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Database: PDB
Entry: 5PH0
LinkDB: 5PH0
Original site: 5PH0 
HEADER    OXIDOREDUCTASE                          07-FEB-17   5PH0              
TITLE     PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF JMJD2D IN    
TITLE    2 COMPLEX WITH N09484A                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4D;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3D,    
COMPND   5 JUMONJI DOMAIN-CONTAINING PROTEIN 2D;                                
COMPND   6 EC: 1.14.11.-;                                                       
COMPND   7 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: KDM4D, JHDM3D, JMJD2D;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PANDDA, SGC - DIAMOND I04-1 FRAGMENT SCREENING, JMJ DOMAIN,           
KEYWDS   2 EPIGENETICS, OXIDOREDUCTASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.M.PEARCE,T.KROJER,R.TALON,A.R.BRADLEY,M.FAIRHEAD,R.SETHI,N.WRIGHT,  
AUTHOR   2 E.MACLEAN,P.COLLINS,J.BRANDAO-NETO,A.DOUANGAMATH,Z.RENJIE,A.DIAS,    
AUTHOR   3 M.VOLLMAR,J.NG,A.SZYKOWSKA,N.BURGESS-BROWN,P.E.BRENNAN,O.COX,        
AUTHOR   4 U.OPPERMANN,C.BOUNTRA,C.H.ARROWSMITH,A.EDWARDS,F.VON DELFT           
REVDAT   4   06-MAR-24 5PH0    1       LINK                                     
REVDAT   3   04-OCT-17 5PH0    1       REMARK                                   
REVDAT   2   27-SEP-17 5PH0    1       JRNL   REMARK                            
REVDAT   1   15-MAR-17 5PH0    0                                                
JRNL        AUTH   N.M.PEARCE,T.KROJER,A.R.BRADLEY,P.COLLINS,R.P.NOWAK,R.TALON, 
JRNL        AUTH 2 B.D.MARSDEN,S.KELM,J.SHI,C.M.DEANE,F.VON DELFT               
JRNL        TITL   A MULTI-CRYSTAL METHOD FOR EXTRACTING OBSCURED               
JRNL        TITL 2 CRYSTALLOGRAPHIC STATES FROM CONVENTIONALLY UNINTERPRETABLE  
JRNL        TITL 3 ELECTRON DENSITY.                                            
JRNL        REF    NAT COMMUN                    V.   8 15123 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   28436492                                                     
JRNL        DOI    10.1038/NCOMMS15123                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1682                                      
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) : 1.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.41                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 87409                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.130                           
REMARK   3   R VALUE            (WORKING SET) : 0.128                           
REMARK   3   FREE R VALUE                     : 0.162                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4300                            
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 29.4176 -  4.1624    1.00     3090   142  0.1510 0.1676        
REMARK   3     2  4.1624 -  3.3052    1.00     2913   144  0.1275 0.1508        
REMARK   3     3  3.3052 -  2.8878    1.00     2838   158  0.1329 0.1876        
REMARK   3     4  2.8878 -  2.6240    1.00     2837   152  0.1416 0.1724        
REMARK   3     5  2.6240 -  2.4360    1.00     2836   143  0.1322 0.1812        
REMARK   3     6  2.4360 -  2.2924    1.00     2796   147  0.1318 0.1695        
REMARK   3     7  2.2924 -  2.1777    1.00     2824   124  0.1265 0.1574        
REMARK   3     8  2.1777 -  2.0829    1.00     2821   126  0.1200 0.1592        
REMARK   3     9  2.0829 -  2.0027    1.00     2797   132  0.1141 0.1505        
REMARK   3    10  2.0027 -  1.9336    1.00     2751   159  0.1166 0.1504        
REMARK   3    11  1.9336 -  1.8732    1.00     2776   153  0.1115 0.1396        
REMARK   3    12  1.8732 -  1.8197    1.00     2773   144  0.1104 0.1437        
REMARK   3    13  1.8197 -  1.7718    1.00     2764   153  0.1096 0.1444        
REMARK   3    14  1.7718 -  1.7285    1.00     2772   143  0.1068 0.1340        
REMARK   3    15  1.7285 -  1.6892    1.00     2746   145  0.1050 0.1250        
REMARK   3    16  1.6892 -  1.6533    1.00     2777   137  0.1075 0.1567        
REMARK   3    17  1.6533 -  1.6202    1.00     2765   132  0.1066 0.1494        
REMARK   3    18  1.6202 -  1.5897    1.00     2727   155  0.1015 0.1529        
REMARK   3    19  1.5897 -  1.5613    1.00     2785   133  0.1093 0.1503        
REMARK   3    20  1.5613 -  1.5348    1.00     2744   133  0.1087 0.1436        
REMARK   3    21  1.5348 -  1.5100    1.00     2754   159  0.1112 0.1484        
REMARK   3    22  1.5100 -  1.4868    1.00     2733   138  0.1157 0.1523        
REMARK   3    23  1.4868 -  1.4649    1.00     2755   156  0.1213 0.1833        
