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Database: PDB
Entry: 5FY8
LinkDB: 5FY8
Original site: 5FY8 
HEADER    OXIDOREDUCTASE                          04-MAR-16   5FY8              
TITLE     CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH D-THREO-ISOCITRATE  
CAVEAT     5FY8    N81 B 1354 HAS WRONG CHIRALITY AT ATOM C02                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4A;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 4-354;                                            
COMPND   5 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3A,    
COMPND   6 JUMONJI DOMAIN-CONTAINING PROTEIN 2A;                                
COMPND   7 EC: 1.14.11.-;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    OXIDOREDUCTASE, JMJD2A, KDM4A, TCA INTERMEDIATE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.NOWAK,J.KOPEC,C.JOHANSSON,A.SZYKOWSKA,F.VON DELFT,C.H.ARROWSMITH,   
AUTHOR   2 C.BOUNTRA,A.EDWARDS,U.OPPERMANN                                      
REVDAT   3   10-JAN-24 5FY8    1       CAVEAT REMARK LINK                       
REVDAT   2   24-JAN-18 5FY8    1       AUTHOR JRNL                              
REVDAT   1   16-MAR-16 5FY8    0                                                
JRNL        AUTH   R.NOWAK,J.KOPEC,C.JOHANSSON,A.SZYKOWSKA,F.VON DELFT,         
JRNL        AUTH 2 C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,U.OPPERMANN               
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH            
JRNL        TITL 2 D-THREO-ISOCITRATE                                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 36843                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1758                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.9818 -  5.4972    1.00     2888   149  0.1610 0.1980        
REMARK   3     2  5.4972 -  4.3681    1.00     2766   121  0.1389 0.1691        
REMARK   3     3  4.3681 -  3.8173    1.00     2729   144  0.1549 0.1830        
REMARK   3     4  3.8173 -  3.4689    1.00     2698   158  0.1862 0.2272        
REMARK   3     5  3.4689 -  3.2206    1.00     2696   135  0.1997 0.2550        
REMARK   3     6  3.2206 -  3.0310    1.00     2695   138  0.2113 0.2701        
REMARK   3     7  3.0310 -  2.8793    1.00     2683   125  0.2212 0.2716        
REMARK   3     8  2.8793 -  2.7541    1.00     2706   124  0.2266 0.3120        
REMARK   3     9  2.7541 -  2.6481    1.00     2666   130  0.2272 0.2867        
REMARK   3    10  2.6481 -  2.5568    1.00     2668   151  0.2485 0.3005        
REMARK   3    11  2.5568 -  2.4769    1.00     2635   126  0.2456 0.2904        
REMARK   3    12  2.4769 -  2.4061    1.00     2682   134  0.2527 0.3417        
REMARK   3    13  2.4061 -  2.3428    0.97     2573   123  0.2717 0.3618        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: SOME RESIDUE SIDECHAINS ARE IN DUAL       
REMARK   3  CONFORMATION. SOME RESIDUES DO NOT HAVE SIDECHAINS.                 
REMARK   4                                                                      
REMARK   4 5FY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1290066375.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36894                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.980                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: DIMPLE                                                
REMARK 200 STARTING MODEL: PDB NETRY 5A7W                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.0 -- 0.15M AMMONIUM   
REMARK 280  SULFATE -- 28% PEG3350                                              
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       50.46500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.45500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.46500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       74.45500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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 NH2  ARG A 322  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     MET A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     VAL A   -11                                                      
REMARK 465     ASP A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     THR A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     LEU A   354                                                      
REMARK 465     LYS A   355                                                      
REMARK 465     GLU A   356                                                      
REMARK 465     SER A   357                                                      
REMARK 465     GLU A   358                                                      
REMARK 465     LEU A   359                                                      
REMARK 465     MET B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     VAL B   -11                                                      
