HEADER SIGNALING PROTEIN 16-DEC-15 5FE9
TITLE CRYSTAL STRUCTURE OF HUMAN PCAF BROMODOMAIN IN COMPLEX WITH COMPOUND
TITLE 2 SL1122 (COMPOUND 13)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE KAT2B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 715-831;
COMPND 5 SYNONYM: HISTONE ACETYLTRANSFERASE PCAF,HISTONE ACETYLASE PCAF,LYSINE
COMPND 6 ACETYLTRANSFERASE 2B,P300/CBP-ASSOCIATED FACTOR,P/CAF;
COMPND 7 EC: 2.3.1.48;
COMPND 8 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: KAT2B, PCAF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS SIGNALING PROTEIN, BROMODOMAIN, HISTONE ACETYLTRANSFERASE KAT2B,
KEYWDS 2 HISTONE, ACETYLATION, ACETYLLYSINE, EPIGENETICS, STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM (SGC)
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHAIKUAD,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,S.KNAPP,
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 10-JAN-24 5FE9 1 REMARK
REVDAT 3 21-JUL-21 5FE9 1 REMARK
REVDAT 2 30-MAR-16 5FE9 1 JRNL
REVDAT 1 13-JAN-16 5FE9 0
JRNL AUTH A.CHAIKUAD,S.LANG,P.E.BRENNAN,C.TEMPERINI,O.FEDOROV,
JRNL AUTH 2 J.HOLLANDER,R.NACHANE,C.ABELL,S.MULLER,G.SIEGAL,S.KNAPP
JRNL TITL STRUCTURE-BASED IDENTIFICATION OF INHIBITORY FRAGMENTS
JRNL TITL 2 TARGETING THE P300/CBP-ASSOCIATED FACTOR BROMODOMAIN.
JRNL REF J.MED.CHEM. V. 59 1648 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26731131
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01719
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 14724
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 776
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1051
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1805
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
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): 0.258
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.226
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.194
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.691
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1903 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1798 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2570 ; 1.337 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4151 ; 1.183 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 218 ; 5.704 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;36.882 ;23.793
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 345 ;15.239 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;24.764 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 263 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2083 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 443 ; 0.006 ; 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): 872 ; 1.286 ; 3.045
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 871 ; 1.285 ; 3.042
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1087 ; 2.179 ; 4.553
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1088 ; 2.178 ; 4.558
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1031 ; 1.722 ; 3.327
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1031 ; 1.721 ; 3.327
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1483 ; 2.877 ; 4.939
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2327 ; 6.258 ;26.845
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2328 ; 6.256 ;26.869
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 723 831 B 723 831 12186 0.13 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 723 A 728
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5602 30.8859 89.4310
REMARK 3 T TENSOR
REMARK 3 T11: 0.7914 T22: 0.7623
REMARK 3 T33: 0.7891 T12: 0.1000
REMARK 3 T13: -0.1563 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 11.8649 L22: 18.9370
REMARK 3 L33: 21.1723 L12: 14.1167
