Header list of 2cqc.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 19-MAY-05 2CQC TITLE SOLUTION STRUCTURE OF THE RNA RECOGNITION MOTIF IN ARGININE/SERINE- TITLE 2 RICH SPLICING FACTOR 10 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ARGININE/SERINE-RICH SPLICING FACTOR 10; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 SYNONYM: TRANSFORMER-2-BETA, HTRA2- BETA, TRANSFORMER 2 PROTEIN COMPND 6 HOMOLOG; 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: SFRS10; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040517-05; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RNA RECOGNITION MOTIF, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT KEYWDS 2 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.SOMEYA,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 2CQC 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CQC 1 VERSN REVDAT 1 19-NOV-05 2CQC 0 JRNL AUTH T.SOMEYA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE RNA RECOGNITION MOTIF IN JRNL TITL 2 ARGININE/SERINE-RICH SPLICING FACTOR 10 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 2CQC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024503. 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 : 1.14MM PROTEIN U-15N,13C; 20MM D REMARK 210 -TRIS-HCL(PH7.0); 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 : 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, 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 ALA A 112 -54.28 -124.34 REMARK 500 1 PRO A 114 94.36 -69.79 REMARK 500 1 LEU A 127 -70.77 -41.92 REMARK 500 1 GLN A 154 -71.49 -90.90 REMARK 500 1 ARG A 156 41.71 -87.08 REMARK 500 1 PRO A 194 -166.03 -69.79 REMARK 500 2 SER A 107 39.60 34.39 REMARK 500 2 ASP A 115 72.86 -107.19 REMARK 500 2 PHE A 161 145.56 -171.04 REMARK 500 2 GLU A 167 -73.14 -51.52 REMARK 500 2 LYS A 176 -36.20 -35.30 REMARK 500 2 ARG A 178 31.19 -91.44 REMARK 500 2 ALA A 179 -47.71 -132.32 REMARK 500 2 PRO A 194 -175.06 -69.74 REMARK 500 2 SER A 196 40.22 36.77 REMARK 500 3 ASN A 110 76.17 -113.99 REMARK 500 3 ASN A 117 110.88 -175.09 REMARK 500 3 SER A 126 154.15 -44.92 REMARK 500 3 ALA A 145 -65.22 -93.95 REMARK 500 3 GLN A 154 -62.42 -103.50 REMARK 500 3 SER A 155 177.76 -59.69 REMARK 500 3 PRO A 194 84.99 -69.78 REMARK 500 4 ASN A 110 41.08 -100.30 REMARK 500 4 PRO A 116 2.38 -69.76 REMARK 500 4 LYS A 176 -33.69 -34.38 REMARK 500 4 ARG A 178 34.34 -94.82 REMARK 500 4 ALA A 179 -57.20 -133.29 REMARK 500 4 ASN A 180 129.63 -37.08 REMARK 500 4 PRO A 194 0.39 -69.77 REMARK 500 5 ALA A 112 42.74 -97.08 REMARK 500 5 PRO A 116 2.52 -69.68 REMARK 500 5 SER A 126 150.24 -47.82 REMARK 500 5 LYS A 140 -36.54 -39.06 REMARK 500 5 LYS A 176 -30.17 -36.99 REMARK 500 5 ASN A 180 121.49 -34.89 REMARK 500 5 PRO A 194 87.50 -69.81 REMARK 500 6 ASP A 115 98.96 -36.75 REMARK 500 6 PRO A 116 0.09 -69.76 REMARK 500 6 CYS A 118 43.02 -108.16 REMARK 500 6 GLN A 153 -63.98 -91.85 REMARK 500 6 SER A 158 136.49 -34.56 REMARK 500 6 GLU A 167 -72.22 -37.49 REMARK 500 6 LYS A 176 -30.11 -38.91 REMARK 500 6 ARG A 178 32.35 -87.54 REMARK 500 6 ALA A 179 -54.79 -130.18 REMARK 500 7 CYS A 118 43.57 -83.94 REMARK 500 7 ARG A 156 49.30 -94.33 REMARK 500 7 SER A 158 141.44 -35.38 REMARK 500 7 LYS A 176 -34.36 -36.74 REMARK 500 7 ALA A 179 -57.59 -125.21 REMARK 500 REMARK 500 THIS ENTRY HAS 151 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: HSS001003317 RELATED DB: TARGETDB DBREF 2CQC A 110 191 UNP P62995 TRA2B_HUMAN 110 191 SEQADV 2CQC GLY A 103 UNP P62995 CLONING ARTIFACT SEQADV 2CQC SER A 104 UNP P62995 CLONING ARTIFACT SEQADV 2CQC SER A 105 UNP P62995 CLONING ARTIFACT SEQADV 2CQC GLY A 106 UNP P62995 CLONING ARTIFACT SEQADV 2CQC SER A 107 UNP P62995 CLONING ARTIFACT SEQADV 2CQC SER A 108 UNP P62995 CLONING ARTIFACT SEQADV 2CQC GLY A 109 UNP P62995 CLONING ARTIFACT SEQADV 2CQC SER A 192 UNP P62995 CLONING ARTIFACT SEQADV 2CQC GLY A 193 UNP P62995 CLONING ARTIFACT SEQADV 2CQC PRO A 194 UNP P62995 CLONING ARTIFACT SEQADV 2CQC SER A 195 UNP P62995 CLONING ARTIFACT SEQADV 2CQC SER A 196 UNP P62995 CLONING ARTIFACT SEQADV 2CQC GLY A 197 UNP P62995 CLONING ARTIFACT SEQRES 1 A 95 GLY SER SER GLY SER SER GLY ASN ARG ALA ASN PRO ASP SEQRES 2 A 95 PRO ASN CYS CYS LEU GLY VAL PHE GLY LEU SER LEU TYR SEQRES 3 A 95 THR THR GLU ARG ASP LEU ARG GLU VAL PHE SER LYS TYR SEQRES 4 A 95 GLY PRO ILE ALA ASP VAL SER ILE VAL TYR ASP GLN GLN SEQRES 5 A 95 SER ARG ARG SER ARG GLY PHE ALA PHE VAL TYR PHE GLU SEQRES 6 A 95 ASN VAL ASP ASP ALA LYS GLU ALA LYS GLU ARG ALA ASN SEQRES 7 A 95 GLY MET GLU LEU ASP GLY ARG ARG ILE ARG VAL SER GLY SEQRES 8 A 95 PRO SER SER GLY HELIX 1 1 GLU A 131 PHE A 138 1 8 HELIX 2 2 VAL A 169 ARG A 178 1 10 SHEET 1 A 5 LEU A 120 PHE A 123 0 SHEET 2 A 5 VAL A 147 ILE A 149 -1 SHEET 3 A 5 PHE A 161 VAL A 164 -1 SHEET 4 A 5 MET A 182 LEU A 184 -1 SHEET 5 A 5 ARG A 187 SER A 192 -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