GenomeNet

Database: PDB
Entry: 4U6Q
LinkDB: 4U6Q
Original site: 4U6Q 
HEADER    OXIDOREDUCTASE                          29-JUL-14   4U6Q              
TITLE     CTBP1 BOUND TO INHIBITOR 2-(HYDROXYIMINO)-3-PHENYLPROPANOIC ACID      
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, INHIBITOR,             
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 4U6Q    1       JRNL                                     
REVDAT   1   11-FEB-15 4U6Q    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 15450                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 771                             
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 30.0209 -  4.1743    1.00     2635   136  0.1895 0.2192        
REMARK   3     2  4.1743 -  3.3146    1.00     2464   127  0.1834 0.2029        
REMARK   3     3  3.3146 -  2.8960    1.00     2412   129  0.2178 0.3281        
REMARK   3     4  2.8960 -  2.6314    1.00     2385   141  0.2356 0.2973        
REMARK   3     5  2.6314 -  2.4429    1.00     2401   113  0.2424 0.2744        
REMARK   3     6  2.4429 -  2.3000    1.00     2382   125  0.2476 0.2918        
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.720           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.34                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.80                          
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           2554                                  
REMARK   3   ANGLE     :  0.836           3475                                  
REMARK   3   CHIRALITY :  0.045            411                                  
REMARK   3   PLANARITY :  0.003            447                                  
REMARK   3   DIHEDRAL  : 16.214            917                                  
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 4U6Q 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_1000202834.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-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   : 15450                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 18.10                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.49100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.480                              
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 CRYSTAL                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 75 MM CACL2, 100 MM HEPES PH 7.5, AND    
REMARK 280  1 MM NADH, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 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       53.15733            
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      106.31467            
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       53.15733            
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      106.31467            
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       53.15733            
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      106.31467            
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       53.15733            
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      106.31467            
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: 8510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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      -42.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       72.74613            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -53.15733            
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 539  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 540  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 571  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 572  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 573  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 574  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 671  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     GLN A  60    CG   CD   OE1  NE2                                  
REMARK 470     HIS A  63    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  84    CG   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 160    CG   CD   OE1  OE2                                  
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 277    CD   OE1  NE2                                       
REMARK 470     ARG A 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 301    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 306    CG   OD1  OD2                                       
REMARK 470     ARG A 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 348    CD   CE   NZ                                        
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   525     O    HOH A   529     4565     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       53.66   -103.19                                   
REMARK 500    ASP A  55       51.23     39.48                                   
REMARK 500    TYR A  76     -140.39    -91.19                                   
REMARK 500    LEU A 182       63.01   -103.21                                   
REMARK 500    HIS A 236       30.96   -146.84                                   
REMARK 500    ALA A 265      -89.27    -99.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 671        DISTANCE =  6.98 ANGSTROMS                       
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 590   O    91.3                                              
REMARK 620 3 FMT A 404   O1   47.5  93.6                                        
REMARK 620 4 HOH A 581   O   124.9  73.4  80.2                                  
REMARK 620 5 HOH A 620   O    83.6 174.9  83.5 110.0                            
REMARK 620 6 HOH A 626   O    79.5  98.2 125.9 153.6  80.3                      
REMARK 620 7 HOH A 664   O   163.0  96.3 146.2  72.0  88.4  84.4                
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 NAI A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 3CR 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: 4U6S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LCE   RELATED DB: PDB                                   
DBREF  4U6Q A   28   353  UNP    Q13363   CTBP1_HUMAN     28    353             
SEQADV 4U6Q MET A    7  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q GLY A    8  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q SER A    9  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q SER A   10  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q HIS A   11  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q HIS A   12  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q HIS A   13  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q HIS A   14  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q HIS A   15  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q HIS A   16  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q SER A   17  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q SER A   18  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q GLY A   19  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q LEU A   20  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q VAL A   21  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q PRO A   22  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q ARG A   23  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q GLY A   24  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q SER A   25  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q HIS A   26  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4U6Q 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    NAI  A 401      44                                                       
HET    3CR  A 402      13                                                       
HET     CA  A 403       1                                                       
HET    FMT  A 404       3                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETNAM     3CR (2E)-2-(HYDROXYIMINO)-3-PHENYLPROPANOIC ACID                     
HETNAM      CA CALCIUM ION                                                      
HETNAM     FMT FORMIC ACID                                                      
HETSYN     NAI NADH                                                             
FORMUL   2  NAI    C21 H29 N7 O14 P2                                            
FORMUL   3  3CR    C9 H9 N O3                                                   
FORMUL   4   CA    CA 2+                                                        
FORMUL   5  FMT    C H2 O2                                                      
FORMUL   6  HOH   *175(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  GLY A  153  1                                  12    
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  LEU A  215  1                                   6    
HELIX   11 AB2 THR A  222  SER A  230  1                                   9    
HELIX   12 AB3 ASN A  248  GLN A  254  1                                   7    
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  LEU A 177   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  ALA A 287           
LINK        CA    CA A 403                 O2  FMT A 404     1555   1555  2.53  
LINK        CA    CA A 403                 O   HOH A 590     1555   1555  2.28  
LINK        CA    CA A 403                 O1  FMT A 404     1555   1555  2.78  
LINK        CA    CA A 403                 O   HOH A 581     1555   1555  2.73  
LINK        CA    CA A 403                 O   HOH A 620     1555   1555  2.75  
LINK        CA    CA A 403                 O   HOH A 626     1555   1555  2.62  
LINK        CA    CA A 403                 O   HOH A 664     1555   1555  2.30  
CISPEP   1 GLU A  295    PRO A  296          0         4.44                     
CISPEP   2 ILE A  343    PRO A  344          0        -4.12                     
SITE     1 AC1 29 SER A 100  GLY A 101  THR A 128  GLY A 181                    
SITE     2 AC1 29 GLY A 183  ARG A 184  VAL A 185  TYR A 203                    
SITE     3 AC1 29 ASP A 204  PRO A 205  TYR A 206  HIS A 236                    
SITE     4 AC1 29 CYS A 237  GLY A 238  ASN A 240  ASN A 243                    
SITE     5 AC1 29 THR A 264  ALA A 265  ARG A 266  ASP A 290                    
SITE     6 AC1 29 HIS A 315  TRP A 318  3CR A 402  HOH A 516                    
SITE     7 AC1 29 HOH A 575  HOH A 579  HOH A 588  HOH A 661                    
SITE     8 AC1 29 HOH A 675                                                     
SITE     1 AC2 12 TYR A  76  ARG A  97  ILE A  98  GLY A  99                    
SITE     2 AC2 12 SER A 100  GLY A 101  ARG A 266  HIS A 315                    
SITE     3 AC2 12 TRP A 318  MET A 327  NAI A 401  HOH A 674                    
SITE     1 AC3  6 FMT A 404  HOH A 581  HOH A 590  HOH A 620                    
SITE     2 AC3  6 HOH A 626  HOH A 664                                          
SITE     1 AC4  4 GLU A 175  GLY A 258  ARG A 285   CA A 403                    
CRYST1   84.000   84.000  159.472  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      0.011905  0.006873  0.000000        0.00000                         
SCALE2      0.000000  0.013746  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006271        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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