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Database: PDB
Entry: 3DAL
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Original site: 3DAL 
HEADER    TRANSFERASE                             29-MAY-08   3DAL              
TITLE     METHYLTRANSFERASE DOMAIN OF HUMAN PR DOMAIN-CONTAINING PROTEIN 1      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PR DOMAIN ZINC FINGER PROTEIN 1;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PR DOMAIN-CONTAINING PROTEIN 1, BETA-INTERFERON GENE        
COMPND   5 POSITIVE REGULATORY DOMAIN I-BINDING FACTOR, BLIMP-1, POSITIVE       
COMPND   6 REGULATORY DOMAIN I-BINDING FACTOR 1, PRDI-BINDING FACTOR 1, PRDI-   
COMPND   7 BF1;                                                                 
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRDM1, BLIMP1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI                                  
KEYWDS    METHYLTRANSFERASE, PRDM1, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS    
KEYWDS   2 CONSORTIUM, SGC, DNA-BINDING, METAL-BINDING, NUCLEUS, POLYMORPHISM,  
KEYWDS   3 REPRESSOR, TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC, ZINC-      
KEYWDS   4 FINGER, DNA BINDING PROTEIN, TRANSFERASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.AMAYA,H.ZENG,T.ANTOSHENKO,A.DONG,P.LOPPNAU,C.BOUNTRA,J.WEIGELT,   
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,J.MIN,A.N.PLOTNIKOV,H.WU,     
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   3   25-OCT-17 3DAL    1       REMARK                                   
REVDAT   2   24-FEB-09 3DAL    1       VERSN                                    
REVDAT   1   12-AUG-08 3DAL    0                                                
JRNL        AUTH   H.ZENG,M.F.AMAYA,T.ANTOSHENKO,A.DONG,P.LOPPNAU,A.BOCHKAREV,  
JRNL        AUTH 2 J.MIN,A.N.PLOTNIKOV,H.WU                                     
JRNL        TITL   THE CRYSTAL STRUCTURE OF METHYLTRANSFERASE DOMAIN OF HUMAN   
JRNL        TITL 2 PR DOMAIN-CONTAINING PROTEIN 1                               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 57644                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2930                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3832                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 222                          
REMARK   3   BIN FREE R VALUE                    : 0.3990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2805                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 307                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.34000                                              
REMARK   3    B22 (A**2) : -0.05000                                             
REMARK   3    B33 (A**2) : -0.29000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.091         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.088         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.061         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.764         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2983 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4066 ; 1.571 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   358 ; 6.435 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   146 ;36.035 ;23.699       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   478 ;12.643 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;15.941 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   423 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2345 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1278 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2039 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   246 ; 0.148 ; 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):    68 ; 0.221 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.130 ; 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):  1837 ; 1.294 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2899 ; 1.918 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1348 ; 3.019 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1167 ; 4.609 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 3DAL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047799.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28268                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57924                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66400                            
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: NULL                         
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PURIFIED PRDM1 WAS CRYSTALLIZED USING    
REMARK 280  HANGING DROP VAPOR DIFFUSION METHOD AT 20 C BY MIXING 1.5 L OF      
REMARK 280  THE PROTEIN SOLUTION WITH 1.5 L OF THE RESERVOIR SOLUTION           
REMARK 280  CONTAINING 2.0 M NA FORMIDE, 0.1 M SODIUM ACETATE, PH 4.6.,         
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
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       32.41700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.33150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.48000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.33150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.41700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.48000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -64.96000            