REMARK   3    24  1.4649 -  1.4443    1.00     2719   145  0.1263 0.1519        
REMARK   3    25  1.4443 -  1.4248    1.00     2740   147  0.1335 0.1628        
REMARK   3    26  1.4248 -  1.4063    1.00     2735   151  0.1463 0.2041        
REMARK   3    27  1.4063 -  1.3887    1.00     2727   164  0.1585 0.2023        
REMARK   3    28  1.3887 -  1.3720    0.99     2714   126  0.1729 0.2117        
REMARK   3    29  1.3720 -  1.3560    0.97     2647   141  0.1750 0.2266        
REMARK   3    30  1.3560 -  1.3408    0.89     2453   118  0.1887 0.1958        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.090            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.99                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.88                          
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      :  0.006           3123                                  
REMARK   3   ANGLE     :  1.092           4275                                  
REMARK   3   CHIRALITY :  0.049            422                                  
REMARK   3   PLANARITY :  0.006            567                                  
REMARK   3   DIHEDRAL  : 12.715           1199                                  
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: NULL                                      
REMARK   4                                                                      
REMARK   4 5PH0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1001400648.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97630                            
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          : AIMLESS 0.1.27                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87517                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.410                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 11.80                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 4D6R                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG3350 -- 0.1M HEPES PH 7.0 --      
REMARK 280  0.25M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       75.13200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       35.73350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       35.73350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      112.69800            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       35.73350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       35.73350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       37.56600            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       35.73350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.73350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      112.69800            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       35.73350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.73350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       37.56600            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       75.13200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 832  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     GLU A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     CYS A    10                                                      
REMARK 465     ARG A   342                                                      
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  61    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  92    NZ                                                  
REMARK 470     ARG A 225    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 255    CD   CE   NZ                                        
REMARK 470     ARG A 316    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 338    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 341    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   569     O    HOH A   851              2.17            
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    LYS A 186       -5.33     75.26                                   
REMARK 500    MET A 196       19.46     58.59                                   
REMARK 500    ARG A 316       94.87     46.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 954        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A 955        DISTANCE =  6.56 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 <JMJD2DA-X336> <USED_FOR_STATISTICAL_MAP>YES</USED_FOR_STATISTICAL_  
REMARK 600 MAP> <SMILES_OF_COMPOUND_ADDED>C1CC2C(CC1N)NC(C(F)(F)F)[NH]2</       
REMARK 600 SMILES_OF_COMPOUND_ADDED> <SITE12> <LABEL>NONE</LABEL> <COORDINATE>- 
REMARK 600 10.78 -7.18 -7.18</COORDINATE> <SMILES>C1CC2C(CC1N)NC(C(F)(F)F)[NH]  
