATOM                
REVDAT   1   31-DEC-14 4X3G    0                                                
JRNL        AUTH   J.R.WALKER,A.DONG,Q.ZHANG,X.HUANG,Y.LI,C.BOUNTRA,            
JRNL        AUTH 2 A.M.EDWARDS,C.H.ARROWSMITH,Y.TONG,                           
JRNL        AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   CRYSTAL STRUCTURE OF SIAH1 SINA DOMAIN IN COMPLEX WITH A     
JRNL        TITL 2 USP19 PEPTIDE                                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT BUSTER 2.10.0                             
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 15802                          
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)  : 0.223                          
REMARK   3   R VALUE            (WORKING SET)  : 0.222                          
REMARK   3   FREE R VALUE                      : 0.251                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.940                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 780                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 8                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.34                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.50                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 89.68                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2173                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2350                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2074                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2334                   
REMARK   3   BIN FREE R VALUE                        : 0.2700                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.56                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 99                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3079                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 56                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.92                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.77680                                              
REMARK   3    B22 (A**2) : -19.35440                                            
REMARK   3    B33 (A**2) : 14.57760                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.85720                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.500               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.508               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.265               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.540               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.271               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3190   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4335   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1068   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 77     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 464    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3190   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 4      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 429    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3399   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.95                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.97                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.94                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|91 - A|602 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):    1.1113    1.3490    8.9114           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1890 T22:    0.2088                                    
REMARK   3     T33:   -0.2220 T12:    0.0877                                    
REMARK   3     T13:    0.0554 T23:    0.0270                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5397 L22:    3.5326                                    
REMARK   3     L33:    1.0883 L12:    0.7306                                    
REMARK   3     L13:   -0.1151 L23:   -0.9236                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0894 S12:    0.5033 S13:    0.1379                     
REMARK   3     S21:   -0.1022 S22:    0.3811 S23:   -0.0983                     
REMARK   3     S31:   -0.0781 S32:   -0.3051 S33:   -0.2917                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|93 - B|602 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):    4.6407  -32.1396   20.7236           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1227 T22:    0.0658                                    
REMARK   3     T33:   -0.2069 T12:   -0.2242                                    
REMARK   3     T13:    0.0648 T23:    0.0391                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8854 L22:    3.7359                                    
REMARK   3     L33:    2.9621 L12:    1.0955                                    
