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Database: PDB
Entry: 2A25
LinkDB: 2A25
Original site: 2A25 
HEADER    LIGASE                                  21-JUN-05   2A25              
TITLE     CRYSTAL STRUCTURE OF SIAH1 SBD BOUND TO THE PEPTIDE EKPAAVVAPITTG FROM
TITLE    2 SIP                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN LIGASE SIAH1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SUBSTRATE BINDING DOMAIN (RESIDUES 90-282);                
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: CALCYCLIN-BINDING PROTEIN PEPTIDE;                         
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: CACYBP, HCACYBP, SIAH-INTERACTING PROTEIN, S100A6-BINDING   
COMPND  12 PROTEIN, PNAS-107;                                                   
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: SIAH BINDING MOTIF                                    
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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE  
SOURCE  14 OF THE PEPTIDE CAN BE NATURALLY FOUND IN HOMO SAPIENS (HUMAN)        
KEYWDS    PROTEIN-PEPTIDE COMPLEX, LIGASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.SANTELLI,M.LEONE,C.LI,T.FUKUSHIMA,N.E.PREECE,A.J.OLSON,K.R.ELY,     
AUTHOR   2 J.C.REED,M.PELLECCHIA,R.C.LIDDINGTON,S.MATSUZAWA                     
REVDAT   4   13-JUL-11 2A25    1       VERSN                                    
REVDAT   3   24-FEB-09 2A25    1       VERSN                                    
REVDAT   2   18-OCT-05 2A25    1       JRNL                                     
REVDAT   1   09-AUG-05 2A25    0                                                
JRNL        AUTH   E.SANTELLI,M.LEONE,C.LI,T.FUKUSHIMA,N.E.PREECE,A.J.OLSON,    
JRNL        AUTH 2 K.R.ELY,J.C.REED,M.PELLECCHIA,R.C.LIDDINGTON,S.MATSUZAWA     
JRNL        TITL   STRUCTURAL ANALYSIS OF SIAH1-SIAH-INTERACTING PROTEIN        
JRNL        TITL 2 INTERACTIONS AND INSIGHTS INTO THE ASSEMBLY OF AN E3 LIGASE  
JRNL        TITL 3 MULTIPROTEIN COMPLEX                                         
JRNL        REF    J.BIOL.CHEM.                  V. 280 34278 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16085652                                                     
JRNL        DOI    10.1074/JBC.M506707200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 10527                          
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 524                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1392                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1219                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 100                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 39.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.66000                                             
REMARK   3    B22 (A**2) : 1.36000                                              
REMARK   3    B33 (A**2) : 0.30000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.253         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.205         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.140         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.472         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1249 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1683 ; 1.554 ; 1.928       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   150 ; 6.167 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   191 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   927 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   524 ; 0.217 ; 0.200       
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):    84 ; 0.239 ; 0.200       
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):    40 ; 0.211 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.133 ; 0.200       
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):   771 ; 1.084 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1241 ; 1.960 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   478 ; 3.420 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   442 ; 5.144 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   125        A   282                          
REMARK   3    RESIDUE RANGE :   A   601        A   601                          
REMARK   3    RESIDUE RANGE :   B    59        B    67                          
REMARK   3    RESIDUE RANGE :   A   602        A   691                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6082  38.1424   8.8587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0910 T22:   0.0020                                     
REMARK   3      T33:   0.1279 T12:   0.0131                                     
REMARK   3      T13:   0.0107 T23:   0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0570 L22:   3.1063                                     
REMARK   3      L33:   6.0939 L12:   0.5473                                     
REMARK   3      L13:   3.4563 L23:  -0.6595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:  -0.2343 S13:  -0.6125                       
REMARK   3      S21:  -0.2312 S22:   0.1068 S23:  -0.0205                       
REMARK   3      S31:   0.1452 S32:  -0.3148 S33:  -0.1012                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2A25 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033397.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10567                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -4.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.04300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
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: PDB ENTRY 1K2F CHAIN A                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM DIHYDROGEN PHOSPAHTE, DI-         
REMARK 280  POTASSIUM HYDROGEN PHOSPHATE, DITHIOTHREITHOL, PH 6.0, VAPOR        
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
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                                         
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       39.20700            
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       39.20700            
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       23.81750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.88050            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       23.81750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.88050            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.20700            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       23.81750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       53.88050            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       39.20700            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       23.81750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       53.88050            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED      
REMARK 300 BY THE TWO FOLD AXIS:  1-X, Y, 1/2-Z                                 
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       47.63500            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       39.20700            
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     VAL A    90                                                      
REMARK 465     ALA A    91                                                      
REMARK 465     ASN A    92                                                      
REMARK 465     SER A    93                                                      
REMARK 465     VAL A    94                                                      
REMARK 465     LEU A    95                                                      
