HEADER TRANSCRIPTION/TRANSFERASE 18-APR-16 2NCZ
TITLE SOLUTION NMR STRUCTURES OF BRD4 ET DOMAIN IN COMPLEX WITH NSD3_1
TITLE 2 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: HISTONE-LYSINE N-METHYLTRANSFERASE NSD3;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 152-163;
COMPND 11 SYNONYM: NUCLEAR SET DOMAIN-CONTAINING PROTEIN 3, PROTEIN WHISTLE,
COMPND 12 WHSC1-LIKE 1 ISOFORM 9 WITH METHYLTRANSFERASE ACTIVITY TO LYSINE,
COMPND 13 WOLF-HIRSCHHORN SYNDROME CANDIDATE 1-LIKE PROTEIN 1, WHSC1-LIKE
COMPND 14 PROTEIN 1;
COMPND 15 EC: 2.1.1.43;
COMPND 16 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: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS TRANSCRIPTION, TRANSFERASE, TRANSCRIPTION-TRANSFERASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.ZENG,M.ZHOU
REVDAT 2 20-JUL-16 2NCZ 1 JRNL
REVDAT 1 29-JUN-16 2NCZ 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 2NCZ 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 RCSB104709.
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-13C NOESY ALIPHATIC; 3D 1H-13C
REMARK 210 NOESY AROMATIC; 3D FILTERED 1H-
REMARK 210 13C NOESY ALIPHATIC; 3D FILTERED
REMARK 210 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 2.3, NMRVIEW 5.04, CNS
REMARK 210 1.2, TOPSPIN 2.1, PROCHECKNMR
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
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 O ILE B 206 HZ2 LYS B 208 1.58
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 GLU A 41 77.99 -111.69
REMARK 500 1 ARG A 76 28.06 -76.41
REMARK 500 1 THR B 209 17.28 59.23
REMARK 500 2 LYS A 78 -89.77 -89.24
REMARK 500 2 ARG A 79 80.72 51.51
REMARK 500 2 LYS B 208 -158.67 -177.10
REMARK 500 3 PRO A 42 1.37 -68.79
REMARK 500 3 PRO A 81 74.81 -66.84
REMARK 500 3 LEU B 204 98.70 -166.24
REMARK 500 3 LYS B 208 -151.08 -176.69
REMARK 500 4 LYS A 78 78.75 -111.32
REMARK 500 4 LYS B 208 -152.99 -160.31
REMARK 500 5 LYS A 78 -87.57 -118.21
REMARK 500 5 ARG A 79 89.38 52.96
REMARK 500 5 LYS A 80 73.86 -161.61
REMARK 500 5 LYS B 208 -159.65 -178.57
REMARK 500 6 LYS A 77 -159.44 -136.59
REMARK 500 6 LYS A 80 80.47 179.17
REMARK 500 6 LYS B 208 -156.02 -172.04
REMARK 500 7 GLU A 2 -61.73 -100.00
REMARK 500 7 LYS A 78 70.29 57.61
REMARK 500 7 LYS B 208 -165.61 -164.24
REMARK 500 7 THR B 209 118.87 65.41
REMARK 500 8 LYS A 77 -85.29 63.37
REMARK 500 8 LYS A 78 -91.25 37.21
REMARK 500 8 ILE B 202 78.95 61.11
REMARK 500 8 LYS B 208 -163.59 -178.10
REMARK 500 9 LYS A 80 57.56 -160.24
REMARK 500 9 LYS B 208 -155.55 -175.36
REMARK 500 9 THR B 209 113.10 68.34
REMARK 500 9 ILE B 210 85.38 61.13
REMARK 500 10 LYS B 208 -159.54 -169.51
REMARK 500 10 ILE B 210 98.43 -60.04
REMARK 500 11 LYS A 78 87.62 64.79
REMARK 500 11 GLN A 82 -86.99 -130.77
REMARK 500 11 LYS B 208 178.78 179.52
REMARK 500 11 THR B 209 65.88 39.91
REMARK 500 11 GLN B 211 -54.43 -128.13
REMARK 500 12 ARG A 79 112.12 67.36
REMARK 500 12 LYS A 80 67.21 -115.55
REMARK 500 12 PRO A 81 96.22 -55.03
REMARK 500 12 LYS B 208 -158.38 -172.31
REMARK 500 12 THR B 209 160.93 64.04
REMARK 500 13 ARG A 76 30.26 -91.37
REMARK 500 13 ARG A 79 87.05 42.48
REMARK 500 13 LYS B 208 -165.75 -173.03
REMARK 500 13 THR B 209 -10.50 65.07
REMARK 500 14 LYS A 77 103.54 -162.65
REMARK 500 14 LYS A 80 76.39 -150.42
REMARK 500 14 LYS B 208 -166.27 -167.25
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 26041 RELATED DB: BMRB
REMARK 900 RELATED ID: 2ND0 RELATED DB: PDB
REMARK 900 RELATED ID: 2ND1 RELATED DB: PDB
DBREF 2NCZ A 1 83 UNP O60885 BRD4_HUMAN 601 683
DBREF 2NCZ B 201 212 UNP Q9BZ95 NSD3_HUMAN 152 163
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 12 GLU ILE LYS LEU LYS ILE THR LYS THR ILE GLN ASN
HELIX 1 1 SER A 1 LYS A 6 1 6
HELIX 2 2 SER A 11 ASN A 23 1 13
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 GLU A 51 ASP A 55 0
SHEET 2 A 2 LYS B 203 THR B 207 -1 O LEU B 204 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