Header list of 1wg5.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 27-MAY-04 1WG5
TITLE SOLUTION STRUCTURE OF THE FIRST RRM DOMAIN IN HETEROGENEOUS NUCLEAR
TITLE 2 RIBONUCLEOPROTEIN H
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RRM 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: CBL00922;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040223-24;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURAL GENOMICS, RRM DOMAIN, HETEROGENEOUS NUCLEAR
KEYWDS 2 RIBONUCLEOPROTEIN H, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.HE,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WG5 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WG5 1 VERSN
REVDAT 1 27-NOV-04 1WG5 0
JRNL AUTH F.HE,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST RRM DOMAIN IN HETEROGENEOUS
JRNL TITL 2 NUCLEAR RIBONUCLEOPROTEIN H
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.29
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WG5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023544.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM U-15,13C; 20MM D-TRIS
REMARK 210 -HCL(PH 7.0); 100MM NACL; 1MM D-
REMARK 210 DTT; 0.02% 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 : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.863, CYANA 2.0.29
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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
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 SER A 2 121.59 66.22
REMARK 500 1 SER A 5 -54.14 -137.21
REMARK 500 1 SER A 6 111.79 64.38
REMARK 500 1 SER A 9 143.91 61.52
REMARK 500 1 ASP A 11 96.62 52.75
REMARK 500 1 THR A 12 122.62 -179.75
REMARK 500 1 ALA A 13 174.40 58.90
REMARK 500 1 ASN A 14 101.44 69.01
REMARK 500 1 GLU A 30 -37.74 -39.94
REMARK 500 1 LYS A 76 31.42 -85.22
REMARK 500 1 HIS A 83 38.35 168.70
REMARK 500 1 VAL A 96 102.02 -45.28
REMARK 500 1 THR A 98 35.69 -157.62
REMARK 500 1 SER A 99 79.82 51.94
REMARK 500 1 SER A 102 91.75 -45.28
REMARK 500 1 SER A 103 143.51 -171.41
REMARK 500 2 SER A 5 90.87 57.22
REMARK 500 2 SER A 9 -62.56 163.26
REMARK 500 2 THR A 12 84.63 34.01
REMARK 500 2 ALA A 13 -52.47 -150.04
REMARK 500 2 GLU A 30 -36.47 -38.90
REMARK 500 2 SER A 56 138.40 -34.68
REMARK 500 2 LYS A 76 34.71 -83.96
REMARK 500 2 HIS A 83 43.88 -178.19
REMARK 500 2 ARG A 84 109.43 -165.36
REMARK 500 2 VAL A 96 112.60 -34.72
REMARK 500 2 ARG A 97 169.24 -45.91
REMARK 500 2 THR A 98 36.05 -176.07
REMARK 500 2 SER A 99 163.08 63.19
REMARK 500 2 PRO A 101 91.44 -69.76
REMARK 500 3 ASN A 8 94.68 -58.49
REMARK 500 3 ASP A 11 -178.53 -55.43
REMARK 500 3 ALA A 13 -46.56 -132.91
REMARK 500 3 SER A 56 135.29 -35.94
REMARK 500 3 LYS A 76 32.13 -85.77
REMARK 500 3 HIS A 83 43.90 -178.49
REMARK 500 3 ARG A 84 112.32 -166.08
REMARK 500 3 VAL A 96 112.64 -39.75
REMARK 500 3 ARG A 97 160.28 57.26
REMARK 500 3 THR A 98 42.38 177.55
REMARK 500 3 SER A 99 156.42 59.13
REMARK 500 3 SER A 103 134.45 -171.70
REMARK 500 4 SER A 2 -34.06 -172.92
REMARK 500 4 SER A 6 117.71 -177.78
REMARK 500 4 THR A 12 -38.32 -139.44
REMARK 500 4 ALA A 13 96.69 178.87
REMARK 500 4 LYS A 76 31.64 -85.36
REMARK 500 4 LYS A 78 10.79 59.12
REMARK 500 4 HIS A 83 42.75 170.24
REMARK 500 4 ARG A 84 107.10 -164.40
REMARK 500
REMARK 500 THIS ENTRY HAS 252 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WEZ RELATED DB: PDB
REMARK 900 RELATED ID: HSS001000551.1 RELATED DB: TARGETDB
DBREF 1WG5 A 8 98 UNP P55795 HNRH2_HUMAN 103 193
SEQADV 1WG5 GLY A 1 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 SER A 2 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 SER A 3 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 GLY A 4 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 SER A 5 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 SER A 6 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 GLY A 7 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 SER A 99 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 GLY A 100 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 PRO A 101 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 SER A 102 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 SER A 103 UNP P55795 CLONING ARTIFACT
SEQADV 1WG5 GLY A 104 UNP P55795 CLONING ARTIFACT
SEQRES 1 A 104 GLY SER SER GLY SER SER GLY ASN SER PRO ASP THR ALA
SEQRES 2 A 104 ASN ASP GLY PHE VAL ARG LEU ARG GLY LEU PRO PHE GLY
SEQRES 3 A 104 CYS SER LYS GLU GLU ILE VAL GLN PHE PHE SER GLY LEU
SEQRES 4 A 104 GLU ILE VAL PRO ASN GLY MET THR LEU PRO VAL ASP PHE
SEQRES 5 A 104 GLN GLY ARG SER THR GLY GLU ALA PHE VAL GLN PHE ALA
SEQRES 6 A 104 SER GLN GLU ILE ALA GLU LYS ALA LEU LYS LYS HIS LYS
SEQRES 7 A 104 GLU ARG ILE GLY HIS ARG TYR ILE GLU ILE PHE LYS SER
SEQRES 8 A 104 SER ARG ALA GLU VAL ARG THR SER GLY PRO SER SER GLY
HELIX 1 1 LYS A 29 PHE A 35 1 7
HELIX 2 2 GLN A 67 LEU A 74 1 8
SHEET 1 A 4 ILE A 41 THR A 47 0
SHEET 2 A 4 GLU A 59 PHE A 64 -1 O PHE A 61 N THR A 47
SHEET 3 A 4 PHE A 17 ARG A 21 -1 N LEU A 20 O ALA A 60
SHEET 4 A 4 GLU A 87 SER A 91 -1 O GLU A 87 N ARG A 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 - r 2 2 Bytes