REMARK 600 2</SMILES> <CONFIDENCE>4 - HIGH CONFIDENCE</CONFIDENCE> <COMMENT>    
REMARK 600 NONE</COMMENT> <OCCUPANCY>0.22</OCCUPANCY> <B_AVERAGE>16.785</B_     
REMARK 600 AVERAGE> <B_RATIO>1.2954969316716323</B_RATIO> <RSCC>0.875</RSCC> <  
REMARK 600 RSR>0.157</RSR> <RSZD>1.8</RSZD> <RMSD>0.1456880228433346</RMSD> </  
REMARK 600 SITE12> </JMJD2DA-X336>                                              
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                              MG A 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  65   O                                                      
REMARK 620 2 VAL A 171   O   101.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 402  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 192   NE2                                                    
REMARK 620 2 GLU A 194   OE1  98.7                                              
REMARK 620 3 HIS A 280   NE2  85.8  90.0                                        
REMARK 620 4 OGA A 404   O1  168.2  93.0  95.3                                  
REMARK 620 5 OGA A 404   O2'  91.0 169.3  95.2  77.2                            
REMARK 620 6 HOH A 598   O    90.3  87.1 174.7  89.2  88.4                      
REMARK 620 N                    1     2     3     4     5                       
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 238   SG                                                     
REMARK 620 2 HIS A 244   NE2 108.4                                              
REMARK 620 3 CYS A 310   SG  116.9 110.3                                        
REMARK 620 4 CYS A 312   SG  114.2  98.8 106.6                                  
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 NI A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OGA A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 71N A 417                 
DBREF  5PH0 A    1   342  UNP    Q6B0I6   KDM4D_HUMAN      1    342             
SEQADV 5PH0 MET A  -21  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 HIS A  -20  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 HIS A  -19  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 HIS A  -18  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 HIS A  -17  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 HIS A  -16  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 HIS A  -15  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 SER A  -14  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 SER A  -13  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 GLY A  -12  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 VAL A  -11  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 ASP A  -10  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 LEU A   -9  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 GLY A   -8  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 THR A   -7  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 GLU A   -6  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 ASN A   -5  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 LEU A   -4  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 TYR A   -3  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 PHE A   -2  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 GLN A   -1  UNP  Q6B0I6              EXPRESSION TAG                 
SEQADV 5PH0 SER A    0  UNP  Q6B0I6              EXPRESSION TAG                 
SEQRES   1 A  364  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  364  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU THR MET          
SEQRES   3 A  364  LYS SER LYS ALA ASN CYS ALA GLN ASN PRO ASN CYS ASN          
SEQRES   4 A  364  ILE MET ILE PHE HIS PRO THR LYS GLU GLU PHE ASN ASP          
SEQRES   5 A  364  PHE ASP LYS TYR ILE ALA TYR MET GLU SER GLN GLY ALA          
SEQRES   6 A  364  HIS ARG ALA GLY LEU ALA LYS ILE ILE PRO PRO LYS GLU          
SEQRES   7 A  364  TRP LYS ALA ARG GLU THR TYR ASP ASN ILE SER GLU ILE          
SEQRES   8 A  364  LEU ILE ALA THR PRO LEU GLN GLN VAL ALA SER GLY ARG          
SEQRES   9 A  364  ALA GLY VAL PHE THR GLN TYR HIS LYS LYS LYS LYS ALA          
SEQRES  10 A  364  MET THR VAL GLY GLU TYR ARG HIS LEU ALA ASN SER LYS          
SEQRES  11 A  364  LYS TYR GLN THR PRO PRO HIS GLN ASN PHE GLU ASP LEU          
SEQRES  12 A  364  GLU ARG LYS TYR TRP LYS ASN ARG ILE TYR ASN SER PRO          
SEQRES  13 A  364  ILE TYR GLY ALA ASP ILE SER GLY SER LEU PHE ASP GLU          
SEQRES  14 A  364  ASN THR LYS GLN TRP ASN LEU GLY HIS LEU GLY THR ILE          
SEQRES  15 A  364  GLN ASP LEU LEU GLU LYS GLU CYS GLY VAL VAL ILE GLU          
SEQRES  16 A  364  GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP LYS          
