HEADER TRANSCRIPTION 03-APR-15 4UIV
TITLE BROMODOMAIN OF HUMAN BRD9 WITH N-(1,1-DIOXO-1-THIAN-4-YL)-5-METHYL-4-
TITLE 2 OXO-7-3-(TRIFLUOROMETHYL)PHENYL-4H,5H-THIENO-3,2-C-PYRIDINE-2-
TITLE 3 CARBOXIMIDAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BROMODOMAIN OF BRD9, UNP RESIDUES 134-238;
COMPND 5 SYNONYM: RHABDOMYOSARCOMA ANTIGEN MU-RMS-40.8, HUMAN BRD9;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS TRANSCRIPTION, INHIBITOR, HISTONE, EPIGENETIC READER
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHUNG,N.T.THEODOULOU,P.BAMBOROUGH,P.G.HUMPHREYS
REVDAT 4 15-MAY-19 4UIV 1 REMARK
REVDAT 3 28-JUN-17 4UIV 1 REMARK
REVDAT 2 09-MAR-16 4UIV 1 JRNL
REVDAT 1 22-APR-15 4UIV 0
JRNL AUTH N.H.THEODOULOU,P.BAMBOROUGH,A.J.BANNISTER,I.BECHER,R.A.BIT,
JRNL AUTH 2 K.H.CHE,C.CHUNG,A.DITTMANN,G.DREWES,D.H.DREWRY,L.GORDON,
JRNL AUTH 3 P.GRANDI,M.LEVERIDGE,M.LINDON,A.MICHON,J.MOLNAR,S.C.ROBSON,
JRNL AUTH 4 N.C.O.TOMKINSON,T.KOUZARIDES,R.K.PRINJHA,P.G.HUMPHREYS
JRNL TITL THE DISCOVERY OF I-BRD9, A SELECTIVE CELL ACTIVE CHEMICAL
JRNL TITL 2 PROBE FOR BROMODOMAIN CONTAINING PROTEIN 9 INHIBITION.
JRNL REF J.MED.CHEM. V. 59 1425 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 25856009
JRNL DOI 10.1021/ACS.JMEDCHEM.5B00256
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 10171
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 517
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) : 1.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 675
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 23
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 821
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 208
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : 0.05000
REMARK 3 B12 (A**2) : 0.02000
REMARK 3 B13 (A**2) : 0.07000
REMARK 3 B23 (A**2) : -0.21000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.387
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 911 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 640 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1238 ; 1.642 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1567 ; 1.014 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 110 ; 4.226 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 37 ;36.293 ;23.784
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 166 ;13.046 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;10.659 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 128 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 976 ; 0.056 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 186 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
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 22 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7418 4.8553 3.6407
REMARK 3 T TENSOR
REMARK 3 T11: 0.0403 T22: 0.0092
REMARK 3 T33: 0.0127 T12: 0.0053
REMARK 3 T13: -0.0051 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 1.3164 L22: 0.2640
REMARK 3 L33: 0.2151 L12: 0.2436
REMARK 3 L13: -0.1357 L23: 0.1837
REMARK 3 S TENSOR
REMARK 3 S11: 0.0162 S12: -0.0394 S13: 0.0653
REMARK 3 S21: -0.0045 S22: -0.0115 S23: 0.0163
REMARK 3 S31: -0.0001 S32: 0.0007 S33: -0.0047
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4UIV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063537.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10790
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 28.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.5
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.02000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.06000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MORPHEUS BUFFER PH 6.5, 30%
REMARK 280 MORPHEUS_EDO_P8K,0.1M MORPHEUS AMINO ACIDS 4C, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
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
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 GLY A 17
REMARK 465 ALA A 18
REMARK 465 GLU A 19
