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Database: PDB
Entry: 6CDF
LinkDB: 6CDF
Original site: 6CDF 
HEADER    TRANSCRIPTION                           08-FEB-18   6CDF              
TITLE     HUMAN CTBP1 (28-378)                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-TERMINAL-BINDING PROTEIN 1;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 28-379;                                       
COMPND   5 SYNONYM: CTBP1;                                                      
COMPND   6 EC: 1.1.1.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CTBP1, CTBP;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CTBP, NADH, CANCER TARGET, TRANSCRIPTION                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.E.ROYER,A.G.BELLESIS                                                
REVDAT   4   01-JAN-20 6CDF    1       REMARK                                   
REVDAT   3   20-FEB-19 6CDF    1       REMARK                                   
REVDAT   2   20-JUN-18 6CDF    1       JRNL                                     
REVDAT   1   09-MAY-18 6CDF    0                                                
JRNL        AUTH   A.G.BELLESIS,A.M.JECROIS,J.A.HAYES,C.A.SCHIFFER,W.E.ROYER    
JRNL        TITL   ASSEMBLY OF HUMAN C-TERMINAL BINDING PROTEIN (CTBP) INTO     
JRNL        TITL 2 TETRAMERS.                                                   
JRNL        REF    J. BIOL. CHEM.                V. 293  9101 2018              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   29700119                                                     
JRNL        DOI    10.1074/JBC.RA118.002514                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 11835                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 592                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.9950 -  4.1261    0.99     3094   160  0.1697 0.2057        
REMARK   3     2  4.1261 -  3.2755    0.97     2808   152  0.2182 0.2392        
REMARK   3     3  3.2755 -  2.8616    0.96     2760   144  0.2556 0.3246        
REMARK   3     4  2.8616 -  2.6000    0.91     2581   136  0.2618 0.3005        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.940           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           2670                                  
REMARK   3   ANGLE     :  0.665           3620                                  
REMARK   3   CHIRALITY :  0.043            418                                  
REMARK   3   PLANARITY :  0.003            468                                  
REMARK   3   DIHEDRAL  : 17.555           1612                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232573.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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 MICROMAX-007 HF             
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15115                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
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     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
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: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4U6Q                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG400, 140 MM CALCIUM CHLORIDE, PH   
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.63800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      109.27600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       54.63800            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      109.27600            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.63800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      109.27600            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       54.63800            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      109.27600            
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: TETRAMERIC                        
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: A                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      177.31400            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      153.55843            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      153.55843            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      177.31400            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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   BIOMT1   2 -1.000000  0.000000  0.000000      177.31400            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 565  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     VAL A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     ARG A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     ALA A   358                                                      
REMARK 465     ALA A   359                                                      
REMARK 465     THR A   360                                                      
REMARK 465     HIS A   361                                                      
REMARK 465     TRP A   362                                                      
REMARK 465     ALA A   363                                                      
REMARK 465     SER A   364                                                      
REMARK 465     MET A   365                                                      
REMARK 465     ASP A   366                                                      
REMARK 465     PRO A   367                                                      
REMARK 465     ALA A   368                                                      
