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Database: PDB
Entry: 2GP3
LinkDB: 2GP3
Original site: 2GP3 
HEADER    METAL BINDING PROTEIN                   16-APR-06   2GP3              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC CORE DOMAIN OF JMJD2A              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: JUMONJI DOMAIN-CONTAINING PROTEIN 2A;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 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: JMJD2A;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX 4T2                                  
KEYWDS    BETA BARREL, ZINC FINGER, METAL BINDING PROTEIN                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.CHEN,J.ZANG,J.WHETSTINE,X.HONG,F.DAVRAZOU,T.G.KUTATELADZE,          
AUTHOR   2 M.SIMPSON,S.DAI,J.HAGMAN,Y.SHI,G.ZHANG                               
REVDAT   5   14-FEB-24 2GP3    1       REMARK LINK                              
REVDAT   4   27-NOV-13 2GP3    1       HET    HETATM HETNAM REMARK              
REVDAT   4 2                   1       VERSN                                    
REVDAT   3   13-OCT-09 2GP3    1       TITLE                                    
REVDAT   2   20-MAY-08 2GP3    1       JRNL   VERSN                             
REVDAT   1   23-MAY-06 2GP3    0                                                
JRNL        AUTH   Z.CHEN,J.ZANG,J.WHETSTINE,X.HONG,F.DAVRAZOU,T.G.KUTATELADZE, 
JRNL        AUTH 2 M.SIMPSON,Q.MAO,C.H.PAN,S.DAI,J.HAGMAN,K.HANSEN,Y.SHI,       
JRNL        AUTH 3 G.ZHANG                                                      
JRNL        TITL   STRUCTURAL INSIGHTS INTO HISTONE DEMETHYLATION BY JMJD2      
JRNL        TITL 2 FAMILY MEMBERS                                               
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 125   691 2006              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   16677698                                                     
JRNL        DOI    10.1016/J.CELL.2006.04.024                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 33706                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1360                            
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3401                       
REMARK   3   BIN FREE R VALUE                    : 0.3422                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 38                           
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            : 5653                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 103                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
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) : 1.390                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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 2GP3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000037385.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795 0.9793, 0.9600              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33706                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
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     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 50.00                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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   (%): 53.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG8000, 200 MM MGCL2, 100 MM        
REMARK 280  TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+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       50.43350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.77000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.43350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       74.77000            
REMARK 290   SMTRY3   4  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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     ALA B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     ASN B     9                                                      
REMARK 465     GLU B   349                                                      
REMARK 465     ALA B   350                                                      
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    ASN A     9     N    SER A    11              2.07            
REMARK 500   O    SER A     3     N    SER A     5              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG1  THR A    76     O    THR B   126     4545     2.19            
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    PRO A  10   C   -  N   -  CA  ANGL. DEV. =   9.6 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    GLU A   4       27.72    -32.73                                   
REMARK 500    GLU A   6       34.15    -54.05                                   
REMARK 500    ASN A   9      136.55    -36.78                                   
REMARK 500    PRO A  10       43.32    -27.11                                   
REMARK 500    ALA A  12       56.47     23.12                                   
REMARK 500    LYS A  51      -50.10    -28.05                                   
REMARK 500    GLU A  52       31.72    -75.71                                   
REMARK 500    ILE A  62      -22.81   -165.86                                   
REMARK 500    ASP A  63       -5.38    -56.58                                   
REMARK 500    SER A  79       71.82     34.92                                   
REMARK 500    LYS A  89     -135.97    -74.74                                   
REMARK 500    ALA A  91      131.92    -15.51                                   
