Header list of 1f68.pdb file
Complete list - v 3 2 Bytes
HEADER TRANSFERASE 20-JUN-00 1F68
TITLE NMR SOLUTION STRUCTURE OF THE BROMODOMAIN FROM HUMAN GCN5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BROMODOMAIN;
COMPND 5 SYNONYM: GCN5;
COMPND 6 EC: 2.3.1.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS LEFT-HANDED FOUR-HELIX BUNDLE, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR P.E.WRIGHT,B.P.HUDSON,H.J.DYSON
REVDAT 3 03-NOV-21 1F68 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1F68 1 VERSN
REVDAT 1 13-DEC-00 1F68 0
JRNL AUTH B.P.HUDSON,M.A.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
JRNL TITL SOLUTION STRUCTURE AND ACETYL-LYSINE BINDING ACTIVITY OF THE
JRNL TITL 2 GCN5 BROMODOMAIN.
JRNL REF J.MOL.BIOL. V. 304 355 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11090279
JRNL DOI 10.1006/JMBI.2000.4207
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, DYANA 1.5, SANE 1.0
REMARK 3 AUTHORS : BRUKER INSTRUMENTS (XWINNMR), GUNTERT (DYANA),
REMARK 3 DUGGAN (SANE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED UPON 2232 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINTS (365 LONG-RANGE, 379 MEDIUM-RANGE,
REMARK 3 403 SEQUENTIAL, 1085 INTRARESIDUE, AND 426 AMBIGUOUS), 155
REMARK 3 TORSION ANGLE RESTRAINTS, AND 47 STEREOSPECIFIC ASSIGNMENTS.
REMARK 4
REMARK 4 1F68 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011293.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 293; 293
REMARK 210 PH : 6.0; 6.0; 6.0
REMARK 210 IONIC STRENGTH : 50MM NACL; 50MM NACL; 50MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4MM BROMODOMAIN, U-15N; 20MM
REMARK 210 SODIUM PHOSPHATE BUFFER; 50MM
REMARK 210 NACL; 10MM DTT-D10; 0.4MM
REMARK 210 BROMODOMAIN, U-15N,13C; 20MM
REMARK 210 SODIUM PHOSPHATE BUFFER; 50MM
REMARK 210 NACL; 10MM DTT-D10; 0.4MM
REMARK 210 BROMODOMAIN, U-15N,13C; 20MM
REMARK 210 SODIUM PHOSPHATE BUFFER; 50MM
REMARK 210 NACL; 10MM DTT-D10
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY; HNHA; HNHB;
REMARK 210 HACAHB_COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, NMRVIEW 3.0, AMBER
REMARK 210 6.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS (DYANA)
REMARK 210 FOR GENERATION OF INITIAL
REMARK 210 STRUCTURES; STRUCTURE-MEDIATED
REMARK 210 ASSIGNMENT OF AMBIGUOUS
REMARK 210 EXPERIMENTAL RESTRAINTS (SANE);
REMARK 210 ITERATION BETWEEN DYANA AND SANE;
REMARK 210 SIMULATED ANNEALING AND ENERGY
REMARK 210 MINIMIZATION IN AMBER USING FULL
REMARK 210 RESTRAINT SET.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 185
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO DISTANCE OR ANGLE VIOLATIONS
REMARK 210 GREATER THAN 0.15 A OR 5 DEGREES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
