HEADER TRANSCRIPTION/INHIBITOR 17-JUN-16 5KJ0
TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX
TITLE 2 WITH DB-1-264-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 44-168;
COMPND 5 SYNONYM: PROTEIN HUNK1;
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: BRD4, HUNK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS BROMODOMAIN, CAP, HUNK1, MCAP, PROTEIN BINDING-INHIBITOR COMPLEX,
KEYWDS 2 MITOTIC CHROMOSOME ASSOCIATED PROTEIN, CELL CYCLE, INHIBITOR,
KEYWDS 3 TRANSCRIPTION-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-Y.ZHU,S.W.EMBER,E.SCHONBRUNN
REVDAT 2 27-SEP-23 5KJ0 1 REMARK
REVDAT 1 09-AUG-17 5KJ0 0
JRNL AUTH L.W.KOBLAN,D.L.BUCKLEY,C.J.OTT,M.E.FITZGERALD,S.W.EMBER,
JRNL AUTH 2 J.Y.ZHU,S.LIU,J.M.ROBERTS,D.REMILLARD,S.VITTORI,W.ZHANG,
JRNL AUTH 3 E.SCHONBRUNN,J.E.BRADNER
JRNL TITL ASSESSMENT OF BROMODOMAIN TARGET ENGAGEMENT BY A SERIES OF
JRNL TITL 2 BI2536 ANALOGUES WITH MINIATURIZED BET-BRET.
JRNL REF CHEMMEDCHEM V. 11 2575 2016
JRNL REFN ESSN 1860-7187
JRNL PMID 27862999
JRNL DOI 10.1002/CMDC.201600502
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 20265
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1014
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.3758 - 2.8858 1.00 2990 158 0.1492 0.1609
REMARK 3 2 2.8858 - 2.2917 1.00 2860 150 0.1405 0.1734
REMARK 3 3 2.2917 - 2.0023 1.00 2833 149 0.1303 0.1633
REMARK 3 4 2.0023 - 1.8194 1.00 2810 148 0.1311 0.1847
REMARK 3 5 1.8194 - 1.6891 0.98 2734 144 0.1377 0.1738
REMARK 3 6 1.6891 - 1.5896 0.95 2656 140 0.1322 0.2092
REMARK 3 7 1.5896 - 1.5100 0.85 2368 125 0.1291 0.1548
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.55
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 1175
REMARK 3 ANGLE : 1.323 1591
REMARK 3 CHIRALITY : 0.052 164
REMARK 3 PLANARITY : 0.007 201
REMARK 3 DIHEDRAL : 14.920 485
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 42 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8345 -9.2831 15.0330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0859 T22: 0.0630
REMARK 3 T33: 0.0561 T12: -0.0095
REMARK 3 T13: -0.0358 T23: 0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 4.6823 L22: 2.2195
REMARK 3 L33: 4.6358 L12: 0.5799
REMARK 3 L13: 0.6543 L23: -3.0425
REMARK 3 S TENSOR
REMARK 3 S11: 0.1789 S12: 0.0653 S13: -0.2472
REMARK 3 S21: -0.0105 S22: -0.0378 S23: -0.0510
REMARK 3 S31: 0.3036 S32: -0.0462 S33: -0.0688
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0861 10.8302 16.8529
REMARK 3 T TENSOR
REMARK 3 T11: 0.1025 T22: 0.0851
REMARK 3 T33: 0.0654 T12: 0.0145
REMARK 3 T13: -0.0094 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.7594 L22: 1.0774
REMARK 3 L33: 2.5518 L12: -0.3082
REMARK 3 L13: 0.9282 L23: -1.0094
REMARK 3 S TENSOR
REMARK 3 S11: -0.1034 S12: -0.1409 S13: 0.0191
REMARK 3 S21: 0.2092 S22: -0.0118 S23: -0.0336
REMARK 3 S31: -0.2704 S32: -0.1387 S33: 0.0922
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 76 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1004 -5.1551 1.4140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0384 T22: 0.0442
REMARK 3 T33: 0.0541 T12: -0.0142
REMARK 3 T13: -0.0122 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 2.2419 L22: 3.4501
