Header list of 1ns1.pdb file
Complete list - b 23 2 Bytes
HEADER NONSTRUCTURAL PROTEIN 02-OCT-97 1NS1
TITLE RNA-BINDING DOMAIN OF NON-STRUCTURAL PROTEIN 1 FROM INFLUENZA VIRUS,
TITLE 2 NMR, 16 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NONSTRUCTURAL PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RNA-BINDING DOMAIN, RESIDUES 1 - 73;
COMPND 5 SYNONYM: NS1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE 3 ORGANISM_TAXID: 11320;
SOURCE 4 STRAIN: UDORN/307/72;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 GENE: J02169;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A-NS1A(1-73)CC
KEYWDS NONSTRUCTURAL PROTEIN, RNA-BINDING, SSRNA-BINDING, DSRNA-BINDING,
KEYWDS 2 POLYA-RNA-BINDING, DIMERIC SIX HELICAL STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR G.T.MONTELIONE,C.-Y.CHIEN,R.TEJERO
REVDAT 3 23-FEB-22 1NS1 1 REMARK
REVDAT 2 24-FEB-09 1NS1 1 VERSN
REVDAT 1 14-JAN-98 1NS1 0
JRNL AUTH C.Y.CHIEN,R.TEJERO,Y.HUANG,D.E.ZIMMERMAN,C.B.RIOS,R.M.KRUG,
JRNL AUTH 2 G.T.MONTELIONE
JRNL TITL A NOVEL RNA-BINDING MOTIF IN INFLUENZA A VIRUS
JRNL TITL 2 NON-STRUCTURAL PROTEIN 1.
JRNL REF NAT.STRUCT.BIOL. V. 4 891 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9360601
JRNL DOI 10.1038/NSB1197-891
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.Y.QIAN,C.Y.CHIEN,Y.LU,G.T.MONTELIONE,R.M.KRUG
REMARK 1 TITL AN AMINO-TERMINAL POLYPEPTIDE FRAGMENT OF THE INFLUENZA
REMARK 1 TITL 2 VIRUS NS1 PROTEIN POSSESSES SPECIFIC RNA-BINDING ACTIVITY
REMARK 1 TITL 3 AND LARGELY HELICAL BACKBONE STRUCTURE
REMARK 1 REF RNA V. 1 948 1995
REMARK 1 REFN ISSN 1355-8382
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA
REMARK 3 AUTHORS : WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1NS1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175379.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : MD-TRIPLE RESONANCE NMR
REMARK 210 EXPERIMENTS; MD-NOESY
REMARK 210 EXPERIMENTS; H/D EXCHANGE
REMARK 210 EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA
REMARK 210 METHOD USED : VARIABLE TARGET FUNCTION
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESIDUAL CONSTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
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 30 -44.26 172.97
REMARK 500 1 GLU A 72 97.08 -170.27
REMARK 500 1 ALA B 30 -44.10 172.82
REMARK 500 1 GLU B 72 97.02 -170.02
REMARK 500 2 ALA A 30 -44.49 173.71
REMARK 500 2 GLU A 72 97.33 -170.87
REMARK 500 2 ALA B 30 -44.41 174.22
REMARK 500 2 GLU B 72 97.28 -170.76
REMARK 500 3 ALA A 30 -44.46 174.04
REMARK 500 3 GLU A 72 97.18 -170.47
REMARK 500 3 ALA B 30 -44.15 173.70