REMARK 465     PHE A    96                                                      
REMARK 465     PRO A    97                                                      
REMARK 465     CYS A    98                                                      
REMARK 465     LYS A    99                                                      
REMARK 465     TYR A   100                                                      
REMARK 465     ALA A   101                                                      
REMARK 465     SER A   102                                                      
REMARK 465     SER A   103                                                      
REMARK 465     GLY A   104                                                      
REMARK 465     CYS A   105                                                      
REMARK 465     GLU A   106                                                      
REMARK 465     ILE A   107                                                      
REMARK 465     THR A   108                                                      
REMARK 465     LEU A   109                                                      
REMARK 465     PRO A   110                                                      
REMARK 465     HIS A   111                                                      
REMARK 465     THR A   112                                                      
REMARK 465     GLU A   113                                                      
REMARK 465     LYS A   114                                                      
REMARK 465     ALA A   115                                                      
REMARK 465     ASP A   116                                                      
REMARK 465     HIS A   117                                                      
REMARK 465     GLU A   118                                                      
REMARK 465     GLU A   119                                                      
REMARK 465     LEU A   120                                                      
REMARK 465     CYS A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     PHE A   123                                                      
REMARK 465     ARG A   124                                                      
REMARK 465     GLY A   132                                                      
REMARK 465     ALA A   133                                                      
REMARK 465     LEU A   172                                                      
REMARK 465     PRO A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     ALA A   175                                                      
REMARK 465     GLU A   197                                                      
REMARK 465     LYS A   198                                                      
REMARK 465     TYR A   199                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     GLY A   201                                                      
REMARK 465     HIS A   202                                                      
REMARK 465     GLU B    58                                                      
REMARK 465     THR B    68                                                      
REMARK 465     THR B    69                                                      
REMARK 465     GLY B    70                                                      
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   O    HOH A   629     O    HOH A   684              1.84            
REMARK 500   O    HOH A   626     O    HOH A   666              1.99            
REMARK 500   O    HOH A   605     O    HOH A   652              2.01            
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    ASP A 177   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 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    ILE A 170        5.51    -68.93                                   
REMARK 500    HIS A 230      102.16    -58.59                                   
REMARK 500    CYS A 256     -174.82   -178.85                                   
REMARK 500    GLU A 269     -104.92    -69.40                                   
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 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 128   SG                                                     
REMARK 620 2 CYS A 135   SG  111.1                                              
REMARK 620 3 HIS A 147   NE2 109.6 113.0                                        
REMARK 620 4 HIS A 152   NE2 100.7 120.0 101.4                                  
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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1K2F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2A26   RELATED DB: PDB                                   
DBREF  2A25 A   90   282  UNP    Q8IUQ4   SIAH1_HUMAN     90    282             
DBREF  2A25 B   58    70  UNP    Q9HB71   CYBP_HUMAN      58     70             
SEQRES   1 A  193  VAL 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   13  GLU LYS PRO ALA ALA VAL VAL ALA PRO ILE THR THR GLY          
HET     ZN  A 601       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  HOH   *100(H2 O)                                                    
HELIX    1   1 ALA A  143  HIS A  152  1                                  10    
HELIX    2   2 THR A  214  GLU A  219  1                                   6    
HELIX    3   3 ILE A  247  ASN A  253  1                                   7    
HELIX    4   4 THR A  261  ALA A  268  1                                   8    
SHEET    1   A 2 TYR A 126  SER A 127  0                                        
SHEET    2   A 2 GLN A 138  GLY A 139 -1  O  GLY A 139   N  TYR A 126           
SHEET    1   B 5 THR A 157  GLN A 159  0                                        
SHEET    2   B 5 ASP A 177  CYS A 184  1  O  SER A 183   N  LEU A 158           
SHEET    3   B 5 PHE A 187  LYS A 195 -1  O  LEU A 191   N  MET A 180           
SHEET    4   B 5 GLN A 204  LEU A 211 -1  O  PHE A 206   N  GLU A 194           
SHEET    5   B 5 ARG A 241  SER A 242  1  O  ARG A 241   N  LEU A 211           
SHEET    1   C 5 THR A 157  GLN A 159  0                                        
SHEET    2   C 5 ASP A 177  CYS A 184  1  O  SER A 183   N  LEU A 158           
SHEET    3   C 5 PHE A 187  LYS A 195 -1  O  LEU A 191   N  MET A 180           
SHEET    4   C 5 GLN A 204  LEU A 211 -1  O  PHE A 206   N  GLU A 194           
SHEET    5   C 5 LEU A 257  ASP A 260 -1  O  PHE A 259   N  PHE A 205           
SHEET    1   D 5 ARG A 232  ALA A 238  0                                        
SHEET    2   D 5 PHE A 221  GLY A 229 -1  N  LEU A 227   O  LEU A 234           
SHEET    3   D 5 ASN A 272  MET A 281 -1  O  ASN A 276   N  GLU A 226           
SHEET    4   D 5 ASP A 162  THR A 168 -1  N  PHE A 165   O  ILE A 275           
SHEET    5   D 5 ALA B  61  VAL B  64  1  O  ALA B  62   N  LEU A 166           
LINK         SG  CYS A 128                ZN    ZN A 601     1555   1555  2.28  
LINK         SG  CYS A 135                ZN    ZN A 601     1555   1555  2.29  
LINK         NE2 HIS A 147                ZN    ZN A 601     1555   1555  2.05  
LINK         NE2 HIS A 152                ZN    ZN A 601     1555   1555  2.08  
SITE     1 AC1  4 CYS A 128  CYS A 135  HIS A 147  HIS A 152                    
CRYST1   47.635  107.761   78.414  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020993  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009280  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012753        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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