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Entry: 3RAY
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HEADER    TRANSCRIPTION                           28-MAR-11   3RAY              
TITLE     CRYSTAL STRUCTURE OF METHYLTRANSFERASE DOMAIN OF HUMAN PR DOMAIN-     
TITLE    2 CONTAINING PROTEIN 11                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PR DOMAIN-CONTAINING PROTEIN 11;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 79-314;                                           
COMPND   5 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: PRDM11, PFM8;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)V2RPRARE;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    STRUCTURAL GENOMICS CONSORTIUM, SGC, HISTONE METHYLATION, ZN-FINGER,  
KEYWDS   2 TRANSCRIPTIONAL REGULATION, CHROMATIN, TRANSCRIPTION                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,H.ZENG,P.LOPPNAU,J.R.WALKER,C.BOUNTRA,J.WEIGELT,               
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM 
AUTHOR   3 (SGC)                                                                
REVDAT   2   08-NOV-17 3RAY    1       REMARK                                   
REVDAT   1   20-APR-11 3RAY    0                                                
JRNL        AUTH   A.DONG,H.ZENG,P.LOPPNAU,J.R.WALKER,C.BOUNTRA,J.WEIGELT,      
JRNL        AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,H.WU,                       
JRNL        AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   CRYSTAL STRUCTURE OF METHYLTRANSFERASE DOMAIN OF HUMAN PR    
JRNL        TITL 2 DOMAIN-CONTAINING PROTEIN 11                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.73 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 19693                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.196                          
REMARK   3   R VALUE            (WORKING SET)  : 0.194                          
REMARK   3   FREE R VALUE                      : 0.228                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.190                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1022                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.73                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.82                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2690                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2280                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2525                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2264                   
REMARK   3   BIN FREE R VALUE                        : 0.2532                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 6.13                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 165                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1266                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 119                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.63                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.54020                                              
REMARK   3    B22 (A**2) : 1.53870                                              
REMARK   3    B33 (A**2) : -8.07890                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.247               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 1358   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 1855   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 456    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 34     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 203    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 1358   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 171    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 1623   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.99                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.45                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.40                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   26.5547   31.1919   13.9838           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1451 T22:   -0.1225                                    
REMARK   3     T33:   -0.0716 T12:    0.0164                                    
REMARK   3     T13:   -0.0080 T23:    0.0266                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.6009 L22:    3.4138                                    
REMARK   3     L33:    2.5324 L12:    0.2641                                    
REMARK   3     L13:   -0.1296 L23:    0.1599                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0819 S12:    0.0285 S13:    0.0900                     
REMARK   3     S21:   -0.1276 S22:   -0.0254 S23:    0.2014                     
REMARK   3     S31:    0.0890 S32:    0.0037 S33:   -0.0565                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3RAY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000064706.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : VERIMAX HR                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19744                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.730                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : 0.03600                            
REMARK 200  R SYM                      (I) : 0.03600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 59.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.67800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: 3DB5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 25.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%PEG 3350, 0.2M KCL , VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 297K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       15.57700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.14150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.57800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.14150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       15.57700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       27.57800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     GLY A     0                                                      