REMARK 465 ASN A 20
REMARK 465 GLU A 21
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 O HOH A 2056 O HOH A 2060 2.04
REMARK 500 O HOH A 2027 O HOH A 2037 2.10
REMARK 500 O HOH A 2091 O HOH A 2092 2.13
REMARK 500 O HOH A 2094 O HOH A 2155 2.14
REMARK 500 O HOH A 2075 O HOH A 2135 2.15
REMARK 500 O HOH A 2137 O HOH A 2145 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 2160 O HOH A 2207 1455 2.17
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 A2035 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A2048 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH A2054 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A2102 DISTANCE = 7.24 ANGSTROMS
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 1123
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XZB A 1124
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UIT RELATED DB: PDB
REMARK 900 BROMODOMAIN OF HUMAN BRD9 WITH 7-(3,4-DIMETHOXYPHENYL )-2-(4-
REMARK 900 METHANESULFONYLPIPERAZINE-1-CARBONYL)-5-METHYL- 4H,5H-THIENO-3,2-C-
REMARK 900 PYRIDIN-4-ONE
REMARK 900 RELATED ID: 4UIU RELATED DB: PDB
REMARK 900 BROMODOMAIN OF HUMAN BRD9 WITH 7-(3,4-DIMETHOXYPHENYL )-N-(1,1-
REMARK 900 DIOXO-1-THIAN-4-YL)-5-METHYL-4-OXO- 4H,5H-THIENO-3,2-C-PYRIDINE-2-
REMARK 900 CARBOXAMIDE
REMARK 900 RELATED ID: 4UIW RELATED DB: PDB
REMARK 900 BROMODOMAIN OF HUMAN BRD9 WITH N-(1,1-DIOXO-1- THIAN-4-YL)-5-ETHYL-
REMARK 900 4-OXO-7-3-(TRIFLUOROMETHYL) PHENYL-4H,5H-THIENO-3,2-C-PYRIDINE-2-
REMARK 900 CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UIX RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD4 WITH 7-(3,4- DIMETHOXYPHENYL)-
REMARK 900 N-(1,1-DIOXO-1-THIAN-4-YL)-5- METHYL-4-OXO-4H,5H-THIENO-3,2-C-
REMARK 900 PYRIDINE-2- CARBOXAMIDE
REMARK 900 RELATED ID: 4UIY RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD4 WITH N-(1,1- DIOXO-1-THIAN-4-
REMARK 900 YL)-5-METHYL-4-OXO-7-3-( TRIFLUOROMETHYL)PHENYL-4H,5H-THIENO-3,2-C-
REMARK 900 PYRIDINE-2 -CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UIZ RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD4 WITH 7-(3,4- DIMETHOXYPHENYL)-
REMARK 900 2-(4-METHANESULFONYLPIPERAZINE-1-CARBONYL )-5-METHYL-4H,5H-THIENO-3,
REMARK 900 2-C-PYRIDIN-4-ONE
DBREF 4UIV A 18 122 UNP Q9H8M2 BRD9_HUMAN 134 238
SEQADV 4UIV GLY A 17 UNP Q9H8M2 EXPRESSION TAG
SEQRES 1 A 106 GLY ALA GLU ASN GLU SER THR PRO ILE GLN GLN LEU LEU
SEQRES 2 A 106 GLU HIS PHE LEU ARG GLN LEU GLN ARG LYS ASP PRO HIS
SEQRES 3 A 106 GLY PHE PHE ALA PHE PRO VAL THR ASP ALA ILE ALA PRO
SEQRES 4 A 106 GLY TYR SER MET ILE ILE LYS HIS PRO MET ASP PHE GLY
SEQRES 5 A 106 THR MET LYS ASP LYS ILE VAL ALA ASN GLU TYR LYS SER
SEQRES 6 A 106 VAL THR GLU PHE LYS ALA ASP PHE LYS LEU MET CYS ASP
SEQRES 7 A 106 ASN ALA MET THR TYR ASN ARG PRO ASP THR VAL TYR TYR
SEQRES 8 A 106 LYS LEU ALA LYS LYS ILE LEU HIS ALA GLY PHE LYS MET
SEQRES 9 A 106 MET SER
HET EDO A1123 4
HET XZB A1124 32
HETNAM EDO 1,2-ETHANEDIOL
HETNAM XZB N-(1,1-DIOXO-1-THIAN-4-YL)-5-METHYL-4-OXO-7-3-
HETNAM 2 XZB (TRIFLUOROMETHYL)PHENYL-4H,5H-THIENO-3,2-C-PYRIDINE-2-
HETNAM 3 XZB CARBOXIMIDAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO C2 H6 O2
FORMUL 3 XZB C21 H20 F3 N3 O3 S2
FORMUL 4 HOH *208(H2 O)
HELIX 1 1 THR A 23 LYS A 39 1 17
HELIX 2 2 GLY A 56 ILE A 61 1 6
HELIX 3 3 ASP A 66 ALA A 76 1 11
HELIX 4 4 SER A 81 ASN A 100 1 20
HELIX 5 5 THR A 104 MET A 121 1 18
SITE 1 AC1 7 GLN A 37 ALA A 46 GLY A 68 PHE A 118
SITE 2 AC1 7 HOH A2039 HOH A2130 HOH A2207
SITE 1 AC2 13 PHE A 44 PHE A 45 VAL A 49 ILE A 53
SITE 2 AC2 13 ALA A 54 TYR A 99 ASN A 100 ARG A 101
SITE 3 AC2 13 THR A 104 TYR A 106 LYS A 111 HOH A2110
SITE 4 AC2 13 HOH A2208
CRYST1 24.682 33.836 39.542 68.09 73.70 73.35 P 1 1
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 0.040515 -0.012117 -0.008429 0.00000
SCALE2 0.000000 0.030848 -0.010359 0.00000
SCALE3 0.000000 0.000000 0.027795 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
