HEADER PROTEIN BINDING 03-JUN-15 2N3K
TITLE HUMAN BRD4 ET DOMAIN IN COMPLEX WITH MLV INTEGRASE C-TERM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BRD4 ET DOMAIN (UNP RESIDUES 600-678);
COMPND 5 SYNONYM: PROTEIN HUNK1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MLV INTEGRASE;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: MLV INTEGRASE C-TERMINAL EBM (UNP RESIDUES 1719-1735);
COMPND 11 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);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEX-N-HIS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: MOLONEY MURINE LEUKEMIA VIRUS;
SOURCE 14 ORGANISM_COMMON: MOMLV;
SOURCE 15 ORGANISM_TAXID: 11801
KEYWDS BRD4 ET, MLV INTEGRASE, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.L.CROWE,M.P.FOSTER
REVDAT 3 14-JUN-23 2N3K 1 REMARK SEQADV
REVDAT 2 23-MAR-16 2N3K 1 JRNL
REVDAT 1 02-MAR-16 2N3K 0
JRNL AUTH B.L.CROWE,R.C.LARUE,C.YUAN,S.HESS,M.KVARATSKHELIA,M.P.FOSTER
JRNL TITL STRUCTURE OF THE BRD4 ET DOMAIN BOUND TO A C-TERMINAL MOTIF
JRNL TITL 2 FROM GAMMA-RETROVIRAL INTEGRASES REVEALS A CONSERVED
JRNL TITL 3 MECHANISM OF INTERACTION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 2086 2016
JRNL REFN ISSN 0027-8424
JRNL PMID 26858406
JRNL DOI 10.1073/PNAS.1516813113
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CYANA 3.97
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), GUNTERT, MUMENTHALER AND
REMARK 3 WUTHRICH (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2N3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000104377.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0.25
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4-0.8 MM [U-99% 13C; U-99%
REMARK 210 15N] BRD4 ET, 0.4-0.8 MM MLV IN
REMARK 210 EBM, 20 MM [U-2H] TRIS, 100 MM
REMARK 210 SODIUM CHLORIDE, 0.002 V/V
REMARK 210 SODIUM AZIDE, 0.5 MM DSS, 2 MM
REMARK 210 [U-2H] DTT, 90% H2O/10% D2O; 0.4-
REMARK 210 0.8 MM [U-99% 13C; U-99% 15N]
REMARK 210 BRD4 ET, 0.4-0.8 MM MLV IN EBM,
REMARK 210 20 MM [U-2H] TRIS, 100 MM SODIUM
REMARK 210 CHLORIDE, 0.002 V/V SODIUM AZIDE,
REMARK 210 0.5 MM DSS, 2 MM [U-2H] DTT,
REMARK 210 100% D2O; 0.4-0.8 MM [U-99% 15N]
REMARK 210 BRD4 ET, 0.4-0.8 MM MLV IN EBM,
REMARK 210 20 MM [U-2H] TRIS, 100 MM SODIUM
REMARK 210 CHLORIDE, 0.002 V/V SODIUM AZIDE,
REMARK 210 0.5 MM DSS, 2 MM [U-2H] DTT, 90%
REMARK 210 H2O/10% D2O; 0.4-0.8 MM [U-99%
REMARK 210 15N] BRD4 ET, 20 MM [U-2H] TRIS,
REMARK 210 100 MM SODIUM CHLORIDE, 0.002 V/
REMARK 210 V SODIUM AZIDE, 0.5 MM DSS, 2 MM
REMARK 210 [U-2H] DTT, 90% H2O/10% D2O; 1
REMARK 210 MM MLV IN EBM, 0.5 MM DSS, 0.002
REMARK 210 V/V SODIUM AZIDE, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC
REMARK 210 ALIPHATIC; 1D 13C,15N-FILTERED
REMARK 210 WATERGATE 1H; 3D HNCO; 3D HNCA;
REMARK 210 3D HNCACB; 3D CBCA(CO)NH; 3D
REMARK 210 HBHA(CO)NH; 3D HCCH-TOCSY; 3D
REMARK 210 CC(CO)NH-TOCSY; 2D 13C,15N-
REMARK 210 FILTERED 1H-1H COSY; 2D 13C,15N-
REMARK 210 FILTERED 1H-1H TOCSY; 2D 13C,15N-
REMARK 210 FILTERED 1H-1H NOESY; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-13C NOESY ALIPHATIC;
REMARK 210 3D 13C,15N-FILTERED(F1) 1H-
REMARK 210 15N(F2) NOESY; 3D 13C,15N-
REMARK 210 FILTERED(F1) 1H-13C(F2) NOESY
REMARK 210 ALIPHATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE III HD ULTRASHIELD;
REMARK 210 AVANCE III HD ASCEND
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TOPSPIN, NMRPIPE, NMRVIEWJ
REMARK 210 8.1.17, PINE, TALOS-N, CYANA
