Header list of 2d9e.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 09-DEC-05 2D9E
TITLE SOLUTION STRUCTURE OF THE BROMODOMAIN OF PEREGRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEREGRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BROMODOMAIN;
COMPND 5 SYNONYM: BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 1, BR140
COMPND 6 PROTEIN;
COMPND 7 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: BRPF1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050314-10;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS FOUR-HELIX BUNDLE, TRANSCRIPTION ACTIVATOR, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.HATTA,F.HAYASHI,K.IZUMI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D9E 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D9E 1 VERSN
REVDAT 1 09-JUN-06 2D9E 0
JRNL AUTH R.HATTA,F.HAYASHI,K.IZUMI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE BROMODOMAIN OF PEREGRIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D9E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025149.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 294.5
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.26 MM 13C, 15N-LABELED
REMARK 210 PROTEIN; 20MM D-TRIS-HCL (PH7.0);
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 90% H2O; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.932, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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: 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 ILE A 75 -38.40 -36.23
REMARK 500 1 THR A 87 174.71 -57.70
REMARK 500 1 PHE A 89 -25.62 -38.90
REMARK 500 1 SER A 116 88.19 -62.14
REMARK 500 2 SER A 3 44.59 -80.06
REMARK 500 2 SER A 5 35.45 -86.49
REMARK 500 2 PHE A 89 -25.75 -38.84
REMARK 500 3 SER A 5 89.72 -55.16
REMARK 500 3 ASP A 42 -36.33 -38.13
REMARK 500 3 PRO A 47 93.76 -69.82
REMARK 500 3 ILE A 75 -27.93 -38.93
REMARK 500 3 PHE A 89 -25.68 -39.03
REMARK 500 3 SER A 120 -55.80 -126.31
REMARK 500 4 SER A 5 53.58 -100.31
REMARK 500 4 ASP A 42 -30.47 -37.08
REMARK 500 4 PHE A 89 -26.65 -37.92
REMARK 500 4 SER A 116 114.58 -173.68
REMARK 500 5 SER A 29 -18.73 -49.32
REMARK 500 5 ASN A 78 -31.16 -36.18
REMARK 500 5 THR A 87 170.87 -49.07
REMARK 500 5 PHE A 89 -26.33 -38.16
REMARK 500 5 MET A 114 -38.74 -39.37
REMARK 500 6 PRO A 47 97.80 -69.79
REMARK 500 6 SER A 77 -70.83 -56.08
REMARK 500 6 ASN A 78 -28.58 -37.33
REMARK 500 6 PHE A 89 -26.11 -38.46
REMARK 500 6 PRO A 118 95.45 -69.65
REMARK 500 7 SER A 77 -70.30 -55.07
REMARK 500 7 LYS A 85 -30.34 -39.85
REMARK 500 7 PHE A 89 -26.03 -38.60
REMARK 500 8 ASP A 42 -39.82 -34.41
REMARK 500 8 SER A 77 -70.43 -62.31
REMARK 500 8 ASN A 78 -32.98 -36.18
REMARK 500 8 LYS A 85 -37.91 -37.48
REMARK 500 8 PHE A 89 -26.21 -38.53
REMARK 500 8 SER A 116 110.53 -173.21
REMARK 500 8 PRO A 118 95.65 -69.71
REMARK 500 9 SER A 5 43.23 -82.87
REMARK 500 9 ASP A 66 -36.49 -38.67
REMARK 500 9 ASN A 78 -35.69 -38.11
REMARK 500 9 ASP A 86 45.84 -102.99
REMARK 500 9 PHE A 89 -26.19 -38.29
REMARK 500 10 SER A 5 43.91 -99.90
REMARK 500 10 ILE A 75 -35.23 -36.12
REMARK 500 10 ASN A 78 -32.91 -37.60
REMARK 500 10 LYS A 85 -35.16 -35.87
REMARK 500 10 PHE A 89 -26.63 -37.92
REMARK 500 10 ALA A 111 -17.99 -49.81
REMARK 500 11 SER A 3 -57.05 -126.52
REMARK 500 11 SER A 5 82.30 -66.32
REMARK 500
REMARK 500 THIS ENTRY HAS 99 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK003000027.1 RELATED DB: TARGETDB
DBREF 2D9E A 8 115 GB 19584408 CAD28495 633 740
SEQADV 2D9E GLY A 1 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E SER A 2 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E SER A 3 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E GLY A 4 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E SER A 5 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E SER A 6 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E GLY A 7 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E SER A 116 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E GLY A 117 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E PRO A 118 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E SER A 119 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E SER A 120 GB 19584408 CLONING ARTIFACT
SEQADV 2D9E GLY A 121 GB 19584408 CLONING ARTIFACT
SEQRES 1 A 121 GLY SER SER GLY SER SER GLY PHE LEU ILE LEU LEU ARG
SEQRES 2 A 121 LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY ASN
SEQRES 3 A 121 ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO ASP
SEQRES 4 A 121 TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE THR
SEQRES 5 A 121 MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN PHE
SEQRES 6 A 121 ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER ASN
SEQRES 7 A 121 CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR ARG
SEQRES 8 A 121 ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL LEU
SEQRES 9 A 121 ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY SER GLY
SEQRES 10 A 121 PRO SER SER GLY
HELIX 1 1 SER A 6 ASP A 23 1 18
HELIX 2 2 ASP A 39 ILE A 44 1 6
HELIX 3 3 ASP A 49 ALA A 59 1 11
HELIX 4 4 ASN A 64 ASN A 83 1 20
HELIX 5 5 THR A 87 MET A 114 1 28
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 - r 9 2 Bytes