Header list of 2cq2.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 19-MAY-05 2CQ2
TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN HYPOTHETICAL PROTEIN
TITLE 2 LOC91801
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN LOC91801;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN BC015183;
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: LOC9180;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041012-04;
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 2CQ2 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQ2 1 VERSN
REVDAT 1 19-NOV-05 2CQ2 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 HYPOTHETICAL
JRNL TITL 2 PROTEIN LOC91801
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 2CQ2 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_1000024493.
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 : 1.16MM 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 : 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 0.9297, 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 ALA A 25 -175.97 -65.11
REMARK 500 1 LEU A 29 -34.72 -33.45
REMARK 500 1 HIS A 32 -70.79 -55.99
REMARK 500 1 GLU A 33 -38.39 -36.52
REMARK 500 1 TYR A 40 -178.18 -68.01
REMARK 500 1 GLN A 43 -36.84 -37.17
REMARK 500 1 ASN A 54 33.16 -88.95
REMARK 500 1 THR A 99 -62.83 -99.99
REMARK 500 1 GLN A 124 75.98 -66.49
REMARK 500 1 SER A 126 43.62 -93.12
REMARK 500 2 THR A 28 30.88 -84.52
REMARK 500 2 ASN A 54 34.28 -92.35
REMARK 500 2 THR A 99 -63.77 -96.48
REMARK 500 2 ASP A 107 -175.46 -65.36
REMARK 500 2 SER A 126 137.38 -175.02
REMARK 500 2 SER A 129 99.01 -37.89
REMARK 500 3 ASN A 54 33.65 -86.26
REMARK 500 3 THR A 99 -60.60 -91.86
REMARK 500 3 ASN A 101 107.57 -44.64
REMARK 500 3 GLN A 124 73.39 -69.63
REMARK 500 4 ALA A 25 -175.09 -53.00
REMARK 500 4 LEU A 29 -37.53 -35.39
REMARK 500 4 GLN A 43 -32.59 -39.80
REMARK 500 4 ASN A 54 32.01 -91.71
REMARK 500 4 THR A 99 -63.72 -92.15
REMARK 500 4 GLN A 124 70.98 -69.09
REMARK 500 5 THR A 28 31.25 -98.40
REMARK 500 5 ASN A 54 34.98 -90.70
REMARK 500 5 THR A 99 -64.03 -99.11
REMARK 500 5 GLN A 124 77.63 -63.08
REMARK 500 6 SER A 20 -45.84 -130.31
REMARK 500 6 LEU A 29 -38.59 -33.92
REMARK 500 6 HIS A 32 -74.72 -46.17
REMARK 500 6 THR A 99 -62.07 -93.75
REMARK 500 6 GLN A 124 72.79 -66.22
REMARK 500 6 PRO A 128 93.17 -69.77
REMARK 500 7 SER A 22 42.71 34.61
REMARK 500 7 SER A 23 41.79 -99.33
REMARK 500 7 ALA A 25 138.29 -36.20
REMARK 500 7 ASN A 49 26.61 48.25
REMARK 500 7 ASN A 54 32.28 -88.42
REMARK 500 7 THR A 99 -62.90 -98.60
REMARK 500 7 ASP A 107 -176.46 -67.42
REMARK 500 7 GLN A 124 77.79 -60.65
REMARK 500 7 SER A 129 153.75 -46.61
REMARK 500 8 SER A 19 131.96 -35.24
REMARK 500 8 SER A 20 144.12 -171.79
REMARK 500 8 SER A 22 51.94 37.49
REMARK 500 8 ALA A 25 -73.21 -71.53
REMARK 500 8 LYS A 26 52.52 36.17
REMARK 500
REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002010820.1 RELATED DB: TARGETDB
DBREF 2CQ2 A 25 125 UNP Q8N989 Q8N989_HUMAN 25 125
SEQADV 2CQ2 GLY A 18 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 SER A 19 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 SER A 20 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 GLY A 21 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 SER A 22 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 SER A 23 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 GLY A 24 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 SER A 126 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 GLY A 127 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 PRO A 128 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 SER A 129 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 SER A 130 UNP Q8N989 CLONING ARTIFACT
SEQADV 2CQ2 GLY A 131 UNP Q8N989 CLONING ARTIFACT
SEQRES 1 A 114 GLY SER SER GLY SER SER GLY ALA LYS HIS THR LEU LEU
SEQRES 2 A 114 ARG HIS GLU GLY ILE GLU THR VAL SER TYR ALA THR GLN
SEQRES 3 A 114 SER LEU VAL VAL ALA ASN GLY GLY LEU GLY ASN GLY VAL
SEQRES 4 A 114 SER ARG ASN GLN LEU LEU PRO VAL LEU GLU LYS CYS GLY
SEQRES 5 A 114 LEU VAL ASP ALA LEU LEU MET PRO PRO ASN LYS PRO TYR
SEQRES 6 A 114 SER PHE ALA ARG TYR ARG THR THR GLU GLU SER LYS ARG
SEQRES 7 A 114 ALA TYR VAL THR LEU ASN GLY LYS GLU VAL VAL ASP ASP
SEQRES 8 A 114 LEU GLY GLN LYS ILE THR LEU TYR LEU ASN PHE VAL GLU
SEQRES 9 A 114 LYS VAL GLN TRP SER GLY PRO SER SER GLY
HELIX 1 1 THR A 28 GLY A 34 1 7
HELIX 2 2 GLY A 51 GLY A 55 5 5
HELIX 3 3 SER A 57 GLY A 69 1 13
HELIX 4 4 THR A 89 LEU A 100 1 12
SHEET 1 A 4 VAL A 71 LEU A 75 0
SHEET 2 A 4 SER A 83 TYR A 87 -1 O PHE A 84 N LEU A 75
SHEET 3 A 4 SER A 44 ALA A 48 -1 N LEU A 45 O ALA A 85
SHEET 4 A 4 TYR A 116 VAL A 120 -1 O TYR A 116 N ALA A 48
SHEET 1 B 2 GLU A 104 VAL A 106 0
SHEET 2 B 2 LYS A 112 THR A 114 -1 O ILE A 113 N VAL A 105
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