REMARK 465     VAL A   369                                                      
REMARK 465     VAL A   370                                                      
REMARK 465     HIS A   371                                                      
REMARK 465     PRO A   372                                                      
REMARK 465     GLU A   373                                                      
REMARK 465     LEU A   374                                                      
REMARK 465     ASN A   375                                                      
REMARK 465     GLY A   376                                                      
REMARK 465     ALA A   377                                                      
REMARK 465     ALA A   378                                                      
REMARK 465     TYR A   379                                                      
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   594     O    HOH A   610              1.97            
REMARK 500   OE2  GLU A   329     O    HOH A   501              2.15            
REMARK 500   O    HOH A   566     O    HOH A   606              2.16            
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  34       57.86   -107.03                                   
REMARK 500    TYR A  76     -140.52   -100.64                                   
REMARK 500    ASP A 106       99.02    -68.62                                   
REMARK 500    LEU A 182       60.94   -106.38                                   
REMARK 500    HIS A 236       30.00   -144.33                                   
REMARK 500    ALA A 265      -87.05    -96.60                                   
REMARK 500    ASN A 352       37.26   -151.23                                   
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                              CA A 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 547   O                                                      
REMARK 620 2 HOH A 556   O    63.9                                              
REMARK 620 3 HOH A 615   O    97.9 106.8                                        
REMARK 620 4 FMT A 403   O1  103.5  79.7 158.2                                  
REMARK 620 5 FMT A 403   O2   65.1  84.0 154.1  45.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAI A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 403                 
DBREF  6CDF A   28   379  UNP    Q13363   CTBP1_HUMAN     28    379             
SEQADV 6CDF MET A    7  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF GLY A    8  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF SER A    9  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF SER A   10  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF HIS A   11  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF HIS A   12  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF HIS A   13  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF HIS A   14  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF HIS A   15  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF HIS A   16  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF SER A   17  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF SER A   18  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF GLY A   19  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF LEU A   20  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF VAL A   21  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF PRO A   22  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF ARG A   23  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF GLY A   24  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF SER A   25  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF HIS A   26  UNP  Q13363              EXPRESSION TAG                 
SEQADV 6CDF MET A   27  UNP  Q13363              EXPRESSION TAG                 
SEQRES   1 A  373  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  373  LEU VAL PRO ARG GLY SER HIS MET PRO LEU VAL ALA LEU          
SEQRES   3 A  373  LEU ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU          
SEQRES   4 A  373  LYS ASP VAL ALA THR VAL ALA PHE CYS ASP ALA GLN SER          
SEQRES   5 A  373  THR GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL          
SEQRES   6 A  373  GLY ALA LEU MET TYR HIS THR ILE THR LEU THR ARG GLU          
SEQRES   7 A  373  ASP LEU GLU LYS PHE LYS ALA LEU ARG ILE ILE VAL ARG          
SEQRES   8 A  373  ILE GLY SER GLY PHE ASP ASN ILE ASP ILE LYS SER ALA          
SEQRES   9 A  373  GLY ASP LEU GLY ILE ALA VAL CYS ASN VAL PRO ALA ALA          
SEQRES  10 A  373  SER VAL GLU GLU THR ALA ASP SER THR LEU CYS HIS ILE          
SEQRES  11 A  373  LEU ASN LEU TYR ARG ARG ALA THR TRP LEU HIS GLN ALA          
SEQRES  12 A  373  LEU ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE          
SEQRES  13 A  373  ARG GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU          
SEQRES  14 A  373  THR LEU GLY ILE ILE GLY LEU GLY ARG VAL GLY GLN ALA          
SEQRES  15 A  373  VAL ALA LEU ARG ALA LYS ALA PHE GLY PHE ASN VAL LEU          
SEQRES  16 A  373  PHE TYR ASP PRO TYR LEU SER ASP GLY VAL GLU ARG ALA          
SEQRES  17 A  373  LEU GLY LEU GLN ARG VAL SER THR LEU GLN ASP LEU LEU          
SEQRES  18 A  373  PHE HIS SER ASP CYS VAL THR LEU HIS CYS GLY LEU ASN          
SEQRES  19 A  373  GLU HIS ASN HIS HIS LEU ILE ASN ASP PHE THR VAL LYS          
SEQRES  20 A  373  GLN MET ARG GLN GLY ALA PHE LEU VAL ASN THR ALA ARG          
SEQRES  21 A  373  GLY GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU          
