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Database: PDB
Entry: 3EP0
LinkDB: 3EP0
Original site: 3EP0 
HEADER    TRANSFERASE                             29-SEP-08   3EP0              
TITLE     METHYLTRANSFERASE DOMAIN OF HUMAN PR DOMAIN-CONTAINING                
TITLE    2 PROTEIN 12                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PR DOMAIN ZINC FINGER PROTEIN 12;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PR DOMAIN-CONTAINING PROTEIN 12;                            
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: MAN;                                                
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRDM12, PFM9;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PR DOMAIN-CONTAINING PROTEIN 12, PR DOMAIN ZINC FINGER                
KEYWDS   2 PROTEIN 12, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS                 
KEYWDS   3 CONSORTIUM, SGC, DNA-BINDING, METAL-BINDING, NUCLEUS,                
KEYWDS   4 TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC, ZINC-FINGER,          
KEYWDS   5 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.AMAYA,H.ZENG,P.LOPPNAU,C.BOUNTRA,J.WEIGELT,                       
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOTCHKAREV,J.MIN,                       
AUTHOR   3 A.N.PLOTNIKOV,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)              
REVDAT   3   25-AUG-09 3EP0    1       REMARK                                   
REVDAT   2   24-FEB-09 3EP0    1       VERSN                                    
REVDAT   1   04-NOV-08 3EP0    0                                                
JRNL        AUTH   H.ZENG,M.F.AMAYA,P.LOPPNAU,J.MIN,A.N.PLOTNIKOV,H.WU          
JRNL        TITL   THE CRYSTAL STRUCTURE OF METHYLTRANSFERASE DOMAIN            
JRNL        TITL 2 OF HUMAN PR DOMAIN-CONTAINING PROTEIN 12.                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21829                          
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) : 0.259                           
REMARK   3   R VALUE            (WORKING SET) : 0.257                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1124                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1363                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1741                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 68                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.76000                                              
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : -0.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.15000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.202         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.182         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.137         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.916         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.908                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1781 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2419 ; 1.287 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   220 ; 6.784 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    71 ;32.861 ;25.211       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   286 ;14.024 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;25.198 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   271 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1326 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   721 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1202 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   100 ; 0.136 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.166 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.166 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1148 ; 0.848 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1792 ; 1.388 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   759 ; 1.696 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   627 ; 2.526 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3EP0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049595.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
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 DW                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21829                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 3DAL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PURIFIED PRDM12 WAS CRYSTALLIZED         
REMARK 280  USING HANGING DROP VAPOR DIFFUSION METHOD AT 293K BY MIXING         
REMARK 280  THE PROTEIN SOLUTION WITH THE RESERVOIR SOLUTION CONTAINING         
REMARK 280  19% PEG 2,000 MME, 0.1 M KSCN., VAPOR DIFFUSION, HANGING DROP       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       69.44100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       17.17900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       69.44100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       17.17900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LYS A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     GLN A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     PHE A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     GLU A    66                                                      
REMARK 465     HIS A    67                                                      
REMARK 465     VAL A    68                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     ILE A    70                                                      
REMARK 465     CYS A    71                                                      
REMARK 465     LYS A    72                                                      
REMARK 465     ASN A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     ASN A    75                                                      
REMARK 465     SER A    94                                                      
REMARK 465     GLN A    95                                                      