REMARK 500    ASP A 104       -7.65    -48.21                                   
REMARK 500    SER A 112      -77.51    -80.23                                   
REMARK 500    PRO A 129      104.81    -42.56                                   
REMARK 500    LYS A 182       -2.91     74.67                                   
REMARK 500    MET A 192       16.98     55.33                                   
REMARK 500    ALA A 236       53.03   -143.61                                   
REMARK 500    ASP A 337      103.50    -31.13                                   
REMARK 500    ASN A 338       44.27   -104.60                                   
REMARK 500    THR A 347      -66.35    -24.93                                   
REMARK 500    LYS B  51      -48.25    -29.66                                   
REMARK 500    GLU B  52       33.07    -77.22                                   
REMARK 500    ILE B  62      -23.09   -169.16                                   
REMARK 500    ASP B  63       -1.51    -56.40                                   
REMARK 500    SER B  79       69.30     35.21                                   
REMARK 500    LYS B  89     -135.97    -77.04                                   
REMARK 500    ALA B  91      133.39    -17.39                                   
REMARK 500    ASP B 104       -6.03    -47.90                                   
REMARK 500    SER B 112      -76.57    -79.64                                   
REMARK 500    PRO B 129      109.06    -42.29                                   
REMARK 500    VAL B 171      -60.09    -99.57                                   
REMARK 500    LYS B 182       -2.28     74.52                                   
REMARK 500    MET B 192       19.30     55.64                                   
REMARK 500    ALA B 236       56.00   -144.05                                   
REMARK 500    THR B 344      -19.95    102.95                                   
REMARK 500    LEU B 345      -84.10     -3.55                                   
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                             FE2 A 402  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 188   NE2                                                    
REMARK 620 2 GLU A 190   OE1 112.2                                              
REMARK 620 3 HIS A 276   NE2  97.7  79.5                                        
REMARK 620 4 HOH A 521   O    96.2 151.3 102.3                                  
REMARK 620 5 HOH A 529   O   111.3  88.1 150.9  76.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 234   SG                                                     
REMARK 620 2 HIS A 240   NE2 106.0                                              
REMARK 620 3 CYS A 306   SG  115.5 115.9                                        
REMARK 620 4 CYS A 308   SG  113.5  90.8 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 B 402  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 188   NE2                                                    
REMARK 620 2 GLU B 190   OE1 110.2                                              
REMARK 620 3 HIS B 276   NE2  93.8  77.4                                        
REMARK 620 4 HOH B 532   O   107.9 141.8  96.9                                  
REMARK 620 5 HOH B 535   O   100.2  93.4 165.2  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 234   SG                                                     
REMARK 620 2 HIS B 240   NE2 107.2                                              
REMARK 620 3 CYS B 306   SG  126.0 112.4                                        
REMARK 620 4 CYS B 308   SG  110.4  83.7 109.1                                  
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 402                 
DBREF  2GP3 A    2   350  UNP    O75164   JHD3A_HUMAN      2    350             
DBREF  2GP3 B    2   350  UNP    O75164   JHD3A_HUMAN      2    350             
SEQRES   1 A  349  ALA SER GLU SER GLU THR LEU ASN PRO SER ALA ARG ILE          
SEQRES   2 A  349  MET THR PHE TYR PRO THR MET GLU GLU PHE ARG ASN PHE          
SEQRES   3 A  349  SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY ALA HIS          
SEQRES   4 A  349  ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP          
SEQRES   5 A  349  LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP LEU VAL          
SEQRES   6 A  349  ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY GLN SER          
SEQRES   7 A  349  GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS ALA MET          
SEQRES   8 A  349  THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER ASP LYS          
SEQRES   9 A  349  TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU LEU GLU          
SEQRES  10 A  349  ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO PRO ILE          
SEQRES  11 A  349  TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU LYS HIS          
SEQRES  12 A  349  VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR ILE LEU          
SEQRES  13 A  349  ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE GLU GLY          
SEQRES  14 A  349  VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP LYS THR          
SEQRES  15 A  349  SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU TYR SER          
SEQRES  16 A  349  ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER TRP TYR          
SEQRES  17 A  349  SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU          
SEQRES  18 A  349  ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER CYS GLU          
SEQRES  19 A  349  ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER PRO LEU          
