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Database: PDB
Entry: 4U6S
LinkDB: 4U6S
Original site: 4U6S 
HEADER    OXIDOREDUCTASE                          29-JUL-14   4U6S              
TITLE     CTBP1 IN COMPLEX WITH SUBSTRATE PHENYLPYRUVATE                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-TERMINAL-BINDING PROTEIN 1;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: NAD NUCLEOTIDE BINDING RESIDUES 28-353;                    
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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: RIL+;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ROSSMAN FOLD, TRANSCRIPTION REGULATOR, CANCER, SUBSTRATE,             
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.HILBERT,B.L.MORRIS,K.C.ELLIS,J.L.PAULSEN,C.A.SCHIFFER,            
AUTHOR   2 S.R.GROSSMAN,W.E.ROYER JR.                                           
REVDAT   2   29-APR-15 4U6S    1       JRNL                                     
REVDAT   1   11-FEB-15 4U6S    0                                                
JRNL        AUTH   B.J.HILBERT,B.L.MORRIS,K.C.ELLIS,J.L.PAULSEN,C.A.SCHIFFER,   
JRNL        AUTH 2 S.R.GROSSMAN,W.E.ROYER                                       
JRNL        TITL   STRUCTURE-GUIDED DESIGN OF A HIGH AFFINITY INHIBITOR TO      
JRNL        TITL 2 HUMAN CTBP.                                                  
JRNL        REF    ACS CHEM.BIOL.                V.  10  1118 2015              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   25636004                                                     
JRNL        DOI    10.1021/CB500820B                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 19617                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 997                             
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 30.0074 -  4.0104    0.99     2947   138  0.1700 0.2056        
REMARK   3     2  4.0104 -  3.1843    0.99     2757   137  0.1624 0.1880        
REMARK   3     3  3.1843 -  2.7821    0.96     2640   126  0.1900 0.2414        
REMARK   3     4  2.7821 -  2.5279    0.97     2597   150  0.1979 0.2712        
REMARK   3     5  2.5279 -  2.3468    0.97     2597   144  0.2140 0.3063        
REMARK   3     6  2.3468 -  2.2084    0.96     2542   168  0.2119 0.2677        
REMARK   3     7  2.2084 -  2.1000    0.95     2540   134  0.2144 0.2794        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.630           
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      :  0.004           2619                                  
REMARK   3   ANGLE     :  0.837           3563                                  
REMARK   3   CHIRALITY :  0.049            415                                  
REMARK   3   PLANARITY :  0.003            464                                  
REMARK   3   DIHEDRAL  : 16.575            951                                  
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 4U6S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202908.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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) : 0.99                               
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19617                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 28.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.4600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 17.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.390                              
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: 4LCE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: BI-PYRAMIDAL CRYSTALS                                        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM CALCIUM CHLORIDE, 100 MM HEPES    
REMARK 280  PH 7.5, 2.5 MM NAD+, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  277K                                                                
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       52.91767            
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      105.83533            
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       52.91767            
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      105.83533            
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       52.91767            
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      105.83533            
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       52.91767            
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      105.83533            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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  0.500000  0.866025  0.000000      -42.06050            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       72.85092            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -52.91767            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 23480 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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      -42.06050            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       72.85092            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      -52.91767            
REMARK 350   BIOMT1   4  0.500000  0.866025  0.000000      -42.06050            
REMARK 350   BIOMT2   4  0.866025 -0.500000  0.000000       72.85092            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      -52.91767            
