HEADER TRANSCRIPTION/VIRAL PROTEIN 18-APR-16 2ND0
TITLE SOLUTION NMR STRUCTURES OF BRD4 ET DOMAIN WITH LANA PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 601-683;
COMPND 5 SYNONYM: PROTEIN HUNK1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LANA;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 1086-1104;
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: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET32A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 8;
SOURCE 12 ORGANISM_COMMON: HHV-8;
SOURCE 13 ORGANISM_TAXID: 37296
KEYWDS TRANSCRIPTION, VIRAL PROTEIN, TRANSCRIPTION-VIRAL PROTEIN COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.ZENG,M.ZHOU
REVDAT 2 20-JUL-16 2ND0 1 JRNL
REVDAT 1 29-JUN-16 2ND0 0
JRNL AUTH Q.ZHANG,L.ZENG,C.SHEN,Y.JU,T.KONUMA,C.ZHAO,C.R.VAKOC,
JRNL AUTH 2 M.M.ZHOU
JRNL TITL STRUCTURAL MECHANISM OF TRANSCRIPTIONAL REGULATOR NSD3
JRNL TITL 2 RECOGNITION BY THE ET DOMAIN OF BRD4.
JRNL REF STRUCTURE V. 24 1201 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 27291650
JRNL DOI 10.1016/J.STR.2016.04.019
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 2.3, TALOS, CNS 1.2
REMARK 3 AUTHORS : LINGE, O'DONOGHUE AND NILGES (ARIA), CORNILESCU,
REMARK 3 DELAGLIO AND BAX (TALOS), BRUNGER, ADAMS, CLORE,
REMARK 3 GROS, NILGES AND READ (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ND0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-16.
REMARK 100 THE RCSB ID CODE IS RCSB104710.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 MM SODIUM PHOSPHATE, 100 MM
REMARK 210 SODIUM CHLORIDE, 2 MM [U-100% 2H]
REMARK 210 DTT, 100% D2O; 10 MM SODIUM
REMARK 210 PHOSPHATE, 100 MM SODIUM
REMARK 210 CHLORIDE, 2 MM [U-100% 2H] DTT,
REMARK 210 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCACB; 3D
REMARK 210 CBCA(CO)NH; 3D 1H-15N NOESY; 3D
REMARK 210 1H-15N TOCSY; 3D 1H-13C NOESY
REMARK 210 ALIPHATIC; 3D 1H-13C NOESY
REMARK 210 AROMATIC; 2D 1H-13C HSQC; 3D
REMARK 210 FILTERED 1H-13C NOESY ALIPHATIC;
REMARK 210 3D FILTERED 1H-13C NOESY AROMATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ; 600 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.04, CNS 1.2,
REMARK 210 TOPSPIN, PROCHECKNMR
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, DISTANCE
REMARK 210 GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 OE2 GLU A 53 HZ1 LYS B 206 1.60
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 46 36.92 -89.46
REMARK 500 1 GLN B 201 99.45 -64.15
REMARK 500 1 LEU B 211 95.56 66.67
REMARK 500 3 LYS A 78 -144.30 -141.23
REMARK 500 3 ARG A 79 -51.73 -150.71
REMARK 500 3 LYS A 80 122.91 178.33
REMARK 500 3 LEU B 200 -48.11 -132.18