SEQRES  22 A  373  LYS GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS          
SEQRES  23 A  373  GLU SER GLU PRO PHE SER PHE SER GLN GLY PRO LEU LYS          
SEQRES  24 A  373  ASP ALA PRO ASN LEU ILE CYS THR PRO HIS ALA ALA TRP          
SEQRES  25 A  373  TYR SER GLU GLN ALA SER ILE GLU MET ARG GLU GLU ALA          
SEQRES  26 A  373  ALA ARG GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO          
SEQRES  27 A  373  ASP SER LEU LYS ASN CYS VAL ASN LYS ASP HIS LEU THR          
SEQRES  28 A  373  ALA ALA THR HIS TRP ALA SER MET ASP PRO ALA VAL VAL          
SEQRES  29 A  373  HIS PRO GLU LEU ASN GLY ALA ALA TYR                          
HET    NAI  A 401      71                                                       
HET     CA  A 402       1                                                       
HET    FMT  A 403       5                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETNAM      CA CALCIUM ION                                                      
HETNAM     FMT FORMIC ACID                                                      
HETSYN     NAI NADH                                                             
FORMUL   2  NAI    C21 H29 N7 O14 P2                                            
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  FMT    C H2 O2                                                      
FORMUL   5  HOH   *115(H2 O)                                                    
HELIX    1 AA1 GLU A   41  LYS A   46  1                                   6    
HELIX    2 AA2 SER A   58  ILE A   62  5                                   5    
HELIX    3 AA3 HIS A   63  ALA A   70  1                                   8    
HELIX    4 AA4 THR A   82  LYS A   88  1                                   7    
HELIX    5 AA5 ASP A  106  LEU A  113  1                                   8    
HELIX    6 AA6 SER A  124  ARG A  142  1                                  19    
HELIX    7 AA7 ARG A  142  GLU A  152  1                                  11    
HELIX    8 AA8 SER A  158  ALA A  166  1                                   9    
HELIX    9 AA9 GLY A  183  PHE A  196  1                                  14    
HELIX   10 AB1 GLY A  210  LEU A  215  1                                   6    
HELIX   11 AB2 THR A  222  SER A  230  1                                   9    
HELIX   12 AB3 ASN A  248  LYS A  253  1                                   6    
HELIX   13 AB4 ARG A  266  VAL A  270  5                                   5    
HELIX   14 AB5 ASP A  271  GLU A  281  1                                  11    
HELIX   15 AB6 SER A  320  GLY A  341  1                                  22    
HELIX   16 AB7 ASN A  352  LEU A  356  5                                   5    
SHEET    1 AA1 5 THR A  50  PHE A  53  0                                        
SHEET    2 AA1 5 LEU A  29  LEU A  32  1  N  VAL A  30   O  THR A  50           
SHEET    3 AA1 5 GLY A  72  MET A  75  1  O  LEU A  74   N  ALA A  31           
SHEET    4 AA1 5 ILE A  94  ARG A  97  1  O  VAL A  96   N  ALA A  73           
SHEET    5 AA1 5 ALA A 116  CYS A 118  1  O  CYS A 118   N  ARG A  97           
SHEET    1 AA2 7 GLN A 218  ARG A 219  0                                        
SHEET    2 AA2 7 ASN A 199  TYR A 203  1  N  VAL A 200   O  GLN A 218           
SHEET    3 AA2 7 THR A 176  ILE A 180  1  N  ILE A 179   O  LEU A 201           
SHEET    4 AA2 7 CYS A 232  LEU A 235  1  O  CYS A 232   N  GLY A 178           
SHEET    5 AA2 7 ALA A 259  ASN A 263  1  O  PHE A 260   N  VAL A 233           
SHEET    6 AA2 7 ILE A 284  LEU A 289  1  O  ALA A 288   N  LEU A 261           
SHEET    7 AA2 7 LEU A 310  CYS A 312  1  O  ILE A 311   N  ALA A 287           
LINK        CA    CA A 402                 O   HOH A 547     1555   1555  2.32  
LINK        CA    CA A 402                 O   HOH A 556     1555   1555  2.56  
LINK        CA    CA A 402                 O   HOH A 615     1555   1555  2.21  
LINK        CA    CA A 402                 O1  FMT A 403     1555   1555  2.81  
LINK        CA    CA A 402                 O2  FMT A 403     1555   1555  2.78  
CISPEP   1 GLU A  295    PRO A  296          0         3.27                     
CISPEP   2 ILE A  343    PRO A  344          0        -2.68                     
SITE     1 AC1 29 SER A 100  GLY A 101  THR A 128  ILE A 180                    
SITE     2 AC1 29 GLY A 181  GLY A 183  ARG A 184  VAL A 185                    
SITE     3 AC1 29 TYR A 203  ASP A 204  PRO A 205  TYR A 206                    
SITE     4 AC1 29 HIS A 236  CYS A 237  GLY A 238  ASN A 240                    
SITE     5 AC1 29 ASN A 243  THR A 264  ALA A 265  ARG A 266                    
SITE     6 AC1 29 ASP A 290  HIS A 315  TRP A 318  HOH A 530                    
SITE     7 AC1 29 HOH A 534  HOH A 541  HOH A 551  HOH A 564                    
SITE     8 AC1 29 HOH A 570                                                     
SITE     1 AC2  4 FMT A 403  HOH A 547  HOH A 556  HOH A 615                    
SITE     1 AC3  5 GLU A 175  GLY A 258  ARG A 285   CA A 402                    
SITE     2 AC3  5 HOH A 547                                                     
CRYST1   88.657   88.657  163.914  90.00  90.00 120.00 P 64 2 2     12          
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      0.011279  0.006512  0.000000        0.00000                         
SCALE2      0.000000  0.013024  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006101        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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