Header list of 1vtx.pdb file
Complete list - v 29 2 Bytes
HEADER NEUROTOXIN 13-MAR-97 1VTX
TITLE DELTA-ATRACOTOXIN-HV1 (VERSUTOXIN) FROM HADRONYCHE VERSUTA, NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA-ATRACOTOXIN-HV1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: VERSUTOXIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HADRONYCHE VERSUTA;
SOURCE 3 ORGANISM_TAXID: 6904;
SOURCE 4 SECRETION: VENOM
KEYWDS NEUROTOXIN, SODIUM CHANNEL TOXIN, CYSTEINE KNOT, VENOM
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.I.FLETCHER,B.E.CHAPMAN,G.F.KING
REVDAT 3 29-NOV-17 1VTX 1 REMARK HELIX
REVDAT 2 24-FEB-09 1VTX 1 VERSN
REVDAT 1 28-JAN-98 1VTX 0
JRNL AUTH J.I.FLETCHER,B.E.CHAPMAN,J.P.MACKAY,M.E.HOWDEN,G.F.KING
JRNL TITL THE STRUCTURE OF VERSUTOXIN (DELTA-ATRACOTOXIN-HV1) PROVIDES
JRNL TITL 2 INSIGHTS INTO THE BINDING OF SITE 3 NEUROTOXINS TO THE
JRNL TITL 3 VOLTAGE-GATED SODIUM CHANNEL.
JRNL REF STRUCTURE V. 5 1525 1997
JRNL REFN ISSN 0969-2126
JRNL PMID 9384567
JRNL DOI 10.1016/S0969-2126(97)00301-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.M.NICHOLSON,M.J.LITTLE,M.TYLER,T.NARAHASHI
REMARK 1 TITL SELECTIVE ALTERATION OF SODIUM CHANNEL GATING BY AUSTRALIAN
REMARK 1 TITL 2 FUNNEL-WEB SPIDER TOXINS
REMARK 1 REF TOXICON V. 34 1443 1996
REMARK 1 REFN ISSN 0041-0101
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.R.BROWN,D.D.SHEUMACK,M.I.TYLER,M.E.HOWDEN
REMARK 1 TITL ERRATUM. AMINO ACID SEQUENCE OF VERSUTOXIN, A LETHAL
REMARK 1 TITL 2 NEUROTOXIN FROM THE VENOM OF THE FUNNEL-WEB SPIDER ATRAX
REMARK 1 TITL 3 VERSUTUS
REMARK 1 REF BIOCHEM.J. V. 257 F.934 1989
REMARK 1 REFN ISSN 0264-6021
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.R.BROWN,D.D.SHEUMACK,M.I.TYLER,M.E.HOWDEN
REMARK 1 TITL AMINO ACID SEQUENCE OF VERSUTOXIN, A LETHAL NEUROTOXIN FROM
REMARK 1 TITL 2 THE VENOM OF THE FUNNEL-WEB SPIDER ATRAX VERSUTUS
REMARK 1 REF BIOCHEM.J. V. 250 401 1988
REMARK 1 REFN ISSN 0264-6021
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE PRIMARY REFERENCE ABOVE. OTHER
REMARK 3 PROGRAM USED DIANA VERSION 2.8 BY GUNTERT.
