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Database: PDB
Entry: 2PUY
LinkDB: 2PUY
Original site: 2PUY 
HEADER    TRANSCRIPTION                           09-MAY-07   2PUY              
TITLE     CRYSTAL STRUCTURE OF THE BHC80 PHD FINGER                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHD FINGER PROTEIN 21A;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PHD FINGER RESIDUES: 486-543;                              
COMPND   5 SYNONYM: BRAF35-HDAC COMPLEX PROTEIN BHC80, BHC80A;                  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HISTONE H3;                                                
COMPND   9 CHAIN: E;                                                            
COMPND  10 FRAGMENT: H3 1-10;                                                   
COMPND  11 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: PHF21A, BHC80, KIAA1696;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SYNTHESIZED PEPTIDE                                   
KEYWDS    PHD FINGER, HISTONE CODE, BRAF-HDAC COMPLEX, TRANSCRIPTION            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.HORTON,X.CHENG,R.E.COLLINS                                        
REVDAT   4   21-FEB-24 2PUY    1       REMARK SEQADV LINK                       
REVDAT   3   24-FEB-09 2PUY    1       VERSN                                    
REVDAT   2   20-NOV-07 2PUY    1       JRNL                                     
REVDAT   1   14-AUG-07 2PUY    0                                                
JRNL        AUTH   F.LAN,R.E.COLLINS,R.DE CEGLI,R.ALPATOV,J.R.HORTON,X.SHI,     
JRNL        AUTH 2 O.GOZANI,X.CHENG,Y.SHI                                       
JRNL        TITL   RECOGNITION OF UNMETHYLATED HISTONE H3 LYSINE 4 LINKS BHC80  
JRNL        TITL 2 TO LSD1-MEDIATED GENE REPRESSION.                            
JRNL        REF    NATURE                        V. 448   718 2007              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   17687328                                                     
JRNL        DOI    10.1038/NATURE06034                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -3.000                         
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23287                          
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 SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1114                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.43                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.47                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1890                       
REMARK   3   BIN FREE R VALUE                    : 0.2080                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 98                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1018                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.84000                                              
REMARK   3    B22 (A**2) : -0.15000                                             
REMARK   3    B33 (A**2) : -0.69000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.41000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : -0.0                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 40.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.18                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.900                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2PUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000042800.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 173                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97917, 1.28295, 1.28341          
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23287                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ISOPROPANOL, 5-10% POLYETHYLENE      
REMARK 280  GLYCOL 4000, 100MM MES 6.2-6.5, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 289K, PH 6.5                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       39.75550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       12.69300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       39.75550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       12.69300            
REMARK 290   SMTRY3   4  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 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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
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 B  43  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     HIS A   484                                                      
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     GLU A 541    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 543    CG1  CG2  CD1                                       
REMARK 470     GLU B 541    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 543    CG1  CG2  CD1                                       
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 355  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 491   SG                                                     
REMARK 620 2 CYS A 494   SG  113.1                                              
REMARK 620 3 HIS A 511   ND1 101.5  95.4                                        
REMARK 620 4 CYS A 514   SG  115.0 114.5 115.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 356  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 503   SG                                                     
REMARK 620 2 CYS A 506   SG  112.1                                              
REMARK 620 3 CYS A 529   SG  107.9 108.0                                        
REMARK 620 4 CYS A 532   SG  110.9 103.7 114.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 357  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 491   SG                                                     
