Header list of 2fc8.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 12-DEC-05 2FC8
TITLE SOLUTION STRUCTURE OF THE RRM_1 DOMAIN OF NCL PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NCL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RRM_1 DOMAIN, RESIDUES 8-96;
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 EXPRESSION_SYSTEM: CELL-FREE SYNTHESIS;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050516-05
KEYWDS STRUCTURE GENOMICS, RRM_1 DOMAIN, NCL PROTEIN, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA
KEYWDS 4 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.DANG,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2FC8 1 REMARK SEQADV
REVDAT 2 24-JUN-08 2FC8 1 SOURCE REMARK DBREF SEQADV
REVDAT 2 2 1 VERSN
REVDAT 1 12-JUN-06 2FC8 0
JRNL AUTH W.DANG,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RRM_1 DOMAIN OF NCL PROTEIN
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 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FC8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035706.
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 : 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 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9321, 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 : 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 2 103.67 -41.51
REMARK 500 1 ASN A 9 33.65 72.68
REMARK 500 1 THR A 27 115.32 -38.83
REMARK 500 1 SER A 35 -37.06 -35.78
REMARK 500 1 ASP A 37 97.92 -69.20
REMARK 500 1 SER A 39 165.58 -49.44
REMARK 500 1 ALA A 89 91.01 -57.71
REMARK 500 1 PRO A 91 -171.41 -69.73
REMARK 500 1 LYS A 92 -55.65 -134.86
REMARK 500 2 PRO A 14 -172.98 -69.75
REMARK 500 2 THR A 27 114.95 -34.86
REMARK 500 2 SER A 35 -30.98 -38.51
REMARK 500 2 ASP A 37 83.39 -69.37
REMARK 500 2 SER A 39 161.04 -47.57
REMARK 500 2 SER A 53 103.90 -58.56
REMARK 500 2 ALA A 89 144.48 -34.30
REMARK 500 3 PRO A 14 -168.74 -69.77
REMARK 500 3 THR A 27 110.76 -39.92
REMARK 500 3 SER A 35 -31.92 -35.27
REMARK 500 3 SER A 39 164.32 -42.95
REMARK 500 3 SER A 53 108.01 -53.56
REMARK 500 3 TRP A 88 102.39 -57.56
REMARK 500 3 ALA A 89 105.34 -33.92
REMARK 500 3 PRO A 99 97.26 -69.74
REMARK 500 4 SER A 6 77.15 -100.23
REMARK 500 4 PRO A 14 -165.99 -69.76
REMARK 500 4 THR A 27 120.17 -35.60
REMARK 500 4 SER A 35 -34.80 -38.47
REMARK 500 4 ASP A 37 90.56 -65.42
REMARK 500 4 SER A 39 162.57 -46.29
REMARK 500 4 ALA A 89 97.87 -55.21
REMARK 500 4 LYS A 92 104.81 -44.44
REMARK 500 4 GLU A 94 40.04 -108.78
REMARK 500 4 SER A 100 157.26 -45.89
REMARK 500 5 PRO A 8 2.89 -69.82
REMARK 500 5 ARG A 11 50.70 35.07
REMARK 500 5 THR A 27 116.24 -38.88
REMARK 500 5 SER A 35 -36.05 -37.60
REMARK 500 5 ASP A 37 99.28 -67.23
REMARK 500 5 SER A 39 167.04 -44.04
REMARK 500 5 ALA A 89 162.48 -41.15
REMARK 500 5 PRO A 91 99.40 -69.76
REMARK 500 5 PRO A 99 -179.22 -69.77
REMARK 500 6 ALA A 10 39.22 -89.86
REMARK 500 6 SER A 12 165.82 -43.63
REMARK 500 6 GLN A 13 142.30 -37.28
REMARK 500 6 PRO A 14 -166.07 -69.82
REMARK 500 6 SER A 39 159.43 -41.70
REMARK 500 6 SER A 53 107.49 -56.24
REMARK 500 7 ASN A 9 38.55 -83.84
REMARK 500
REMARK 500 THIS ENTRY HAS 152 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FC9 RELATED DB: PDB
REMARK 900 THE DIFFERENT FRAGMENT OF THE SAME PROTEIN
REMARK 900 RELATED ID: HSI002005757.2 RELATED DB: TARGETDB
DBREF 2FC8 A 8 96 UNP Q9BQ02 Q9BQ02_HUMAN 336 424
SEQADV 2FC8 GLY A 1 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 SER A 2 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 SER A 3 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 GLY A 4 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 SER A 5 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 SER A 6 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 GLY A 7 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 SER A 97 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 GLY A 98 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 PRO A 99 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 SER A 100 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 SER A 101 UNP Q9BQ02 EXPRESSION TAG
SEQADV 2FC8 GLY A 102 UNP Q9BQ02 EXPRESSION TAG
SEQRES 1 A 102 GLY SER SER GLY SER SER GLY PRO ASN ALA ARG SER GLN
SEQRES 2 A 102 PRO SER LYS THR LEU PHE VAL LYS GLY LEU SER GLU ASP
SEQRES 3 A 102 THR THR GLU GLU THR LEU LYS GLU SER PHE ASP GLY SER
SEQRES 4 A 102 VAL ARG ALA ARG ILE VAL THR ASP ARG GLU THR GLY SER
SEQRES 5 A 102 SER LYS GLY PHE GLY PHE VAL ASP PHE ASN SER GLU GLU
SEQRES 6 A 102 ASP ALA LYS ALA ALA LYS GLU ALA MET GLU ASP GLY GLU
SEQRES 7 A 102 ILE ASP GLY ASN LYS VAL THR LEU ASP TRP ALA LYS PRO
SEQRES 8 A 102 LYS GLY GLU GLY GLY SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 29 SER A 35 1 7
HELIX 2 2 GLU A 64 MET A 74 1 11
SHEET 1 A 4 ARG A 41 VAL A 45 0
SHEET 2 A 4 PHE A 56 ASP A 60 -1 O PHE A 58 N ARG A 43
SHEET 3 A 4 LEU A 18 LYS A 21 -1 N VAL A 20 O GLY A 57
SHEET 4 A 4 THR A 85 TRP A 88 -1 O ASP A 87 N PHE A 19
SHEET 1 B 2 GLU A 78 ILE A 79 0
SHEET 2 B 2 ASN A 82 LYS A 83 -1 O ASN A 82 N ILE A 79
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