REMARK   3     L13:    0.9953 L23:   -1.2797                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0252 S12:   -0.1945 S13:   -0.2247                     
REMARK   3     S21:   -0.3883 S22:    0.0574 S23:   -0.4302                     
REMARK   3     S31:    0.7702 S32:   -0.6147 S33:   -0.0322                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4X3G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205000.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15818                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 58.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4I7B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SIAH1 AT 17.6 MG/ML WAS MIXED WITH A     
REMARK 280  TWO-FOLD EXCESS OF USP19 PEPTIDE ON ICE FOR 30 MIN. BEFORE          
REMARK 280  SETTING UP FOR CRYSTALLIZATION. CRYSTALS WERE GROWN AT 298K         
REMARK 280  USING THE SITTING DROP METHOD BY MIXING 0.5 UL PROTEIN:PEPTIDE      
REMARK 280  MIX WITH 0.5 UL WELL SOLUTION CONSISTING OF 20% PEG6000, 0.1 M      
REMARK 280  BICINE PH 9.0. THE CRYSTALS WERE CRYOPROTECTED BY FIRST             
REMARK 280  IMMERSION IN WELL SOLUTION MIXED WITH 15% (FINAL) ETHYLENE          
REMARK 280  GLYCOL, THEN IMMERSION IN N-PARATONE., VAPOR DIFFUSION, SITTING     
REMARK 280  DROP                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       44.04600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    90                                                      
REMARK 465     GLY A   132                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     GLY A   201                                                      
REMARK 465     HIS A   202                                                      
REMARK 465     GLY B    90                                                      
REMARK 465     ALA B    91                                                      
REMARK 465     ASN B    92                                                      
REMARK 465     SER C   461                                                      
REMARK 465     HIS C   473                                                      
REMARK 465     SER C   474                                                      
REMARK 465     SER D   461                                                      
REMARK 465     PRO D   462                                                      
REMARK 465     HIS D   473                                                      
REMARK 465     SER D   474                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  92    CG   OD1  ND2                                       
REMARK 470     LYS A  99    CD   CE   NZ                                        
REMARK 470     LYS A 136    NZ                                                  
REMARK 470     LYS A 153    CG   CD   CE   NZ                                   
REMARK 470     TYR A 199    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 216    CG   CD   CE   NZ                                   
REMARK 470     LEU B 109    CG   CD1  CD2                                       
REMARK 470     GLU B 113    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 119    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 150    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B 200    CG   OD1  OD2                                       
REMARK 470     LYS B 216    CG   CD   CE   NZ                                   
REMARK 470     HIS B 230    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B 231    CD   NE   CZ   NH1  NH2                             
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    ASN A  92      -11.66     62.68                                   
REMARK 500    CYS A 256     -178.33   -170.28                                   
REMARK 500    ASP A 260     -164.38   -107.74                                   
REMARK 500    TYR B 100       33.53    -98.10                                   
REMARK 500    ASP B 255       55.56    -91.06                                   
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 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  98   SG                                                     
REMARK 620 2 CYS A 105   SG  111.1                                              
REMARK 620 3 HIS A 117   NE2 117.2  99.6                                        
REMARK 620 4 CYS A 121   SG  108.4 119.2 101.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 128   SG                                                     
REMARK 620 2 CYS A 135   SG  109.7                                              
REMARK 620 3 HIS A 147   NE2  90.9 109.3                                        
REMARK 620 4 HIS A 152   NE2 115.7 127.9  94.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  98   SG                                                     
REMARK 620 2 CYS B 105   SG  111.0                                              
REMARK 620 3 HIS B 117   NE2 112.4 101.9                                        
REMARK 620 4 CYS B 121   SG  126.7 105.5  95.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 128   SG                                                     
