HEADER SIGNALING PROTEIN 16-DEC-15 5FE7
TITLE CRYSTAL STRUCTURE OF HUMAN PCAF BROMODOMAIN IN COMPLEX WITH FRAGMENT
TITLE 2 ZB2216 (FRAGMENT 11)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE KAT2B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PCAF BROMODOMAIN, 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 3 10-JAN-24 5FE7 1 REMARK
REVDAT 2 30-MAR-16 5FE7 1 JRNL
REVDAT 1 13-JAN-16 5FE7 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. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
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) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 21469
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1063
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) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1565
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1810
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 172
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : -0.27000
REMARK 3 B12 (A**2) : 0.04000
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): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.138
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.743
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1908 ; 0.016 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1831 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2564 ; 1.503 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4238 ; 1.086 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 221 ; 5.285 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 89 ;38.666 ;23.708
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 355 ;14.185 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;17.872 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 263 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2107 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 440 ; 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 ; 2.331 ; 2.985
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 873 ; 2.330 ; 2.988
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1089 ; 3.282 ; 4.460
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1089 ; 3.279 ; 4.458
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1036 ; 3.650 ; 3.466
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1036 ; 3.650 ; 3.466
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1473 ; 5.522 ; 5.008
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2423 ; 9.138 ;26.112
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2424 ; 9.136 ;26.124
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 723 829 B 723 829 6054 0.15 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 831
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6656 31.9483 20.5356
REMARK 3 T TENSOR
REMARK 3 T11: 0.1079 T22: 0.0662
REMARK 3 T33: 0.0653 T12: -0.0169
REMARK 3 T13: -0.0353 T23: 0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 5.5510 L22: 3.1813
REMARK 3 L33: 4.0150 L12: 1.2597
REMARK 3 L13: -0.3952 L23: -0.8689
REMARK 3 S TENSOR
REMARK 3 S11: -0.2260 S12: -0.0511 S13: -0.0259
REMARK 3 S21: 0.0811 S22: 0.1844 S23: -0.1312
REMARK 3 S31: -0.0297 S32: 0.2026 S33: 0.0416
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 : B 723 B 830
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8166 21.5577 39.7396
REMARK 3 T TENSOR
REMARK 3 T11: 0.0359 T22: 0.0457
REMARK 3 T33: 0.0866 T12: 0.0319
REMARK 3 T13: 0.0121 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 4.9466 L22: 4.1342
REMARK 3 L33: 5.8766 L12: -0.3403
REMARK 3 L13: 0.8628 L23: 0.7083
REMARK 3 S TENSOR
REMARK 3 S11: -0.2637 S12: -0.1463 S13: 0.3705
REMARK 3 S21: 0.0992 S22: 0.2884 S23: -0.1255
REMARK 3 S31: -0.0790 S32: 0.1547 S33: -0.0248
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 5FE7 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_1000216438.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22541
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 31.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.83600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: PDB ID 3GG3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
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 49.80500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.75493
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.85133
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 49.80500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 28.75493
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.85133
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 49.80500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 28.75493
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.85133
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.50986
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 67.70267
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 57.50986
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 67.70267
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 57.50986
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 67.70267
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465 ASP B 831
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 ASP A 831 CG OD1 OD2
REMARK 470 ARG B 723 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU B 808 O HOH B 1001 2.08
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 58.63 -156.35
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 EDO A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5WU A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 903
DBREF 5FE7 A 715 831 UNP Q92831 KAT2B_HUMAN 715 831
DBREF 5FE7 B 715 831 UNP Q92831 KAT2B_HUMAN 715 831
SEQADV 5FE7 SER A 713 UNP Q92831 EXPRESSION TAG
SEQADV 5FE7 MET A 714 UNP Q92831 EXPRESSION TAG
SEQADV 5FE7 SER B 713 UNP Q92831 EXPRESSION TAG
SEQADV 5FE7 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 EDO A 901 4
HET 5WU A 902 14
HET EDO B 901 4
HET EDO B 902 8
HET DMS B 903 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 5WU 1-(2-HYDROXYETHYL)-3-METHYL-6,7-DIHYDRO-5~{H}-INDAZOL-
HETNAM 2 5WU 4-ONE
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 4 5WU C10 H14 N2 O2
FORMUL 7 DMS C2 H6 O S
FORMUL 8 HOH *172(H2 O)
HELIX 1 AA1 ARG A 723 HIS A 742 1 20
HELIX 2 AA2 ALA A 745 MET A 749 5 5
HELIX 3 AA3 LYS A 753 ALA A 757 5 5
HELIX 4 AA4 GLY A 759 ILE A 764 1 6
HELIX 5 AA5 ASP A 769 ASN A 779 1 11
HELIX 6 AA6 SER A 784 ASN A 803 1 20
HELIX 7 AA7 SER A 807 ALA A 827 1 21
HELIX 8 AA8 ASP B 724 HIS B 742 1 19
HELIX 9 AA9 ALA B 745 MET B 749 5 5
HELIX 10 AB1 LYS B 753 ALA B 757 5 5
HELIX 11 AB2 GLY B 759 ILE B 764 1 6
HELIX 12 AB3 ASP B 769 ASN B 779 1 11
HELIX 13 AB4 SER B 784 ASN B 803 1 20
HELIX 14 AB5 SER B 807 ALA B 827 1 21
SITE 1 AC1 4 LYS A 733 GLN A 737 SER A 774 HOH A1016
SITE 1 AC2 10 PRO A 747 VAL A 752 LYS A 753 GLU A 756
SITE 2 AC2 10 ALA A 757 TYR A 802 ASN A 803 TYR A 809
SITE 3 AC2 10 HOH A1007 HOH A1014
SITE 1 AC3 8 GLU A 750 LYS B 740 HIS B 742 GLN B 743
SITE 2 AC3 8 ALA B 745 TRP B 746 HOH B1009 HOH B1028
SITE 1 AC4 7 VAL B 752 LYS B 753 ARG B 754 TYR B 761
SITE 2 AC4 7 HOH B1003 HOH B1030 HOH B1031
SITE 1 AC5 3 PRO B 747 ASN B 803 HOH B1011
CRYST1 99.610 99.610 101.554 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 0.010039 0.005796 0.000000 0.00000
SCALE2 0.000000 0.011592 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009847 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
