Header list of 2cqj.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 20-MAY-05 2CQJ
TITLE SOLUTION STRUCTURE OF THE S4 DOMAIN OF U3 SMALL NUCLEOLAR
TITLE 2 RIBONUCLEOPROTEIN PROTEIN IMP3 HOMOLOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: U3 SMALL NUCLEOLAR RIBONUCLEOPROTEIN PROTEIN IMP3 HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: S4 DOMAIN;
COMPND 5 SYNONYM: BRMS2;
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: C15ORF12;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041213-13;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS S4 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 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 2CQJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQJ 1 VERSN
REVDAT 1 20-NOV-05 2CQJ 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 S4 DOMAIN OF U3 SMALL NUCLEOLAR
JRNL TITL 2 RIBONUCLEOPROTEIN PROTEIN IMP3 HOMOLOG
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 2CQJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024510.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1MM 13C/15N-PROTEIN; 20MM D
REMARK 210 -TRIS-HCL; 100MM NACL; 1MM D-DTT;
REMARK 210 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 : 700 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 0.9295, 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 ARG A 119 29.43 48.73
REMARK 500 1 PRO A 140 3.38 -69.71
REMARK 500 1 PHE A 157 33.35 -93.12
REMARK 500 1 ILE A 166 130.40 -39.07
REMARK 500 2 GLN A 122 -70.50 -80.50
REMARK 500 2 PRO A 140 3.42 -69.74
REMARK 500 3 ARG A 119 27.51 47.52
REMARK 500 3 PRO A 140 3.48 -69.81
REMARK 500 3 PHE A 157 34.49 -91.67
REMARK 500 3 SER A 163 47.71 -108.06
REMARK 500 3 ILE A 166 145.20 -36.07
REMARK 500 4 PRO A 140 3.38 -69.76
REMARK 500 4 PHE A 157 34.48 -91.78
REMARK 500 4 SER A 163 63.82 -113.88
REMARK 500 4 SER A 171 137.56 -39.00
REMARK 500 5 GLN A 122 -68.20 -90.52
REMARK 500 5 PRO A 140 3.50 -69.74
REMARK 500 5 ILE A 166 140.71 -33.95
REMARK 500 6 SER A 107 44.38 -104.17
REMARK 500 6 ARG A 119 25.11 48.80
REMARK 500 6 GLN A 122 -74.25 -100.49
REMARK 500 6 PRO A 140 3.70 -69.76
REMARK 500 6 ARG A 152 -70.06 -34.07
REMARK 500 6 PHE A 157 33.70 -86.49
REMARK 500 6 PRO A 169 99.98 -69.79
REMARK 500 7 GLN A 122 -66.16 -90.76
REMARK 500 7 PRO A 140 3.47 -69.83
REMARK 500 7 SER A 164 -74.41 -50.60
REMARK 500 7 PRO A 169 -178.57 -69.81
REMARK 500 8 SER A 106 93.97 -65.16
REMARK 500 8 ARG A 119 27.37 48.60
REMARK 500 8 GLN A 122 -70.66 -89.65
REMARK 500 8 PRO A 140 3.58 -69.84
REMARK 500 8 SER A 171 106.09 -59.42
REMARK 500 9 GLN A 122 -68.22 -93.03
REMARK 500 9 PRO A 140 3.64 -69.82
REMARK 500 9 LYS A 165 40.83 -102.21
REMARK 500 9 SER A 170 152.36 -39.06
REMARK 500 10 PRO A 140 3.60 -69.79
REMARK 500 10 PHE A 157 31.20 -97.13
REMARK 500 10 SER A 171 -52.01 -125.47
REMARK 500 11 GLN A 122 -67.74 -96.81
REMARK 500 11 PRO A 140 3.39 -69.69
REMARK 500 11 SER A 170 121.73 -37.78
REMARK 500 12 ARG A 119 29.30 45.78
REMARK 500 12 PRO A 140 3.55 -69.74
REMARK 500 13 GLN A 122 -72.84 -62.46
REMARK 500 13 PRO A 140 3.47 -69.79
REMARK 500 13 ARG A 152 -30.78 -37.77
REMARK 500 13 SER A 163 40.71 -101.20
REMARK 500
REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001002801.1 RELATED DB: TARGETDB
DBREF 2CQJ A 109 166 UNP Q9NV31 IMP3_HUMAN 109 166
SEQADV 2CQJ GLY A 102 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ SER A 103 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ SER A 104 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ GLY A 105 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ SER A 106 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ SER A 107 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ GLY A 108 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ SER A 167 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ GLY A 168 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ PRO A 169 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ SER A 170 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ SER A 171 UNP Q9NV31 CLONING ARTIFACT
SEQADV 2CQJ GLY A 172 UNP Q9NV31 CLONING ARTIFACT
SEQRES 1 A 71 GLY SER SER GLY SER SER GLY ARG ARG LEU PRO THR VAL
SEQRES 2 A 71 LEU LEU LYS LEU ARG MET ALA GLN HIS LEU GLN ALA ALA
SEQRES 3 A 71 VAL ALA PHE VAL GLU GLN GLY HIS VAL ARG VAL GLY PRO
SEQRES 4 A 71 ASP VAL VAL THR ASP PRO ALA PHE LEU VAL THR ARG SER
SEQRES 5 A 71 MET GLU ASP PHE VAL THR TRP VAL ASP SER SER LYS ILE
SEQRES 6 A 71 SER GLY PRO SER SER GLY
HELIX 1 1 LEU A 111 LYS A 117 1 7
HELIX 2 2 LEU A 124 GLU A 132 1 9
HELIX 3 3 ARG A 152 GLU A 155 1 4
SHEET 1 A 2 ARG A 109 ARG A 110 0
SHEET 2 A 2 LEU A 149 THR A 151 -1 O VAL A 150 N ARG A 109
SHEET 1 B 3 ASP A 141 VAL A 142 0
SHEET 2 B 3 VAL A 136 VAL A 138 -1
SHEET 3 B 3 VAL A 158 TRP A 160 -1 O THR A 159 N ARG A 137
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