Header list of 2db2.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 14-DEC-05 2DB2
TITLE SOLUTION STRUCTURE OF THE DOUBLE-STRANDED RNA BINDING DOMAIN IN
TITLE 2 KIAA0890 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA0890 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOUBLE-STRANDED RNA BINDING MOTIF;
COMPND 5 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: KIAA0890;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050725-08;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS DSRM 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 C.ABE,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 2DB2 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DB2 1 VERSN
REVDAT 1 14-JUN-06 2DB2 0
JRNL AUTH C.ABE,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE DOUBLE-STRANDED RNA BINDING DOMAIN
JRNL TITL 2 IN KIAA0890 PROTEIN
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
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT,P (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DB2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025203.
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 : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20MM D-TRIS-HCL (PH 7.0), 100MM
REMARK 210 NACL, 1MM D-DTT, 0.02% NAN; 90%
REMARK 210 H2O, 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 0.93191, CYANA 2.0
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 GLN A 68 74.64 -114.14
REMARK 500 1 VAL A 76 -73.62 -57.62
REMARK 500 1 LEU A 81 -66.54 -102.61
REMARK 500 1 ALA A 86 -37.21 -37.44
REMARK 500 1 LEU A 143 -63.31 -104.95
REMARK 500 1 LEU A 149 175.70 -48.64
REMARK 500 2 VAL A 76 -71.52 -53.14
REMARK 500 2 LEU A 81 -68.35 -99.09
REMARK 500 2 ILE A 83 -32.48 -39.05
REMARK 500 2 LEU A 149 168.21 -44.75
REMARK 500 2 ARG A 161 -28.28 -38.63
REMARK 500 2 SER A 164 38.91 -86.98
REMARK 500 3 SER A 52 48.58 -87.65
REMARK 500 3 VAL A 76 -72.08 -38.97
REMARK 500 3 LEU A 81 -67.17 -97.75
REMARK 500 3 ALA A 86 -31.27 -37.61
REMARK 500 3 LYS A 89 -34.46 -39.12
REMARK 500 3 PRO A 166 94.49 -69.72
REMARK 500 4 VAL A 76 -74.70 -56.55
REMARK 500 4 LEU A 81 -66.03 -95.75
REMARK 500 4 ILE A 83 -37.62 -38.59
REMARK 500 4 ALA A 86 -39.13 -39.29
REMARK 500 4 LEU A 143 -61.86 -106.91
REMARK 500 4 LEU A 149 166.83 -46.64
REMARK 500 4 SER A 164 155.80 -38.40
REMARK 500 4 PRO A 166 -178.08 -69.78
REMARK 500 5 SER A 53 42.14 34.90
REMARK 500 5 VAL A 76 -74.57 -51.93
REMARK 500 5 LEU A 81 -65.35 -96.93
REMARK 500 5 ILE A 83 -38.44 -37.13
REMARK 500 5 LEU A 143 -69.30 -126.90
REMARK 500 5 ARG A 146 31.36 -99.66
REMARK 500 6 SER A 52 -53.94 -123.19
REMARK 500 6 VAL A 76 -72.40 -56.65
REMARK 500 6 LEU A 81 -61.60 -95.52
REMARK 500 6 PRO A 98 -176.93 -69.82
REMARK 500 6 LEU A 143 -65.63 -108.05
REMARK 500 6 SER A 168 49.54 35.16
REMARK 500 7 SER A 59 40.03 -89.10
REMARK 500 7 VAL A 76 -72.11 -61.12
REMARK 500 7 LEU A 81 -69.85 -104.35
REMARK 500 7 ARG A 146 34.79 -97.28
