HEADER OXIDOREDUCTASE 16-FEB-09 3GA0
TITLE CTBP1/BARS GLY172->GLU MUTANT STRUCTURE: IMPAIRING NAD(H) BINDING AND
TITLE 2 DIMERIZATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-TERMINAL-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-350;
COMPND 5 SYNONYM: CTBP1, C-TERMINAL-BINDING PROTEIN 3, CTBP3, 50 KDA BFA-
COMPND 6 DEPENDENT ADP-RIBOSYLATION SUBSTRATE, BARS-50;
COMPND 7 EC: 1.1.1.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CTBP1, BARS, CTBP3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11D-HIS
KEYWDS TRANSCRIPTION CO-REPRESSION, ACYLTRANSFERASE, BREFELDIN A, NAD, GOLGI
KEYWDS 2 MEMBRANE, ACYL-COA, ADP-RIBOSYLATION, CYTOPLASM, NUCLEUS,
KEYWDS 3 OXIDOREDUCTASE, PHOSPHOPROTEIN, UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.NARDINI,C.VALENTE,S.RICAGNO,A.LUINI,D.CORDA,M.BOLOGNESI
REVDAT 3 01-NOV-23 3GA0 1 REMARK
REVDAT 2 10-NOV-21 3GA0 1 REMARK SEQADV
REVDAT 1 21-APR-09 3GA0 0
JRNL AUTH M.NARDINI,C.VALENTE,S.RICAGNO,A.LUINI,D.CORDA,M.BOLOGNESI
JRNL TITL CTBP1/BARS GLY172-->GLU MUTANT STRUCTURE: IMPAIRING
JRNL TITL 2 NAD(H)-BINDING AND DIMERIZATION
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 381 70 2009
JRNL REFN ISSN 0006-291X
JRNL PMID 19351597
JRNL DOI 10.1016/J.BBRC.2009.02.010
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 5053
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) : 0.270
REMARK 3 R VALUE (WORKING SET) : 0.262
REMARK 3 FREE R VALUE : 0.334
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 560
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) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 355
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 38
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2609
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.83000
REMARK 3 B22 (A**2) : 1.83000
REMARK 3 B33 (A**2) : -2.75000
REMARK 3 B12 (A**2) : 0.92000
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): 0.665
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.846
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.667
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.232
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.882
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.850
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 : 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: NULL
REMARK 4
REMARK 4 3GA0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1000051610.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-04
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 : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5615
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 29.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
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) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1HKU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8-2.1M AMMONIUM FORMATE, 1.0M HEPES
REMARK 280 (PH7.5), CROSS-SEEDING TECHNIQUE, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 294K
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 53.41967
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 106.83933