SEQRES  17 A  364  THR THR PHE ALA TRP HIS THR GLU ASP MET ASP LEU TYR          
SEQRES  18 A  364  SER ILE ASN TYR LEU HIS LEU GLY GLU PRO LYS THR TRP          
SEQRES  19 A  364  TYR VAL VAL PRO PRO GLU HIS GLY GLN ARG LEU GLU ARG          
SEQRES  20 A  364  LEU ALA ARG GLU LEU PHE PRO GLY SER SER ARG GLY CYS          
SEQRES  21 A  364  GLY ALA PHE LEU ARG HIS LYS VAL ALA LEU ILE SER PRO          
SEQRES  22 A  364  THR VAL LEU LYS GLU ASN GLY ILE PRO PHE ASN ARG ILE          
SEQRES  23 A  364  THR GLN GLU ALA GLY GLU PHE MET VAL THR PHE PRO TYR          
SEQRES  24 A  364  GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS ALA          
SEQRES  25 A  364  GLU ALA ILE ASN PHE ALA THR PRO ARG TRP ILE ASP TYR          
SEQRES  26 A  364  GLY LYS MET ALA SER GLN CYS SER CYS GLY GLU ALA ARG          
SEQRES  27 A  364  VAL THR PHE SER MET ASP ALA PHE VAL ARG ILE LEU GLN          
SEQRES  28 A  364  PRO GLU ARG TYR ASP LEU TRP LYS ARG GLY GLN ASP ARG          
HET     ZN  A 401       1                                                       
HET     NI  A 402       1                                                       
HET     MG  A 403       1                                                       
HET    OGA  A 404      10                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HET    EDO  A 408       4                                                       
HET    EDO  A 409       4                                                       
HET    EDO  A 410       4                                                       
HET    EDO  A 411       4                                                       
HET    EDO  A 412       4                                                       
HET    SO4  A 413       5                                                       
HET    SO4  A 414       5                                                       
HET    SO4  A 415       5                                                       
HET    SO4  A 416       5                                                       
HET    71N  A 417      14                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      NI NICKEL (II) ION                                                  
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     OGA N-OXALYLGLYCINE                                                  
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM     71N 2-(TRIFLUOROMETHYL)-1H-BENZIMIDAZOL-5-AMINE                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   NI    NI 2+                                                        
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  OGA    C4 H5 N O5                                                   
FORMUL   6  EDO    8(C2 H6 O2)                                                  
FORMUL  14  SO4    4(O4 S 2-)                                                   
FORMUL  18  71N    C8 H6 F3 N3                                                  
FORMUL  19  HOH   *455(H2 O)                                                    
HELIX    1 AA1 ASP A   30  GLN A   41  1                                  12    
HELIX    2 AA2 GLY A   42  ALA A   46  5                                   5    
HELIX    3 AA3 VAL A   98  ASN A  106  1                                   9    
HELIX    4 AA4 ASN A  117  ARG A  129  1                                  13    
HELIX    5 AA5 ILE A  130  ASN A  132  5                                   3    
HELIX    6 AA6 THR A  159  GLY A  169  1                                  11    
HELIX    7 AA7 GLU A  194  LEU A  198  5                                   5    
HELIX    8 AA8 PRO A  216  GLU A  218  5                                   3    
HELIX    9 AA9 HIS A  219  PHE A  231  1                                  13    
HELIX   10 AB1 PHE A  231  CYS A  238  1                                   8    
HELIX   11 AB2 ALA A  240  LYS A  245  5                                   6    
HELIX   12 AB3 SER A  250  ASN A  257  1                                   8    
HELIX   13 AB4 ARG A  299  ALA A  307  1                                   9    
HELIX   14 AB5 PHE A  319  GLN A  329  1                                  11    
HELIX   15 AB6 GLN A  329  ASP A  341  1                                  13    
SHEET    1 AA110 MET A  19  PHE A  21  0                                        
SHEET    2 AA110 LEU A  48  ILE A  51  1  O  LYS A  50   N  PHE A  21           
SHEET    3 AA110 PHE A 271  THR A 274 -1  O  PHE A 271   N  ILE A  51           
SHEET    4 AA110 TYR A 199  GLY A 207 -1  N  ASN A 202   O  MET A 272           
SHEET    5 AA110 ASN A 288  PHE A 295 -1  O  GLU A 291   N  TYR A 203           
SHEET    6 AA110 TYR A 179  GLY A 183 -1  N  TYR A 181   O  ALA A 290           