REMARK 465     ASP B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     THR B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     ASN B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     TYR B    -3                                                      
REMARK 465     PHE B    -2                                                      
REMARK 465     GLN B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
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     LEU B   354                                                      
REMARK 465     LYS B   355                                                      
REMARK 465     GLU B   356                                                      
REMARK 465     SER B   357                                                      
REMARK 465     GLU B   358                                                      
REMARK 465     LEU B   359                                                      
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   4    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  13    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A  22    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  29    CZ   NH1  NH2                                       
REMARK 470     LYS A  54    CG   CD   CE   NZ                                   
REMARK 470     LYS A  90    CD   CE   NZ                                        
REMARK 470     ARG A  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  99    CG   CD   CE   NZ                                   
REMARK 470     ARG A 110    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 112    OG                                                  
REMARK 470     GLU A 113    CD   OE1  OE2                                       
REMARK 470     GLU A 115    CD   OE1  OE2                                       
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     ARG A 154    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     ARG A 221    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 224    CD   CE   NZ                                        
REMARK 470     GLN A 232    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 252    CE   NZ                                             
REMARK 470     ARG A 309    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 330    CD   CE   NZ                                        
REMARK 470     LYS A 336    CG   CD   CE   NZ                                   
REMARK 470     THR B   7    OG1  CG2                                            
REMARK 470     GLU B  22    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  29    CZ   NH1  NH2                                       
REMARK 470     LYS B  51    CD   CE   NZ                                        
REMARK 470     LYS B  54    CE   NZ                                             
REMARK 470     LYS B  90    CG   CD   CE   NZ                                   
REMARK 470     LYS B  99    CD   CE   NZ                                        
REMARK 470     ARG B 110    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 113    OE1  OE2                                            
REMARK 470     GLU B 115    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 143    CG   CD   CE   NZ                                   
REMARK 470     ARG B 154    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 161    CD   OE1  OE2                                       
REMARK 470     LYS B 162    CD   CE   NZ                                        
REMARK 470     GLU B 163    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 224    CG   CD   CE   NZ                                   
REMARK 470     GLN B 232    CD   OE1  NE2                                       
REMARK 470     LYS B 310    CG   CD   CE   NZ                                   
REMARK 470     LYS B 323    NZ                                                  
REMARK 470     LYS B 336    CG   CD   CE   NZ                                   
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   OE2  GLU B   349     O    HOH B  2087              2.06            
REMARK 500   O    DMS A  1355     O    HOH A  2068              2.09            
REMARK 500   O    VAL B    66     O    HOH B  2013              2.11            
REMARK 500   OE1  GLU A   142     O    HOH A  2037              2.12            
REMARK 500   O    ASP B    60     O    HOH B  2011              2.13            
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   CZ   ARG A   322     NH2  ARG A   322     2455     1.33            
REMARK 500   NH1  ARG A   322     NH2  ARG A   322     2455     1.91            
REMARK 500   NE   ARG A   322     NH2  ARG A   322     2455     2.16            
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    ARG A 322   NH1 -  CZ  -  NH2 ANGL. DEV. = -28.2 DEGREES          
REMARK 500    ARG A 322   NE  -  CZ  -  NH2 ANGL. DEV. = -12.1 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    TYR A  59       48.37   -102.75                                   