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 53.41967
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 106.83933
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 53.41967
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 106.83933
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 53.41967
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 106.83933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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: 6540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.1 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 0.00000
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 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 -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 VAL A 4
REMARK 465 ARG A 5
REMARK 465 PRO A 6
REMARK 465 PRO A 7
REMARK 465 ILE A 8
REMARK 465 MET A 9
REMARK 465 ALA A 347
REMARK 465 ALA A 348
REMARK 465 THR A 349
REMARK 465 HIS A 350
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 HIS A 14 -74.37 -139.42
REMARK 500 PRO A 15 -87.25 -18.01
REMARK 500 ASP A 44 43.99 37.93
REMARK 500 TYR A 65 -144.54 -103.67
REMARK 500 GLU A 141 29.03 -74.90
REMARK 500 GLN A 146 -65.20 -134.45
REMARK 500 ARG A 173 -126.35 47.01
REMARK 500 ALA A 254 -142.02 -65.74
REMARK 500 ASP A 260 90.76 -67.19
REMARK 500 GLU A 282 83.41 -68.72
REMARK 500 SER A 283 91.95 179.05
REMARK 500 PRO A 285 -71.08 0.37
REMARK 500 SER A 287 -154.37 -164.96
REMARK 500 PHE A 288 -26.13 63.26
REMARK 500 ASP A 295 18.93 59.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 11 PRO A 12 -138.67
REMARK 500 MET A 13 HIS A 14 -146.61
REMARK 500 HIS A 14 PRO A 15 -139.09
REMARK 500 ARG A 16 PRO A 17 -143.24
REMARK 500 SER A 283 GLU A 284 -141.76
REMARK 500 PHE A 286 SER A 287 142.54
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 FMT A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HL3 RELATED DB: PDB
REMARK 900 CTBP/BARS: A DUAL-FUNCTION CTBP/BARS IN TERNARY COMPLEX WITH NAD(H)
REMARK 900 AND PIDLSKK PEPTIDE
REMARK 900 RELATED ID: 1HKU RELATED DB: PDB
REMARK 900 CTBP/BARS: A DUAL-FUNCTION PROTEIN INVOLVED IN TRANSCRIPTION
REMARK 900 COREPRESSION AND GOLGI MEMBRANE FISSION
REMARK 900 RELATED ID: 2HU2 RELATED DB: PDB
REMARK 900 CTBP/BARS IN TERNARY COMPLEX WITH NAD(H) AND RRTGAPPAL PEPTIDE
DBREF 3GA0 A 1 350 UNP Q9Z2F5 CTBP1_RAT 1 350
SEQADV 3GA0 MET A -7 UNP Q9Z2F5 EXPRESSION TAG
SEQADV 3GA0 GLY A -6 UNP Q9Z2F5 EXPRESSION TAG
SEQADV 3GA0 HIS A -5 UNP Q9Z2F5 EXPRESSION TAG
SEQADV 3GA0 HIS A -4 UNP Q9Z2F5 EXPRESSION TAG
SEQADV 3GA0 HIS A -3 UNP Q9Z2F5 EXPRESSION TAG
SEQADV 3GA0 HIS A -2 UNP Q9Z2F5 EXPRESSION TAG
SEQADV 3GA0 HIS A -1 UNP Q9Z2F5 EXPRESSION TAG
SEQADV 3GA0 HIS A 0 UNP Q9Z2F5 EXPRESSION TAG
SEQADV 3GA0 GLU A 172 UNP Q9Z2F5 GLY 172 ENGINEERED MUTATION
SEQRES 1 A 358 MET GLY HIS HIS HIS HIS HIS HIS MET SER GLY VAL ARG
SEQRES 2 A 358 PRO PRO ILE MET ASN GLY PRO MET HIS PRO ARG PRO LEU
SEQRES 3 A 358 VAL ALA LEU LEU ASP GLY ARG ASP CYS THR VAL GLU MET
SEQRES 4 A 358 PRO ILE LEU LYS ASP VAL ALA THR VAL ALA PHE CYS ASP
SEQRES 5 A 358 ALA GLN SER THR GLN GLU ILE HIS GLU LYS VAL LEU ASN
SEQRES 6 A 358 GLU ALA VAL GLY ALA LEU MET TYR HIS THR ILE THR LEU