REMARK 500 3 LEU B 211 70.16 48.59
REMARK 500 4 CYS A 7 98.29 62.34
REMARK 500 4 ASN A 46 41.86 -98.71
REMARK 500 4 LYS A 78 75.38 -151.53
REMARK 500 4 LYS A 80 74.89 58.15
REMARK 500 4 LEU B 211 65.37 60.70
REMARK 500 5 LYS A 80 82.41 65.07
REMARK 500 5 LEU B 211 87.32 -154.89
REMARK 500 5 GLN B 215 -52.08 -169.77
REMARK 500 6 CYS A 7 102.23 63.86
REMARK 500 6 LEU A 44 41.95 -95.59
REMARK 500 6 ASN A 46 35.10 -96.52
REMARK 500 6 LYS A 80 71.71 59.53
REMARK 500 6 PRO A 81 41.45 -75.39
REMARK 500 6 LYS B 206 77.95 -105.63
REMARK 500 6 PRO B 216 45.28 -89.15
REMARK 500 7 SER A 47 97.84 -67.48
REMARK 500 7 PRO A 81 -152.44 -75.71
REMARK 500 7 SER B 203 -55.09 -173.37
REMARK 500 7 ILE B 204 77.51 51.92
REMARK 500 8 CYS A 7 100.29 64.55
REMARK 500 8 LYS A 77 -50.34 -120.65
REMARK 500 8 PRO A 81 49.29 -79.46
REMARK 500 8 GLN B 201 100.45 -160.34
REMARK 500 8 SER B 202 -63.33 -138.87
REMARK 500 8 SER B 203 132.02 -172.76
REMARK 500 8 PRO B 212 45.37 -78.06
REMARK 500 9 SER B 203 91.95 -177.48
REMARK 500 9 GLN B 215 66.32 61.75
REMARK 500 10 SER A 47 99.37 -69.78
REMARK 500 10 GLN A 82 49.43 -85.48
REMARK 500 10 SER B 202 -70.77 -65.37
REMARK 500 10 SER B 203 72.84 -150.96
REMARK 500 11 ASN A 46 41.51 -95.61
REMARK 500 11 LYS A 78 106.02 -161.79
REMARK 500 11 SER B 203 63.01 -166.22
REMARK 500 11 GLN B 215 79.48 61.21
REMARK 500 12 PRO A 81 66.68 -67.16
REMARK 500 12 LEU B 200 -49.36 -160.98
REMARK 500 12 GLN B 201 50.41 -143.11
REMARK 500 12 PRO B 216 34.86 -78.39
REMARK 500 13 CYS A 7 99.58 66.24
REMARK 500 13 GLU A 41 78.98 -116.90
REMARK 500
REMARK 500 THIS ENTRY HAS 77 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 26042 RELATED DB: BMRB
DBREF 2ND0 A 1 83 UNP O60885 BRD4_HUMAN 601 683
DBREF 2ND0 B 199 217 UNP E5LC01 E5LC01_HHV8 1086 1104
SEQRES 1 A 83 SER GLU GLU GLU ASP LYS CYS LYS PRO MET SER TYR GLU
SEQRES 2 A 83 GLU LYS ARG GLN LEU SER LEU ASP ILE ASN LYS LEU PRO
SEQRES 3 A 83 GLY GLU LYS LEU GLY ARG VAL VAL HIS ILE ILE GLN SER
SEQRES 4 A 83 ARG GLU PRO SER LEU LYS ASN SER ASN PRO ASP GLU ILE
SEQRES 5 A 83 GLU ILE ASP PHE GLU THR LEU LYS PRO SER THR LEU ARG
SEQRES 6 A 83 GLU LEU GLU ARG TYR VAL THR SER CYS LEU ARG LYS LYS
SEQRES 7 A 83 ARG LYS PRO GLN ALA
SEQRES 1 B 19 ASN LEU GLN SER SER ILE VAL LYS PHE LYS LYS PRO LEU
SEQRES 2 B 19 PRO LEU THR GLN PRO GLY
HELIX 1 1 GLU A 2 CYS A 7 1 6
HELIX 2 2 SER A 11 LEU A 25 1 15
HELIX 3 3 PRO A 26 GLU A 41 1 16
HELIX 4 4 PRO A 42 LYS A 45 5 4
HELIX 5 5 LYS A 60 ARG A 76 1 17
SHEET 1 A 2 ILE A 52 ILE A 54 0
SHEET 2 A 2 VAL B 205 PHE B 207 -1 O VAL B 205 N ILE A 54
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