REMARK 3 L13: -0.0143 L23: -6.7108
REMARK 3 S TENSOR
REMARK 3 S11: -1.1572 S12: 0.4973 S13: -0.1829
REMARK 3 S21: -0.8045 S22: -0.3380 S23: -0.7621
REMARK 3 S31: -1.4480 S32: 3.1760 S33: 1.4952
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 729 A 831
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4912 25.4625 80.6007
REMARK 3 T TENSOR
REMARK 3 T11: 0.2271 T22: 0.1902
REMARK 3 T33: 0.1197 T12: 0.0601
REMARK 3 T13: 0.0998 T23: 0.1265
REMARK 3 L TENSOR
REMARK 3 L11: 4.6331 L22: 3.1520
REMARK 3 L33: 3.1788 L12: -1.3566
REMARK 3 L13: 0.9347 L23: -0.6636
REMARK 3 S TENSOR
REMARK 3 S11: -0.5940 S12: -0.2262 S13: -0.2653
REMARK 3 S21: -0.0346 S22: 0.5514 S23: 0.1688
REMARK 3 S31: 0.0604 S32: 0.0178 S33: 0.0425
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 723 B 734
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3780 25.2334 49.2955
REMARK 3 T TENSOR
REMARK 3 T11: 0.6806 T22: 0.4558
REMARK 3 T33: 0.3823 T12: -0.3691
REMARK 3 T13: -0.0778 T23: -0.2521
REMARK 3 L TENSOR
REMARK 3 L11: 18.1500 L22: 6.2562
REMARK 3 L33: 6.3005 L12: -4.0183
REMARK 3 L13: 2.9855 L23: 4.9226
REMARK 3 S TENSOR
REMARK 3 S11: 0.7386 S12: 1.5040 S13: -1.9863
REMARK 3 S21: 0.0009 S22: -0.2071 S23: 0.2327
REMARK 3 S31: 0.2872 S32: 0.3703 S33: -0.5315
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 735 B 831
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2160 37.5167 63.3775
REMARK 3 T TENSOR
REMARK 3 T11: 0.1266 T22: 0.0986
REMARK 3 T33: 0.1037 T12: -0.0568
REMARK 3 T13: -0.0613 T23: 0.0678
REMARK 3 L TENSOR
REMARK 3 L11: 4.4116 L22: 3.9931
REMARK 3 L33: 3.3070 L12: 0.7701
REMARK 3 L13: 0.0829 L23: 0.6146
REMARK 3 S TENSOR
REMARK 3 S11: -0.4290 S12: 0.0213 S13: -0.2479
REMARK 3 S21: 0.0163 S22: 0.4263 S23: -0.0192
REMARK 3 S31: -0.0333 S32: 0.1643 S33: 0.0027
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5FE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54167
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER PLATINUM 135
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROTEUM PLUS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15504
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 32.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.62200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3GG3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21-35% PEG 3350, 0.1 M BIS-TRIS PH 5.5
REMARK 280 -7.0 OR 21-40% MEDIUM-MOLECULAR-WEIGHT PEG SMEARS (MMW PEG
REMARK 280 SMEARS) BUFFERED EITHER WITH 0.1 M BIS-TRIS PH 6.0-7.5 OR 0.1 M
REMARK 280 TRIS PH 7.5-8.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.03800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.88945
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.27367
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 50.03800
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 28.88945
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.27367
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 50.03800
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 28.88945
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.27367
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.77891
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 66.54733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 57.77891
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 66.54733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 57.77891
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 66.54733
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: 1690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 SER A 713
REMARK 465 MET A 714
REMARK 465 GLY A 715
REMARK 465 LYS A 716
REMARK 465 GLU A 717
REMARK 465 LYS A 718
REMARK 465 SER A 719
REMARK 465 LYS A 720
REMARK 465 GLU A 721
