Header list of 2dgr.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 15-MAR-06 2DGR
TITLE SOLUTION STRUCTURE OF THE SECOND KH DOMAIN IN RING FINGER AND KH
TITLE 2 DOMAIN CONTAINING PROTEIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RING FINGER AND KH DOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: K HOMOLOGY DOMAIN;
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: RKHD1;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050829-12;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS KH 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 2DGR 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DGR 1 VERSN
REVDAT 1 15-SEP-06 2DGR 0
JRNL AUTH C.ABE,Y.MUTO,M.INOUE,T.TERADA,T.KIGAWA,M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND KH DOMAIN IN RING FINGER
JRNL TITL 2 AND KH DOMAIN CONTAINING PROTEIN 1
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 2DGR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025399.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
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
REMARK 210 DYNAMICS,RESTRAINTED MOLECULAR
REMARK 210 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 107 -178.02 -57.51
REMARK 500 1 VAL A 119 -74.86 -39.30
REMARK 500 1 PRO A 125 91.90 -47.97
REMARK 500 1 PRO A 144 -179.78 -69.79
REMARK 500 1 PRO A 150 99.25 -69.74
REMARK 500 2 SER A 103 45.04 -102.18
REMARK 500 2 PRO A 125 93.88 -47.96
REMARK 500 2 PRO A 144 -178.27 -69.81
REMARK 500 2 ASP A 147 42.24 -105.54
REMARK 500 2 PRO A 150 82.78 -69.78
REMARK 500 2 MET A 157 158.36 -49.27
REMARK 500 2 PRO A 158 0.49 -69.74
REMARK 500 2 LEU A 174 175.33 -52.07
REMARK 500 3 TYR A 116 -35.53 -36.40
REMARK 500 3 PRO A 125 100.66 -47.93
REMARK 500 3 PRO A 150 96.78 -69.80
REMARK 500 3 MET A 157 159.41 -42.51
REMARK 500 3 PRO A 158 0.83 -69.75
REMARK 500 3 HIS A 171 -34.62 -35.38
REMARK 500 3 THR A 173 44.18 -94.83
REMARK 500 3 ARG A 175 54.42 -108.00
REMARK 500 3 SER A 176 42.66 34.41
REMARK 500 3 SER A 180 155.46 -44.40
REMARK 500 4 SER A 103 100.73 -45.35
REMARK 500 4 TYR A 116 -33.21 -35.26
REMARK 500 4 PRO A 125 97.49 -47.95
REMARK 500 4 ASP A 147 42.75 -101.70
REMARK 500 4 PRO A 150 89.12 -69.73
REMARK 500 4 PRO A 158 0.56 -69.81
REMARK 500 4 THR A 173 42.10 -93.95
REMARK 500 4 PRO A 178 2.70 -69.76
REMARK 500 4 SER A 179 119.34 -34.58
REMARK 500 5 TYR A 116 -33.40 -36.44
REMARK 500 5 PRO A 125 105.47 -47.96
REMARK 500 5 ASP A 147 43.81 -102.02
REMARK 500 5 PRO A 150 91.38 -69.80
REMARK 500 5 MET A 157 159.56 -41.68
REMARK 500 5 PRO A 158 0.81 -69.76
REMARK 500 5 HIS A 171 -38.94 -37.13
REMARK 500 6 TYR A 116 -31.16 -36.59
REMARK 500 6 VAL A 119 -70.68 -41.63
REMARK 500 6 PRO A 125 99.65 -48.04
REMARK 500 6 ASP A 147 41.74 -103.22
REMARK 500 6 MET A 157 158.31 -49.59
REMARK 500 6 THR A 173 37.05 -87.34
REMARK 500 7 TYR A 116 -35.53 -34.52
REMARK 500 7 PRO A 125 92.81 -48.01
REMARK 500 7 ASP A 147 40.95 -103.79
REMARK 500 7 PRO A 150 99.25 -69.78
REMARK 500 7 MET A 157 159.44 -43.49
REMARK 500
REMARK 500 THIS ENTRY HAS 135 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002002000.1 RELATED DB: TARGETDB
DBREF 2DGR A 106 175 UNP Q86XN8 RKHD1_HUMAN 106 177
SEQADV 2DGR GLY A 99 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR SER A 100 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR SER A 101 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR GLY A 102 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR SER A 103 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR SER A 104 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR GLY A 105 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR SER A 176 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR GLY A 177 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR PRO A 178 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR SER A 179 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR SER A 180 UNP Q86XN8 CLONING ARTIFACT
SEQADV 2DGR GLY A 181 UNP Q86XN8 CLONING ARTIFACT
SEQRES 1 A 83 GLY SER SER GLY SER SER GLY GLY GLN THR THR ILE GLN
SEQRES 2 A 83 VAL ARG VAL PRO TYR ARG VAL VAL GLY LEU VAL VAL GLY
SEQRES 3 A 83 PRO LYS GLY ALA THR ILE LYS ARG ILE GLN GLN ARG THR
SEQRES 4 A 83 HIS THR TYR ILE VAL THR PRO GLY ARG ASP LYS GLU PRO
SEQRES 5 A 83 VAL PHE ALA VAL THR GLY MET PRO GLU ASN VAL ASP ARG
SEQRES 6 A 83 ALA ARG GLU GLU ILE GLU ALA HIS ILE THR LEU ARG SER
SEQRES 7 A 83 GLY PRO SER SER GLY
HELIX 1 1 PRO A 115 GLY A 124 1 10
HELIX 2 2 THR A 129 THR A 137 1 9
HELIX 3 3 ASN A 160 LEU A 174 1 15
SHEET 1 A 3 THR A 108 ARG A 113 0
SHEET 2 A 3 VAL A 151 GLY A 156 -1 O GLY A 156 N THR A 108
SHEET 3 A 3 TYR A 140 VAL A 142 -1 N VAL A 142 O ALA A 153
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