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Database: PDB
Entry: 4LCE
LinkDB: 4LCE
Original site: 4LCE 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE SUBSTRATE 21-JUN-13   4LCE              
TITLE     CTBP1 IN COMPLEX WITH SUBSTRATE MTOB                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-TERMINAL-BINDING PROTEIN 1;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: DEHYDROGENASE DOMAIN (UNP 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: CTBP, CTBP1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIL;                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ROSSMANN FOLD, TRANSCRIPTIONAL CO-REPRESSOR, D-ISOMER 2-HYDROXYACID   
KEYWDS   2 DEHYDROGENASE, OXIDOREDUCTASE-OXIDOREDUCTASE SUBSTRATE COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.HILBERT,C.A.SCHIFFER,W.E.ROYER JR.                                
REVDAT   5   15-NOV-17 4LCE    1       REMARK                                   
REVDAT   4   12-NOV-14 4LCE    1       KEYWDS                                   
REVDAT   3   14-MAY-14 4LCE    1       JRNL                                     
REVDAT   2   09-APR-14 4LCE    1       JRNL                                     
REVDAT   1   19-MAR-14 4LCE    0                                                
JRNL        AUTH   B.J.HILBERT,S.R.GROSSMANN,C.A.SCHIFFER,W.E.ROYER             
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN CTBP IN COMPLEX WITH SUBSTRATE   
JRNL        TITL 2 MTOB REVEAL ACTIVE SITE FEATURES USEFUL FOR INHIBITOR        
JRNL        TITL 3 DESIGN.                                                      
JRNL        REF    FEBS LETT.                    V. 588  1743 2014              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   24657618                                                     
JRNL        DOI    10.1016/J.FEBSLET.2014.03.026                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0025                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 15420                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 769                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.38                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1074                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 47                           
REMARK   3   BIN FREE R VALUE                    : 0.4050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2450                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 84                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : -0.13000                                             
REMARK   3    B33 (A**2) : 0.19000                                              
REMARK   3    B12 (A**2) : -0.06000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.394         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.248         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.190         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.305         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2608 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2436 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3561 ; 1.349 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5566 ; 0.761 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   330 ; 6.437 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   111 ;33.552 ;23.784       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   400 ;14.475 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;18.568 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   419 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2969 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   603 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4LCE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080453.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99                               
REMARK 200  MONOCHROMATOR                  : BENT GE(111) MONOCHROMATOR         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15565                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.380                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 10.70                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
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: PHASER 2.3.0                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 250 MM MAGNESIUM CHLORIDE, 140 MM        
REMARK 280  SODIUM FORMATE, 100 MM HEPES, 2.5 MM NAD+, PH 7.5, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       53.84600            
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      107.69200            
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       53.84600            
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      107.69200            
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       53.84600            
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      107.69200            
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       53.84600            
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      107.69200            
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: 8160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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       88.97000            
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 574  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 579  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 465     HIS A    26                                                      
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     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  60    OE1  NE2                                            
REMARK 470     HIS A  63    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  65    CG   CD   CE   NZ                                   
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     LYS A 253    CG   CD   CE   NZ                                   
REMARK 470     LYS A 273    CG   CD   CE   NZ                                   
REMARK 470     GLN A 277    CG   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     LYS A 305    CG   CD   CE   NZ                                   