REMARK 350   BIOMT3   2  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     MET A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     SER A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     THR A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     LYS A    91                                                      
REMARK 465     ASN A    92                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     VAL B    -6                                                      
REMARK 465     PRO B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     LYS B    -1                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     TRP B    30                                                      
REMARK 465     ASP B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     GLY B    33                                                      
REMARK 465     ALA B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     GLY B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     THR B    38                                                      
REMARK 465     SER B    39                                                      
REMARK 465     ASN B    57                                                      
REMARK 465     LYS B    91                                                      
REMARK 465     ASN B    92                                                      
REMARK 465     ALA B    93                                                      
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     SER A -10    OG                                                  
REMARK 470     LYS A  -1    CG   CD   CE   NZ                                   
REMARK 470     TRP A  30    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  30    CZ3  CH2                                            
REMARK 470     ASP A  31    CG   OD1  OD2                                       
REMARK 470     GLU A  59    CD   OE1  OE2                                       
REMARK 470     ARG A 132    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 186    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  59    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  60    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  87    CG   OD1  OD2                                       
REMARK 470     LYS B  96    CE   NZ                                             
REMARK 470     GLU B 106    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 132    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B 186    CG   CD   OE1  NE2                                  
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   335     O    HOH A   340              2.04            
REMARK 500   OE2  GLU A    43     O    HOH A   361              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 123   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP A  30      -36.20   -145.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3DAL A    1   186  UNP    O75626   PRDM1_HUMAN      2    187             
DBREF  3DAL B    1   186  UNP    O75626   PRDM1_HUMAN      2    187             
SEQADV 3DAL SER A  -10  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL SER A   -9  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL GLY A   -8  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL LEU A   -7  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL VAL A   -6  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL PRO A   -5  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL ARG A   -4  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL GLY A   -3  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL SER A   -2  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL LYS A   -1  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL SER B  -10  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL SER B   -9  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL GLY B   -8  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL LEU B   -7  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL VAL B   -6  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL PRO B   -5  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL ARG B   -4  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL GLY B   -3  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL SER B   -2  UNP  O75626              EXPRESSION TAG                 
SEQADV 3DAL LYS B   -1  UNP  O75626              EXPRESSION TAG                 
SEQRES   1 A  196  SER SER GLY LEU VAL PRO ARG GLY SER LYS LYS MET ASP          
SEQRES   2 A  196  MET GLU ASP ALA ASP MET THR LEU TRP THR GLU ALA GLU          
SEQRES   3 A  196  PHE GLU GLU LYS CYS THR TYR ILE VAL ASN ASP HIS PRO          
SEQRES   4 A  196  TRP ASP SER GLY ALA ASP GLY GLY THR SER VAL GLN ALA          
SEQRES   5 A  196  GLU ALA SER LEU PRO ARG ASN LEU LEU PHE LYS TYR ALA          
SEQRES   6 A  196  THR ASN SER GLU GLU VAL ILE GLY VAL MET SER LYS GLU          
SEQRES   7 A  196  TYR ILE PRO LYS GLY THR ARG PHE GLY PRO LEU ILE GLY          
SEQRES   8 A  196  GLU ILE TYR THR ASN ASP THR VAL PRO LYS ASN ALA ASN          
SEQRES   9 A  196  ARG LYS TYR PHE TRP ARG ILE TYR SER ARG GLY GLU LEU          