REMARK 465     ASP A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     ILE A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     PHE A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     GLN A    26                                                      
REMARK 465     VAL A    27                                                      
REMARK 465     ASP A   109                                                      
REMARK 465     LYS A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     ALA A   112                                                      
REMARK 465     GLY A   113                                                      
REMARK 465     MET A   192                                                      
REMARK 465     SER A   193                                                      
REMARK 465     GLN A   194                                                      
REMARK 465     GLU A   195                                                      
REMARK 465     THR A   196                                                      
REMARK 465     ILE A   197                                                      
REMARK 465     HIS A   198                                                      
REMARK 465     ARG A   199                                                      
REMARK 465     ASN A   200                                                      
REMARK 465     LEU A   201                                                      
REMARK 465     ALA A   202                                                      
REMARK 465     ARG A   203                                                      
REMARK 465     GLY A   204                                                      
REMARK 465     GLU A   205                                                      
REMARK 465     LYS A   206                                                      
REMARK 465     ARG A   207                                                      
REMARK 465     LEU A   208                                                      
REMARK 465     GLN A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     GLU A   211                                                      
REMARK 465     LYS A   212                                                      
REMARK 465     SER A   213                                                      
REMARK 465     GLU A   214                                                      
REMARK 465     GLN A   215                                                      
REMARK 465     VAL A   216                                                      
REMARK 465     LEU A   217                                                      
REMARK 465     ASP A   218                                                      
REMARK 465     ASN A   219                                                      
REMARK 465     PRO A   220                                                      
REMARK 465     GLU A   221                                                      
REMARK 465     ASP A   222                                                      
REMARK 465     LEU A   223                                                      
REMARK 465     ARG A   224                                                      
REMARK 465     GLY A   225                                                      
REMARK 465     PRO A   226                                                      
REMARK 465     ILE A   227                                                      
REMARK 465     HIS A   228                                                      
REMARK 465     LEU A   229                                                      
REMARK 465     SER A   230                                                      
REMARK 465     VAL A   231                                                      
REMARK 465     LEU A   232                                                      
REMARK 465     ARG A   233                                                      
REMARK 465     GLN A   234                                                      
REMARK 465     GLY A   235                                                      
REMARK 465     LYS A   236                                                      
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     PHE A  29    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A  40    CG1  CG2                                            
REMARK 470     ASN A  45    CG   OD1  ND2                                       
REMARK 470     GLN A 108    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 122    CG   CD   CE   NZ                                   
REMARK 470     ASN A 123    CG   OD1  ND2                                       
REMARK 470     ARG A 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 148    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 149    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 150    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 172    NH1  NH2                                            
REMARK 470     LYS A 187    CD   CE   NZ                                        
REMARK 470     SER A 191    OG                                                  
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   UNK  UNX A   240     UNK  UNX A   241              1.90            
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    ASP A  41      -10.67   -149.06                                   
REMARK 500    ASN A  89      -61.73     77.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  43   SG                                                     
REMARK 620 2 HIS A  46   ND1 119.0                                              
REMARK 620 3 CYS A  32   SG  110.7  93.5                                        
REMARK 620 4 CYS A  35   SG  119.8  88.5 120.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1002  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  90   O                                                      
REMARK 620 2 GLY A  72   O   129.8                                              
REMARK 620 3 VAL A  88   O    82.5  64.0                                        