REMARK 3 L33: 1.4377 L12: -1.7902
REMARK 3 L13: 0.5213 L23: 0.0688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: 0.0347 S13: -0.1142
REMARK 3 S21: -0.0677 S22: 0.0276 S23: 0.0776
REMARK 3 S31: 0.0340 S32: 0.0097 S33: -0.0448
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2447 -2.2808 10.2683
REMARK 3 T TENSOR
REMARK 3 T11: 0.0678 T22: 0.0533
REMARK 3 T33: 0.0384 T12: -0.0043
REMARK 3 T13: -0.0112 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 2.6394 L22: 3.9049
REMARK 3 L33: 3.1423 L12: -2.3841
REMARK 3 L13: -0.9978 L23: 2.4764
REMARK 3 S TENSOR
REMARK 3 S11: -0.0762 S12: -0.0920 S13: -0.0069
REMARK 3 S21: 0.1478 S22: 0.1193 S23: -0.0409
REMARK 3 S31: 0.1355 S32: 0.0908 S33: 0.0176
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 116 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0278 5.5966 10.8617
REMARK 3 T TENSOR
REMARK 3 T11: 0.0643 T22: 0.0563
REMARK 3 T33: 0.0575 T12: -0.0020
REMARK 3 T13: -0.0163 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.8967 L22: 2.0570
REMARK 3 L33: 6.7002 L12: -1.0008
REMARK 3 L13: -1.3671 L23: 2.7437
REMARK 3 S TENSOR
REMARK 3 S11: -0.0071 S12: -0.1038 S13: 0.0245
REMARK 3 S21: 0.0322 S22: 0.0768 S23: -0.1469
REMARK 3 S31: -0.1707 S32: 0.0632 S33: -0.0676
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1124 -2.5313 -8.6437
REMARK 3 T TENSOR
REMARK 3 T11: 0.1712 T22: 0.2070
REMARK 3 T33: 0.0759 T12: -0.0270
REMARK 3 T13: 0.0297 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 5.2215 L22: 3.9502
REMARK 3 L33: 3.1399 L12: -0.0893
REMARK 3 L13: -0.7166 L23: -3.4532
REMARK 3 S TENSOR
REMARK 3 S11: 0.1129 S12: 0.6805 S13: -0.1375
REMARK 3 S21: -0.7535 S22: -0.0112 S23: -0.1807
REMARK 3 S31: 0.1921 S32: 0.3722 S33: 0.1007
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3918 12.8836 3.1163
REMARK 3 T TENSOR
REMARK 3 T11: 0.0677 T22: 0.0512
REMARK 3 T33: 0.0666 T12: -0.0081
REMARK 3 T13: -0.0179 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 1.9743 L22: 2.8912
REMARK 3 L33: 2.0081 L12: 0.1649
REMARK 3 L13: 0.1460 L23: 0.6549
REMARK 3 S TENSOR
REMARK 3 S11: -0.0595 S12: -0.0291 S13: 0.1943
REMARK 3 S21: -0.0736 S22: 0.0840 S23: -0.0337
REMARK 3 S31: -0.2462 S32: 0.1189 S33: 0.0243
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5KJ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20265
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 19.374
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.02100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 41.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.06500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.90
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: 4O74
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5 MG/ML BRD4, 5MM HEPES PH 7.5,
REMARK 280 50MM SODIUM CHLORIDE, 0.5MM DTT, 50MM TRIS PH8.5, 0.1M AMMONIUM,
REMARK 280 SULFATE, 12.5% PEG 3,350, 10% DMSO, 1 MM DB-1-264-2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 18.55500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.86000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.35000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.86000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.55500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.35000
