Header list of 1fw5.pdb file
Complete list - 23 202 Bytes
HEADER VIRAL PROTEIN 21-SEP-00 1FW5
TITLE SOLUTION STRUCTURE OF MEMBRANE BINDING PEPTIDE OF SEMLIKI FOREST VIRUS
TITLE 2 MRNA CAPPING ENZYME NSP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NONSTRUCTURAL PROTEIN NSP1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 245-364 OF NSP1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN SEMLIKI FOREST VIRUS (SFV).
KEYWDS VIRAL PROTEIN
EXPDTA SOLUTION NMR
AUTHOR A.LAMPIO,I.KILPELINEN,S.PESONEN,K.KARHI,P.AUVINEN,P.SOMERHARJU,
AUTHOR 2 L.KRIINEN
REVDAT 3 23-FEB-22 1FW5 1 REMARK
REVDAT 2 24-FEB-09 1FW5 1 VERSN
REVDAT 1 21-SEP-01 1FW5 0
JRNL AUTH A.LAMPIO,I.KILPELAINEN,S.PESONEN,K.KARHI,P.AUVINEN,
JRNL AUTH 2 P.SOMERHARJU,L.KAARIAINEN
JRNL TITL MEMBRANE BINDING MECHANISM OF AN RNA VIRUS-CAPPING ENZYME.
JRNL REF J.BIOL.CHEM. V. 275 37853 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 10984480
JRNL DOI 10.1074/JBC.M004865200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FW5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000011953.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
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: 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: 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 O LEU A 12 HD1 HIS A 16 1.31
REMARK 500 O SER A 2 H THR A 6 1.48
REMARK 500 O GLY A 1 H TYR A 5 1.53
REMARK 500 O LEU A 12 ND1 HIS A 16 2.03
REMARK 500 O TRP A 15 N LEU A 17 2.06
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 THR A 3 -57.08 -26.87
REMARK 500 HIS A 16 -6.63 -38.87
REMARK 500 LEU A 17 -66.31 -10.27
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FW5 A 1 20 UNP P08411 POLN_SFV 245 264
SEQRES 1 A 20 GLY SER THR LEU TYR THR GLU SER ARG LYS LEU LEU ARG
SEQRES 2 A 20 SER TRP HIS LEU PRO SER VAL
HELIX 1 1 GLY A 1 HIS A 16 1 16
CRYST1 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 - 23 202 Bytes