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Database: PDB
Entry: 1MX3
LinkDB: 1MX3
Original site: 1MX3 
HEADER    TRANSCRIPTION REPRESSOR                 01-OCT-02   1MX3              
TITLE     CRYSTAL STRUCTURE OF CTBP DEHYDROGENASE CORE HOLO FORM                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-TERMINAL BINDING PROTEIN 1;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 28-353;                                           
COMPND   5 SYNONYM: CTBP1;                                                      
COMPND   6 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;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3) PLYSS;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    NUCLEAR PROTEIN, PHOSPHORYLATION, TRANSCRIPTIONAL COREPRESSOR,        
KEYWDS   2 TRANSCRIPTION REPRESSOR                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.KUMAR,J.E.CARLSON,K.E.OHGI,T.E.EDWARDS,D.W.ROSE,C.R.ESCALANTE,      
AUTHOR   2 A.K.AGGARWAL                                                         
REVDAT   3   13-JUL-11 1MX3    1       VERSN                                    
REVDAT   2   24-FEB-09 1MX3    1       VERSN                                    
REVDAT   1   18-DEC-02 1MX3    0                                                
JRNL        AUTH   V.KUMAR,J.E.CARLSON,K.E.OHGI,T.E.EDWARDS,D.W.ROSE,           
JRNL        AUTH 2 C.R.ESCALANTE,A.K.AGGARWAL                                   
JRNL        TITL   TRANSCRIPTION COREPRESSOR CTBP IS AN NAD+-REGULATED          
JRNL        TITL 2 DEHYDROGENASE                                                
JRNL        REF    MOL.CELL                      V.  10   857 2002              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   12419229                                                     
JRNL        DOI    10.1016/S1097-2765(02)00650-0                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 52834                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2642                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2512                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 415                                     
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MX3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017268.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : NULL; NULL                         
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : NSLS; APS                          
REMARK 200  BEAMLINE                       : X25; 32-ID                         
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.140; 0.97957, 0.97941, 0.96859   
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : NULL; NULL                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52854                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, MAGNESIUM ACETATE,       
REMARK 280  HEPES, PH 7, VAPOR DIFFUSION, HANGING DROP                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.66667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      109.33333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       54.66667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      109.33333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.66667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      109.33333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       54.66667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      109.33333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25590 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  0.500000  0.866025  0.000000      -44.55000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       77.16286            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      109.33333            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
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      -44.55000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       77.16286            
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      109.33333            
REMARK 350   BIOMT1   4  0.500000  0.866025  0.000000      -44.55000            
REMARK 350   BIOMT2   4  0.866025 -0.500000  0.000000       77.16286            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      109.33333            
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 465     LYS A   353                                                      
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   NH1  ARG A   336     NH1  ARG A   336    11556     1.55            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL A 200   N     VAL A 200   CA      0.269                       
REMARK 500    CYS A 350   C     VAL A 351   N      -0.145                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A 200   N   -  CA  -  CB  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    VAL A 200   C   -  N   -  CA  ANGL. DEV. = -24.4 DEGREES          
REMARK 500    CYS A 350   O   -  C   -  N   ANGL. DEV. =   9.6 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       52.03   -106.73                                   
REMARK 500    TYR A  76     -153.61    -93.87                                   
REMARK 500    LEU A 182       62.58   -103.93                                   
REMARK 500    ASP A 204       91.79   -160.47                                   
REMARK 500    HIS A 236       31.77   -145.81                                   
REMARK 500    ALA A 265      -86.32    -93.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR A 319        24.5      L          L   OUTSIDE RANGE           
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 A2067        DISTANCE =  7.79 ANGSTROMS                       
REMARK 525    HOH A2119        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A2127        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A2236        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH A2244        DISTANCE =  7.41 ANGSTROMS                       
REMARK 525    HOH A2255        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH A2259        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A2273        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH A2299        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A2311        DISTANCE =  9.22 ANGSTROMS                       
REMARK 525    HOH A2328        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH A2330        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH A2335        DISTANCE =  7.60 ANGSTROMS                       
REMARK 525    HOH A2340        DISTANCE =  8.83 ANGSTROMS                       
REMARK 525    HOH A2348        DISTANCE =  8.01 ANGSTROMS                       
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 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 4000                
DBREF  1MX3 A   28   353  UNP    Q13363   CTBP1_HUMAN     28    353             
SEQADV 1MX3 MET A    7  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 GLY A    8  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 SER A    9  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 SER A   10  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 HIS A   11  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 HIS A   12  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 HIS A   13  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 HIS A   14  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 HIS A   15  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 HIS A   16  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 SER A   17  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 SER A   18  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 GLY A   19  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 LEU A   20  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 VAL A   21  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 PRO A   22  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 ARG A   23  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 GLY A   24  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 SER A   25  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 HIS A   26  UNP  Q13363              EXPRESSION TAG                 
SEQADV 1MX3 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  A1000      44                                                       
HET    ACY  A4000       4                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     ACY ACETIC ACID                                                      
FORMUL   2  NAD    C21 H27 N7 O14 P2                                            
FORMUL   3  ACY    C2 H4 O2                                                     
FORMUL   4  HOH   *415(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  GLU A   87  1                                   6    
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  LYS A  253  1                                   6    
HELIX   13  13 ASP A  271  GLU A  281  1                                  11    
HELIX   14  14 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  VAL A  30   O  THR A  50           
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  ALA A 116   N  ILE A  95           
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  PHE A 260   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         0.21                     
CISPEP   2 ILE A  343    PRO A  344          0        -0.12                     
SITE     1 AC1 37 SER A 100  GLY A 101  THR A 128  ILE A 180                    
SITE     2 AC1 37 GLY A 181  GLY A 183  ARG A 184  VAL A 185                    
SITE     3 AC1 37 TYR A 203  ASP A 204  PRO A 205  TYR A 206                    
SITE     4 AC1 37 HIS A 236  CYS A 237  GLY A 238  ASN A 240                    
SITE     5 AC1 37 ASN A 243  THR A 264  ALA A 265  ARG A 266                    
SITE     6 AC1 37 ASP A 290  VAL A 291  HIS A 315  ALA A 317                    
SITE     7 AC1 37 TRP A 318  HOH A2008  HOH A2011  HOH A2012                    
SITE     8 AC1 37 HOH A2014  HOH A2059  HOH A2086  HOH A2192                    
SITE     9 AC1 37 HOH A2264  HOH A2347  HOH A2349  HOH A2360                    
SITE    10 AC1 37 ACY A4000                                                     
SITE     1 AC2  8 ARG A  97  SER A 100  GLY A 101  ARG A 266                    
SITE     2 AC2  8 HIS A 315  NAD A1000  HOH A2349  HOH A2354                    
CRYST1   89.100   89.100  164.000  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      0.011223  0.006480  0.000000        0.00000                         
SCALE2      0.000000  0.012960  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006098        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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