SEQRES  20 A  349  MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS VAL THR          
SEQRES  21 A  349  GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO TYR GLY          
SEQRES  22 A  349  TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU          
SEQRES  23 A  349  SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU TYR GLY          
SEQRES  24 A  349  LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP MET VAL          
SEQRES  25 A  349  LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE GLN PRO          
SEQRES  26 A  349  GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP ASN THR          
SEQRES  27 A  349  VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA                  
SEQRES   1 B  349  ALA SER GLU SER GLU THR LEU ASN PRO SER ALA ARG ILE          
SEQRES   2 B  349  MET THR PHE TYR PRO THR MET GLU GLU PHE ARG ASN PHE          
SEQRES   3 B  349  SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY ALA HIS          
SEQRES   4 B  349  ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP          
SEQRES   5 B  349  LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP LEU VAL          
SEQRES   6 B  349  ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY GLN SER          
SEQRES   7 B  349  GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS ALA MET          
SEQRES   8 B  349  THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER ASP LYS          
SEQRES   9 B  349  TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU LEU GLU          
SEQRES  10 B  349  ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO PRO ILE          
SEQRES  11 B  349  TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU LYS HIS          
SEQRES  12 B  349  VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR ILE LEU          
SEQRES  13 B  349  ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE GLU GLY          
SEQRES  14 B  349  VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP LYS THR          
SEQRES  15 B  349  SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU TYR SER          
SEQRES  16 B  349  ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER TRP TYR          
SEQRES  17 B  349  SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU          
SEQRES  18 B  349  ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER CYS GLU          
SEQRES  19 B  349  ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER PRO LEU          
SEQRES  20 B  349  MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS VAL THR          
SEQRES  21 B  349  GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO TYR GLY          
SEQRES  22 B  349  TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU          
SEQRES  23 B  349  SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU TYR GLY          
SEQRES  24 B  349  LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP MET VAL          
SEQRES  25 B  349  LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE GLN PRO          
SEQRES  26 B  349  GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP ASN THR          
SEQRES  27 B  349  VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA                  
HET     ZN  A 401       1                                                       
HET    FE2  A 402       1                                                       
HET     ZN  B 401       1                                                       
HET    FE2  B 402       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     FE2 FE (II) ION                                                      
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  FE2    2(FE 2+)                                                     
FORMUL   7  HOH   *103(H2 O)                                                    
HELIX    1   1 SER A    5  ASN A    9  5                                   5    
HELIX    2   2 THR A   20  ASN A   26  1                                   7    
HELIX    3   3 ASN A   26  GLN A   37  1                                  12    
HELIX    4   4 GLY A   38  ALA A   42  5                                   5    
HELIX    5   5 VAL A   94  SER A  103  1                                  10    
HELIX    6   6 GLU A  113  LEU A  125  1                                  13    
HELIX    7   7 LEU A  157  GLY A  165  1                                   9    
HELIX    8   8 GLU A  190  LEU A  194  5                                   5    
HELIX    9   9 PRO A  212  GLU A  214  5                                   3    
HELIX   10  10 HIS A  215  PHE A  227  1                                  13    
HELIX   11  11 PHE A  227  CYS A  234  1                                   8    
HELIX   12  12 ALA A  236  LYS A  241  5                                   6    
HELIX   13  13 SER A  246  TYR A  253  1                                   8    
HELIX   14  14 ARG A  295  ALA A  303  1                                   9    
HELIX   15  15 MET A  317  GLN A  325  1                                   9    
HELIX   16  16 ARG A  328  ALA A  334  1                                   7    
HELIX   17  17 THR B   20  ASN B   26  1                                   7    
HELIX   18  18 ASN B   26  GLN B   37  1                                  12    
HELIX   19  19 GLY B   38  ALA B   42  5                                   5    
HELIX   20  20 VAL B   94  SER B  103  1                                  10    
HELIX   21  21 GLU B  113  LEU B  125  1                                  13    
HELIX   22  22 LEU B  157  GLY B  165  1                                   9    