REMARK 500    SER A 112      -85.29    -96.22                                   
REMARK 500    ARG A 152       70.27   -155.58                                   
REMARK 500    ALA A 236       56.75   -146.18                                   
REMARK 500    ARG A 309       -0.12     77.23                                   
REMARK 500    ASN A 338       44.90   -103.78                                   
REMARK 500    TYR B  59       46.04   -104.06                                   
REMARK 500    SER B 112      -83.86    -99.23                                   
REMARK 500    ARG B 152       68.00   -153.01                                   
REMARK 500    ALA B 236       54.69   -146.29                                   
REMARK 500    ASP B 311       45.64   -102.27                                   
REMARK 500    ASN B 338       46.00   -104.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 322         0.36    SIDE CHAIN                              
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                              NI A 501  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 188   NE2                                                    
REMARK 620 2 GLU A 190   OE2 103.4                                              
REMARK 620 3 HIS A 276   NE2  94.9  82.3                                        
REMARK 620 4 N81 A1354   O12 156.0  93.5 104.3                                  
REMARK 620 5 N81 A1354   O01  94.9 157.7  83.6  73.4                            
REMARK 620 6 HOH A2050   O    76.1  91.9 168.0  86.5 104.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 234   SG                                                     
REMARK 620 2 HIS A 240   NE2 105.3                                              
REMARK 620 3 CYS A 306   SG  113.6 114.3                                        
REMARK 620 4 CYS A 308   SG  117.7  98.3 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 501  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 188   NE2                                                    
REMARK 620 2 GLU B 190   OE2 110.8                                              
REMARK 620 3 HIS B 276   NE2  87.8  79.5                                        
REMARK 620 4 N81 B1354   O01  95.6 152.0  92.7                                  
REMARK 620 5 N81 B1354   O12 161.1  84.1  83.4  68.2                            
REMARK 620 6 HOH B2048   O    93.8  95.4 174.9  91.9  96.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 234   SG                                                     
REMARK 620 2 HIS B 240   NE2 105.4                                              
REMARK 620 3 CYS B 306   SG  115.3 116.9                                        
REMARK 620 4 CYS B 308   SG  113.8  92.6 110.8                                  
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 NI A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N81 A 1354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N81 B 1354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1355                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1355                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1356                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1356                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1357                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1357                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1358                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1358                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1359                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FXV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY    
REMARK 900 IN COMPLEX WITH N05859B                                              
REMARK 900 RELATED ID: 5FXW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY    
REMARK 900 IN COMPLEX WITH FUMARATE                                             
REMARK 900 RELATED ID: 5FXX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY    
REMARK 900 IN COMPLEX WITH OXALOACETATE                                         
REMARK 900 RELATED ID: 5FXZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY    
REMARK 900 IN COMPLEX WITH CITRATE                                              
REMARK 900 RELATED ID: 5FY0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY    
REMARK 900 IN COMPLEX WITH L-MALATE                                             
REMARK 900 RELATED ID: 5FY1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY    
REMARK 900 IN COMPLEX WITH N08619B                                              
REMARK 900 RELATED ID: 5FY4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN        
REMARK 900 COMPLEX WITH SUCCINATE                                               
REMARK 900 RELATED ID: 5FY5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN        