REMARK 470     ARG A 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 353    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 141   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 333   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  34       46.19   -106.24                                   
REMARK 500    TYR A  76     -148.81    -98.58                                   
REMARK 500    ASP A 106       96.31    -69.87                                   
REMARK 500    LEU A 113        9.54    -64.80                                   
REMARK 500    LEU A 182       55.39   -119.10                                   
REMARK 500    HIS A 236       27.42   -144.70                                   
REMARK 500    ALA A 265      -89.72    -94.34                                   
REMARK 500    ASN A 352       38.11   -146.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 KMT A 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LCJ   RELATED DB: PDB                                   
DBREF  4LCE A   28   353  UNP    Q13363   CTBP1_HUMAN     28    353             
SEQADV 4LCE MET A    7  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE GLY A    8  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE SER A    9  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE SER A   10  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE HIS A   11  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE HIS A   12  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE HIS A   13  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE HIS A   14  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE HIS A   15  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE HIS A   16  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE SER A   17  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE SER A   18  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE GLY A   19  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE LEU A   20  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE VAL A   21  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE PRO A   22  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE ARG A   23  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE GLY A   24  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE SER A   25  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE HIS A   26  UNP  Q13363              EXPRESSION TAG                 
SEQADV 4LCE 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      88                                                       
HET    KMT  A 402       9                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     KMT 4-(METHYLSULFANYL)-2-OXOBUTANOIC ACID                            
FORMUL   2  NAD    C21 H27 N7 O14 P2                                            
FORMUL   3  KMT    C5 H8 O3 S                                                   
FORMUL   4  HOH   *84(H2 O)                                                     
HELIX    1   1 GLU A   41  LYS A   46  1                                   6    
HELIX    2   2 SER A   58  ILE A   62  5                                   5    
HELIX    3   3 HIS A   63  GLU A   69  1                                   7    
HELIX    4   4 THR A   82  LYS A   88  1                                   7    
HELIX    5   5 ASP A  106  LEU A  113  1                                   8    
HELIX    6   6 SER A  124  ARG A  142  1                                  19    
HELIX    7   7 ARG A  142  GLU A  152  1                                  11    
HELIX    8   8 SER A  158  ALA A  166  1                                   9    
HELIX    9   9 GLY A  183  ALA A  195  1                                  13    
HELIX   10  10 GLY A  210  GLY A  216  1                                   7    
HELIX   11  11 THR A  222  SER A  230  1                                   9    
HELIX   12  12 ASN A  248  MET A  255  1                                   8    
HELIX   13  13 ARG A  266  VAL A  270  5                                   5    
HELIX   14  14 ASP A  271  GLU A  281  1                                  11    
HELIX   15  15 SER A  320  GLY A  341  1                                  22    
SHEET    1   A 5 THR A  50  PHE A  53  0                                        
SHEET    2   A 5 LEU A  29  LEU A  32  1  N  LEU A  32   O  ALA A  52           
SHEET    3   A 5 ALA A  70  MET A  75  1  O  VAL A  71   N  LEU A  29           
SHEET    4   A 5 ILE A  94  ARG A  97  1  O  VAL A  96   N  ALA A  73           
SHEET    5   A 5 ALA A 116  CYS A 118  1  O  CYS A 118   N  ARG A  97           
SHEET    1   B 7 GLN A 218  ARG A 219  0                                        
SHEET    2   B 7 ASN A 199  TYR A 203  1  N  PHE A 202   O  GLN A 218           
SHEET    3   B 7 THR A 176  ILE A 180  1  N  ILE A 179   O  LEU A 201           
SHEET    4   B 7 CYS A 232  LEU A 235  1  O  CYS A 232   N  GLY A 178           
SHEET    5   B 7 ALA A 259  ASN A 263  1  O  VAL A 262   N  VAL A 233           
SHEET    6   B 7 ILE A 284  LEU A 289  1  O  ALA A 288   N  ASN A 263           
SHEET    7   B 7 LEU A 310  CYS A 312  1  O  ILE A 311   N  ALA A 287           
CISPEP   1 GLU A  295    PRO A  296          0         5.06                     
CISPEP   2 ILE A  343    PRO A  344          0        -6.52                     
SITE     1 AC1 32 SER A 100  GLY A 101  SER A 124  THR A 128                    
SITE     2 AC1 32 ILE A 180  GLY A 181  GLY A 183  ARG A 184                    
SITE     3 AC1 32 VAL A 185  TYR A 203  ASP A 204  PRO A 205                    
SITE     4 AC1 32 TYR A 206  LEU A 207  HIS A 236  CYS A 237                    
SITE     5 AC1 32 GLY A 238  ASN A 240  ASN A 243  THR A 264                    
SITE     6 AC1 32 ALA A 265  ARG A 266  ASP A 290  HIS A 315                    
SITE     7 AC1 32 ALA A 317  TRP A 318  KMT A 402  HOH A 534                    
SITE     8 AC1 32 HOH A 567  HOH A 569  HOH A 570  HOH A 582                    
SITE     1 AC2 11 HIS A  77  ARG A  97  ILE A  98  GLY A  99                    
SITE     2 AC2 11 SER A 100  GLY A 101  ARG A 266  HIS A 315                    
SITE     3 AC2 11 MET A 327  NAD A 401  HOH A 536                               
CRYST1   88.970   88.970  161.538  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      0.011240  0.006489  0.000000        0.00000                         
SCALE2      0.000000  0.012979  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006190        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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