HELIX   23  23 GLU B  190  LEU B  194  5                                   5    
HELIX   24  24 PRO B  212  GLU B  214  5                                   3    
HELIX   25  25 HIS B  215  PHE B  227  1                                  13    
HELIX   26  26 PHE B  227  CYS B  234  1                                   8    
HELIX   27  27 ALA B  236  LYS B  241  5                                   6    
HELIX   28  28 SER B  246  TYR B  253  1                                   8    
HELIX   29  29 ARG B  295  ALA B  303  1                                   9    
HELIX   30  30 MET B  317  GLN B  325  1                                   9    
HELIX   31  31 ARG B  328  ALA B  334  1                                   7    
SHEET    1   A10 MET A  15  PHE A  17  0                                        
SHEET    2   A10 LEU A  44  VAL A  47  1  O  LYS A  46   N  MET A  15           
SHEET    3   A10 PHE A 267  THR A 270 -1  O  PHE A 267   N  VAL A  47           
SHEET    4   A10 TYR A 195  GLY A 203 -1  N  ASN A 198   O  MET A 268           
SHEET    5   A10 ASN A 284  PHE A 291 -1  O  GLU A 287   N  TYR A 199           
SHEET    6   A10 TYR A 175  PHE A 178 -1  N  TYR A 177   O  ALA A 286           
SHEET    7   A10 ILE A 131  ASN A 137 -1  N  GLY A 133   O  PHE A 178           
SHEET    8   A10 ILE A  71  GLN A  78 -1  N  ILE A  71   O  TYR A 132           
SHEET    9   A10 LEU A  81  GLN A  88 -1  O  TYR A  85   N  LEU A  74           
SHEET   10   A10 THR A 243  ILE A 245 -1  O  LEU A 244   N  PHE A  82           
SHEET    1   B 2 VAL A  66  ILE A  67  0                                        
SHEET    2   B 2 MET A  92  THR A  93 -1  O  MET A  92   N  ILE A  67           
SHEET    1   C 4 SER A 184  HIS A 188  0                                        
SHEET    2   C 4 TYR A 275  ASN A 280 -1  O  GLY A 278   N  PHE A 185           
SHEET    3   C 4 LYS A 206  VAL A 211 -1  N  TYR A 209   O  ALA A 277           
SHEET    4   C 4 ASP A 258  GLN A 262 -1  O  VAL A 260   N  TRP A 208           
SHEET    1   D10 MET B  15  PHE B  17  0                                        
SHEET    2   D10 LEU B  44  VAL B  47  1  O  LYS B  46   N  MET B  15           
SHEET    3   D10 PHE B 267  THR B 270 -1  O  ILE B 269   N  ALA B  45           
SHEET    4   D10 TYR B 195  GLY B 203 -1  N  SER B 196   O  THR B 270           
SHEET    5   D10 ASN B 284  PHE B 291 -1  O  GLU B 287   N  TYR B 199           
SHEET    6   D10 TYR B 175  PHE B 178 -1  N  TYR B 177   O  ALA B 286           
SHEET    7   D10 ILE B 131  ASN B 137 -1  N  GLY B 133   O  PHE B 178           
SHEET    8   D10 ILE B  71  GLN B  78 -1  N  ILE B  71   O  TYR B 132           
SHEET    9   D10 LEU B  81  GLN B  88 -1  O  TYR B  85   N  LEU B  74           
SHEET   10   D10 THR B 243  ILE B 245 -1  O  LEU B 244   N  PHE B  82           
SHEET    1   E 2 VAL B  66  ILE B  67  0                                        
SHEET    2   E 2 MET B  92  THR B  93 -1  O  MET B  92   N  ILE B  67           
SHEET    1   F 4 SER B 184  HIS B 188  0                                        
SHEET    2   F 4 TYR B 275  ASN B 280 -1  O  GLY B 278   N  PHE B 185           
SHEET    3   F 4 LYS B 206  VAL B 211 -1  N  TYR B 209   O  ALA B 277           
SHEET    4   F 4 ASP B 258  GLN B 262 -1  O  VAL B 260   N  TRP B 208           
LINK         NE2 HIS A 188                FE   FE2 A 402     1555   1555  2.24  
LINK         OE1 GLU A 190                FE   FE2 A 402     1555   1555  2.09  
LINK         SG  CYS A 234                ZN    ZN A 401     1555   1555  2.34  
LINK         NE2 HIS A 240                ZN    ZN A 401     1555   1555  2.09  
LINK         NE2 HIS A 276                FE   FE2 A 402     1555   1555  2.15  
LINK         SG  CYS A 306                ZN    ZN A 401     1555   1555  2.18  
LINK         SG  CYS A 308                ZN    ZN A 401     1555   1555  2.38  
LINK        FE   FE2 A 402                 O   HOH A 521     1555   1555  2.49  
LINK        FE   FE2 A 402                 O   HOH A 529     1555   1555  2.67  
LINK         NE2 HIS B 188                FE   FE2 B 402     1555   1555  2.20  
LINK         OE1 GLU B 190                FE   FE2 B 402     1555   1555  2.13  
LINK         SG  CYS B 234                ZN    ZN B 401     1555   1555  2.22  
LINK         NE2 HIS B 240                ZN    ZN B 401     1555   1555  2.22  
LINK         NE2 HIS B 276                FE   FE2 B 402     1555   1555  2.26  
LINK         SG  CYS B 306                ZN    ZN B 401     1555   1555  2.26  
LINK         SG  CYS B 308                ZN    ZN B 401     1555   1555  2.43  
LINK        FE   FE2 B 402                 O   HOH B 532     1555   1555  2.34  
LINK        FE   FE2 B 402                 O   HOH B 535     1555   1555  2.47  
SITE     1 AC1  4 CYS A 234  HIS A 240  CYS A 306  CYS A 308                    
SITE     1 AC2  5 HIS A 188  GLU A 190  HIS A 276  HOH A 521                    
SITE     2 AC2  5 HOH A 529                                                     
SITE     1 AC3  4 CYS B 234  HIS B 240  CYS B 306  CYS B 308                    
SITE     1 AC4  5 HIS B 188  GLU B 190  HIS B 276  HOH B 532                    
SITE     2 AC4  5 HOH B 535                                                     
CRYST1  100.867  149.540   56.815  90.00  90.00  90.00 P 21 21 2     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      0.009914  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006687  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017601        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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