REMARK 4
REMARK 4 1VTX 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_1000177121.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 2.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQFCOSY; TOCSY; ECOSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX500; AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND DYNAMICAL
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 75
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
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
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 LYS A 10 -179.23 -57.48
REMARK 500 1 GLU A 12 -47.39 -174.03
REMARK 500 1 ASP A 13 153.10 72.31
REMARK 500 1 CYS A 16 147.87 -37.41
REMARK 500 1 ALA A 23 -102.70 -98.81
REMARK 500 1 TRP A 24 -83.26 -152.74
REMARK 500 1 LYS A 41 112.59 -34.45
REMARK 500 2 CYS A 8 -173.35 -66.40
REMARK 500 2 LYS A 10 -73.73 -61.37
REMARK 500 2 THR A 11 -150.80 33.89
REMARK 500 2 ASP A 13 150.48 61.44
REMARK 500 2 CYS A 16 147.41 -38.41
REMARK 500 2 CYS A 20 109.51 -49.11
REMARK 500 2 ALA A 23 -105.29 -118.05
REMARK 500 2 TRP A 24 -79.58 -155.11
REMARK 500 2 LYS A 41 112.60 -38.12
REMARK 500 3 CYS A 8 133.57 -36.15
REMARK 500 3 LYS A 10 -52.78 80.58
REMARK 500 3 GLU A 12 -60.75 -137.31
REMARK 500 3 ASP A 13 134.64 156.86
REMARK 500 3 CYS A 14 175.02 -48.43
REMARK 500 3 CYS A 16 148.32 -36.88
REMARK 500 3 ALA A 23 -102.73 -89.99
REMARK 500 3 TRP A 24 -73.98 -156.51
REMARK 500 3 LYS A 41 114.80 -33.53
REMARK 500 4 CYS A 8 -164.28 -71.42
REMARK 500 4 LYS A 10 -79.31 67.10
REMARK 500 4 GLU A 12 114.40 65.07
REMARK 500 4 ASP A 13 42.82 -87.99
REMARK 500 4 CYS A 14 -176.75 54.25
REMARK 500 4 CYS A 16 149.35 -37.05
REMARK 500 4 ALA A 23 -104.40 -89.70
REMARK 500 4 TRP A 24 -74.71 -153.50
REMARK 500 4 LYS A 41 102.26 -42.28
REMARK 500 5 LYS A 10 -161.96 60.58
REMARK 500 5 THR A 11 -171.42 44.12
REMARK 500 5 ASP A 13 97.34 164.70
REMARK 500 5 CYS A 16 148.34 -37.21
REMARK 500 5 CYS A 20 102.64 -51.99
REMARK 500 5 ALA A 23 -100.84 -111.43
REMARK 500 5 TRP A 24 -76.43 -156.63
REMARK 500 5 LYS A 41 100.08 -33.38
REMARK 500 6 TRP A 7 156.47 -46.28
REMARK 500 6 THR A 11 95.22 64.04
REMARK 500 6 GLU A 12 -44.65 -161.91
REMARK 500 6 ASP A 13 144.87 62.80
REMARK 500 6 CYS A 16 149.54 -38.55
REMARK 500 6 CYS A 20 101.65 -50.39
REMARK 500 6 ALA A 23 -106.23 -119.50
REMARK 500 6 TRP A 24 -65.23 -166.28
REMARK 500
REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VTX A 1 42 UNP P13494 TXDT1_HADVE 1 42
SEQRES 1 A 42 CYS ALA LYS LYS ARG ASN TRP CYS GLY LYS THR GLU ASP
SEQRES 2 A 42 CYS CYS CYS PRO MET LYS CYS VAL TYR ALA TRP TYR ASN
SEQRES 3 A 42 GLU GLN GLY SER CYS GLN SER THR ILE SER ALA LEU TRP
SEQRES 4 A 42 LYS LYS CYS
HELIX 1 H1 ILE A 35 LYS A 41 5 7
SHEET 1 B1 3 ASN A 6 TRP A 7 0
SHEET 2 B1 3 MET A 18 VAL A 21 1
SHEET 3 B1 3 SER A 30 SER A 33 -1
SSBOND 1 CYS A 1 CYS A 15 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 20 1555 1555 2.02
SSBOND 3 CYS A 14 CYS A 31 1555 1555 2.02
SSBOND 4 CYS A 16 CYS A 42 1555 1555 2.02
CISPEP 1 CYS A 16 PRO A 17 1 0.20
CISPEP 2 CYS A 16 PRO A 17 2 0.19
CISPEP 3 CYS A 16 PRO A 17 3 -0.04
CISPEP 4 CYS A 16 PRO A 17 4 -0.22
CISPEP 5 CYS A 16 PRO A 17 5 0.16
CISPEP 6 CYS A 16 PRO A 17 6 -0.27
CISPEP 7 CYS A 16 PRO A 17 7 0.07
CISPEP 8 CYS A 16 PRO A 17 8 -0.12
CISPEP 9 CYS A 16 PRO A 17 9 0.19
CISPEP 10 CYS A 16 PRO A 17 10 -0.01
CISPEP 11 CYS A 16 PRO A 17 11 0.25
CISPEP 12 CYS A 16 PRO A 17 12 0.02
CISPEP 13 CYS A 16 PRO A 17 13 -0.10
CISPEP 14 CYS A 16 PRO A 17 14 0.00
CISPEP 15 CYS A 16 PRO A 17 15 -0.03
CISPEP 16 CYS A 16 PRO A 17 16 -0.06
CISPEP 17 CYS A 16 PRO A 17 17 -0.13
CISPEP 18 CYS A 16 PRO A 17 18 0.24
CISPEP 19 CYS A 16 PRO A 17 19 -0.04
CISPEP 20 CYS A 16 PRO A 17 20 -0.03
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 - v 29 2 Bytes