Header list of 1d9a.pdb file
Complete list - 16 20 Bytes
HEADER RNA BINDING PROTEIN 26-OCT-99 1D9A
TITLE SOLUTION STRUCTURE OF THE SECOND RNA-BINDING DOMAIN (RBD2) OF HU
TITLE 2 ANTIGEN C (HUC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HU ANTIGEN C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SECOND RNA-BINDING DOMAIN (RBD2);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PK7
KEYWDS RNA-BINDING DOMAIN, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 2 RSGI, STRUCTURAL GENOMICS, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR M.INOUE,Y.MUTO,H.SAKAMOTO,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 16-FEB-22 1D9A 1 REMARK
REVDAT 2 24-FEB-09 1D9A 1 VERSN
REVDAT 1 07-APR-00 1D9A 0
JRNL AUTH M.INOUE,Y.MUTO,H.SAKAMOTO,S.YOKOYAMA
JRNL TITL NMR STUDIES ON FUNCTIONAL STRUCTURES OF THE AU-RICH
JRNL TITL 2 ELEMENT-BINDING DOMAINS OF HU ANTIGEN C.
JRNL REF NUCLEIC ACIDS RES. V. 28 1743 2000
JRNL REFN ISSN 0305-1048
JRNL PMID 10734193
JRNL DOI 10.1093/NAR/28.8.1743
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1D9A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009904.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.6
REMARK 210 IONIC STRENGTH : 20 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM PROTEIN; 20 MM POTASSIUM
REMARK 210 OXALATE BUFFER; 90% H2O; 10% D2O;
REMARK 210 2MM PROTEIN U-15N; 20 MM
REMARK 210 POTASSIUM OXALATE BUFFER; 90%
REMARK 210 H2O; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR AND
REMARK 210 15N-SEPARATED
REMARK 210 HETERONUCLEAR TECHNIQUES.
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 ALA A 2 63.03 -116.40
REMARK 500 ARG A 27 105.54 -43.00
REMARK 500 ILE A 29 -73.55 -88.43
REMARK 500 ARG A 32 152.58 175.55
REMARK 500 LEU A 35 102.49 -162.73
REMARK 500 GLN A 37 62.36 -150.08
REMARK 500 ALA A 38 -42.70 -176.52
REMARK 500 LEU A 63 -46.76 -133.61
REMARK 500 ASN A 64 136.07 -39.28
REMARK 500 LYS A 67 102.35 -160.81
REMARK 500 ALA A 71 105.84 -43.01
REMARK 500 ALA A 72 -26.54 171.82
REMARK 500 THR A 76 82.91 -159.72
REMARK 500 ASN A 82 118.97 59.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 27 0.31 SIDE CHAIN
REMARK 500 ARG A 32 0.29 SIDE CHAIN
REMARK 500 ARG A 43 0.21 SIDE CHAIN
REMARK 500 ARG A 49 0.25 SIDE CHAIN
REMARK 500 ARG A 53 0.26 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D8Z RELATED DB: PDB
REMARK 900 FIRST RNA-BINDING DOMAIN (RBD1) OF HUC
REMARK 900 RELATED ID: TRT001000186.1 RELATED DB: TARGETDB
DBREF 1D9A A 1 85 UNP Q60900 ELAV3_MOUSE 124 208
SEQRES 1 A 85 ASP ALA ASN LEU TYR VAL SER GLY LEU PRO LYS THR MET
SEQRES 2 A 85 SER GLN LYS GLU MET GLU GLN LEU PHE SER GLN TYR GLY
SEQRES 3 A 85 ARG ILE ILE THR SER ARG ILE LEU LEU ASP GLN ALA THR
SEQRES 4 A 85 GLY VAL SER ARG GLY VAL GLY PHE ILE ARG PHE ASP LYS
SEQRES 5 A 85 ARG ILE GLU ALA GLU GLU ALA ILE LYS GLY LEU ASN GLY
SEQRES 6 A 85 GLN LYS PRO LEU GLY ALA ALA GLU PRO ILE THR VAL LYS
SEQRES 7 A 85 PHE ALA ASN ASN PRO SER GLN
HELIX 1 1 SER A 14 GLN A 24 1 11
HELIX 2 2 LYS A 52 ASN A 64 1 13
SHEET 1 A 4 ILE A 28 LEU A 34 0
SHEET 2 A 4 VAL A 45 PHE A 50 -1 N VAL A 45 O LEU A 34
SHEET 3 A 4 TYR A 5 SER A 7 -1 N VAL A 6 O GLY A 46
SHEET 4 A 4 THR A 76 LYS A 78 -1 O THR A 76 N SER A 7
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
Complete list - 16 20 Bytes