HEADER UNKNOWN FUNCTION 12-JUL-11 3SVG
TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX
TITLE 2 WITH A 3,5-DIMETHYLISOXAZOL LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN HUNK1;
COMPND 5 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: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS ISOXAZOLE, BROMODOMAIN, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, SGC, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.FILIPPAKOPOULOS,S.PICAUD,I.FELLETAR,S.D.HEWINGS,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,S.J.CONWAY,S.KNAPP,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 2 13-SEP-23 3SVG 1 REMARK SEQADV
REVDAT 1 10-AUG-11 3SVG 0
JRNL AUTH P.FILIPPAKOPOULOS,S.PICAUD,I.FELLETAR,S.D.HEWINGS,
JRNL AUTH 2 F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,
JRNL AUTH 3 S.J.CONWAY,S.KNAPP
JRNL TITL CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN
JRNL TITL 2 COMPLEX WITH A 3,5-DIMETHYLISOXAZOL LIGAND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 15383
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 767
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) : 1.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1043
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.4570
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.4540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1052
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 125
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.28000
REMARK 3 B22 (A**2) : -0.65000
REMARK 3 B33 (A**2) : -0.63000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.948
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
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): 1146 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 792 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1563 ; 1.552 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1941 ; 0.953 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 136 ; 5.169 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;36.355 ;25.714
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 201 ;11.653 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;14.411 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 166 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1237 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 205 ; 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): 659 ; 2.791 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 248 ; 0.870 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1090 ; 4.135 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 487 ; 5.472 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 468 ; 7.388 ;11.000
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 : 3
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 42 A 59
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8116 20.7976 20.5355
REMARK 3 T TENSOR
REMARK 3 T11: 0.0678 T22: 0.0520
REMARK 3 T33: 0.0239 T12: -0.0097
REMARK 3 T13: -0.0161 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.3593 L22: 1.1125
REMARK 3 L33: 0.9487 L12: 0.1176
REMARK 3 L13: 0.0623 L23: 1.2835
REMARK 3 S TENSOR
REMARK 3 S11: 0.0222 S12: -0.0393 S13: -0.0203
REMARK 3 S21: -0.0255 S22: -0.0998 S23: 0.0138
REMARK 3 S31: -0.0158 S32: 0.0118 S33: 0.0777
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 60 A 157
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8371 24.9104 6.5086
REMARK 3 T TENSOR
REMARK 3 T11: 0.0392 T22: 0.0400
REMARK 3 T33: 0.0355 T12: 0.0002
REMARK 3 T13: -0.0095 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.1812 L22: 0.8145
REMARK 3 L33: 0.2797 L12: -0.1446
REMARK 3 L13: 0.0753 L23: 0.1053
REMARK 3 S TENSOR
REMARK 3 S11: -0.0394 S12: 0.0113 S13: 0.0029
REMARK 3 S21: 0.0328 S22: 0.0204 S23: -0.0199
REMARK 3 S31: -0.0291 S32: -0.0094 S33: 0.0190
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 : A 158 A 168
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9419 41.9211 9.4666
REMARK 3 T TENSOR
REMARK 3 T11: 0.1070 T22: 0.0064
REMARK 3 T33: 0.0517 T12: 0.0274
REMARK 3 T13: -0.0111 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 0.0843 L22: 7.0542
REMARK 3 L33: 3.5525 L12: 0.9349
REMARK 3 L13: -0.8782 L23: 2.7198
REMARK 3 S TENSOR
REMARK 3 S11: -0.0100 S12: 0.0743 S13: 0.1524
REMARK 3 S21: 0.2197 S22: 0.1031 S23: 0.1154
REMARK 3 S31: -0.2862 S32: 0.1149 S33: -0.0931
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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. U VALUES WITH TLS ADDED.
REMARK 4
REMARK 4 3SVG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066701.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 1.52
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15429
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 25.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : 0.58000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: PDB ENTRY 2OSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NA2SO4, 0.1M BTPROP, 20% PEG
REMARK 280 3350, 10% ETGLY, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 18.83000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.92500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.09500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.92500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.83000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.09500
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 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 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 LYS A 91 CD CE NZ
REMARK 470 GLN A 123 CD OE1 NE2
REMARK 470 LYS A 141 CD CE NZ
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ODR A 169
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SVF RELATED DB: PDB
REMARK 900 RELATED ID: 3SVH RELATED DB: PDB
DBREF 3SVG A 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 3SVG SER A 42 UNP O60885 EXPRESSION TAG
SEQADV 3SVG 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 EDO A 1 4
HET EDO A 2 4
HET EDO A 3 4
HET ODR A 169 19
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ODR (1R)-1-[3-(3,5-DIMETHYL-1,2-OXAZOL-4-YL)-5-
HETNAM 2 ODR ETHOXYPHENYL]ETHANOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 3(C2 H6 O2)
FORMUL 5 ODR C15 H19 N O3
FORMUL 6 HOH *125(H2 O)
HELIX 1 1 THR A 60 VAL A 69 1 10
HELIX 2 2 VAL A 69 LYS A 76 1 8
HELIX 3 3 ALA A 80 GLN A 84 5 5
HELIX 4 4 ASP A 96 ILE A 101 1 6
HELIX 5 5 ASP A 106 ASN A 116 1 11
HELIX 6 6 ASN A 121 ASN A 140 1 20
HELIX 7 7 ASP A 144 GLU A 163 1 20
SITE 1 AC1 5 ILE A 100 ILE A 101 LYS A 102 THR A 103
SITE 2 AC1 5 ASN A 135
SITE 1 AC2 6 TYR A 137 ILE A 138 GLN A 159 LYS A 160
SITE 2 AC2 6 GLU A 163 HOH A 238
SITE 1 AC3 9 VAL A 69 TYR A 137 ASN A 140 LYS A 141
SITE 2 AC3 9 PRO A 142 VAL A 147 LYS A 160 HOH A 239
SITE 3 AC3 9 HOH A 253
SITE 1 AC4 11 HOH A 7 HOH A 18 HOH A 23 TRP A 81
SITE 2 AC4 11 PRO A 82 GLN A 85 ASP A 96 LYS A 99
SITE 3 AC4 11 ASN A 140 ILE A 146 MET A 149
CRYST1 37.660 44.190 77.850 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 0.026553 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022630 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012845 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