REMARK 500 3 GLU B 72 97.07 -170.20
REMARK 500 4 ALA A 30 -44.36 173.54
REMARK 500 4 GLU A 72 97.26 -170.85
REMARK 500 4 ALA B 30 -44.31 175.16
REMARK 500 4 GLU B 72 97.25 -170.62
REMARK 500 5 ASP A 2 -155.95 60.58
REMARK 500 5 SER A 3 42.63 -149.20
REMARK 500 5 ASP A 24 -6.78 -59.95
REMARK 500 5 GLU A 26 39.73 35.44
REMARK 500 5 ASP A 29 -58.78 -146.89
REMARK 500 5 ALA A 30 -40.22 172.25
REMARK 500 5 ARG A 44 -39.04 -38.90
REMARK 500 5 GLU A 72 -94.78 -100.08
REMARK 500 5 ASP B 2 -152.76 60.90
REMARK 500 5 SER B 3 40.75 -146.01
REMARK 500 5 ASP B 24 -7.48 -59.97
REMARK 500 5 GLU B 26 39.77 35.79
REMARK 500 5 ASP B 29 -58.44 -145.92
REMARK 500 5 ALA B 30 -39.67 171.94
REMARK 500 5 GLU B 72 -94.57 -100.58
REMARK 500 6 ASP A 2 -97.67 52.54
REMARK 500 6 SER A 3 -85.82 155.93
REMARK 500 6 ASP A 29 -48.04 -137.85
REMARK 500 6 ALA A 30 -41.25 168.57
REMARK 500 6 LEU A 52 -120.68 -90.33
REMARK 500 6 ASN A 53 97.96 -166.94
REMARK 500 6 ILE A 54 -38.25 -39.73
REMARK 500 6 GLU A 72 94.25 -166.15
REMARK 500 6 ASP B 2 -96.71 51.47
REMARK 500 6 SER B 3 -86.36 155.86
REMARK 500 6 ASP B 29 -47.68 -137.27
REMARK 500 6 ALA B 30 -41.51 168.28
REMARK 500 6 LEU B 52 -118.93 -91.23
REMARK 500 6 ASN B 53 98.75 -164.02
REMARK 500 6 GLU B 72 94.99 -166.30
REMARK 500 7 ASP A 2 -152.63 61.54
REMARK 500 7 SER A 3 53.69 -142.69
REMARK 500 7 GLU A 26 40.91 35.65
REMARK 500 7 ASP A 29 -64.54 -151.57
REMARK 500
REMARK 500 THIS ENTRY HAS 203 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NS1 A 1 73 UNP P03495 VNS1_IAUDO 1 73
DBREF 1NS1 B 1 73 UNP P03495 VNS1_IAUDO 1 73
SEQRES 1 A 73 MET ASP SER ASN THR VAL SER SER PHE GLN VAL ASP CYS
SEQRES 2 A 73 PHE LEU TRP HIS VAL ARG LYS GLN VAL VAL ASP GLN GLU
SEQRES 3 A 73 LEU GLY ASP ALA PRO PHE LEU ASP ARG LEU ARG ARG ASP
SEQRES 4 A 73 GLN LYS SER LEU ARG GLY ARG GLY SER THR LEU GLY LEU
SEQRES 5 A 73 ASN ILE GLU ALA ALA THR HIS VAL GLY LYS GLN ILE VAL
SEQRES 6 A 73 GLU LYS ILE LEU LYS GLU GLU SER
SEQRES 1 B 73 MET ASP SER ASN THR VAL SER SER PHE GLN VAL ASP CYS
SEQRES 2 B 73 PHE LEU TRP HIS VAL ARG LYS GLN VAL VAL ASP GLN GLU
SEQRES 3 B 73 LEU GLY ASP ALA PRO PHE LEU ASP ARG LEU ARG ARG ASP
SEQRES 4 B 73 GLN LYS SER LEU ARG GLY ARG GLY SER THR LEU GLY LEU
SEQRES 5 B 73 ASN ILE GLU ALA ALA THR HIS VAL GLY LYS GLN ILE VAL
SEQRES 6 B 73 GLU LYS ILE LEU LYS GLU GLU SER
HELIX 1 H1 THR A 5 ASP A 24 1 20
HELIX 2 H2 PRO A 31 THR A 49 1 19
HELIX 3 H3 ILE A 54 LYS A 70 1 17
HELIX 4 H4 THR B 5 ASP B 24 1 20
HELIX 5 H5 PRO B 31 THR B 49 1 19
HELIX 6 H6 ILE B 54 LYS B 70 1 17
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 - b 23 2 Bytes