Header list of 2cq3.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 19-MAY-05 2CQ3
TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN RNA BINDING MOTIF PROTEIN
TITLE 2 9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA-BINDING PROTEIN 9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: RNA BINDING MOTIF PROTEIN 9, HEXARIBONUCLEOTIDE BINDING
COMPND 6 PROTEIN 2, REPRESSOR OF TAMOXIFEN TRANSCRIPTIONAL ACTIVITY;
COMPND 7 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: RBM9;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041108-03;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RRM 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 K.TSUDA,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 2CQ3 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQ3 1 VERSN
REVDAT 1 19-NOV-05 2CQ3 0
JRNL AUTH K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN RNA BINDING
JRNL TITL 2 MOTIF PROTEIN 9
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 2CQ3 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_1000024494.
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 : 1.36MM 13C/15N-PROTEIN, 20MM D
REMARK 210 -TRIS-HCL (PH 7.0), 100MM NACL,
REMARK 210 1MM D-DTT, 0.02% NAN3, 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 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9297, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR 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 ARG A 157 79.33 -66.99
REMARK 500 1 HIS A 181 78.93 -61.93
REMARK 500 1 THR A 201 130.09 -35.60
REMARK 500 1 SER A 203 87.16 -64.78
REMARK 500 2 SER A 114 43.48 -87.88
REMARK 500 2 ASP A 136 -70.69 -63.02
REMARK 500 2 ARG A 157 40.83 36.69
REMARK 500 2 HIS A 181 94.20 -60.73
REMARK 500 2 ALA A 197 41.47 -97.82
REMARK 500 3 SER A 110 140.94 -170.90
REMARK 500 3 LYS A 117 137.03 -36.07
REMARK 500 3 ASN A 127 40.54 73.27
REMARK 500 3 PHE A 154 -70.02 -116.43
REMARK 500 3 SER A 159 114.94 -165.46
REMARK 500 3 LYS A 160 108.92 -173.93
REMARK 500 3 HIS A 181 93.54 -55.38
REMARK 500 3 ASN A 202 126.61 -171.71
REMARK 500 4 PRO A 129 168.63 -46.39
REMARK 500 4 ARG A 157 74.00 -65.51
REMARK 500 4 SER A 159 -74.94 -51.30
REMARK 500 4 ALA A 195 -62.30 -91.16
REMARK 500 5 ASN A 113 -179.79 -63.75
REMARK 500 5 SER A 116 105.37 -34.51
REMARK 500 5 HIS A 181 109.28 -36.62
REMARK 500 5 THR A 201 -71.07 -116.19
REMARK 500 6 SER A 114 118.82 -164.76
REMARK 500 6 PRO A 120 166.01 -46.92
REMARK 500 6 PRO A 129 178.00 -46.44
REMARK 500 6 HIS A 181 86.55 -63.76
REMARK 500 7 PRO A 120 158.48 -45.60
REMARK 500 7 GLU A 156 76.94 -100.12
REMARK 500 7 SER A 159 41.71 -95.77
REMARK 500 7 HIS A 181 100.18 -43.77
REMARK 500 7 THR A 196 42.48 -93.77
REMARK 500 7 MET A 200 43.22 -98.80
REMARK 500 8 ASN A 113 124.81 -172.37
REMARK 500 8 SER A 114 172.85 -51.95
REMARK 500 8 PRO A 129 176.78 -46.65
REMARK 500 8 ASP A 136 -70.75 -58.91
REMARK 500 8 HIS A 181 93.50 -34.39
REMARK 500 8 SER A 203 104.49 -57.49
REMARK 500 8 SER A 207 108.68 -46.64
REMARK 500 9 PRO A 129 153.57 -45.83
REMARK 500 9 ASN A 155 -176.96 -171.64
REMARK 500 9 SER A 159 54.81 34.19
REMARK 500 9 ARG A 177 -75.05 -72.82
REMARK 500 9 THR A 196 43.08 34.45
REMARK 500 10 PRO A 129 -179.98 -47.21
REMARK 500 10 SER A 159 113.05 -35.21
REMARK 500 10 HIS A 181 90.75 -63.71
REMARK 500
REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002014071.1 RELATED DB: TARGETDB
DBREF 2CQ3 A 113 202 UNP O43251 RBM9_HUMAN 113 202
SEQADV 2CQ3 GLY A 106 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 SER A 107 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 SER A 108 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 GLY A 109 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 SER A 110 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 SER A 111 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 GLY A 112 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 SER A 203 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 GLY A 204 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 PRO A 205 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 SER A 206 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 SER A 207 UNP O43251 CLONING ARTIFACT
SEQADV 2CQ3 GLY A 208 UNP O43251 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY ASN SER GLU SER LYS SER
SEQRES 2 A 103 THR PRO LYS ARG LEU HIS VAL SER ASN ILE PRO PHE ARG
SEQRES 3 A 103 PHE ARG ASP PRO ASP LEU ARG GLN MET PHE GLY GLN PHE
SEQRES 4 A 103 GLY LYS ILE LEU ASP VAL GLU ILE ILE PHE ASN GLU ARG
SEQRES 5 A 103 GLY SER LYS GLY PHE GLY PHE VAL THR PHE GLU ASN SER
SEQRES 6 A 103 ALA ASP ALA ASP ARG ALA ARG GLU LYS LEU HIS GLY THR
SEQRES 7 A 103 VAL VAL GLU GLY ARG LYS ILE GLU VAL ASN ASN ALA THR
SEQRES 8 A 103 ALA ARG VAL MET THR ASN SER GLY PRO SER SER GLY
HELIX 1 1 ARG A 133 PHE A 141 1 9
HELIX 2 2 GLY A 142 PHE A 144 5 3
HELIX 3 3 ASN A 169 HIS A 181 1 13
SHEET 1 A 4 ILE A 147 ILE A 153 0
SHEET 2 A 4 PHE A 162 PHE A 167 -1 O THR A 166 N LEU A 148
SHEET 3 A 4 ARG A 122 SER A 126 -1 N LEU A 123 O VAL A 165
SHEET 4 A 4 GLU A 191 ASN A 194 -1 O ASN A 193 N HIS A 124
SHEET 1 B 2 VAL A 184 VAL A 185 0
SHEET 2 B 2 ARG A 188 LYS A 189 -1 O ARG A 188 N VAL A 185
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