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 505  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 560  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 576  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 585  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 592  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 594  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 596  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     SER A    25                                                      
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     HIS A  26    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  57    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  84    CD   OE1  OE2                                       
REMARK 470     LYS A  90    CG   CD   CE   NZ                                   
REMARK 470     LYS A 108    CG   CD   CE   NZ                                   
REMARK 470     ARG A 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 164    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 241    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 253    CG   CD   CE   NZ                                   
REMARK 470     GLN A 301    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 305    CG   CD   CE   NZ                                   
REMARK 470     ASP A 306    CG   OD1  OD2                                       
REMARK 470     ARG A 342    CG   CD   NE   CZ   NH1  NH2                        
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   O3   PPY A   402     O    HOH A   597              1.08            
REMARK 500   CB   ALA A   123     O    HOH A   506              1.46            
REMARK 500   NZ   LYS A    46     O    HOH A   501              1.98            
REMARK 500   CA   ALA A   123     O    HOH A   506              2.01            
REMARK 500   C2   PPY A   402     O    HOH A   597              2.06            
REMARK 500   C    ALA A   123     O    HOH A   506              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   542     O    HOH A   553     4565     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  34       51.14   -103.90                                   
REMARK 500    TYR A  76     -149.46    -94.77                                   
REMARK 500    ALA A 123      106.47    -56.75                                   
REMARK 500    LEU A 182       61.59   -102.20                                   
REMARK 500    HIS A 236       31.53   -146.48                                   
REMARK 500    ALA A 265      -89.21    -91.07                                   
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 403  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT A 404   O2                                                     
REMARK 620 2 HOH A 682   O    84.0                                              
REMARK 620 3 FMT A 404   O1   49.2  96.0                                        
REMARK 620 4 HOH A 637   O    78.4  86.8 126.5                                  
REMARK 620 5 HOH A 638   O   128.3  76.0  85.8 145.2                            
REMARK 620 6 HOH A 681   O   160.5  99.0 148.0  82.5  70.7                      
REMARK 620 7 HOH A 684   O    87.2 165.2  87.1  79.8 118.6  85.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PPY A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 404                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4U6Q   RELATED DB: PDB                                   
REMARK 900 4U6Q CONTAINS THE SAME PROTEIN COMPLEXED WITH AN INHIBITOR           
REMARK 900 RELATED ID: 4LCE   RELATED DB: PDB                                   
REMARK 900 4LCE CONTAINS THE SAME PROTEIN COMPLEXED WITH A DIFFERENT SUBSTRATE  
DBREF  4U6S A   28   353  UNP    Q13363   CTBP1_HUMAN     28    353             
SEQADV 4U6S MET A    7  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S GLY A    8  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S SER A    9  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S SER A   10  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S HIS A   11  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S HIS A   12  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S HIS A   13  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S HIS A   14  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S HIS A   15  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S HIS A   16  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S SER A   17  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S SER A   18  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S GLY A   19  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S LEU A   20  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S VAL A   21  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S PRO A   22  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S ARG A   23  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S GLY A   24  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S SER A   25  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S HIS A   26  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6S MET A   27  UNP  Q13363              EXPRESSION TAG                 
SEQRES   1 A  347  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  347  LEU VAL PRO ARG GLY SER HIS MET PRO LEU VAL ALA LEU          
SEQRES   3 A  347  LEU ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU          
SEQRES   4 A  347  LYS ASP VAL ALA THR VAL ALA PHE CYS ASP ALA GLN SER          
SEQRES   5 A  347  THR GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL          
SEQRES   6 A  347  GLY ALA LEU MET TYR HIS THR ILE THR LEU THR ARG GLU          