REMARK 465     GLU A    96                                                      
REMARK 465     ASP A    97                                                      
REMARK 465     HIS A    98                                                      
REMARK 465     ARG A    99                                                      
REMARK 465     SER A   146                                                      
REMARK 465     HIS A   147                                                      
REMARK 465     ASN A   148                                                      
REMARK 465     THR A   149                                                      
REMARK 465     PHE A   150                                                      
REMARK 465     LEU A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     ILE A   153                                                      
REMARK 465     PRO A   154                                                      
REMARK 465     GLY A   155                                                      
REMARK 465     VAL A   156                                                      
REMARK 465     PRO A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     LEU A   159                                                      
REMARK 465     GLU A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     ASP A   162                                                      
REMARK 465     GLN A   163                                                      
REMARK 465     LYS A   164                                                      
REMARK 465     LYS A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     LYS A   167                                                      
REMARK 465     HIS A   168                                                      
REMARK 465     GLU A   169                                                      
REMARK 465     ASP A   170                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     PHE B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     GLN B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     PHE B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     GLU B    16                                                      
REMARK 465     GLU B    66                                                      
REMARK 465     HIS B    67                                                      
REMARK 465     VAL B    68                                                      
REMARK 465     ASP B    69                                                      
REMARK 465     ILE B    70                                                      
REMARK 465     CYS B    71                                                      
REMARK 465     LYS B    72                                                      
REMARK 465     ASN B    73                                                      
REMARK 465     ASN B    74                                                      
REMARK 465     ASN B    75                                                      
REMARK 465     SER B    94                                                      
REMARK 465     GLN B    95                                                      
REMARK 465     GLU B    96                                                      
REMARK 465     ASP B    97                                                      
REMARK 465     HIS B    98                                                      
REMARK 465     ARG B    99                                                      
REMARK 465     SER B   146                                                      
REMARK 465     HIS B   147                                                      
REMARK 465     ASN B   148                                                      
REMARK 465     THR B   149                                                      
REMARK 465     PHE B   150                                                      
REMARK 465     LEU B   151                                                      
REMARK 465     GLY B   152                                                      
REMARK 465     ILE B   153                                                      
REMARK 465     PRO B   154                                                      
REMARK 465     GLY B   155                                                      
REMARK 465     VAL B   156                                                      
REMARK 465     PRO B   157                                                      
REMARK 465     GLY B   158                                                      
REMARK 465     LEU B   159                                                      
REMARK 465     GLU B   160                                                      
REMARK 465     GLU B   161                                                      
REMARK 465     ASP B   162                                                      
REMARK 465     GLN B   163                                                      
REMARK 465     LYS B   164                                                      
REMARK 465     LYS B   165                                                      
REMARK 465     ASN B   166                                                      
REMARK 465     LYS B   167                                                      
REMARK 465     HIS B   168                                                      
REMARK 465     GLU B   169                                                      
REMARK 465     ASP B   170                                                      
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     VAL A  17    CG1  CG2                                            
REMARK 470     LEU A  23    CD1  CD2                                            
REMARK 470     ILE A  36    CB   CG1  CG2  CD1                                  
REMARK 470     LYS A  50    CG   CD   CE   NZ                                   
REMARK 470     ARG A  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA A  64    CB                                                  
REMARK 470     GLU A 131    CD   OE1  OE2                                       
