Header list of 1i6f.pdb file
Complete list - 23 202 Bytes
HEADER TOXIN 02-MAR-01 1I6F
TITLE NMR SOLUTION STRUCTURE OF THE INSECT-SPECIFIC NEUROTOXIN VARIANT 5
TITLE 2 (CSE-V5) FROM THE SCORPION CENTRUROIDES SCULPTURATUS EWING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROTOXIN V-5;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CSE-V5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CENTRUROIDES SCULPTURATUS;
SOURCE 3 ORGANISM_COMMON: BARK SCORPION;
SOURCE 4 ORGANISM_TAXID: 218467;
SOURCE 5 VARIANT: 5
KEYWDS SCORPION, NEUROTOXIN, SODIUM CHANNEL, ALPHA HELIX, BETA SHEET,
KEYWDS 2 DISULFIDE LINKAGES, TOXIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR M.J.JABLONSKY,P.L.JACKSON,N.R.KRISHNA
REVDAT 3 23-FEB-22 1I6F 1 REMARK
REVDAT 2 24-FEB-09 1I6F 1 VERSN
REVDAT 1 01-AUG-01 1I6F 0
JRNL AUTH M.J.JABLONSKY,P.L.JACKSON,N.R.KRISHNA
JRNL TITL SOLUTION STRUCTURE OF AN INSECT-SPECIFIC NEUROTOXIN FROM THE
JRNL TITL 2 NEW WORLD SCORPION CENTRUROIDES SCULPTURATUS EWING.
JRNL REF BIOCHEMISTRY V. 40 8273 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11444973
JRNL DOI 10.1021/BI010223H
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISNMR DISR88, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (DISNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1010
REMARK 3 TOTAL RESTRAINTS: 849 DISTANCE,
REMARK 3 70 H-BONDS, 91 DIHEDRAL ANGLE
REMARK 4
REMARK 4 1I6F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000012962.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM CSE-V5, PH 4.0; 1MM CSE-V5,
REMARK 210 PH 4.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AM
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 9.80
REMARK 210 METHOD USED : DISTANCE GEOMETRY 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: THIS STRUCTURE WAS DETERMINED USING STANDARD HOMONUCLEAR
REMARK 210 2D-NMR 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: 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 H3 LYS A 1 O LEU A 45 1.59
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 MET A 38 14.49 59.29
REMARK 500 ASP A 53 30.51 -92.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NRB RELATED DB: PDB
REMARK 900 NEUROTOXIN CSE-V
REMARK 900 RELATED ID: 1B3C RELATED DB: PDB
REMARK 900 NEUROTOXIN CSE-I
REMARK 900 RELATED ID: 1I6G RELATED DB: PDB
REMARK 900 NEUROTOXIN CSE-V5, 20 CONFORMERS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS HAVE FOUND THAT THE PREVIOUSLY PUBLISHED
REMARK 999 SEQUENCE (PIR C23727) WAS INCORRECT. THEY HAVE
REMARK 999 DEMONSTRATED THE EXISTENCE OF AN ADDITIONAL GLY, 60,
REMARK 999 FROM SEQUENCING, NMR, AND MASS SPEC. (DATA INCLUDED
REMARK 999 IN THE PRIMARY CITATION ARTICLE).
DBREF 1I6F A 1 59 UNP P58779 SCX5_CENSC 1 59
SEQADV 1I6F GLY A 60 UNP P58779 SEE REMARK 999
SEQRES 1 A 60 LYS ASP GLY TYR PRO VAL ASP SER LYS GLY CYS LYS LEU
SEQRES 2 A 60 SER CYS VAL ALA ASN ASN TYR CYS ASP ASN GLN CYS LYS
SEQRES 3 A 60 MET LYS LYS ALA SER GLY GLY HIS CYS TYR ALA MET SER
SEQRES 4 A 60 CYS TYR CYS GLU GLY LEU PRO GLU ASN ALA LYS VAL SER
SEQRES 5 A 60 ASP SER ALA THR ASN ILE CYS GLY
HELIX 1 1 ALA A 17 LYS A 28 1 12
SHEET 1 A 4 HIS A 34 TYR A 36 0
SHEET 2 A 4 SER A 39 GLU A 43 -1 N SER A 39 O TYR A 36
SHEET 3 A 4 ASP A 2 PRO A 5 -1 O GLY A 3 N CYS A 42
SHEET 4 A 4 VAL A 51 SER A 52 -1 N SER A 52 O TYR A 4
SSBOND 1 CYS A 11 CYS A 59 1555 1555 2.02
SSBOND 2 CYS A 15 CYS A 35 1555 1555 2.02
SSBOND 3 CYS A 21 CYS A 40 1555 1555 2.02
SSBOND 4 CYS A 25 CYS A 42 1555 1555 2.02
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