REMARK 900 COMPLEX WITH FUMARATE                                                
REMARK 900 RELATED ID: 5FY7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY    
REMARK 900 IN COMPLEX WITH SUCCINATE                                            
REMARK 900 RELATED ID: 5FY9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN        
REMARK 900 COMPLEX WITH PYRUVATE                                                
REMARK 900 RELATED ID: 5FYB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN        
REMARK 900 COMPLEX WITH MC1648                                                  
REMARK 900 RELATED ID: 5FYC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH SUCCINATE          
REMARK 900 RELATED ID: 5FYH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH FUMARATE           
REMARK 900 RELATED ID: 5FYI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH PYRUVATE           
REMARK 900 RELATED ID: 5FYM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY    
REMARK 900 IN COMPLEX WITH D-2-HYDROXYGLUTARATE                                 
DBREF  5FY8 A    1   359  UNP    O75164   KDM4A_HUMAN      1    359             
DBREF  5FY8 B    1   359  UNP    O75164   KDM4A_HUMAN      1    359             
SEQADV 5FY8 MET A  -21  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS A  -20  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS A  -19  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS A  -18  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS A  -17  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS A  -16  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS A  -15  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 SER A  -14  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 SER A  -13  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 GLY A  -12  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 VAL A  -11  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 ASP A  -10  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 LEU A   -9  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 GLY A   -8  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 THR A   -7  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 GLU A   -6  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 ASN A   -5  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 LEU A   -4  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 TYR A   -3  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 PHE A   -2  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 GLN A   -1  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 SER A    0  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 MET B  -21  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS B  -20  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS B  -19  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS B  -18  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS B  -17  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS B  -16  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 HIS B  -15  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 SER B  -14  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 SER B  -13  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 GLY B  -12  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 VAL B  -11  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 ASP B  -10  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 LEU B   -9  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 GLY B   -8  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 THR B   -7  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 GLU B   -6  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 ASN B   -5  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 LEU B   -4  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 TYR B   -3  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 PHE B   -2  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 GLN B   -1  UNP  O75164              EXPRESSION TAG                 
SEQADV 5FY8 SER B    0  UNP  O75164              EXPRESSION TAG                 
SEQRES   1 A  381  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  381  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER GLU          
SEQRES   3 A  381  SER GLU THR LEU ASN PRO SER ALA ARG ILE MET THR PHE          
SEQRES   4 A  381  TYR PRO THR MET GLU GLU PHE ARG ASN PHE SER ARG TYR          
SEQRES   5 A  381  ILE ALA TYR ILE GLU SER GLN GLY ALA HIS ARG ALA GLY          
SEQRES   6 A  381  LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP LYS PRO ARG          
SEQRES   7 A  381  ALA SER TYR ASP ASP ILE ASP ASP LEU VAL ILE PRO ALA          
SEQRES   8 A  381  PRO ILE GLN GLN LEU VAL THR GLY GLN SER GLY LEU PHE          
SEQRES   9 A  381  THR GLN TYR ASN ILE GLN LYS LYS ALA MET THR VAL ARG          
SEQRES  10 A  381  GLU PHE ARG LYS ILE ALA ASN SER ASP LYS TYR CYS THR          
