Header list of 1d8z.pdb file
Complete list - 16 20 Bytes
HEADER RNA BINDING PROTEIN 26-OCT-99 1D8Z
TITLE SOLUTION STRUCTURE OF THE FIRST RNA-BINDING DOMAIN (RBD1) OF HU
TITLE 2 ANTIGEN C (HUC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HU ANTIGEN C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST RNA-BINDING DOMAIN (RBD1);
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 1D8Z 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1D8Z 1 VERSN
REVDAT 1 07-APR-00 1D8Z 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 1D8Z 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_1000009903.
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 SER A 2 -48.80 -159.07
REMARK 500 LYS A 3 89.79 61.75
REMARK 500 THR A 4 71.48 -118.40
REMARK 500 THR A 16 -154.79 -157.89
REMARK 500 SER A 26 42.64 -90.02
REMARK 500 ILE A 27 -39.08 -141.20
REMARK 500 ILE A 30 90.49 -55.11
REMARK 500 GLU A 31 -29.66 -37.11
REMARK 500 SER A 32 115.70 -172.65
REMARK 500 LYS A 34 71.36 -175.41
REMARK 500 ASP A 38 161.83 -43.71
REMARK 500 ILE A 40 -91.65 -111.72
REMARK 500 TYR A 47 143.56 -179.09
REMARK 500 THR A 64 -31.58 -133.29
REMARK 500 THR A 72 21.42 -154.56
REMARK 500 SER A 83 161.05 -48.70
REMARK 500 ALA A 85 62.82 67.58
REMARK 500 ILE A 87 -62.70 -142.90
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 37 0.32 SIDE CHAIN
REMARK 500 ARG A 81 0.30 SIDE CHAIN
REMARK 500 ARG A 88 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D9A RELATED DB: PDB
REMARK 900 SECOND RNA-BINDING DOMAIN (RBD1) OF HUC
REMARK 900 RELATED ID: TRT001000201.1 RELATED DB: TARGETDB
DBREF 1D8Z A 1 88 UNP Q60900 ELAV3_MOUSE 36 123
SEQADV 1D8Z MET A 0 UNP Q60900 ASP 35 CONFLICT
SEQRES 1 A 89 MET ASP SER LYS THR ASN LEU ILE VAL ASN TYR LEU PRO
SEQRES 2 A 89 GLN ASN MET THR GLN ASP GLU PHE LYS SER LEU PHE GLY
SEQRES 3 A 89 SER ILE GLY ASP ILE GLU SER CYS LYS LEU VAL ARG ASP
SEQRES 4 A 89 LYS ILE THR GLY GLN SER LEU GLY TYR GLY PHE VAL ASN
SEQRES 5 A 89 TYR SER ASP PRO ASN ASP ALA ASP LYS ALA ILE ASN THR
SEQRES 6 A 89 LEU ASN GLY LEU LYS LEU GLN THR LYS THR ILE LYS VAL
SEQRES 7 A 89 SER TYR ALA ARG PRO SER SER ALA SER ILE ARG
HELIX 1 1 THR A 16 SER A 26 1 11
HELIX 2 2 ASP A 54 ASN A 66 1 13
SHEET 1 A 5 SER A 32 LEU A 35 0
SHEET 2 A 5 TYR A 47 ASN A 51 -1 O PHE A 49 N LYS A 34
SHEET 3 A 5 LEU A 6 ASN A 9 -1 N LEU A 6 O VAL A 50
SHEET 4 A 5 THR A 74 SER A 78 -1 N LYS A 76 O ASN A 9
SHEET 5 A 5 LEU A 68 LYS A 69 -1 O LEU A 68 N ILE A 75
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