REMARK 290 SMTRY3 4 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 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 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 413 O HOH A 420 2.12
REMARK 500 O HOH A 426 O HOH A 434 2.17
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 353 O HOH A 430 3645 2.17
REMARK 500 O HOH A 368 O HOH A 404 4445 2.18
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 6TB A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 208
DBREF 5KJ0 A 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 5KJ0 SER A 42 UNP O60885 EXPRESSION TAG
SEQADV 5KJ0 MET A 43 UNP O60885 EXPRESSION TAG
SEQRES 1 A 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 A 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 A 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 A 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 A 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 A 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 A 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 A 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 A 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 A 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
HET 6TB A 201 80
HET EDO A 202 10
HET EDO A 203 10
HET EDO A 204 10
HET EDO A 205 10
HET EDO A 206 10
HET EDO A 207 10
HET EDO A 208 10
HETNAM 6TB 4-[[(7~{R})-8-CYCLOPENTYL-7-ETHYL-5-METHYL-6-
HETNAM 2 6TB OXIDANYLIDENE-7~{H}-PTERIDIN-2-YL]-METHYL-AMINO]-3-
HETNAM 3 6TB METHOXY-~{N}-(1-METHYLPIPERIDIN-4-YL)BENZAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN 6TB (R)-4-((8-CYCLOPENTYL-7-ETHYL-5-METHYL-6-OXO-5,6,7,8-
HETSYN 2 6TB TETRAHYDROPTERIDIN-2-YL)(METHYL)AMINO)-3-METHOXY-N-(1-
HETSYN 3 6TB METHYLPIPERIDIN-4-YL)BENZAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 6TB C29 H41 N7 O3
FORMUL 3 EDO 7(C2 H6 O2)
FORMUL 10 HOH *143(H2 O)
HELIX 1 AA1 THR A 60 VAL A 69 1 10
HELIX 2 AA2 VAL A 69 LYS A 76 1 8
HELIX 3 AA3 ALA A 80 GLN A 84 5 5
HELIX 4 AA4 ASP A 96 ILE A 101 1 6
HELIX 5 AA5 ASP A 106 ASN A 116 1 11
HELIX 6 AA6 ASN A 121 ASN A 140 1 20
HELIX 7 AA7 ASP A 144 ASN A 162 1 19
SITE 1 AC1 12 TRP A 81 PRO A 82 GLN A 85 VAL A 87
SITE 2 AC1 12 LEU A 92 ASP A 96 ASN A 140 ILE A 146
SITE 3 AC1 12 HOH A 310 HOH A 316 HOH A 340 HOH A 391
SITE 1 AC2 6 ILE A 100 ILE A 101 LYS A 102 THR A 103
SITE 2 AC2 6 ASN A 135 HOH A 363
SITE 1 AC3 5 ARG A 68 LYS A 72 VAL A 147 GLU A 151
SITE 2 AC3 5 HOH A 309
SITE 1 AC4 4 TYR A 137 LYS A 160 GLU A 163 HOH A 354
SITE 1 AC5 7 HIS A 77 GLN A 78 ILE A 126 ASN A 130
SITE 2 AC5 7 LEU A 158 ILE A 161 HOH A 350
SITE 1 AC6 6 PRO A 53 TRP A 81 LYS A 99 MET A 149
SITE 2 AC6 6 HOH A 311 HOH A 323
SITE 1 AC7 7 HIS A 77 ASN A 130 THR A 134 LEU A 156
SITE 2 AC7 7 HOH A 312 HOH A 350 HOH A 356
SITE 1 AC8 7 GLN A 59 LEU A 63 GLN A 64 LEU A 114
SITE 2 AC8 7 ASN A 117 HOH A 321 HOH A 396
CRYST1 37.110 44.700 77.720 90.00 90.00 90.00 P 21 21 21 4
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 0.026947 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022371 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012867 0.00000
(ATOM LINES ARE NOT SHOWN.)
END