SEQRES  11 A  381  PRO ARG TYR SER GLU PHE GLU GLU LEU GLU ARG LYS TYR          
SEQRES  12 A  381  TRP LYS ASN LEU THR PHE ASN PRO PRO ILE TYR GLY ALA          
SEQRES  13 A  381  ASP VAL ASN GLY THR LEU TYR GLU LYS HIS VAL ASP GLU          
SEQRES  14 A  381  TRP ASN ILE GLY ARG LEU ARG THR ILE LEU ASP LEU VAL          
SEQRES  15 A  381  GLU LYS GLU SER GLY ILE THR ILE GLU GLY VAL ASN THR          
SEQRES  16 A  381  PRO TYR LEU TYR PHE GLY MET TRP LYS THR SER PHE ALA          
SEQRES  17 A  381  TRP HIS THR GLU ASP MET ASP LEU TYR SER ILE ASN TYR          
SEQRES  18 A  381  LEU HIS PHE GLY GLU PRO LYS SER TRP TYR SER VAL PRO          
SEQRES  19 A  381  PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU ALA LYS GLY          
SEQRES  20 A  381  PHE PHE PRO GLY SER ALA GLN SER CYS GLU ALA PHE LEU          
SEQRES  21 A  381  ARG HIS LYS MET THR LEU ILE SER PRO LEU MET LEU LYS          
SEQRES  22 A  381  LYS TYR GLY ILE PRO PHE ASP LYS VAL THR GLN GLU ALA          
SEQRES  23 A  381  GLY GLU PHE MET ILE THR PHE PRO TYR GLY TYR HIS ALA          
SEQRES  24 A  381  GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU SER THR ASN          
SEQRES  25 A  381  PHE ALA THR ARG ARG TRP ILE GLU TYR GLY LYS GLN ALA          
SEQRES  26 A  381  VAL LEU CYS SER CYS ARG LYS ASP MET VAL LYS ILE SER          
SEQRES  27 A  381  MET ASP VAL PHE VAL ARG LYS PHE GLN PRO GLU ARG TYR          
SEQRES  28 A  381  LYS LEU TRP LYS ALA GLY LYS ASP ASN THR VAL ILE ASP          
SEQRES  29 A  381  HIS THR LEU PRO THR PRO GLU ALA ALA GLU PHE LEU LYS          
SEQRES  30 A  381  GLU SER GLU LEU                                              
SEQRES   1 B  381  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  381  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER GLU          
SEQRES   3 B  381  SER GLU THR LEU ASN PRO SER ALA ARG ILE MET THR PHE          
SEQRES   4 B  381  TYR PRO THR MET GLU GLU PHE ARG ASN PHE SER ARG TYR          
SEQRES   5 B  381  ILE ALA TYR ILE GLU SER GLN GLY ALA HIS ARG ALA GLY          
SEQRES   6 B  381  LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP LYS PRO ARG          
SEQRES   7 B  381  ALA SER TYR ASP ASP ILE ASP ASP LEU VAL ILE PRO ALA          
SEQRES   8 B  381  PRO ILE GLN GLN LEU VAL THR GLY GLN SER GLY LEU PHE          
SEQRES   9 B  381  THR GLN TYR ASN ILE GLN LYS LYS ALA MET THR VAL ARG          
SEQRES  10 B  381  GLU PHE ARG LYS ILE ALA ASN SER ASP LYS TYR CYS THR          
SEQRES  11 B  381  PRO ARG TYR SER GLU PHE GLU GLU LEU GLU ARG LYS TYR          
SEQRES  12 B  381  TRP LYS ASN LEU THR PHE ASN PRO PRO ILE TYR GLY ALA          
SEQRES  13 B  381  ASP VAL ASN GLY THR LEU TYR GLU LYS HIS VAL ASP GLU          
SEQRES  14 B  381  TRP ASN ILE GLY ARG LEU ARG THR ILE LEU ASP LEU VAL          
SEQRES  15 B  381  GLU LYS GLU SER GLY ILE THR ILE GLU GLY VAL ASN THR          
SEQRES  16 B  381  PRO TYR LEU TYR PHE GLY MET TRP LYS THR SER PHE ALA          
SEQRES  17 B  381  TRP HIS THR GLU ASP MET ASP LEU TYR SER ILE ASN TYR          
SEQRES  18 B  381  LEU HIS PHE GLY GLU PRO LYS SER TRP TYR SER VAL PRO          
SEQRES  19 B  381  PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU ALA LYS GLY          
SEQRES  20 B  381  PHE PHE PRO GLY SER ALA GLN SER CYS GLU ALA PHE LEU          
SEQRES  21 B  381  ARG HIS LYS MET THR LEU ILE SER PRO LEU MET LEU LYS          
SEQRES  22 B  381  LYS TYR GLY ILE PRO PHE ASP LYS VAL THR GLN GLU ALA          
SEQRES  23 B  381  GLY GLU PHE MET ILE THR PHE PRO TYR GLY TYR HIS ALA          
SEQRES  24 B  381  GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU SER THR ASN          
SEQRES  25 B  381  PHE ALA THR ARG ARG TRP ILE GLU TYR GLY LYS GLN ALA          
SEQRES  26 B  381  VAL LEU CYS SER CYS ARG LYS ASP MET VAL LYS ILE SER          
SEQRES  27 B  381  MET ASP VAL PHE VAL ARG LYS PHE GLN PRO GLU ARG TYR          
SEQRES  28 B  381  LYS LEU TRP LYS ALA GLY LYS ASP ASN THR VAL ILE ASP          
SEQRES  29 B  381  HIS THR LEU PRO THR PRO GLU ALA ALA GLU PHE LEU LYS          
SEQRES  30 B  381  GLU SER GLU LEU                                              
HET     NI  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET    N81  A1354      13                                                       
HET    DMS  A1355       4                                                       
HET    EDO  A1356       4                                                       
HET    EDO  A1357       4                                                       
HET    EDO  A1358       4                                                       
HET     NI  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET    N81  B1354      13                                                       
HET    DMS  B1355       4                                                       
HET    EDO  B1356       4                                                       