REMARK 620 2 CYS B 135   SG  101.8                                              
REMARK 620 3 HIS B 147   NE2 110.3 101.6                                        
REMARK 620 4 HIS B 152   NE2 112.1 104.5 123.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 602                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C9Z   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN DOMAIN AS CHAINS A AND B.                               
DBREF  4X3G A   91   282  UNP    Q8IUQ4   SIAH1_HUMAN     91    282             
DBREF  4X3G B   91   282  UNP    Q8IUQ4   SIAH1_HUMAN     91    282             
DBREF  4X3G C  461   474  UNP    O94966   UBP19_HUMAN    461    474             
DBREF  4X3G D  461   474  UNP    O94966   UBP19_HUMAN    461    474             
SEQADV 4X3G GLY A   90  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4X3G GLY B   90  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQRES   1 A  193  GLY ALA ASN SER VAL LEU PHE PRO CYS LYS TYR ALA SER          
SEQRES   2 A  193  SER GLY CYS GLU ILE THR LEU PRO HIS THR GLU LYS ALA          
SEQRES   3 A  193  ASP HIS GLU GLU LEU CYS GLU PHE ARG PRO TYR SER CYS          
SEQRES   4 A  193  PRO CYS PRO GLY ALA SER CYS LYS TRP GLN GLY SER LEU          
SEQRES   5 A  193  ASP ALA VAL MET PRO HIS LEU MET HIS GLN HIS LYS SER          
SEQRES   6 A  193  ILE THR THR LEU GLN GLY GLU ASP ILE VAL PHE LEU ALA          
SEQRES   7 A  193  THR ASP ILE ASN LEU PRO GLY ALA VAL ASP TRP VAL MET          
SEQRES   8 A  193  MET GLN SER CYS PHE GLY PHE HIS PHE MET LEU VAL LEU          
SEQRES   9 A  193  GLU LYS GLN GLU LYS TYR ASP GLY HIS GLN GLN PHE PHE          
SEQRES  10 A  193  ALA ILE VAL GLN LEU ILE GLY THR ARG LYS GLN ALA GLU          
SEQRES  11 A  193  ASN PHE ALA TYR ARG LEU GLU LEU ASN GLY HIS ARG ARG          
SEQRES  12 A  193  ARG LEU THR TRP GLU ALA THR PRO ARG SER ILE HIS GLU          
SEQRES  13 A  193  GLY ILE ALA THR ALA ILE MET ASN SER ASP CYS LEU VAL          
SEQRES  14 A  193  PHE ASP THR SER ILE ALA GLN LEU PHE ALA GLU ASN GLY          
SEQRES  15 A  193  ASN LEU GLY ILE ASN VAL THR ILE SER MET CYS                  
SEQRES   1 B  193  GLY ALA ASN SER VAL LEU PHE PRO CYS LYS TYR ALA SER          
SEQRES   2 B  193  SER GLY CYS GLU ILE THR LEU PRO HIS THR GLU LYS ALA          
SEQRES   3 B  193  ASP HIS GLU GLU LEU CYS GLU PHE ARG PRO TYR SER CYS          
SEQRES   4 B  193  PRO CYS PRO GLY ALA SER CYS LYS TRP GLN GLY SER LEU          
SEQRES   5 B  193  ASP ALA VAL MET PRO HIS LEU MET HIS GLN HIS LYS SER          
SEQRES   6 B  193  ILE THR THR LEU GLN GLY GLU ASP ILE VAL PHE LEU ALA          
SEQRES   7 B  193  THR ASP ILE ASN LEU PRO GLY ALA VAL ASP TRP VAL MET          
SEQRES   8 B  193  MET GLN SER CYS PHE GLY PHE HIS PHE MET LEU VAL LEU          
SEQRES   9 B  193  GLU LYS GLN GLU LYS TYR ASP GLY HIS GLN GLN PHE PHE          
SEQRES  10 B  193  ALA ILE VAL GLN LEU ILE GLY THR ARG LYS GLN ALA GLU          
SEQRES  11 B  193  ASN PHE ALA TYR ARG LEU GLU LEU ASN GLY HIS ARG ARG          
SEQRES  12 B  193  ARG LEU THR TRP GLU ALA THR PRO ARG SER ILE HIS GLU          
SEQRES  13 B  193  GLY ILE ALA THR ALA ILE MET ASN SER ASP CYS LEU VAL          
SEQRES  14 B  193  PHE ASP THR SER ILE ALA GLN LEU PHE ALA GLU ASN GLY          
SEQRES  15 B  193  ASN LEU GLY ILE ASN VAL THR ILE SER MET CYS                  
SEQRES   1 C   14  SER PRO LYS PRO THR CYS MET VAL PRO PRO MET PRO HIS          
SEQRES   2 C   14  SER                                                          
SEQRES   1 D   14  SER PRO LYS PRO THR CYS MET VAL PRO PRO MET PRO HIS          
SEQRES   2 D   14  SER                                                          
HET     ZN  A 601       1                                                       
HET     ZN  A 602       1                                                       
HET     ZN  B 601       1                                                       
HET     ZN  B 602       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   9  HOH   *56(H2 O)                                                     
HELIX    1 AA1 HIS A  111  CYS A  121  1                                  11    
HELIX    2 AA2 SER A  140  ASP A  142  5                                   3    
HELIX    3 AA3 ALA A  143  HIS A  152  1                                  10    
HELIX    4 AA4 THR A  214  GLU A  219  1                                   6    
HELIX    5 AA5 ILE A  247  ASN A  253  1                                   7    
HELIX    6 AA6 THR A  261  PHE A  267  1                                   7    
HELIX    7 AA7 PRO B  110  GLU B  119  1                                  10    
HELIX    8 AA8 SER B  140  ASP B  142  5                                   3    
HELIX    9 AA9 ALA B  143  GLN B  151  1                                   9    
HELIX   10 AB1 THR B  214  GLU B  219  1                                   6    
HELIX   11 AB2 ILE B  247  ASN B  253  1                                   7    
HELIX   12 AB3 THR B  261  ALA B  268  1                                   8    