REMARK 210 3.97, PSVS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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. (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 GLY A 595
REMARK 465 ALA A 596
REMARK 465 ILE A 597
REMARK 465 ALA A 598
REMARK 465 MET A 599
REMARK 465 THR A 679
REMARK 465 ARG A 680
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 SER A 601 -77.72 -142.56
REMARK 500 1 GLU A 603 -75.99 -172.67
REMARK 500 1 GLU A 604 -68.22 71.97
REMARK 500 1 LEU A 644 -166.56 -60.99
REMARK 500 1 ARG A 676 172.16 61.47
REMARK 500 1 LYS A 677 -70.05 -168.60
REMARK 500 1 ASN B 397 164.62 -47.52
REMARK 500 1 LEU B 399 57.28 -176.68
REMARK 500 2 SER A 601 -74.55 -91.40
REMARK 500 2 GLU A 603 35.51 -179.35
REMARK 500 2 GLU A 604 -55.85 -126.22
REMARK 500 2 GLU A 641 107.17 -48.84
REMARK 500 2 LEU A 644 97.93 -57.04
REMARK 500 2 ARG A 676 -75.24 69.42
REMARK 500 2 LYS A 677 -62.24 -179.25
REMARK 500 2 GLN B 393 119.46 -168.14
REMARK 500 2 ASN B 397 164.56 -47.43
REMARK 500 2 LEU B 399 59.98 -178.59
REMARK 500 3 GLU A 603 -43.76 -163.78
REMARK 500 3 LEU A 644 93.75 -62.44
REMARK 500 3 ARG A 676 176.57 62.33
REMARK 500 3 LYS A 677 -75.17 69.21
REMARK 500 3 ASN B 397 163.87 -47.12
REMARK 500 3 LEU B 399 58.11 -173.43
REMARK 500 4 GLU A 603 48.29 -92.95
REMARK 500 4 LEU A 644 101.57 -51.43
REMARK 500 4 ARG A 676 -68.91 72.28
REMARK 500 4 LYS A 677 84.34 52.99
REMARK 500 4 ASN B 397 164.75 -47.31
REMARK 500 4 LEU B 399 58.68 -179.48
REMARK 500 5 SER A 601 -72.82 -65.54
REMARK 500 5 GLU A 603 -41.61 -168.84
REMARK 500 5 LEU A 644 102.69 -51.92
REMARK 500 5 LYS A 645 41.31 -147.66
REMARK 500 5 ARG A 676 -75.13 69.65
REMARK 500 5 LYS A 677 137.87 -178.13
REMARK 500 5 ASN B 397 162.33 -45.99
REMARK 500 5 LEU B 399 60.76 -175.49
REMARK 500 6 GLU A 603 50.39 -94.48
REMARK 500 6 CYS A 607 108.22 -51.98
REMARK 500 6 LEU A 644 -76.21 -50.04
REMARK 500 6 LYS A 645 85.78 48.69
REMARK 500 6 ASN B 397 164.02 -46.04
REMARK 500 6 LEU B 399 58.11 -177.33
REMARK 500 7 SER A 601 -74.60 -152.38
REMARK 500 7 GLU A 603 35.62 -179.45
REMARK 500 7 LYS A 645 36.55 -94.51
REMARK 500 7 ARG A 676 76.61 56.36
REMARK 500 7 LYS A 677 -72.90 -120.68
REMARK 500 7 GLN B 393 94.04 -164.23
REMARK 500
REMARK 500 THIS ENTRY HAS 138 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 25649 RELATED DB: BMRB
DBREF 2N3K A 600 678 UNP O60885 BRD4_HUMAN 600 678
DBREF 2N3K B 389 405 UNP Q8UN00 Q8UN00_MLVMO 1719 1735
SEQADV 2N3K GLY A 595 UNP O60885 EXPRESSION TAG
SEQADV 2N3K ALA A 596 UNP O60885 EXPRESSION TAG
SEQADV 2N3K ILE A 597 UNP O60885 EXPRESSION TAG
SEQADV 2N3K ALA A 598 UNP O60885 EXPRESSION TAG
SEQADV 2N3K MET A 599 UNP O60885 EXPRESSION TAG
SEQADV 2N3K THR A 679 UNP O60885 EXPRESSION TAG
SEQADV 2N3K ARG A 680 UNP O60885 EXPRESSION TAG
SEQRES 1 A 86 GLY ALA ILE ALA MET GLU SER GLU GLU GLU ASP LYS CYS
SEQRES 2 A 86 LYS PRO MET SER TYR GLU GLU LYS ARG GLN LEU SER LEU
SEQRES 3 A 86 ASP ILE ASN LYS LEU PRO GLY GLU LYS LEU GLY ARG VAL
SEQRES 4 A 86 VAL HIS ILE ILE GLN SER ARG GLU PRO SER LEU LYS ASN
SEQRES 5 A 86 SER ASN PRO ASP GLU ILE GLU ILE ASP PHE GLU THR LEU
SEQRES 6 A 86 LYS PRO SER THR LEU ARG GLU LEU GLU ARG TYR VAL THR
SEQRES 7 A 86 SER CYS LEU ARG LYS LYS THR ARG
SEQRES 1 B 17 THR TRP ARG VAL GLN ARG SER GLN ASN PRO LEU LYS ILE
SEQRES 2 B 17 ARG LEU THR ARG
HELIX 1 1 SER A 611 LEU A 625 1 15
HELIX 2 2 PRO A 626 GLU A 641 1 16
HELIX 3 3 LYS A 660 ARG A 676 1 17
SHEET 1 A 3 GLU A 651 ASP A 655 0
SHEET 2 A 3 LYS B 400 THR B 404 -1 O LEU B 403 N ILE A 652
SHEET 3 A 3 ARG B 391 ARG B 394 -1 N ARG B 391 O THR B 404
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