HET    EDO  B1357       4                                                       
HET    EDO  B1358       4                                                       
HET    EDO  B1359       4                                                       
HETNAM      NI NICKEL (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     N81 3-CARBOXY-2,3-DIDEOXY-D-ERYTHRO-PENTARIC ACID                    
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   NI    2(NI 2+)                                                     
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   5  N81    2(C6 H8 O7)                                                  
FORMUL   6  DMS    2(C2 H6 O S)                                                 
FORMUL   7  EDO    7(C2 H6 O2)                                                  
FORMUL  18  HOH   *196(H2 O)                                                    
HELIX    1   1 THR A   20  ARG A   25  1                                   6    
HELIX    2   2 ASN A   26  GLN A   37  1                                  12    
HELIX    3   3 GLY A   38  ALA A   42  5                                   5    
HELIX    4   4 VAL A   94  SER A  103  1                                  10    
HELIX    5   5 GLU A  113  LEU A  125  1                                  13    
HELIX    6   6 THR A  155  LEU A  157  5                                   3    
HELIX    7   7 ASP A  158  GLY A  165  1                                   8    
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 A  347  PHE A  353  5                                   7    
HELIX   18  18 THR B   20  ASN B   26  1                                   7    
HELIX   19  19 ASN B   26  GLN B   37  1                                  12    
HELIX   20  20 GLY B   38  ALA B   42  5                                   5    
HELIX   21  21 VAL B   94  SER B  103  1                                  10    
HELIX   22  22 GLU B  113  LEU B  125  1                                  13    
HELIX   23  23 THR B  155  LEU B  159  5                                   5    
HELIX   24  24 VAL B  160  GLY B  165  1                                   6    
HELIX   25  25 GLU B  190  LEU B  194  5                                   5    
HELIX   26  26 PRO B  212  GLU B  214  5                                   3    
HELIX   27  27 HIS B  215  PHE B  227  1                                  13    
HELIX   28  28 PHE B  227  CYS B  234  1                                   8    
HELIX   29  29 ALA B  236  LYS B  241  5                                   6    
HELIX   30  30 SER B  246  TYR B  253  1                                   8    
HELIX   31  31 ARG B  295  ALA B  303  1                                   9    
HELIX   32  32 MET B  317  GLN B  325  1                                   9    
HELIX   33  33 ARG B  328  ALA B  334  1                                   7    
HELIX   34  34 THR B  347  PHE B  353  5                                   7    
SHEET    1  AA10 MET A  15  PHE A  17  0                                        
SHEET    2  AA10 LEU A  44  VAL A  47  1  O  LEU A  44   N  MET A  15           
SHEET    3  AA10 PHE A 267  THR A 270 -1  O  PHE A 267   N  VAL A  47           
SHEET    4  AA10 TYR A 195  GLY A 203 -1  O  SER A 196   N  THR A 270           
SHEET    5  AA10 ASN A 284  PHE A 291 -1  O  CYS A 285   N  HIS A 201           
SHEET    6  AA10 TYR A 175  GLY A 179 -1  O  TYR A 175   N  SER A 288           
SHEET    7  AA10 ILE A 131  ASN A 137 -1  O  GLY A 133   N  PHE A 178           
SHEET    8  AA10 ILE A  71  GLN A  78 -1  O  ILE A  71   N  TYR A 132           
SHEET    9  AA10 LEU A  81  GLN A  88 -1  O  LEU A  81   N  GLN A  78           
SHEET   10  AA10 THR A 243  ILE A 245 -1  O  LEU A 244   N  PHE A  82           
SHEET    1  AB 2 VAL A  66  ILE A  67  0                                        
SHEET    2  AB 2 MET A  92  THR A  93 -1  O  MET A  92   N  ILE A  67           
SHEET    1  AC 4 SER A 184  HIS A 188  0                                        
SHEET    2  AC 4 TYR A 275  ASN A 280 -1  O  HIS A 276   N  HIS A 188           
SHEET    3  AC 4 LYS A 206  VAL A 211 -1  O  SER A 207   N  PHE A 279           
SHEET    4  AC 4 ASP A 258  GLN A 262 -1  O  ASP A 258   N  SER A 210           
SHEET    1  BA10 MET B  15  PHE B  17  0                                        
SHEET    2  BA10 LEU B  44  VAL B  47  1  O  LEU B  44   N  MET B  15           
SHEET    3  BA10 PHE B 267  THR B 270 -1  O  PHE B 267   N  VAL B  47           
SHEET    4  BA10 TYR B 195  GLY B 203 -1  O  SER B 196   N  THR B 270           
SHEET    5  BA10 ASN B 284  PHE B 291 -1  O  CYS B 285   N  HIS B 201           
SHEET    6  BA10 TYR B 175  GLY B 179 -1  O  TYR B 175   N  SER B 288           
SHEET    7  BA10 ILE B 131  ASN B 137 -1  O  GLY B 133   N  PHE B 178           
SHEET    8  BA10 ILE B  71  GLN B  78 -1  O  ILE B  71   N  TYR B 132           
SHEET    9  BA10 LEU B  81  GLN B  88 -1  O  LEU B  81   N  GLN B  78           