SEQRES  10 A  196  HIS HIS PHE ILE ASP GLY PHE ASN GLU GLU LYS SER ASN          
SEQRES  11 A  196  TRP MET ARG TYR VAL ASN PRO ALA HIS SER PRO ARG GLU          
SEQRES  12 A  196  GLN ASN LEU ALA ALA CYS GLN ASN GLY MET ASN ILE TYR          
SEQRES  13 A  196  PHE TYR THR ILE LYS PRO ILE PRO ALA ASN GLN GLU LEU          
SEQRES  14 A  196  LEU VAL TRP TYR CYS ARG ASP PHE ALA GLU ARG LEU HIS          
SEQRES  15 A  196  TYR PRO TYR PRO GLY GLU LEU THR MET MET ASN LEU THR          
SEQRES  16 A  196  GLN                                                          
SEQRES   1 B  196  SER SER GLY LEU VAL PRO ARG GLY SER LYS LYS MET ASP          
SEQRES   2 B  196  MET GLU ASP ALA ASP MET THR LEU TRP THR GLU ALA GLU          
SEQRES   3 B  196  PHE GLU GLU LYS CYS THR TYR ILE VAL ASN ASP HIS PRO          
SEQRES   4 B  196  TRP ASP SER GLY ALA ASP GLY GLY THR SER VAL GLN ALA          
SEQRES   5 B  196  GLU ALA SER LEU PRO ARG ASN LEU LEU PHE LYS TYR ALA          
SEQRES   6 B  196  THR ASN SER GLU GLU VAL ILE GLY VAL MET SER LYS GLU          
SEQRES   7 B  196  TYR ILE PRO LYS GLY THR ARG PHE GLY PRO LEU ILE GLY          
SEQRES   8 B  196  GLU ILE TYR THR ASN ASP THR VAL PRO LYS ASN ALA ASN          
SEQRES   9 B  196  ARG LYS TYR PHE TRP ARG ILE TYR SER ARG GLY GLU LEU          
SEQRES  10 B  196  HIS HIS PHE ILE ASP GLY PHE ASN GLU GLU LYS SER ASN          
SEQRES  11 B  196  TRP MET ARG TYR VAL ASN PRO ALA HIS SER PRO ARG GLU          
SEQRES  12 B  196  GLN ASN LEU ALA ALA CYS GLN ASN GLY MET ASN ILE TYR          
SEQRES  13 B  196  PHE TYR THR ILE LYS PRO ILE PRO ALA ASN GLN GLU LEU          
SEQRES  14 B  196  LEU VAL TRP TYR CYS ARG ASP PHE ALA GLU ARG LEU HIS          
SEQRES  15 B  196  TYR PRO TYR PRO GLY GLU LEU THR MET MET ASN LEU THR          
SEQRES  16 B  196  GLN                                                          
FORMUL   3  HOH   *307(H2 O)                                                    
HELIX    1   1 GLY A   -8  GLY A   -3  1                                   6    
HELIX    2   2 THR A   13  CYS A   21  1                                   9    
HELIX    3   3 VAL A   40  SER A   45  1                                   6    
HELIX    4   4 ASN A  120  VAL A  125  5                                   6    
HELIX    5   5 CYS A  164  LEU A  171  1                                   8    
HELIX    6   6 THR A  180  GLN A  186  1                                   7    
HELIX    7   7 THR B   13  CYS B   21  1                                   9    
HELIX    8   8 VAL B   40  SER B   45  1                                   6    
HELIX    9   9 THR B   85  VAL B   89  5                                   5    
HELIX   10  10 ASN B  120  VAL B  125  5                                   6    
HELIX   11  11 CYS B  164  LEU B  171  1                                   8    
HELIX   12  12 THR B  180  THR B  185  1                                   6    
SHEET    1   A 6 TYR A  23  VAL A  25  0                                        
SHEET    2   A 6 THR A  74  PHE A  76  1  O  ARG A  75   N  VAL A  25           
SHEET    3   A 6 ASN A 144  THR A 149 -1  O  PHE A 147   N  PHE A  76           
SHEET    4   A 6 LEU A 136  ASN A 141 -1  N  ALA A 137   O  TYR A 148           
SHEET    5   A 6 LEU A 160  TYR A 163  1  O  TRP A 162   N  ALA A 138           
SHEET    6   A 6 ASN A 126  PRO A 127  1  N  ASN A 126   O  VAL A 161           
SHEET    1   B 2 LEU A  50  TYR A  54  0                                        
SHEET    2   B 2 VAL A  61  SER A  66 -1  O  ILE A  62   N  LYS A  53           
SHEET    1   C 3 GLU A  82  TYR A  84  0                                        
SHEET    2   C 3 GLU A 106  ASP A 112 -1  O  ASP A 112   N  GLU A  82           
SHEET    3   C 3 PHE A  98  SER A 103 -1  N  TRP A  99   O  ILE A 111           
SHEET    1   D 6 TYR B  23  VAL B  25  0                                        
SHEET    2   D 6 THR B  74  PHE B  76  1  O  ARG B  75   N  VAL B  25           
SHEET    3   D 6 ASN B 144  THR B 149 -1  O  PHE B 147   N  PHE B  76           
SHEET    4   D 6 LEU B 136  ASN B 141 -1  N  ALA B 137   O  TYR B 148           
SHEET    5   D 6 LEU B 160  TYR B 163  1  O  TRP B 162   N  ALA B 138           
SHEET    6   D 6 ASN B 126  PRO B 127  1  N  ASN B 126   O  VAL B 161           
SHEET    1   E 2 LEU B  50  TYR B  54  0                                        
SHEET    2   E 2 VAL B  61  SER B  66 -1  O  MET B  65   N  LEU B  51           
SHEET    1   F 3 GLU B  82  TYR B  84  0                                        
SHEET    2   F 3 GLU B 106  ASP B 112 -1  O  ASP B 112   N  GLU B  82           
SHEET    3   F 3 PHE B  98  SER B 103 -1  N  ILE B 101   O  HIS B 108           
CISPEP   1 PRO A   29    TRP A   30          0       -14.28                     
CISPEP   2 GLY A   77    PRO A   78          0        11.47                     
CISPEP   3 GLY B   77    PRO B   78          0         8.72                     
CRYST1   64.834   64.960  112.663  90.00  90.00  90.00 P 21 21 21    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      0.015424  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015394  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008876        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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