SHEET    1 AA1 2 LEU A  95  PRO A  97  0                                        
SHEET    2 AA1 2 THR A 108  PRO A 110 -1  O  LEU A 109   N  PHE A  96           
SHEET    1 AA2 2 TYR A 126  SER A 127  0                                        
SHEET    2 AA2 2 GLN A 138  GLY A 139 -1  O  GLY A 139   N  TYR A 126           
SHEET    1 AA3 5 THR A 157  GLN A 159  0                                        
SHEET    2 AA3 5 ASP A 177  CYS A 184  1  O  SER A 183   N  LEU A 158           
SHEET    3 AA3 5 PHE A 187  GLN A 196 -1  O  LEU A 193   N  TRP A 178           
SHEET    4 AA3 5 GLN A 204  LEU A 211 -1  O  GLN A 204   N  GLN A 196           
SHEET    5 AA3 5 ARG A 241  SER A 242  1  O  ARG A 241   N  LEU A 211           
SHEET    1 AA4 5 THR A 157  GLN A 159  0                                        
SHEET    2 AA4 5 ASP A 177  CYS A 184  1  O  SER A 183   N  LEU A 158           
SHEET    3 AA4 5 PHE A 187  GLN A 196 -1  O  LEU A 193   N  TRP A 178           
SHEET    4 AA4 5 GLN A 204  LEU A 211 -1  O  GLN A 204   N  GLN A 196           
SHEET    5 AA4 5 LEU A 257  ASP A 260 -1  O  PHE A 259   N  PHE A 205           
SHEET    1 AA5 4 ALA A 268  GLU A 269  0                                        
SHEET    2 AA5 4 ASN A 272  MET A 281 -1  O  ASN A 272   N  GLU A 269           
SHEET    3 AA5 4 ASP A 162  THR A 168 -1  N  PHE A 165   O  ILE A 275           
SHEET    4 AA5 4 THR C 465  VAL C 468  1  O  VAL C 468   N  LEU A 166           
SHEET    1 AA6 9 ALA A 268  GLU A 269  0                                        
SHEET    2 AA6 9 ASN A 272  MET A 281 -1  O  ASN A 272   N  GLU A 269           
SHEET    3 AA6 9 PHE A 221  GLY A 229 -1  N  GLU A 226   O  ASN A 276           
SHEET    4 AA6 9 ARG A 232  ALA A 238 -1  O  TRP A 236   N  LEU A 225           
SHEET    5 AA6 9 ARG B 232  ALA B 238 -1  O  THR B 235   N  THR A 235           
SHEET    6 AA6 9 PHE B 221  ASN B 228 -1  N  LEU B 225   O  TRP B 236           
SHEET    7 AA6 9 LEU B 273  MET B 281 -1  O  SER B 280   N  ALA B 222           
SHEET    8 AA6 9 ASP B 162  ALA B 167 -1  N  PHE B 165   O  ILE B 275           
SHEET    9 AA6 9 THR D 465  VAL D 468  1  O  VAL D 468   N  LEU B 166           
SHEET    1 AA7 2 PHE B  96  PRO B  97  0                                        
SHEET    2 AA7 2 THR B 108  LEU B 109 -1  O  LEU B 109   N  PHE B  96           
SHEET    1 AA8 2 TYR B 126  SER B 127  0                                        
SHEET    2 AA8 2 GLN B 138  GLY B 139 -1  O  GLY B 139   N  TYR B 126           
SHEET    1 AA9 5 THR B 157  GLN B 159  0                                        
SHEET    2 AA9 5 VAL B 176  CYS B 184  1  O  SER B 183   N  LEU B 158           
SHEET    3 AA9 5 PHE B 187  TYR B 199 -1  O  LYS B 195   N  VAL B 176           
SHEET    4 AA9 5 HIS B 202  LEU B 211 -1  O  GLN B 204   N  GLN B 196           
SHEET    5 AA9 5 ARG B 241  SER B 242  1  O  ARG B 241   N  LEU B 211           
SHEET    1 AB1 5 THR B 157  GLN B 159  0                                        
SHEET    2 AB1 5 VAL B 176  CYS B 184  1  O  SER B 183   N  LEU B 158           
SHEET    3 AB1 5 PHE B 187  TYR B 199 -1  O  LYS B 195   N  VAL B 176           
SHEET    4 AB1 5 HIS B 202  LEU B 211 -1  O  GLN B 204   N  GLN B 196           
SHEET    5 AB1 5 LEU B 257  ASP B 260 -1  O  PHE B 259   N  PHE B 205           
LINK         SG  CYS A  98                ZN    ZN A 602     1555   1555  2.46  
LINK         SG  CYS A 105                ZN    ZN A 602     1555   1555  2.17  
LINK         NE2 HIS A 117                ZN    ZN A 602     1555   1555  2.66  
LINK         SG  CYS A 121                ZN    ZN A 602     1555   1555  2.19  
LINK         SG  CYS A 128                ZN    ZN A 601     1555   1555  2.17  
LINK         SG  CYS A 135                ZN    ZN A 601     1555   1555  2.40  
LINK         NE2 HIS A 147                ZN    ZN A 601     1555   1555  2.29  
LINK         NE2 HIS A 152                ZN    ZN A 601     1555   1555  1.92  
LINK         SG  CYS B  98                ZN    ZN B 602     1555   1555  2.32  
LINK         SG  CYS B 105                ZN    ZN B 602     1555   1555  2.34  
LINK         NE2 HIS B 117                ZN    ZN B 602     1555   1555  2.58  
LINK         SG  CYS B 121                ZN    ZN B 602     1555   1555  2.33  
LINK         SG  CYS B 128                ZN    ZN B 601     1555   1555  2.46  
LINK         SG  CYS B 135                ZN    ZN B 601     1555   1555  2.27  
LINK         NE2 HIS B 147                ZN    ZN B 601     1555   1555  2.23  
LINK         NE2 HIS B 152                ZN    ZN B 601     1555   1555  1.93  
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                    
CRYST1   41.343   88.092   59.590  90.00 103.24  90.00 P 1 21 1      4          
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      0.024188  0.000000  0.005691        0.00000                         
SCALE2      0.000000  0.011352  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017240        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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