REMARK 470     MET A 132    CG   SD   CE                                        
REMARK 470     ASN A 145    CG   OD1  ND2                                       
REMARK 470     VAL B  17    CG1  CG2                                            
REMARK 470     GLN B  18    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  39    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA B  64    CB                                                  
REMARK 470     GLU B  83    CG   CD   OE1  OE2                                  
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    PRO A  37      -58.61    -29.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3EP0 A    1   170  UNP    Q9H4Q4   PRD12_HUMAN     60    229             
DBREF  3EP0 B    1   170  UNP    Q9H4Q4   PRD12_HUMAN     60    229             
SEQRES   1 A  170  LYS THR ALA PHE THR ALA GLU VAL LEU ALA GLN SER PHE          
SEQRES   2 A  170  SER GLY GLU VAL GLN LYS LEU SER SER LEU VAL LEU PRO          
SEQRES   3 A  170  ALA GLU VAL ILE ILE ALA GLN SER SER ILE PRO GLY GLU          
SEQRES   4 A  170  GLY LEU GLY ILE PHE SER LYS THR TRP ILE LYS ALA GLY          
SEQRES   5 A  170  THR GLU MET GLY PRO PHE THR GLY ARG VAL ILE ALA PRO          
SEQRES   6 A  170  GLU HIS VAL ASP ILE CYS LYS ASN ASN ASN LEU MET TRP          
SEQRES   7 A  170  GLU VAL PHE ASN GLU ASP GLY THR VAL ARG TYR PHE ILE          
SEQRES   8 A  170  ASP ALA SER GLN GLU ASP HIS ARG SER TRP MET THR TYR          
SEQRES   9 A  170  ILE LYS CYS ALA ARG ASN GLU GLN GLU GLN ASN LEU GLU          
SEQRES  10 A  170  VAL VAL GLN ILE GLY THR SER ILE PHE TYR LYS ALA ILE          
SEQRES  11 A  170  GLU MET ILE PRO PRO ASP GLN GLU LEU LEU VAL TRP TYR          
SEQRES  12 A  170  GLY ASN SER HIS ASN THR PHE LEU GLY ILE PRO GLY VAL          
SEQRES  13 A  170  PRO GLY LEU GLU GLU ASP GLN LYS LYS ASN LYS HIS GLU          
SEQRES  14 A  170  ASP                                                          
SEQRES   1 B  170  LYS THR ALA PHE THR ALA GLU VAL LEU ALA GLN SER PHE          
SEQRES   2 B  170  SER GLY GLU VAL GLN LYS LEU SER SER LEU VAL LEU PRO          
SEQRES   3 B  170  ALA GLU VAL ILE ILE ALA GLN SER SER ILE PRO GLY GLU          
SEQRES   4 B  170  GLY LEU GLY ILE PHE SER LYS THR TRP ILE LYS ALA GLY          
SEQRES   5 B  170  THR GLU MET GLY PRO PHE THR GLY ARG VAL ILE ALA PRO          
SEQRES   6 B  170  GLU HIS VAL ASP ILE CYS LYS ASN ASN ASN LEU MET TRP          
SEQRES   7 B  170  GLU VAL PHE ASN GLU ASP GLY THR VAL ARG TYR PHE ILE          
SEQRES   8 B  170  ASP ALA SER GLN GLU ASP HIS ARG SER TRP MET THR TYR          
SEQRES   9 B  170  ILE LYS CYS ALA ARG ASN GLU GLN GLU GLN ASN LEU GLU          
SEQRES  10 B  170  VAL VAL GLN ILE GLY THR SER ILE PHE TYR LYS ALA ILE          
SEQRES  11 B  170  GLU MET ILE PRO PRO ASP GLN GLU LEU LEU VAL TRP TYR          
SEQRES  12 B  170  GLY ASN SER HIS ASN THR PHE LEU GLY ILE PRO GLY VAL          
SEQRES  13 B  170  PRO GLY LEU GLU GLU ASP GLN LYS LYS ASN LYS HIS GLU          
SEQRES  14 B  170  ASP                                                          
FORMUL   3  HOH   *68(H2 O)                                                     
HELIX    1   1 SER A  100  ILE A  105  5                                   6    
HELIX    2   2 SER B  100  ILE B  105  5                                   6    
SHEET    1   A 6 LYS A  19  SER A  21  0                                        
SHEET    2   A 6 GLU A  54  PHE A  58  1  O  GLU A  54   N  LEU A  20           
SHEET    3   A 6 SER A 124  ALA A 129 -1  O  TYR A 127   N  MET A  55           
SHEET    4   A 6 LEU A 116  ILE A 121 -1  N  ILE A 121   O  SER A 124           
SHEET    5   A 6 LEU A 140  TYR A 143  1  O  TRP A 142   N  VAL A 118           
SHEET    6   A 6 LYS A 106  CYS A 107  1  N  LYS A 106   O  VAL A 141           
SHEET    1   B 2 VAL A  29  GLN A  33  0                                        
SHEET    2   B 2 LEU A  41  SER A  45 -1  O  PHE A  44   N  ILE A  30           
SHEET    1   C 3 ARG A  61  ILE A  63  0                                        
SHEET    2   C 3 VAL A  87  ASP A  92 -1  O  ASP A  92   N  ARG A  61           
SHEET    3   C 3 MET A  77  PHE A  81 -1  N  VAL A  80   O  TYR A  89           
SHEET    1   D 7 LYS B  19  SER B  21  0                                        
SHEET    2   D 7 GLU B  54  PHE B  58  1  O  GLU B  54   N  LEU B  20           
SHEET    3   D 7 SER B 124  ALA B 129 -1  O  ILE B 125   N  PHE B  58           
SHEET    4   D 7 LEU B 116  ILE B 121 -1  N  ILE B 121   O  SER B 124           
SHEET    5   D 7 GLU B 138  TYR B 143  1  O  LEU B 140   N  LEU B 116           
SHEET    6   D 7 LEU B  41  SER B  45 -1  N  ILE B  43   O  LEU B 139           
SHEET    7   D 7 VAL B  29  GLN B  33 -1  N  ILE B  30   O  PHE B  44           
SHEET    1   E 6 LYS B  19  SER B  21  0                                        
SHEET    2   E 6 GLU B  54  PHE B  58  1  O  GLU B  54   N  LEU B  20           
SHEET    3   E 6 SER B 124  ALA B 129 -1  O  ILE B 125   N  PHE B  58           
SHEET    4   E 6 LEU B 116  ILE B 121 -1  N  ILE B 121   O  SER B 124           
SHEET    5   E 6 GLU B 138  TYR B 143  1  O  LEU B 140   N  LEU B 116           
SHEET    6   E 6 LYS B 106  CYS B 107  1  N  LYS B 106   O  VAL B 141           
SHEET    1   F 3 ARG B  61  ILE B  63  0                                        
SHEET    2   F 3 VAL B  87  ASP B  92 -1  O  PHE B  90   N  ILE B  63           
SHEET    3   F 3 MET B  77  PHE B  81 -1  N  VAL B  80   O  TYR B  89           
CISPEP   1 GLY A   56    PRO A   57          0        -1.57                     
CISPEP   2 GLY B   56    PRO B   57          0        -0.14                     
CRYST1  138.882   34.358  103.739  90.00 131.09  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007200  0.000000  0.006279        0.00000                         
SCALE2      0.000000  0.029105  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012790        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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