Header list of 1wfq.pdb file
Complete list - r 25 2 Bytes
HEADER RNA BINDING PROTEIN 26-MAY-04 1WFQ
TITLE SOLUTION STRUCTURE OF THE FIRST COLD-SHOCK DOMAIN OF THE HUMAN
TITLE 2 KIAA0885 PROTEIN (UNR PROTEIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST COLD-SHOCK 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: KAZUSA CDNA HK07709;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040114-45;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS BETA-BARREL, TRANSLATIONAL REGULATION, RNA CHAPERONE, RNA/DNA
KEYWDS 2 BINDING, QB FOLD, GREEK-KEY TOPOLOGY, UNR PROTEIN, STRUCTURAL
KEYWDS 3 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA
KEYWDS 4 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.K.GORONCY,T.KIGAWA,S.KOSHIBA,T.TOMIZAWA,N.KOBAYASHI,N.TOCHIO,
AUTHOR 2 M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 3 (RSGI)
REVDAT 3 01-SEP-10 1WFQ 1 JRNL
REVDAT 2 24-FEB-09 1WFQ 1 VERSN
REVDAT 1 26-NOV-04 1WFQ 0
JRNL AUTH A.K.GORONCY,S.KOSHIBA,N.TOCHIO,T.TOMIZAWA,M.INOUE,
JRNL AUTH 2 S.WATANABE,T.HARADA,A.TANAKA,O.OHARA,T.KIGAWA,S.YOKOYAMA
JRNL TITL THE NMR SOLUTION STRUCTURES OF THE FIVE CONSTITUENT
JRNL TITL 2 COLD-SHOCK DOMAINS (CSD) OF THE HUMAN UNR (UPSTREAM OF
JRNL TITL 3 N-RAS) PROTEIN.
JRNL REF J.STRUCT.FUNCT.GENOM. V. 11 181 2010
JRNL REFN ISSN 1345-711X
JRNL PMID 20213426
JRNL DOI 10.1007/S10969-010-9081-Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUENTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WFQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-04.
REMARK 100 THE RCSB ID CODE IS RCSB023529.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.09MM COLD-SHOCK DOMAIN U-15N,
REMARK 210 13C; 20MM PHOSPHATE BUFFER NA;
REMARK 210 100MM NACL; 0.02% NAN3; 90% H2O,
REMARK 210 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 : XWINNMR 2.6, NMRPIPE 20031121,
REMARK 210 NMRVIEW 5.0.14, KUJIRA 0.899
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
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 TYR A 9 156.82 -38.34
REMARK 500 1 LEU A 53 -36.33 -36.87
REMARK 500 1 ASP A 69 174.70 -58.06
REMARK 500 1 PRO A 86 3.59 -69.75
REMARK 500 1 SER A 88 175.18 -56.77
REMARK 500 2 SER A 3 100.88 -58.93
REMARK 500 2 SER A 14 172.68 -50.37
REMARK 500 2 ALA A 15 -179.11 -66.27
REMARK 500 2 LEU A 17 144.91 -171.39
REMARK 500 2 ILE A 23 92.68 -68.80
REMARK 500 2 PRO A 75 95.46 -69.71
REMARK 500 3 LEU A 17 110.60 -173.10
REMARK 500 3 LEU A 53 -35.40 -35.06
REMARK 500 3 PRO A 75 97.48 -69.72
REMARK 500 3 VAL A 81 117.79 -160.99
REMARK 500 3 SER A 84 171.44 -57.28
REMARK 500 4 SER A 5 41.49 -83.26
REMARK 500 4 ILE A 23 91.63 -64.39
REMARK 500 4 PRO A 75 99.87 -69.78
REMARK 500 4 VAL A 81 119.76 -163.40
REMARK 500 5 TYR A 9 149.17 -170.05
REMARK 500 6 THR A 13 139.81 -35.44
REMARK 500 6 ALA A 15 167.14 -44.54
REMARK 500 6 ILE A 23 92.74 -56.12
REMARK 500 6 SER A 88 87.21 -58.92
REMARK 500 7 SER A 2 29.02 47.88
REMARK 500 7 PRO A 10 -176.34 -69.77
REMARK 500 7 ILE A 23 94.32 -61.20
REMARK 500 7 ASP A 69 171.66 -58.07
REMARK 500 8 SER A 2 89.20 -69.78
REMARK 500 8 SER A 14 41.96 -89.63
REMARK 500 8 ASP A 69 170.53 -48.54