SHEET   10  BA10 THR B 243  ILE B 245 -1  O  LEU B 244   N  PHE B  82           
SHEET    1  BB 2 VAL B  66  ILE B  67  0                                        
SHEET    2  BB 2 MET B  92  THR B  93 -1  O  MET B  92   N  ILE B  67           
SHEET    1  BC 4 SER B 184  HIS B 188  0                                        
SHEET    2  BC 4 TYR B 275  ASN B 280 -1  O  HIS B 276   N  HIS B 188           
SHEET    3  BC 4 LYS B 206  VAL B 211 -1  O  SER B 207   N  PHE B 279           
SHEET    4  BC 4 ASP B 258  GLN B 262 -1  O  ASP B 258   N  SER B 210           
LINK         NE2 HIS A 188                NI    NI A 501     1555   1555  2.42  
LINK         OE2 GLU A 190                NI    NI A 501     1555   1555  2.01  
LINK         SG  CYS A 234                ZN    ZN A 502     1555   1555  2.25  
LINK         NE2 HIS A 240                ZN    ZN A 502     1555   1555  2.08  
LINK         NE2 HIS A 276                NI    NI A 501     1555   1555  2.30  
LINK         SG  CYS A 306                ZN    ZN A 502     1555   1555  2.13  
LINK         SG  CYS A 308                ZN    ZN A 502     1555   1555  2.39  
LINK        NI    NI A 501                 O12 N81 A1354     1555   1555  2.78  
LINK        NI    NI A 501                 O01 N81 A1354     1555   1555  2.38  
LINK        NI    NI A 501                 O   HOH A2050     1555   1555  2.41  
LINK         NE2 HIS B 188                NI    NI B 501     1555   1555  2.20  
LINK         OE2 GLU B 190                NI    NI B 501     1555   1555  2.22  
LINK         SG  CYS B 234                ZN    ZN B 502     1555   1555  2.22  
LINK         NE2 HIS B 240                ZN    ZN B 502     1555   1555  2.09  
LINK         NE2 HIS B 276                NI    NI B 501     1555   1555  2.42  
LINK         SG  CYS B 306                ZN    ZN B 502     1555   1555  2.16  
LINK         SG  CYS B 308                ZN    ZN B 502     1555   1555  2.28  
LINK        NI    NI B 501                 O01 N81 B1354     1555   1555  2.28  
LINK        NI    NI B 501                 O12 N81 B1354     1555   1555  2.53  
LINK        NI    NI B 501                 O   HOH B2048     1555   1555  2.43  
SITE     1 AC1  5 HIS A 188  GLU A 190  HIS A 276  N81 A1354                    
SITE     2 AC1  5 HOH A2050                                                     
SITE     1 AC2  4 CYS A 234  HIS A 240  CYS A 306  CYS A 308                    
SITE     1 AC3  5 HIS B 188  GLU B 190  HIS B 276  N81 B1354                    
SITE     2 AC3  5 HOH B2048                                                     
SITE     1 AC4  4 CYS B 234  HIS B 240  CYS B 306  CYS B 308                    
SITE     1 AC5 13 TYR A 132  TYR A 177  PHE A 185  HIS A 188                    
SITE     2 AC5 13 GLU A 190  SER A 196  ASN A 198  TRP A 208                    
SITE     3 AC5 13 LYS A 241  HIS A 276  SER A 288   NI A 501                    
SITE     4 AC5 13 HOH A2050                                                     
SITE     1 AC6 13 TYR B 132  TYR B 177  PHE B 185  HIS B 188                    
SITE     2 AC6 13 GLU B 190  SER B 196  ASN B 198  LYS B 206                    
SITE     3 AC6 13 TRP B 208  HIS B 276  SER B 288   NI B 501                    
SITE     4 AC6 13 HOH B2048                                                     
SITE     1 AC7  6 PHE A 227  PRO A 228  GLY A 229  SER A 230                    
SITE     2 AC7  6 HOH A2068  LYS B 105                                          
SITE     1 AC8  6 LYS A 105  PHE B 226  PHE B 227  PRO B 228                    
SITE     2 AC8  6 GLY B 229  SER B 230                                          
SITE     1 AC9  6 GLU B 235  ALA B 236  PHE B 237  LEU B 238                    
SITE     2 AC9  6 HOH B2059  HOH B2071                                          
SITE     1 BC1  6 CYS A 234  GLU A 235  ALA A 236  PHE A 237                    
SITE     2 BC1  6 LEU A 238  HOH A2085                                          
SITE     1 BC2  3 LEU A  65  GLY A 138  THR A 139                               
SITE     1 BC3  4 ARG B 295  ASP B 342  LEU B 345  HOH B2073                    
SITE     1 BC4  8 ASP B 191  MET B 192  ARG B 239  LEU B 305                    
SITE     2 BC4  8 CYS B 306  MET B 312  VAL B 313  HOH B2076                    
SITE     1 BC5  6 TYR A 253  GLY A 254  HOH A2077  HOH A2108                    
SITE     2 BC5  6 LYS B 259  VAL B 260                                          
SITE     1 BC6  6 ILE B  67  PRO B  68  ALA B  69  ALA B 134                    
SITE     2 BC6  6 ASP B 135  VAL B 136                                          
CRYST1  100.930  148.910   57.050  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      0.009908  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006715  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017528        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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