SEQRES 7 A 358 THR ARG GLU ASP LEU GLU LYS PHE LYS ALA LEU ARG ILE
SEQRES 8 A 358 ILE VAL ARG ILE GLY SER GLY PHE ASP ASN ILE ASP ILE
SEQRES 9 A 358 LYS SER ALA GLY ASP LEU GLY ILE ALA VAL CYS ASN VAL
SEQRES 10 A 358 PRO ALA ALA SER VAL GLU GLU THR ALA ASP SER THR LEU
SEQRES 11 A 358 CYS HIS ILE LEU ASN LEU TYR ARG ARG THR THR TRP LEU
SEQRES 12 A 358 HIS GLN ALA LEU ARG GLU GLY THR ARG VAL GLN SER VAL
SEQRES 13 A 358 GLU GLN ILE ARG GLU VAL ALA SER GLY ALA ALA ARG ILE
SEQRES 14 A 358 ARG GLY GLU THR LEU GLY ILE ILE GLY LEU GLU ARG VAL
SEQRES 15 A 358 GLY GLN ALA VAL ALA LEU ARG ALA LYS ALA PHE GLY PHE
SEQRES 16 A 358 ASN VAL LEU PHE TYR ASP PRO TYR LEU SER ASP GLY ILE
SEQRES 17 A 358 GLU ARG ALA LEU GLY LEU GLN ARG VAL SER THR LEU GLN
SEQRES 18 A 358 ASP LEU LEU PHE HIS SER ASP CYS VAL THR LEU HIS CYS
SEQRES 19 A 358 GLY LEU ASN GLU HIS ASN HIS HIS LEU ILE ASN ASP PHE
SEQRES 20 A 358 THR VAL LYS GLN MET ARG GLN GLY ALA PHE LEU VAL ASN
SEQRES 21 A 358 THR ALA ARG GLY GLY LEU VAL ASP GLU LYS ALA LEU ALA
SEQRES 22 A 358 GLN ALA LEU LYS GLU GLY ARG ILE ARG GLY ALA ALA LEU
SEQRES 23 A 358 ASP VAL HIS GLU SER GLU PRO PHE SER PHE SER GLN GLY
SEQRES 24 A 358 PRO LEU LYS ASP ALA PRO ASN LEU ILE CYS THR PRO HIS
SEQRES 25 A 358 ALA ALA TRP TYR SER GLU GLN ALA SER ILE GLU MET ARG
SEQRES 26 A 358 GLU GLU ALA ALA ARG GLU ILE ARG ARG ALA ILE THR GLY
SEQRES 27 A 358 ARG ILE PRO ASP SER LEU LYS ASN CYS VAL ASN LYS ASP
SEQRES 28 A 358 HIS LEU THR ALA ALA THR HIS
HET FMT A 800 3
HET FMT A 801 3
HETNAM FMT FORMIC ACID
FORMUL 2 FMT 2(C H2 O2)
FORMUL 4 HOH *(H2 O)
HELIX 1 1 GLU A 30 LYS A 35 1 6
HELIX 2 2 SER A 47 ILE A 51 5 5
HELIX 3 3 HIS A 52 ALA A 59 1 8
HELIX 4 4 THR A 71 PHE A 78 1 8
HELIX 5 5 ASP A 95 ASP A 101 1 7
HELIX 6 6 SER A 113 ARG A 131 1 19
HELIX 7 7 ARG A 131 GLU A 141 1 11
HELIX 8 8 SER A 147 ALA A 155 1 9
HELIX 9 9 VAL A 174 PHE A 185 1 12
HELIX 10 10 GLY A 199 LEU A 204 1 6
HELIX 11 11 THR A 211 SER A 219 1 9
HELIX 12 12 ASN A 237 GLN A 243 1 7
HELIX 13 13 ARG A 255 VAL A 259 5 5
HELIX 14 14 ASP A 260 GLU A 270 1 11
HELIX 15 15 SER A 309 GLY A 330 1 22
HELIX 16 16 ASN A 341 LEU A 345 5 5
SHEET 1 A 5 THR A 39 PHE A 42 0
SHEET 2 A 5 LEU A 18 LEU A 21 1 N VAL A 19 O THR A 39
SHEET 3 A 5 GLY A 61 MET A 64 1 O LEU A 63 N ALA A 20
SHEET 4 A 5 ILE A 83 ARG A 86 1 O VAL A 85 N ALA A 62
SHEET 5 A 5 ALA A 105 CYS A 107 1 O ALA A 105 N ILE A 84
SHEET 1 B 7 GLN A 207 ARG A 208 0
SHEET 2 B 7 ASN A 188 TYR A 192 1 N PHE A 191 O GLN A 207
SHEET 3 B 7 THR A 165 ILE A 169 1 N ILE A 168 O TYR A 192
SHEET 4 B 7 CYS A 221 LEU A 224 1 O CYS A 221 N GLY A 167
SHEET 5 B 7 PHE A 249 ASN A 252 1 O VAL A 251 N VAL A 222
SHEET 6 B 7 GLY A 275 LEU A 278 1 O ALA A 277 N LEU A 250
SHEET 7 B 7 LEU A 299 CYS A 301 1 O ILE A 300 N LEU A 278
CISPEP 1 ILE A 332 PRO A 333 0 -11.01
SITE 1 AC1 4 THR A 253 ARG A 255 HIS A 304 FMT A 801
SITE 1 AC2 5 HIS A 66 ARG A 86 ILE A 87 TRP A 307
SITE 2 AC2 5 FMT A 800
CRYST1 89.197 89.197 160.259 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 0.011211 0.006473 0.000000 0.00000
SCALE2 0.000000 0.012946 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006240 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