REMARK 500 9 SER A 3 109.05 -44.37
REMARK 500 9 ASN A 11 131.36 -34.45
REMARK 500 9 ILE A 23 95.06 -62.69
REMARK 500 9 CYS A 35 132.64 -37.82
REMARK 500 9 ASP A 69 175.50 -48.10
REMARK 500 10 ASN A 11 98.38 -57.69
REMARK 500 10 SER A 14 104.94 -37.20
REMARK 500 10 LEU A 53 -39.17 -39.19
REMARK 500 10 ASP A 69 178.79 -55.46
REMARK 500 11 SER A 5 41.57 -98.70
REMARK 500 11 ARG A 71 -60.68 -100.13
REMARK 500 11 PRO A 75 98.19 -69.83
REMARK 500 11 SER A 88 -63.02 -95.39
REMARK 500 12 SER A 5 82.51 -63.99
REMARK 500 12 ILE A 23 95.75 -62.17
REMARK 500 12 VAL A 81 118.81 -164.65
REMARK 500 12 SER A 87 114.58 -36.23
REMARK 500 13 SER A 5 42.01 -93.94
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000864.2 RELATED DB: TARGETDB
DBREF 1WFQ A 8 83 UNP O75534 CSDE1_HUMAN 15 90
SEQADV 1WFQ GLY A 1 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ SER A 2 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ SER A 3 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ GLY A 4 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ SER A 5 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ SER A 6 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ GLY A 7 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ SER A 84 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ GLY A 85 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ PRO A 86 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ SER A 87 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ SER A 88 UNP O75534 CLONING ARTIFACT
SEQADV 1WFQ GLY A 89 UNP O75534 CLONING ARTIFACT
SEQRES 1 A 89 GLY SER SER GLY SER SER GLY GLY TYR PRO ASN GLY THR
SEQRES 2 A 89 SER ALA ALA LEU ARG GLU THR GLY VAL ILE GLU LYS LEU
SEQRES 3 A 89 LEU THR SER TYR GLY PHE ILE GLN CYS SER GLU ARG GLN
SEQRES 4 A 89 ALA ARG LEU PHE PHE HIS CYS SER GLN TYR ASN GLY ASN
SEQRES 5 A 89 LEU GLN ASP LEU LYS VAL GLY ASP ASP VAL GLU PHE GLU
SEQRES 6 A 89 VAL SER SER ASP ARG ARG THR GLY LYS PRO ILE ALA VAL
SEQRES 7 A 89 LYS LEU VAL LYS ILE SER GLY PRO SER SER GLY
SHEET 1 A 6 ARG A 18 LEU A 26 0
SHEET 2 A 6 TYR A 30 CYS A 35 -1 O GLN A 34 N VAL A 22
SHEET 3 A 6 ALA A 40 HIS A 45 -1 O LEU A 42 N ILE A 33
SHEET 4 A 6 PRO A 75 LYS A 82 1 O ALA A 77 N PHE A 43
SHEET 5 A 6 VAL A 62 SER A 68 -1 N GLU A 63 O VAL A 81
SHEET 6 A 6 ARG A 18 LEU A 26 -1 N GLU A 19 O PHE A 64
CISPEP 1 TYR A 9 PRO A 10 1 -0.07
CISPEP 2 TYR A 9 PRO A 10 2 -0.11
CISPEP 3 TYR A 9 PRO A 10 3 -0.04
CISPEP 4 TYR A 9 PRO A 10 4 -0.15
CISPEP 5 TYR A 9 PRO A 10 5 0.03
CISPEP 6 TYR A 9 PRO A 10 6 -0.05
CISPEP 7 TYR A 9 PRO A 10 7 -0.06
CISPEP 8 TYR A 9 PRO A 10 8 -0.12
CISPEP 9 TYR A 9 PRO A 10 9 -0.09
CISPEP 10 TYR A 9 PRO A 10 10 -0.03
CISPEP 11 TYR A 9 PRO A 10 11 0.02
CISPEP 12 TYR A 9 PRO A 10 12 -0.07
CISPEP 13 TYR A 9 PRO A 10 13 -0.07
CISPEP 14 TYR A 9 PRO A 10 14 -0.01
CISPEP 15 TYR A 9 PRO A 10 15 -0.07
CISPEP 16 TYR A 9 PRO A 10 16 -0.07
CISPEP 17 TYR A 9 PRO A 10 17 -0.08
CISPEP 18 TYR A 9 PRO A 10 18 -0.17
CISPEP 19 TYR A 9 PRO A 10 19 -0.07
CISPEP 20 TYR A 9 PRO A 10 20 -0.10
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 25 2 Bytes