REMARK 620 4 HOH A 306   O   106.5 108.1  87.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1003  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 142   O                                                      
REMARK 620 2 SER A  83   O    90.4                                              
REMARK 620 3 HOH A 287   O    77.3 167.1                                        
REMARK 620 N                    1     2                                         
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 1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1003                 
DBREF  3RAY A    1   236  UNP    Q9NQV5   PRD11_HUMAN     79    314             
SEQADV 3RAY GLY A    0  UNP  Q9NQV5              EXPRESSION TAG                 
SEQRES   1 A  237  GLY ASP SER SER ALA MET GLU VAL GLU PRO LYS LYS LEU          
SEQRES   2 A  237  LYS GLY LYS ARG ASP LEU ILE VAL PRO LYS SER PHE GLN          
SEQRES   3 A  237  GLN VAL ASP PHE TRP PHE CYS GLU SER CYS GLN GLU TYR          
SEQRES   4 A  237  PHE VAL ASP GLU CYS PRO ASN HIS GLY PRO PRO VAL PHE          
SEQRES   5 A  237  VAL SER ASP THR PRO VAL PRO VAL GLY ILE PRO ASP ARG          
SEQRES   6 A  237  ALA ALA LEU THR ILE PRO GLN GLY MET GLU VAL VAL LYS          
SEQRES   7 A  237  ASP THR SER GLY GLU SER ASP VAL ARG CYS VAL ASN GLU          
SEQRES   8 A  237  VAL ILE PRO LYS GLY HIS ILE PHE GLY PRO TYR GLU GLY          
SEQRES   9 A  237  GLN ILE SER THR GLN ASP LYS SER ALA GLY PHE PHE SER          
SEQRES  10 A  237  TRP LEU ILE VAL ASP LYS ASN ASN ARG TYR LYS SER ILE          
SEQRES  11 A  237  ASP GLY SER ASP GLU THR LYS ALA ASN TRP MET ARG TYR          
SEQRES  12 A  237  VAL VAL ILE SER ARG GLU GLU ARG GLU GLN ASN LEU LEU          
SEQRES  13 A  237  ALA PHE GLN HIS SER GLU ARG ILE TYR PHE ARG ALA CYS          
SEQRES  14 A  237  ARG ASP ILE ARG PRO GLY GLU TRP LEU ARG VAL TRP TYR          
SEQRES  15 A  237  SER GLU ASP TYR MET LYS ARG LEU HIS SER MET SER GLN          
SEQRES  16 A  237  GLU THR ILE HIS ARG ASN LEU ALA ARG GLY GLU LYS ARG          
SEQRES  17 A  237  LEU GLN ARG GLU LYS SER GLU GLN VAL LEU ASP ASN PRO          
SEQRES  18 A  237  GLU ASP LEU ARG GLY PRO ILE HIS LEU SER VAL LEU ARG          
SEQRES  19 A  237  GLN GLY LYS                                                  
HET     ZN  A1000       1                                                       
HET     CL  A1001       1                                                       
HET     NA  A1002       1                                                       
HET     NA  A1003       1                                                       
HET    UNX  A 237       1                                                       
HET    UNX  A 238       1                                                       
HET    UNX  A 239       1                                                       
HET    UNX  A 240       1                                                       
HET    UNX  A 241       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   CL    CL 1-                                                        
FORMUL   4   NA    2(NA 1+)                                                     
FORMUL   6  UNX    5(X)                                                         
FORMUL  11  HOH   *119(H2 O)                                                    
HELIX    1   1 ASP A   63  THR A   68  1                                   6    
HELIX    2   2 ASN A  138  VAL A  143  5                                   6    
HELIX    3   3 SER A  182  HIS A  190  1                                   9    
SHEET    1   A 2 TRP A  30  CYS A  32  0                                        
SHEET    2   A 2 GLU A  37  PHE A  39 -1  O  GLU A  37   N  CYS A  32           
SHEET    1   B 6 VAL A  50  VAL A  52  0                                        
SHEET    2   B 6 HIS A  96  PHE A  98  1  O  ILE A  97   N  VAL A  52           
SHEET    3   B 6 ARG A 162  ALA A 167 -1  O  PHE A 165   N  PHE A  98           
SHEET    4   B 6 LEU A 154  HIS A 159 -1  N  PHE A 157   O  TYR A 164           
SHEET    5   B 6 ARG A 178  TYR A 181  1  O  TRP A 180   N  ALA A 156           
SHEET    6   B 6 VAL A 144  ILE A 145  1  N  VAL A 144   O  VAL A 179           
SHEET    1   C 2 MET A  73  LYS A  77  0                                        
SHEET    2   C 2 SER A  83  CYS A  87 -1  O  ASP A  84   N  VAL A  76           
SHEET    1   D 3 GLN A 104  SER A 106  0                                        
SHEET    2   D 3 TYR A 126  ASP A 130 -1  O  ASP A 130   N  GLN A 104           
SHEET    3   D 3 SER A 116  VAL A 120 -1  N  TRP A 117   O  ILE A 129           
LINK         SG  CYS A  43                ZN    ZN A1000     1555   1555  2.26  
LINK         ND1 HIS A  46                ZN    ZN A1000     1555   1555  2.39  
LINK         SG  CYS A  32                ZN    ZN A1000     1555   1555  2.43  
LINK         SG  CYS A  35                ZN    ZN A1000     1555   1555  2.47  
LINK         O   GLU A  90                NA    NA A1002     1555   1555  2.69  
LINK         O   TYR A 142                NA    NA A1003     1555   1555  2.78  
LINK         O   GLY A  72                NA    NA A1002     1555   1555  2.78  
LINK         O   SER A  83                NA    NA A1003     1555   1555  2.89  
LINK         O   VAL A  88                NA    NA A1002     1555   1555  2.99  
LINK        NA    NA A1002                 O   HOH A 306     1555   1555  3.18  
LINK        NA    NA A1003                 O   HOH A 287     1555   1555  3.19  
CISPEP   1 GLY A   99    PRO A  100          0         9.03                     
SITE     1 AC1  4 CYS A  32  CYS A  35  CYS A  43  HIS A  46                    
SITE     1 AC2  3 GLN A 158  TYR A 185  ARG A 188                               
SITE     1 AC3  4 GLY A  72  CYS A  87  VAL A  88  GLU A  90                    
SITE     1 AC4  2 SER A  83  TYR A 142                                          
CRYST1   31.154   55.156  106.283  90.00  90.00  90.00 P 21 21 21    4          
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      0.032099  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018130  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009409        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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