REMARK 210
REMARK 210 REMARK: BACKBONE ASSIGNMENTS FROM HNCACB & CBCA(CO)NH (SAMPLE 2);
REMARK 210 SIDECHAIN ASSIGNMENTS FROM C(CO)NH-TOCSY & H(CCO)NH-TOCSY
REMARK 210 (SAMPLE 2); STEREOSPECIFIC ASSIGNMENTS FROM 13C-{13CO} & 13C-{
REMARK 210 15N} SPIN-ECHO DIFFERENCE CT-HSQC (SAMPLE 3); AROMATIC
REMARK 210 ASSIGNMENTS FROM (HB)CB(CGCD)HD, (HB)CB(CGCDCE)HE, & (HC)C(C)CH-
REMARK 210 TOCSY (SAMPLE 3)
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 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 MET A 754 -70.65 -61.23
REMARK 500 1 ARG A 770 39.70 -74.21
REMARK 500 1 PHE A 771 53.07 -146.44
REMARK 500 1 ASP A 774 167.35 177.34
REMARK 500 2 GLU A 761 -62.03 -94.69
REMARK 500 2 ALA A 762 81.08 -160.31
REMARK 500 2 ARG A 770 36.94 -74.44
REMARK 500 2 PHE A 771 51.79 -146.49
REMARK 500 3 PHE A 771 73.88 -110.18
REMARK 500 3 ASP A 811 41.38 -106.18
REMARK 500 4 ASP A 731 -54.31 69.27
REMARK 500 4 SER A 749 -34.16 -36.14
REMARK 500 4 ALA A 762 88.20 -155.58
REMARK 500 4 PHE A 771 77.08 -112.87
REMARK 500 4 GLU A 831 69.12 -68.41
REMARK 500 5 ALA A 762 89.96 -154.71
REMARK 500 5 PHE A 771 74.93 -115.19
REMARK 500 5 GLU A 831 -59.09 71.05
REMARK 500 6 SER A 749 -30.24 -38.77
REMARK 500 6 MET A 754 -74.89 -65.83
REMARK 500 6 ARG A 770 43.71 -77.56
REMARK 500 6 PHE A 771 49.27 -147.63
REMARK 500 7 ASP A 731 -76.63 61.32
REMARK 500 7 ARG A 770 38.89 -73.67
REMARK 500 7 PHE A 771 54.49 -147.24
REMARK 500 7 ILE A 773 146.03 -170.95
REMARK 500 9 SER A 749 -32.55 -39.49
REMARK 500 9 ALA A 762 87.71 -159.56
REMARK 500 9 PHE A 771 76.76 -107.44
REMARK 500 10 MET A 754 -71.60 -66.93
REMARK 500 10 PHE A 771 74.60 -112.01
REMARK 500 11 PHE A 771 70.59 -117.61
REMARK 500 11 ASP A 811 -0.33 70.97
REMARK 500 12 ALA A 762 87.07 -150.64
REMARK 500 12 PHE A 771 74.10 -119.75
REMARK 500 12 GLU A 831 -58.15 67.78
REMARK 500 13 PHE A 771 74.63 -115.29
REMARK 500 14 VAL A 757 105.36 -42.31
REMARK 500 15 SER A 749 -18.59 -49.12
REMARK 500 15 GLU A 761 -62.33 -95.23
REMARK 500 15 ALA A 762 86.11 -160.63
REMARK 500 15 PHE A 771 75.35 -114.00
REMARK 500 16 ALA A 762 88.05 -155.88
REMARK 500 16 GLU A 831 -54.84 67.67
REMARK 500 18 ALA A 762 88.20 -158.91
REMARK 500 18 PHE A 771 74.95 -113.66
REMARK 500 19 HIS A 747 107.65 -52.01
REMARK 500 19 PHE A 771 77.60 -108.35
REMARK 500 19 PRO A 772 98.33 -68.05
REMARK 500 21 ASP A 731 -78.44 56.09
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 781 0.09 SIDE CHAIN
REMARK 500 1 TYR A 786 0.13 SIDE CHAIN
REMARK 500 1 TYR A 787 0.10 SIDE CHAIN
REMARK 500 2 TYR A 786 0.11 SIDE CHAIN
REMARK 500 2 TYR A 787 0.12 SIDE CHAIN
REMARK 500 3 TYR A 786 0.11 SIDE CHAIN
REMARK 500 3 TYR A 787 0.09 SIDE CHAIN
REMARK 500 4 TYR A 766 0.07 SIDE CHAIN
