HEADER REPLICATION, TRANSCRIPTION REGULATOR 02-SEP-06 2I8N
TITLE SOLUTION STRUCTURE OF THE SECOND BROMODOMAIN OF BRD4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL BROMODOMAIN;
COMPND 5 SYNONYM: HUNK1 PROTEIN;
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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(GOLD);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B(+)
KEYWDS BROMODOMAIN, 3D STRUCTURE, STRUCTURAL GENOMICS, REPLICATION,
KEYWDS 2 TRANSCRIPTION REGULATOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.LIU,J.H.WU,Y.Y.SHI
REVDAT 3 09-MAR-22 2I8N 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2I8N 1 VERSN
REVDAT 1 04-SEP-07 2I8N 0
JRNL AUTH Y.LIU,J.H.WU,Y.Y.SHI
JRNL TITL SOLUTION STRUCTURE OF THE SECOND BROMODOMAIN OF BRD4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, CNS 1.1
REMARK 3 AUTHORS : F.DELAGLIO (NMRPIPE),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE NMR STRUCTURES ARE BASED ON A TOTAL
REMARK 3 OF 1688 RESTRAINTS, 1490 ARE NOE-DERIVED DISTANCE CONSTRAINTS,
REMARK 3 144 DIHEDRAL ANGLE RESTRANTS, 54 DISTANCE RESTRAINTS FROM
REMARK 3 HYDROGEN BONDS.
REMARK 4
REMARK 4 2I8N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-SEP-06.
REMARK 100 THE DEPOSITION ID IS D_1000039275.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 20MM NA2HPO4, 50MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0MM 15N, 13C-LABELED BRD4 C
REMARK 210 -TERMINAL DOMAIN, 20MM PHOSPHATE
REMARK 210 BUFFER(PH6.0), 50MM NACL, 5MM
REMARK 210 EDTA, 10%(V/V)D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY; 2D
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3, CNS 1.1, CSI 1.0,
REMARK 210 MOLMOL 2K.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 109
REMARK 465 HIS A 110
REMARK 465 HIS A 111
REMARK 465 HIS A 112
REMARK 465 HIS A 113
REMARK 465 HIS A 114
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 1 HIS A 18 29.61 -143.55
REMARK 500 1 PRO A 28 -173.70 -69.51
REMARK 500 2 HIS A 18 30.16 -145.33
REMARK 500 2 ASP A 30 100.08 -58.15
REMARK 500 2 HIS A 45 77.43 -112.45
REMARK 500 2 ASP A 85 67.91 60.13
REMARK 500 3 HIS A 18 28.63 -140.69
REMARK 500 3 PHE A 25 52.46 -141.70
REMARK 500 3 PRO A 28 177.06 -57.79
REMARK 500 3 ASP A 30 93.13 -61.16
REMARK 500 3 ASP A 85 68.03 62.27
REMARK 500 5 HIS A 18 33.40 -144.45
REMARK 500 5 PRO A 28 -171.71 -62.38
REMARK 500 5 ASP A 30 102.49 -57.92
REMARK 500 5 ASP A 85 71.43 62.52
REMARK 500 6 TYR A 26 -55.06 -127.89
REMARK 500 6 PRO A 28 -177.22 -67.98
REMARK 500 6 ASP A 30 97.69 -60.17
REMARK 500 7 PHE A 25 58.24 -150.54
REMARK 500 7 PRO A 28 -179.56 -59.47
REMARK 500 7 VAL A 29 73.99 -107.70
REMARK 500 7 ASP A 85 68.72 61.51
REMARK 500 8 VAL A 29 76.47 -111.91
REMARK 500 9 VAL A 29 75.14 -113.83
REMARK 500 9 ASP A 30 103.74 -58.60
REMARK 500 10 PHE A 25 36.16 -97.42
REMARK 500 10 TYR A 26 -58.15 -131.51
REMARK 500 10 ASP A 30 104.34 -58.69
REMARK 500 10 ASP A 85 64.31 63.00
REMARK 500 11 PRO A 28 -177.40 -59.18
REMARK 500 11 ASP A 85 69.26 62.51
REMARK 500 12 PRO A 28 -176.07 -60.35
REMARK 500 13 HIS A 18 30.49 -148.58
REMARK 500 13 TYR A 26 -58.09 -121.39
REMARK 500 13 VAL A 29 79.76 -112.60
REMARK 500 13 ASP A 30 104.35 -58.94
REMARK 500 13 ASP A 85 70.58 62.57
REMARK 500 14 VAL A 29 76.35 -113.18
REMARK 500 14 ASP A 30 98.56 -60.10
REMARK 500 14 LEU A 36 71.66 -118.47
REMARK 500 14 ASP A 85 68.07 60.20
REMARK 500 15 PRO A 28 -178.55 -63.19
REMARK 500 16 HIS A 18 29.95 -144.13
REMARK 500 16 ASP A 30 105.10 -59.74
REMARK 500 16 ASP A 85 60.04 60.27
REMARK 500 17 TYR A 26 -48.82 -131.19
REMARK 500 17 ASP A 30 98.97 -59.49
REMARK 500 17 HIS A 45 66.96 -118.68
REMARK 500 17 ASP A 85 71.70 65.53
REMARK 500 18 TYR A 26 -63.95 -137.86
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RESIDUE 107 AND 108 BELONG TO THE PLASMID VECTOR ITSELF
DBREF 2I8N A 1 106 UNP O60885 BRD4_HUMAN 352 457
SEQADV 2I8N LEU A 107 UNP O60885 SEE REMARK 999
SEQADV 2I8N GLN A 108 UNP O60885 SEE REMARK 999
SEQADV 2I8N HIS A 109 UNP O60885 EXPRESSION TAG
SEQADV 2I8N HIS A 110 UNP O60885 EXPRESSION TAG
SEQADV 2I8N HIS A 111 UNP O60885 EXPRESSION TAG
SEQADV 2I8N HIS A 112 UNP O60885 EXPRESSION TAG
SEQADV 2I8N HIS A 113 UNP O60885 EXPRESSION TAG
SEQADV 2I8N HIS A 114 UNP O60885 EXPRESSION TAG
SEQRES 1 A 114 GLU GLN LEU LYS CYS CYS SER GLY ILE LEU LYS GLU MET
SEQRES 2 A 114 PHE ALA LYS LYS HIS ALA ALA TYR ALA TRP PRO PHE TYR
SEQRES 3 A 114 LYS PRO VAL ASP VAL GLU ALA LEU GLY LEU HIS ASP TYR
SEQRES 4 A 114 CYS ASP ILE ILE LYS HIS PRO MET ASP MET SER THR ILE
SEQRES 5 A 114 LYS SER LYS LEU GLU ALA ARG GLU TYR ARG ASP ALA GLN
SEQRES 6 A 114 GLU PHE GLY ALA ASP VAL ARG LEU MET PHE SER ASN CYS
SEQRES 7 A 114 TYR LYS TYR ASN PRO PRO ASP HIS GLU VAL VAL ALA MET
SEQRES 8 A 114 ALA ARG LYS LEU GLN ASP VAL PHE GLU MET ARG PHE ALA
SEQRES 9 A 114 LYS MET LEU GLN HIS HIS HIS HIS HIS HIS
HELIX 1 1 GLU A 1 PHE A 14 1 14
HELIX 2 2 ASP A 30 GLY A 35 1 6
HELIX 3 3 HIS A 37 ILE A 43 1 7
HELIX 4 4 ASP A 48 ALA A 58 1 11
HELIX 5 5 ASP A 63 ASN A 82 1 20
HELIX 6 6 HIS A 86 GLN A 108 1 23
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END