Header list of 2cqg.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 20-MAY-05 2CQG
TITLE SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN OF TAR DNA-BINDING
TITLE 2 PROTEIN-43
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TAR DNA-BINDING PROTEIN-43;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: TDP-43;
COMPND 6 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: TARDBP;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040524-02;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RNA RECOGNITION MOTIF, RRM, RNA BINDING DOMAIN, RBD, RNP, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SUZUKI,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 2CQG 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQG 1 VERSN
REVDAT 1 20-NOV-05 2CQG 0
JRNL AUTH S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN OF TAR
JRNL TITL 2 DNA-BINDING PROTEIN-43
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 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CQG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024507.
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 : 0.86MM 13C/15N-PROTEIN; 20MM D
REMARK 210 -TRIS-HCL(PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3
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 0.9295, OLIVIA 1.10.5,
REMARK 210 CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS,
REMARK 210 SIMULATED ANNEALING
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 91 134.63 -170.82
REMARK 500 1 LYS A 97 101.05 -38.63
REMARK 500 1 THR A 103 141.95 -34.08
REMARK 500 2 THR A 103 153.01 -43.99
REMARK 500 2 PRO A 112 -175.66 -69.74
REMARK 500 2 SER A 163 -72.25 -75.19
REMARK 500 2 PRO A 178 2.86 -69.72
REMARK 500 2 ASN A 179 -36.91 -38.16
REMARK 500 2 SER A 180 46.28 -79.26
REMARK 500 2 LYS A 181 37.37 37.69
REMARK 500 2 GLN A 182 38.28 -90.70
REMARK 500 3 GLN A 101 132.26 -174.77
REMARK 500 3 SER A 144 141.86 -39.08
REMARK 500 3 PRO A 178 2.88 -69.74
REMARK 500 3 ASN A 179 -38.44 -34.37
REMARK 500 4 PRO A 178 2.84 -69.84
REMARK 500 4 ASN A 179 -39.03 -38.54
REMARK 500 5 VAL A 96 40.72 -95.01
REMARK 500 5 PRO A 178 2.94 -69.78
REMARK 500 5 GLN A 182 -70.50 -126.32
REMARK 500 6 SER A 90 107.88 -162.81
REMARK 500 6 ALA A 99 139.87 -35.16
REMARK 500 6 PRO A 112 -178.60 -69.73
REMARK 500 6 LYS A 140 -34.78 -38.17
REMARK 500 6 PRO A 178 1.91 -69.77
REMARK 500 6 ASN A 179 169.28 -46.13
REMARK 500 6 SER A 180 38.88 70.16
REMARK 500 6 PRO A 188 94.75 -69.74
REMARK 500 7 SER A 91 95.74 -60.26
REMARK 500 7 THR A 103 138.49 -39.56
REMARK 500 7 PRO A 112 -164.99 -69.70
REMARK 500 7 THR A 141 -51.79 -128.80
REMARK 500 7 LYS A 181 47.95 34.59
REMARK 500 7 SER A 183 42.57 -91.82
REMARK 500 7 SER A 190 -60.70 -101.54
REMARK 500 8 SER A 94 -42.89 -131.44
REMARK 500 8 THR A 103 108.37 -46.17
REMARK 500 8 SER A 163 -74.53 -56.72
REMARK 500 8 GLN A 182 105.34 -58.95
REMARK 500 8 SER A 190 -50.04 -128.37
REMARK 500 9 PRO A 112 -166.81 -69.75
REMARK 500 9 LYS A 140 -36.09 -34.20
REMARK 500 10 VAL A 96 126.26 -173.08
REMARK 500 10 PRO A 112 -165.81 -69.76
REMARK 500 10 ARG A 165 -175.47 -59.26
REMARK 500 11 LYS A 97 148.07 -34.94
REMARK 500 11 ALA A 99 37.49 71.18
REMARK 500 11 SER A 189 99.31 -46.65
REMARK 500 12 VAL A 100 46.29 -82.66
REMARK 500 12 THR A 141 -60.02 -109.79
REMARK 500
REMARK 500 THIS ENTRY HAS 94 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: HSS001001612 RELATED DB: TARGETDB
DBREF 2CQG A 96 185 UNP Q13148 TADBP_HUMAN 96 185
SEQADV 2CQG GLY A 89 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG SER A 90 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG SER A 91 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG GLY A 92 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG SER A 93 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG SER A 94 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG GLY A 95 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG SER A 186 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG GLY A 187 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG PRO A 188 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG SER A 189 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG SER A 190 UNP Q13148 CLONING ARTIFACT
SEQADV 2CQG GLY A 191 UNP Q13148 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY VAL LYS ARG ALA VAL GLN
SEQRES 2 A 103 LYS THR SER ASP LEU ILE VAL LEU GLY LEU PRO TRP LYS
SEQRES 3 A 103 THR THR GLU GLN ASP LEU LYS GLU TYR PHE SER THR PHE
SEQRES 4 A 103 GLY GLU VAL LEU MET VAL GLN VAL LYS LYS ASP LEU LYS
SEQRES 5 A 103 THR GLY HIS SER LYS GLY PHE GLY PHE VAL ARG PHE THR
SEQRES 6 A 103 GLU TYR GLU THR GLN VAL LYS VAL MET SER GLN ARG HIS
SEQRES 7 A 103 MET ILE ASP GLY ARG TRP CYS ASP CYS LYS LEU PRO ASN
SEQRES 8 A 103 SER LYS GLN SER GLN ASP SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 117 PHE A 127 1 11
HELIX 2 3 TYR A 155 SER A 163 1 9
SHEET 1 A 5 LEU A 106 LEU A 109 0
SHEET 2 A 5 MET A 132 LYS A 136 -1
SHEET 3 A 5 PHE A 147 ARG A 151 -1
SHEET 4 A 5 ARG A 171 CYS A 173 -1
SHEET 5 A 5 ASP A 174 LYS A 176 -1
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