REMARK 500 4 TYR A 787 0.09 SIDE CHAIN
REMARK 500 5 TYR A 766 0.09 SIDE CHAIN
REMARK 500 5 TYR A 786 0.11 SIDE CHAIN
REMARK 500 5 TYR A 814 0.12 SIDE CHAIN
REMARK 500 6 TYR A 734 0.13 SIDE CHAIN
REMARK 500 8 TYR A 787 0.09 SIDE CHAIN
REMARK 500 8 TYR A 807 0.09 SIDE CHAIN
REMARK 500 8 TYR A 814 0.17 SIDE CHAIN
REMARK 500 9 TYR A 766 0.07 SIDE CHAIN
REMARK 500 9 TYR A 787 0.10 SIDE CHAIN
REMARK 500 9 TYR A 807 0.07 SIDE CHAIN
REMARK 500 9 TYR A 826 0.07 SIDE CHAIN
REMARK 500 10 TYR A 766 0.10 SIDE CHAIN
REMARK 500 10 TYR A 786 0.09 SIDE CHAIN
REMARK 500 10 TYR A 787 0.10 SIDE CHAIN
REMARK 500 10 TYR A 826 0.08 SIDE CHAIN
REMARK 500 11 TYR A 766 0.07 SIDE CHAIN
REMARK 500 12 TYR A 766 0.07 SIDE CHAIN
REMARK 500 12 TYR A 786 0.10 SIDE CHAIN
REMARK 500 12 ARG A 805 0.11 SIDE CHAIN
REMARK 500 12 TYR A 807 0.07 SIDE CHAIN
REMARK 500 12 TYR A 814 0.11 SIDE CHAIN
REMARK 500 13 TYR A 766 0.11 SIDE CHAIN
REMARK 500 13 TYR A 787 0.07 SIDE CHAIN
REMARK 500 14 PHE A 753 0.10 SIDE CHAIN
REMARK 500 14 TYR A 786 0.07 SIDE CHAIN
REMARK 500 14 TYR A 787 0.12 SIDE CHAIN
REMARK 500 15 TYR A 766 0.07 SIDE CHAIN
REMARK 500 15 TYR A 814 0.09 SIDE CHAIN
REMARK 500 16 TYR A 766 0.08 SIDE CHAIN
REMARK 500 17 TYR A 766 0.12 SIDE CHAIN
REMARK 500 17 TYR A 787 0.08 SIDE CHAIN
REMARK 500 18 TYR A 734 0.13 SIDE CHAIN
REMARK 500 18 TYR A 766 0.10 SIDE CHAIN
REMARK 500 18 ARG A 799 0.08 SIDE CHAIN
REMARK 500 18 TYR A 814 0.10 SIDE CHAIN
REMARK 500 19 PHE A 753 0.09 SIDE CHAIN
REMARK 500 19 TYR A 766 0.07 SIDE CHAIN
REMARK 500 19 ARG A 770 0.08 SIDE CHAIN
REMARK 500 19 TYR A 787 0.07 SIDE CHAIN
REMARK 500 20 ARG A 781 0.12 SIDE CHAIN
REMARK 500 21 TYR A 766 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 80 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1F68 A 730 832 UNP Q92830 GCNL2_HUMAN 730 832
SEQADV 1F68 GLY A 730 UNP Q92830 PRO 730 ENGINEERED MUTATION
SEQRES 1 A 103 GLY ASP GLN LEU TYR THR THR LEU LYS ASN LEU LEU ALA
SEQRES 2 A 103 GLN ILE LYS SER HIS PRO SER ALA TRP PRO PHE MET GLU
SEQRES 3 A 103 PRO VAL LYS LYS SER GLU ALA PRO ASP TYR TYR GLU VAL
SEQRES 4 A 103 ILE ARG PHE PRO ILE ASP LEU LYS THR MET THR GLU ARG
SEQRES 5 A 103 LEU ARG SER ARG TYR TYR VAL THR ARG LYS LEU PHE VAL
SEQRES 6 A 103 ALA ASP LEU GLN ARG VAL ILE ALA ASN CYS ARG GLU TYR
SEQRES 7 A 103 ASN PRO PRO ASP SER GLU TYR CYS ARG CYS ALA SER ALA
SEQRES 8 A 103 LEU GLU LYS PHE PHE TYR PHE LYS LEU LYS GLU GLY
HELIX 1 1 ASP A 731 HIS A 747 1 17
HELIX 2 2 PRO A 748 MET A 754 5 7
HELIX 3 3 PRO A 763 ILE A 769 1 7
HELIX 4 4 ASP A 774 SER A 784 1 11
HELIX 5 5 THR A 789 ASN A 808 1 20
HELIX 6 6 SER A 812 GLY A 832 1 21
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
Complete list - v 3 2 Bytes