Header list of 2dgp.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 15-MAR-06 2DGP
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL RNA BINDING DOMAIN IN BRUNO-LIKE
TITLE 2 4 RNA-BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRUNO-LIKE 4, RNA BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 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: BRUNOL4;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050704-05;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RRM DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.ABE,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DGP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DGP 1 VERSN
REVDAT 1 15-SEP-06 2DGP 0
JRNL AUTH C.ABE,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL RNA BINDING DOMAIN IN
JRNL TITL 2 BRUNO-LIKE 4 RNA-BINDING PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DGP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025397.
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 : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20MM D-TRIS-HCL(PH7.0), 100MM
REMARK 210 NACL, 1MM D-DTT, 0.02% NAN3, 90%
REMARK 210 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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.932, CYANA 2.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR 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 GLN A 60 42.89 72.22
REMARK 500 1 ARG A 63 41.97 -86.73
REMARK 500 1 LEU A 86 103.98 -49.52
REMARK 500 1 PHE A 90 -71.63 -105.89
REMARK 500 1 MET A 93 -36.96 -33.86
REMARK 500 1 LYS A 95 35.76 -83.34
REMARK 500 1 HIS A 116 137.40 -34.88
REMARK 500 1 GLU A 117 37.36 34.63
REMARK 500 1 PRO A 127 -178.44 -69.70
REMARK 500 1 ALA A 133 48.80 -79.29
REMARK 500 2 SER A 46 173.46 -56.31
REMARK 500 2 HIS A 51 -36.29 -36.17
REMARK 500 2 ARG A 63 42.35 -88.63
REMARK 500 2 LEU A 73 -70.61 -43.76
REMARK 500 2 ILE A 80 162.01 -40.20
REMARK 500 2 TYR A 81 -35.89 -131.95
REMARK 500 2 GLU A 82 114.32 -166.73
REMARK 500 2 LEU A 86 113.57 -39.03
REMARK 500 2 PHE A 90 -73.03 -120.35
REMARK 500 2 LYS A 95 151.74 -49.50
REMARK 500 2 GLN A 118 -43.45 -130.59
REMARK 500 2 PRO A 127 -177.51 -69.69
REMARK 500 2 ALA A 133 -36.18 -37.47
REMARK 500 2 SER A 135 116.45 -173.22
REMARK 500 2 ARG A 138 43.57 36.09
REMARK 500 2 SER A 144 44.66 -82.60
REMARK 500 3 LYS A 49 140.56 -34.79
REMARK 500 3 ASP A 50 -60.43 -108.02
REMARK 500 3 HIS A 51 -60.63 -98.69
REMARK 500 3 ASP A 52 148.93 -171.12
REMARK 500 3 ARG A 63 40.18 -81.58
REMARK 500 3 LEU A 73 -72.14 -42.89
REMARK 500 3 GLU A 82 114.34 -170.74
REMARK 500 3 LEU A 86 101.07 -45.05
REMARK 500 3 PHE A 90 -64.49 -106.66
REMARK 500 3 THR A 91 -33.30 -134.36
REMARK 500 3 MET A 93 -39.90 -35.23
REMARK 500 3 LYS A 95 36.50 -91.27
REMARK 500 3 PRO A 127 -176.57 -69.82
REMARK 500 3 PRO A 143 97.00 -69.74
REMARK 500 4 HIS A 51 -56.64 -121.83
REMARK 500 4 ARG A 63 43.03 -79.92
REMARK 500 4 LEU A 73 -71.82 -42.98
REMARK 500 4 GLU A 75 -30.47 -36.00
REMARK 500 4 ILE A 80 146.48 -36.19
REMARK 500 4 GLU A 82 112.86 -167.84
REMARK 500 4 MET A 93 101.64 -53.97
REMARK 500 4 LEU A 121 150.80 -41.62
REMARK 500 4 PRO A 127 -172.92 -69.74
REMARK 500 4 SER A 137 -54.09 -126.70
REMARK 500
REMARK 500 THIS ENTRY HAS 235 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002003720.1 RELATED DB: TARGETDB
DBREF 2DGP A 48 141 UNP Q9BQ96 Q9BQ96_HUMAN 48 141
SEQADV 2DGP GLY A 41 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP SER A 42 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP SER A 43 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP GLY A 44 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP SER A 45 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP SER A 46 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP GLY A 47 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP GLY A 142 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP PRO A 143 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP SER A 144 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP SER A 145 UNP Q9BQ96 CLONING ARTIFACT
SEQADV 2DGP GLY A 146 UNP Q9BQ96 CLONING ARTIFACT
SEQRES 1 A 106 GLY SER SER GLY SER SER GLY MET LYS ASP HIS ASP ALA
SEQRES 2 A 106 ILE LYS LEU PHE ILE GLY GLN ILE PRO ARG ASN LEU ASP
SEQRES 3 A 106 GLU LYS ASP LEU LYS PRO LEU PHE GLU GLU PHE GLY LYS
SEQRES 4 A 106 ILE TYR GLU LEU THR VAL LEU LYS ASP ARG PHE THR GLY
SEQRES 5 A 106 MET HIS LYS GLY CYS ALA PHE LEU THR TYR CYS GLU ARG
SEQRES 6 A 106 GLU SER ALA LEU LYS ALA GLN SER ALA LEU HIS GLU GLN
SEQRES 7 A 106 LYS THR LEU PRO GLY MET ASN ARG PRO ILE GLN VAL LYS
SEQRES 8 A 106 PRO ALA ASP SER GLU SER ARG GLY GLY SER GLY PRO SER
SEQRES 9 A 106 SER GLY
HELIX 1 1 ASP A 66 GLY A 78 1 13
HELIX 2 2 GLU A 104 HIS A 116 1 13
SHEET 1 A 4 GLU A 82 THR A 84 0
SHEET 2 A 4 CYS A 97 TYR A 102 -1 O PHE A 99 N THR A 84
SHEET 3 A 4 ILE A 54 GLY A 59 -1 N LEU A 56 O LEU A 100
SHEET 4 A 4 GLN A 129 PRO A 132 -1 O LYS A 131 N PHE A 57
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