REMARK 500 7 ASN A 147 53.77 39.96
REMARK 500 8 VAL A 76 -71.19 -50.22
REMARK 500 8 LEU A 81 -66.04 -105.58
REMARK 500 8 ILE A 83 -34.43 -33.83
REMARK 500 8 ALA A 86 -29.74 -36.30
REMARK 500 8 LYS A 89 -25.58 -39.59
REMARK 500 8 PRO A 98 -179.03 -69.73
REMARK 500 9 LEU A 81 -65.38 -95.41
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000869.1 RELATED DB: TARGETDB
DBREF 2DB2 A 58 163 UNP Q9NUQ0 Q9NUQ0_HUMAN 70 176
SEQADV 2DB2 GLY A 51 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 SER A 52 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 SER A 53 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 GLY A 54 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 SER A 55 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 SER A 56 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 GLY A 57 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 SER A 164 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 GLY A 165 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 PRO A 166 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 SER A 167 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 SER A 168 UNP Q9NUQ0 CLONING ARTIFACT
SEQADV 2DB2 GLY A 169 UNP Q9NUQ0 CLONING ARTIFACT
SEQRES 1 A 119 GLY SER SER GLY SER SER GLY ALA SER ARG ASP LEU LEU
SEQRES 2 A 119 LYS GLU PHE PRO GLN PRO LYS ASN LEU LEU ASN SER VAL
SEQRES 3 A 119 ILE GLY ARG ALA LEU GLY ILE SER HIS ALA LYS ASP LYS
SEQRES 4 A 119 LEU VAL TYR VAL HIS THR ASN GLY PRO LYS LYS LYS LYS
SEQRES 5 A 119 VAL THR LEU HIS ILE LYS TRP PRO LYS SER VAL GLU VAL
SEQRES 6 A 119 GLU GLY TYR GLY SER LYS LYS ILE ASP ALA GLU ARG GLN
SEQRES 7 A 119 ALA ALA ALA ALA ALA CYS GLN LEU PHE LYS GLY TRP GLY
SEQRES 8 A 119 LEU LEU GLY PRO ARG ASN GLU LEU PHE ASP ALA ALA LYS
SEQRES 9 A 119 TYR ARG VAL LEU ALA ASP ARG PHE GLY SER GLY PRO SER
SEQRES 10 A 119 SER GLY
HELIX 1 1 GLN A 68 LEU A 81 1 14
HELIX 2 2 GLY A 82 LYS A 89 1 8
HELIX 3 3 LYS A 121 GLY A 141 1 21
HELIX 4 4 ASP A 151 ARG A 161 1 11
SHEET 1 A 3 LEU A 90 HIS A 94 0
SHEET 2 A 3 LYS A 101 ILE A 107 -1 O THR A 104 N VAL A 93
SHEET 3 A 3 VAL A 113 GLY A 119 -1 O VAL A 113 N ILE A 107
CISPEP 1 TRP A 109 PRO A 110 1 -0.06
CISPEP 2 TRP A 109 PRO A 110 2 -0.05
CISPEP 3 TRP A 109 PRO A 110 3 -0.08
CISPEP 4 TRP A 109 PRO A 110 4 0.00
CISPEP 5 TRP A 109 PRO A 110 5 -0.13
CISPEP 6 TRP A 109 PRO A 110 6 -0.05
CISPEP 7 TRP A 109 PRO A 110 7 -0.08
CISPEP 8 TRP A 109 PRO A 110 8 0.01
CISPEP 9 TRP A 109 PRO A 110 9 -0.05
CISPEP 10 TRP A 109 PRO A 110 10 0.00
CISPEP 11 TRP A 109 PRO A 110 11 -0.05
CISPEP 12 TRP A 109 PRO A 110 12 0.00
CISPEP 13 TRP A 109 PRO A 110 13 0.06
CISPEP 14 TRP A 109 PRO A 110 14 -0.04
CISPEP 15 TRP A 109 PRO A 110 15 -0.03
CISPEP 16 TRP A 109 PRO A 110 16 -0.09
CISPEP 17 TRP A 109 PRO A 110 17 -0.07
CISPEP 18 TRP A 109 PRO A 110 18 -0.10
CISPEP 19 TRP A 109 PRO A 110 19 -0.06
CISPEP 20 TRP A 109 PRO A 110 20 -0.08
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