REMARK 620 2 CYS B 494   SG  111.0                                              
REMARK 620 3 HIS B 511   ND1 102.9  94.2                                        
REMARK 620 4 CYS B 514   SG  112.4 118.5 115.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 358  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 503   SG                                                     
REMARK 620 2 CYS B 506   SG  113.5                                              
REMARK 620 3 CYS B 529   SG  106.0 108.6                                        
REMARK 620 4 CYS B 532   SG  111.3 103.2 114.5                                  
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 355                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 356                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 357                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 358                  
DBREF  2PUY A  486   543  UNP    Q96BD5   PF21A_HUMAN    486    543             
DBREF  2PUY B  486   543  UNP    Q96BD5   PF21A_HUMAN    486    543             
DBREF  2PUY E    1    10  UNP    P61836   H3_ZYGBA         2     11             
SEQADV 2PUY HIS A  484  UNP  Q96BD5              EXPRESSION TAG                 
SEQADV 2PUY MET A  485  UNP  Q96BD5              EXPRESSION TAG                 
SEQADV 2PUY HIS B  484  UNP  Q96BD5              EXPRESSION TAG                 
SEQADV 2PUY MET B  485  UNP  Q96BD5              EXPRESSION TAG                 
SEQRES   1 A   60  HIS MET ILE HIS GLU ASP PHE CYS SER VAL CYS ARG LYS          
SEQRES   2 A   60  SER GLY GLN LEU LEU MET CYS ASP THR CYS SER ARG VAL          
SEQRES   3 A   60  TYR HIS LEU ASP CYS LEU ASP PRO PRO LEU LYS THR ILE          
SEQRES   4 A   60  PRO LYS GLY MET TRP ILE CYS PRO ARG CYS GLN ASP GLN          
SEQRES   5 A   60  MET LEU LYS LYS GLU GLU ALA ILE                              
SEQRES   1 B   60  HIS MET ILE HIS GLU ASP PHE CYS SER VAL CYS ARG LYS          
SEQRES   2 B   60  SER GLY GLN LEU LEU MET CYS ASP THR CYS SER ARG VAL          
SEQRES   3 B   60  TYR HIS LEU ASP CYS LEU ASP PRO PRO LEU LYS THR ILE          
SEQRES   4 B   60  PRO LYS GLY MET TRP ILE CYS PRO ARG CYS GLN ASP GLN          
SEQRES   5 B   60  MET LEU LYS LYS GLU GLU ALA ILE                              
SEQRES   1 E   10  ALA ARG THR LYS GLN THR ALA ARG LYS SER                      
HET     ZN  A 355       1                                                       
HET     ZN  A 356       1                                                       
HET     ZN  B 357       1                                                       
HET     ZN  B 358       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   4   ZN    4(ZN 2+)                                                     
FORMUL   8  HOH   *88(H2 O)                                                     
HELIX    1   1 HIS A  511  LEU A  515  5                                   5    
HELIX    2   2 CYS A  529  LYS A  539  1                                  11    
HELIX    3   3 HIS B  511  LEU B  515  5                                   5    
HELIX    4   4 CYS B  529  ILE B  543  1                                  15    
SHEET    1   A 2 LEU A 501  MET A 502  0                                        
SHEET    2   A 2 VAL A 509  TYR A 510 -1  O  TYR A 510   N  LEU A 501           
SHEET    1   B 3 VAL B 509  TYR B 510  0                                        
SHEET    2   B 3 GLY B 498  MET B 502 -1  N  LEU B 501   O  TYR B 510           
SHEET    3   B 3 THR E   3  THR E   6 -1  O  LYS E   4   N  LEU B 500           
LINK        ZN    ZN A 355                 SG  CYS A 491     1555   1555  2.38  
LINK        ZN    ZN A 355                 SG  CYS A 494     1555   1555  2.30  
LINK        ZN    ZN A 355                 ND1 HIS A 511     1555   1555  2.12  
LINK        ZN    ZN A 355                 SG  CYS A 514     1555   1555  2.26  
LINK        ZN    ZN A 356                 SG  CYS A 503     1555   1555  2.31  
LINK        ZN    ZN A 356                 SG  CYS A 506     1555   1555  2.36  
LINK        ZN    ZN A 356                 SG  CYS A 529     1555   1555  2.41  
LINK        ZN    ZN A 356                 SG  CYS A 532     1555   1555  2.27  
LINK        ZN    ZN B 357                 SG  CYS B 491     1555   1555  2.29  
LINK        ZN    ZN B 357                 SG  CYS B 494     1555   1555  2.31  
LINK        ZN    ZN B 357                 ND1 HIS B 511     1555   1555  2.11  
LINK        ZN    ZN B 357                 SG  CYS B 514     1555   1555  2.30  
LINK        ZN    ZN B 358                 SG  CYS B 503     1555   1555  2.33  
LINK        ZN    ZN B 358                 SG  CYS B 506     1555   1555  2.33  
LINK        ZN    ZN B 358                 SG  CYS B 529     1555   1555  2.36  
LINK        ZN    ZN B 358                 SG  CYS B 532     1555   1555  2.32  
CISPEP   1 ASP A  516    PRO A  517          0         0.20                     
CISPEP   2 ASP B  516    PRO B  517          0        -0.19                     
SITE     1 AC1  4 CYS A 491  CYS A 494  HIS A 511  CYS A 514                    
SITE     1 AC2  4 CYS A 503  CYS A 506  CYS A 529  CYS A 532                    
SITE     1 AC3  4 CYS B 491  CYS B 494  HIS B 511  CYS B 514                    
SITE     1 AC4  4 CYS B 503  CYS B 506  CYS B 529  CYS B 532                    
CRYST1   79.511   25.386   62.282  90.00  96.93  90.00 C 1 2 1       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      0.012577  0.000000  0.001529        0.00000                         
SCALE2      0.000000  0.039392  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016174        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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