Header list of 2cqi.pdb file
Complete list - r 25 2 Bytes
HEADER RNA BINDING PROTEIN 20-MAY-05 2CQI
TITLE SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN OF NUCLEOLYSIN TIAR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEOLYSIN TIAR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: TIA-1 RELATED PROTEIN;
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: TIAL1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050111-15;
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 13-JUL-11 2CQI 1 SHEET
REVDAT 2 24-FEB-09 2CQI 1 VERSN
REVDAT 1 20-NOV-05 2CQI 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 NUCLEOLYSIN
JRNL TITL 2 TIAR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CQI 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 RCSB ID CODE IS RCSB024509.
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 : 1.2MM 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 : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE 20031121,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.9295,
REMARK 210 OLIVIA 1.10.5, 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 -5 114.56 -38.14
REMARK 500 1 ASN A 69 101.66 -55.96
REMARK 500 2 ASN A 69 108.91 -50.01
REMARK 500 2 PRO A 86 97.80 -69.73
REMARK 500 2 SER A 87 112.81 -165.66
REMARK 500 2 LYS A 90 38.76 -89.48
REMARK 500 3 SER A -1 165.55 -48.92
REMARK 500 3 THR A 45 99.95 -46.56
REMARK 500 3 ASN A 69 100.81 -58.20
REMARK 500 4 SER A -2 109.60 -46.82
REMARK 500 4 ASP A 4 86.08 -66.05
REMARK 500 4 THR A 45 48.20 -83.94
REMARK 500 4 ASN A 69 106.52 -56.30
REMARK 500 4 SER A 94 123.19 -170.54
REMARK 500 5 ASP A 4 41.44 -91.54
REMARK 500 5 GLN A 7 144.00 -37.00
REMARK 500 5 THR A 45 43.40 -82.92
REMARK 500 5 ASN A 47 -66.19 -125.37
REMARK 500 5 ASN A 69 105.70 -59.01
REMARK 500 5 PRO A 93 1.25 -69.74
REMARK 500 6 SER A -5 42.57 -95.57
REMARK 500 6 GLU A 43 43.37 -93.02
REMARK 500 6 ASN A 47 177.80 -51.11
REMARK 500 6 PRO A 49 -179.46 -69.75
REMARK 500 6 ASN A 69 99.81 -61.49
REMARK 500 6 SER A 88 43.40 73.92
REMARK 500 6 SER A 91 -53.51 -121.05
REMARK 500 7 SER A -4 151.84 -44.32
REMARK 500 7 GLN A 7 139.53 -35.42
REMARK 500 7 GLU A 43 31.84 -99.96
REMARK 500 7 ASP A 48 155.52 -42.60
REMARK 500 7 ASN A 69 106.31 -57.02
REMARK 500 7 SER A 87 139.83 -39.02
REMARK 500 8 ASP A 4 105.43 -49.34
REMARK 500 8 THR A 45 44.16 -86.56
REMARK 500 8 ASP A 48 151.64 -42.66
REMARK 500 8 ASN A 69 103.40 -58.08
REMARK 500 8 LYS A 90 114.23 -164.49
REMARK 500 9 ASP A 48 153.72 -44.49
REMARK 500 9 ASN A 69 101.42 -56.82
REMARK 500 9 SER A 94 151.36 -37.31
REMARK 500 10 THR A 45 -179.79 -54.34
REMARK 500 10 SER A 46 84.31 -63.52
REMARK 500 10 ASN A 69 106.22 -55.98
REMARK 500 10 GLN A 89 39.79 -91.94
REMARK 500 10 SER A 94 117.22 -168.68
REMARK 500 11 THR A 45 39.46 -93.89
REMARK 500 11 ASN A 69 99.84 -61.86
REMARK 500 11 PRO A 93 1.29 -69.76
REMARK 500 12 SER A -5 157.09 -38.16
REMARK 500
REMARK 500 THIS ENTRY HAS 102 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: HSO002000434.1 RELATED DB: TARGETDB
DBREF 2CQI A 1 90 UNP Q01085 TIAR_HUMAN 1 90
SEQADV 2CQI GLY A -6 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI SER A -5 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI SER A -4 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI GLY A -3 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI SER A -2 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI SER A -1 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI GLY A 0 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI SER A 91 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI GLY A 92 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI PRO A 93 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI SER A 94 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI SER A 95 UNP Q01085 EXPRESSION TAG
SEQADV 2CQI GLY A 96 UNP Q01085 EXPRESSION TAG
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY MET MET GLU ASP ASP GLY
SEQRES 2 A 103 GLN PRO ARG THR LEU TYR VAL GLY ASN LEU SER ARG ASP
SEQRES 3 A 103 VAL THR GLU VAL LEU ILE LEU GLN LEU PHE SER GLN ILE
SEQRES 4 A 103 GLY PRO CYS LYS SER CYS LYS MET ILE THR GLU HIS THR
SEQRES 5 A 103 SER ASN ASP PRO TYR CYS PHE VAL GLU PHE TYR GLU HIS
SEQRES 6 A 103 ARG ASP ALA ALA ALA ALA LEU ALA ALA MET ASN GLY ARG
SEQRES 7 A 103 LYS ILE LEU GLY LYS GLU VAL LYS VAL ASN TRP ALA THR
SEQRES 8 A 103 THR PRO SER SER GLN LYS SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 22 ILE A 32 1 11
HELIX 2 2 HIS A 58 MET A 68 1 11
SHEET 1 A 5 SER A 37 ILE A 41 0
SHEET 2 A 5 TYR A 50 GLU A 54 -1 O TYR A 50 N ILE A 41
SHEET 3 A 5 THR A 10 GLY A 14 -1 N VAL A 13 O CYS A 51
SHEET 4 A 5 LYS A 79 TRP A 82 -1 O ASN A 81 N TYR A 12
SHEET 5 A 5 LYS A 76 VAL A 78 -1 N ARG A 71 O VAL A 78
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 25 2 Bytes