REMARK 465 PRO A 722
REMARK 465 SER B 713
REMARK 465 MET B 714
REMARK 465 GLY B 715
REMARK 465 LYS B 716
REMARK 465 GLU B 717
REMARK 465 LYS B 718
REMARK 465 SER B 719
REMARK 465 LYS B 720
REMARK 465 GLU B 721
REMARK 465 PRO B 722
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 723 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 724 CG OD1 OD2
REMARK 470 ARG A 765 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 785 CG CD CE NZ
REMARK 470 ASP A 831 CG OD1 OD2
REMARK 470 ARG B 723 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 724 CG OD1 OD2
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 OH TYR A 809 OE1 GLN B 737 6455 2.14
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 ALA B 757 69.60 -153.10
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 5WS A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5WS B 901
DBREF 5FE9 A 715 831 UNP Q92831 KAT2B_HUMAN 715 831
DBREF 5FE9 B 715 831 UNP Q92831 KAT2B_HUMAN 715 831
SEQADV 5FE9 SER A 713 UNP Q92831 EXPRESSION TAG
SEQADV 5FE9 MET A 714 UNP Q92831 EXPRESSION TAG
SEQADV 5FE9 SER B 713 UNP Q92831 EXPRESSION TAG
SEQADV 5FE9 MET B 714 UNP Q92831 EXPRESSION TAG
SEQRES 1 A 119 SER MET GLY LYS GLU LYS SER LYS GLU PRO ARG ASP PRO
SEQRES 2 A 119 ASP GLN LEU TYR SER THR LEU LYS SER ILE LEU GLN GLN
SEQRES 3 A 119 VAL LYS SER HIS GLN SER ALA TRP PRO PHE MET GLU PRO
SEQRES 4 A 119 VAL LYS ARG THR GLU ALA PRO GLY TYR TYR GLU VAL ILE
SEQRES 5 A 119 ARG PHE PRO MET ASP LEU LYS THR MET SER GLU ARG LEU
SEQRES 6 A 119 LYS ASN ARG TYR TYR VAL SER LYS LYS LEU PHE MET ALA
SEQRES 7 A 119 ASP LEU GLN ARG VAL PHE THR ASN CYS LYS GLU TYR ASN
SEQRES 8 A 119 PRO PRO GLU SER GLU TYR TYR LYS CYS ALA ASN ILE LEU
SEQRES 9 A 119 GLU LYS PHE PHE PHE SER LYS ILE LYS GLU ALA GLY LEU
SEQRES 10 A 119 ILE ASP
SEQRES 1 B 119 SER MET GLY LYS GLU LYS SER LYS GLU PRO ARG ASP PRO
SEQRES 2 B 119 ASP GLN LEU TYR SER THR LEU LYS SER ILE LEU GLN GLN
SEQRES 3 B 119 VAL LYS SER HIS GLN SER ALA TRP PRO PHE MET GLU PRO
SEQRES 4 B 119 VAL LYS ARG THR GLU ALA PRO GLY TYR TYR GLU VAL ILE
SEQRES 5 B 119 ARG PHE PRO MET ASP LEU LYS THR MET SER GLU ARG LEU
SEQRES 6 B 119 LYS ASN ARG TYR TYR VAL SER LYS LYS LEU PHE MET ALA
SEQRES 7 B 119 ASP LEU GLN ARG VAL PHE THR ASN CYS LYS GLU TYR ASN
SEQRES 8 B 119 PRO PRO GLU SER GLU TYR TYR LYS CYS ALA ASN ILE LEU
SEQRES 9 B 119 GLU LYS PHE PHE PHE SER LYS ILE LYS GLU ALA GLY LEU
SEQRES 10 B 119 ILE ASP
HET 5WS A 901 18
HET EDO A 902 4
HET 5WS B 901 18
HETNAM 5WS ~{N}-(1,4-DIMETHYL-2-OXIDANYLIDENE-QUINOLIN-7-YL)
HETNAM 2 5WS METHANESULFONAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 5WS 2(C12 H14 N2 O3 S)
FORMUL 4 EDO C2 H6 O2
FORMUL 6 HOH *116(H2 O)
HELIX 1 AA1 ARG A 723 HIS A 742 1 20
HELIX 2 AA2 GLN A 743 MET A 749 5 7
HELIX 3 AA3 GLY A 759 ILE A 764 1 6
HELIX 4 AA4 ASP A 769 ASN A 779 1 11
HELIX 5 AA5 SER A 784 ASN A 803 1 20
HELIX 6 AA6 SER A 807 ALA A 827 1 21
HELIX 7 AA7 ASP B 724 HIS B 742 1 19
HELIX 8 AA8 GLN B 743 MET B 749 5 7
HELIX 9 AA9 GLY B 759 ILE B 764 1 6
HELIX 10 AB1 ASP B 769 ASN B 779 1 11
HELIX 11 AB2 SER B 784 ASN B 803 1 20
HELIX 12 AB3 SER B 807 ALA B 827 1 21
SITE 1 AC1 9 PRO A 747 GLU A 750 PRO A 751 LYS A 753
SITE 2 AC1 9 GLU A 756 ALA A 757 ASN A 803 HOH A1002
SITE 3 AC1 9 HOH A1003
SITE 1 AC2 4 ARG A 780 HOH A1026 ARG B 776 TYR B 781
SITE 1 AC3 11 PRO B 747 GLU B 750 PRO B 751 VAL B 752
SITE 2 AC3 11 LYS B 753 GLU B 756 ASN B 803 TYR B 809
SITE 3 AC3 11 HOH B1001 HOH B1002 HOH B1033
CRYST1 100.076 100.076 99.821 90.00 90.00 120.00 H 3 18
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 0.009992 0.005769 0.000000 0.00000
SCALE2 0.000000 0.011538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010018 0.00000
(ATOM LINES ARE NOT SHOWN.)
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