SEQRES   7 A  347  ASP LEU GLU LYS PHE LYS ALA LEU ARG ILE ILE VAL ARG          
SEQRES   8 A  347  ILE GLY SER GLY PHE ASP ASN ILE ASP ILE LYS SER ALA          
SEQRES   9 A  347  GLY ASP LEU GLY ILE ALA VAL CYS ASN VAL PRO ALA ALA          
SEQRES  10 A  347  SER VAL GLU GLU THR ALA ASP SER THR LEU CYS HIS ILE          
SEQRES  11 A  347  LEU ASN LEU TYR ARG ARG ALA THR TRP LEU HIS GLN ALA          
SEQRES  12 A  347  LEU ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE          
SEQRES  13 A  347  ARG GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU          
SEQRES  14 A  347  THR LEU GLY ILE ILE GLY LEU GLY ARG VAL GLY GLN ALA          
SEQRES  15 A  347  VAL ALA LEU ARG ALA LYS ALA PHE GLY PHE ASN VAL LEU          
SEQRES  16 A  347  PHE TYR ASP PRO TYR LEU SER ASP GLY VAL GLU ARG ALA          
SEQRES  17 A  347  LEU GLY LEU GLN ARG VAL SER THR LEU GLN ASP LEU LEU          
SEQRES  18 A  347  PHE HIS SER ASP CYS VAL THR LEU HIS CYS GLY LEU ASN          
SEQRES  19 A  347  GLU HIS ASN HIS HIS LEU ILE ASN ASP PHE THR VAL LYS          
SEQRES  20 A  347  GLN MET ARG GLN GLY ALA PHE LEU VAL ASN THR ALA ARG          
SEQRES  21 A  347  GLY GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU          
SEQRES  22 A  347  LYS GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS          
SEQRES  23 A  347  GLU SER GLU PRO PHE SER PHE SER GLN GLY PRO LEU LYS          
SEQRES  24 A  347  ASP ALA PRO ASN LEU ILE CYS THR PRO HIS ALA ALA TRP          
SEQRES  25 A  347  TYR SER GLU GLN ALA SER ILE GLU MET ARG GLU GLU ALA          
SEQRES  26 A  347  ALA ARG GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO          
SEQRES  27 A  347  ASP SER LEU LYS ASN CYS VAL ASN LYS                          
HET    NAD  A 401      44                                                       
HET    PPY  A 402      24                                                       
HET     CA  A 403       1                                                       
HET    FMT  A 404       3                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     PPY 3-PHENYLPYRUVIC ACID                                             
HETNAM      CA CALCIUM ION                                                      
HETNAM     FMT FORMIC ACID                                                      
FORMUL   2  NAD    C21 H27 N7 O14 P2                                            
FORMUL   3  PPY    C9 H8 O3                                                     
FORMUL   4   CA    CA 2+                                                        
FORMUL   5  FMT    C H2 O2                                                      
FORMUL   6  HOH   *200(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  GLU A   69  1                                   7    
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  ALA A  195  1                                  13    
HELIX   10 AB1 GLY A  210  GLY A  216  1                                   7    
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    
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 ALA A  70  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  VAL A 262   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  LEU A 289           
LINK        CA    CA A 403                 O2  FMT A 404     1555   1555  2.46  
LINK        CA    CA A 403                 O   HOH A 682     1555   1555  2.45  
LINK        CA    CA A 403                 O1  FMT A 404     1555   1555  2.69  
LINK        CA    CA A 403                 O   HOH A 637     1555   1555  2.59  
LINK        CA    CA A 403                 O   HOH A 638     1555   1555  2.83  
LINK        CA    CA A 403                 O   HOH A 681     1555   1555  2.36  
LINK        CA    CA A 403                 O   HOH A 684     1555   1555  2.68  
CISPEP   1 GLU A  295    PRO A  296          0         3.20                     
CISPEP   2 ILE A  343    PRO A  344          0        -1.55                     
SITE     1 AC1 32 SER A 100  GLY A 101  THR A 128  GLY A 181                    
SITE     2 AC1 32 GLY A 183  ARG A 184  VAL A 185  TYR A 203                    
SITE     3 AC1 32 ASP A 204  PRO A 205  TYR A 206  HIS A 236                    
SITE     4 AC1 32 CYS A 237  GLY A 238  ASN A 240  ASN A 243                    
SITE     5 AC1 32 THR A 264  ALA A 265  ARG A 266  ASP A 290                    
SITE     6 AC1 32 VAL A 291  HIS A 315  TRP A 318  PPY A 402                    
SITE     7 AC1 32 HOH A 548  HOH A 599  HOH A 600  HOH A 608                    
SITE     8 AC1 32 HOH A 627  HOH A 631  HOH A 652  HOH A 672                    
SITE     1 AC2 14 TYR A  76  HIS A  77  ARG A  97  ILE A  98                    
SITE     2 AC2 14 GLY A  99  SER A 100  GLY A 101  ARG A 266                    
SITE     3 AC2 14 HIS A 315  TRP A 318  MET A 327  NAD A 401                    
SITE     4 AC2 14 HOH A 597  HOH A 632                                          
SITE     1 AC3  6 FMT A 404  HOH A 637  HOH A 638  HOH A 681                    
SITE     2 AC3  6 HOH A 682  HOH A 684                                          
SITE     1 AC4  5 GLU A 175  ASP A 231  GLY A 258  ARG A 285                    
SITE     2 AC4  5  CA A 403                                                     
CRYST1   84.121   84.121  158.753  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      0.011888  0.006863  0.000000        0.00000                         
SCALE2      0.000000  0.013727  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006299        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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