SHEET    7 AA110 ILE A 135  SER A 141 -1  N  ILE A 140   O  LEU A 180           
SHEET    8 AA110 LEU A  75  GLY A  81 -1  N  LEU A  75   O  TYR A 136           
SHEET    9 AA110 VAL A  85  LYS A  92 -1  O  LYS A  91   N  GLN A  76           
SHEET   10 AA110 ALA A 247  ILE A 249 -1  O  LEU A 248   N  PHE A  86           
SHEET    1 AA2 2 LEU A  70  ILE A  71  0                                        
SHEET    2 AA2 2 MET A  96  THR A  97 -1  O  MET A  96   N  ILE A  71           
SHEET    1 AA3 4 THR A 188  HIS A 192  0                                        
SHEET    2 AA3 4 TYR A 279  ASN A 284 -1  O  GLY A 282   N  PHE A 189           
SHEET    3 AA3 4 LYS A 210  VAL A 215 -1  N  TYR A 213   O  ALA A 281           
SHEET    4 AA3 4 ASN A 262  GLN A 266 -1  O  GLN A 266   N  LYS A 210           
LINK         O   ASN A  65                MG    MG A 403     1555   1555  2.78  
LINK         O   VAL A 171                MG    MG A 403     1555   8555  2.74  
LINK         NE2 HIS A 192                NI    NI A 402     1555   1555  2.19  
LINK         OE1 GLU A 194                NI    NI A 402     1555   1555  2.03  
LINK         SG  CYS A 238                ZN    ZN A 401     1555   1555  2.30  
LINK         NE2 HIS A 244                ZN    ZN A 401     1555   1555  2.08  
LINK         NE2 HIS A 280                NI    NI A 402     1555   1555  2.15  
LINK         SG  CYS A 310                ZN    ZN A 401     1555   1555  2.28  
LINK         SG  CYS A 312                ZN    ZN A 401     1555   1555  2.31  
LINK        NI    NI A 402                 O1  OGA A 404     1555   1555  2.12  
LINK        NI    NI A 402                 O2' OGA A 404     1555   1555  2.08  
LINK        NI    NI A 402                 O   HOH A 598     1555   1555  2.13  
SITE     1 AC1  4 CYS A 238  HIS A 244  CYS A 310  CYS A 312                    
SITE     1 AC2  5 HIS A 192  GLU A 194  HIS A 280  OGA A 404                    
SITE     2 AC2  5 HOH A 598                                                     
SITE     1 AC3  7 ASN A  65  ILE A  66  SER A  67  GLU A  68                    
SITE     2 AC3  7 ILE A  69  VAL A 170  VAL A 171                               
SITE     1 AC4 12 TYR A 136  PHE A 189  HIS A 192  GLU A 194                    
SITE     2 AC4 12 SER A 200  ASN A 202  LYS A 210  HIS A 280                    
SITE     3 AC4 12  NI A 402  EDO A 412  HOH A 598  HOH A 763                    
SITE     1 AC5  7 LYS A 150  GLN A 151  TRP A 152  ASN A 153                    
SITE     2 AC5  7 HIS A 156  HOH A 579  HOH A 704                               
SITE     1 AC6  4 PRO A 251  THR A 252  ARG A 263  HOH A 684                    
SITE     1 AC7  8 GLU A 224  ALA A 240  PHE A 241  LEU A 242                    
SITE     2 AC7  8 TYR A 279  SER A 308  HOH A 506  HOH A 634                    
SITE     1 AC8  7 ASP A  64  ASN A  65  ILE A  66  SER A  67                    
SITE     2 AC8  7 GLU A  68  ARG A  82  HOH A 556                               
SITE     1 AC9  4 PHE A 118  ILE A 264  THR A 265  HOH A 548                    
SITE     1 AD1  8 TRP A  57  LYS A  58  ALA A  59  TYR A 203                    
SITE     2 AD1  8 HOH A 503  HOH A 504  HOH A 593  HOH A 697                    
SITE     1 AD2  6 SER A  80  THR A  87  CYS A 168  LYS A 305                    
SITE     2 AD2  6 HOH A 537  HOH A 545                                          
SITE     1 AD3  6 TYR A 179  TYR A 181  SER A 200  ASN A 294                    
SITE     2 AD3  6 OGA A 404  HOH A 598                                          
SITE     1 AD4  6 ARG A 102  HIS A 103  ASN A 106  HOH A 510                    
SITE     2 AD4  6 HOH A 554  HOH A 646                                          
SITE     1 AD5  8 ARG A  60  GLU A  61  THR A  62  ASP A  64                    
SITE     2 AD5  8 HOH A 507  HOH A 546  HOH A 565  HOH A 670                    
SITE     1 AD6  4 ARG A 123  LYS A 124  LYS A 127  ASN A 128                    
SITE     1 AD7  6 PRO A 113  LYS A 124  ASN A 128  TRP A 185                    
SITE     2 AD7  6 LYS A 186  HOH A 628                                          
SITE     1 AD8 11 GLU A  39  HIS A  44  TYR A 199  PHE A 275                    
SITE     2 AD8 11 PRO A 276  ARG A 299  TYR A 303  HOH A 703                    
SITE     3 AD8 11 HOH A 750  HOH A 794  HOH A 894                               
CRYST1   71.467   71.467  150.264  90.00  90.00  90.00 P 43 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      0.013992  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013992  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006655        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system