Header list of 1axh.pdb file
Complete list - 3 20 Bytes
HEADER NEUROTOXIN 04-NOV-96 1AXH
TITLE ATRACOTOXIN-HVI FROM HADRONYCHE VERSUTA (AUSTRALIAN FUNNEL-WEB SPIDER,
TITLE 2 NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATRACOTOXIN-HVI;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACTX-HVI;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HADRONYCHE VERSUTA;
SOURCE 3 ORGANISM_TAXID: 6904
KEYWDS NEUROTOXIN, INSECTICIDAL TOXIN, CYSTINE KNOT, FUNNEL-WEB
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.I.FLETCHER,S.I.O'DONOGHUE,M.NILGES,G.F.KING
REVDAT 5 03-FEB-21 1AXH 1 JRNL
REVDAT 4 29-NOV-17 1AXH 1 REMARK HELIX
REVDAT 3 24-FEB-09 1AXH 1 VERSN
REVDAT 2 01-APR-03 1AXH 1 JRNL
REVDAT 1 12-NOV-97 1AXH 0
JRNL AUTH J.I.FLETCHER,R.SMITH,S.I.O'DONOGHUE,M.NILGES,M.CONNOR,
JRNL AUTH 2 M.E.HOWDEN,M.J.CHRISTIE,G.F.KING
JRNL TITL THE STRUCTURE OF A NOVEL INSECTICIDAL NEUROTOXIN,
JRNL TITL 2 OMEGA-ATRACOTOXIN-HV1, FROM THE VENOM OF AN AUSTRALIAN
JRNL TITL 3 FUNNEL WEB SPIDER.
JRNL REF NAT.STRUCT.BIOL. V. 4 559 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9228949
JRNL DOI 10.1038/NSB0797-559
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.K.ATKINSON,M.I.TYLER,E.J.VONARX,M.E.H.HOWDEN
REMARK 1 TITL INSECTICIDAL TOXINS DERIVED FROM FUNNEL WEB (ATRAX OR
REMARK 1 TITL 2 HADRONYCHE) SPIDERS
REMARK 1 REF PATENT 1993
REMARK 1 PUBL GENEVA : WORLD INTELLECTUAL PROPERTY ORGANIZATION
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: INITIAL STRUCTURES (5000) WERE
REMARK 3 CALCULATED USING THE DISTANCE GEOMETRY PROGRAMME DIANA, USING A
REMARK 3 SINGLE CYCLE OF REDUNDANT DIHEDRAL ANGLE RESTRAINTS [GUNTERT, P.
REMARK 3 AND WUTHRICH, K. (1991) J. BIOMOL. NMR 1, 447-456]. THE 100
REMARK 3 STRUCTURES WITH LOWEST RESIDUAL RESTRAINT VIOLATIONS WERE THEN
REMARK 3 REFINED USING DYNAMICAL SIMULATED ANNEALING [NILGES, M. CLORE,
REMARK 3 G.M. AND GRONENBORN, A.M. (1988) FEBS LETT. 229, 317-324] IN X-
REMARK 3 PLOR. STRUCTURES WERE CALCULATED USING 419 NON-REDUNDANT
REMARK 3 INTERPROTON DISTANCE RESTRAINTS, 43 DIHEDRAL-ANGLE RESTRAINTS
REMARK 3 (27 PHI, 16 CHI1), AND 28 RESTRAINTS DEFINING 14 HYDROGEN BONDS,
REMARK 3 GIVING AN AVERAGE OF 13.2 RESTRAINTS/RESIDUE. THE ATOMIC RMS
REMARK 3 DIFFERENCES FOR RESIDUES 4 - 37 OF THE FINAL FAMILY OF 20
REMARK 3 CONFORMERS WITH RESPECT TO THE MEAN COORDINATE POSITIONS ARE
REMARK 3 0.22 /- 0.06 AND 0.62 +/- 0.08 ANGSTROMS FOR THE BACKBONE AND
REMARK 3 HEAVY ATOMS, RESPECTIVELY. THE CORRESPONDING PAIRWISE RMS
REMARK 3 DIFFERENCES ARE 0.31 +/- 0.07 AND 0.90 +/- 0.12 ANGSTROMS.
REMARK 3 RESIDUES 1 - 3 ARE DISORDERED. THE DEPOSITED STRUCTURES HAVE
REMARK 3 BEEN SUPERIMPOSED FOR MINIMUM RMSD OVER THE HEAVY ATOMS OF THE
REMARK 3 MEAN COORDINATE STRUCTURE. THE FIRST STRUCTURE IS THAT WITH THE
REMARK 3 LOWEST OVERALL ENERGY IN THE SIMPLIFIED ALL-HYDROGEN CHARMM
REMARK 3 FORCE FIELD AS IMPLEMENTED IN X-PLOR.
REMARK 4
REMARK 4 1AXH 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_1000171375.
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 : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY; ECOSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : 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 : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESIDUAL RESTRAINT
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: 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 1 THR A 3 -154.86 -103.75
REMARK 500 3 THR A 3 -48.38 -136.45
REMARK 500 4 THR A 3 -49.40 -156.02
REMARK 500 4 ARG A 35 -169.42 -126.45
REMARK 500 6 THR A 3 -160.04 -128.97
REMARK 500 6 ARG A 35 -169.79 -110.14
REMARK 500 7 THR A 3 -157.12 -95.25
REMARK 500 7 ARG A 35 -169.45 -117.81
REMARK 500 8 ARG A 35 -168.50 -114.04
REMARK 500 9 THR A 3 -86.90 -126.81
REMARK 500 10 THR A 3 -89.46 -124.79
REMARK 500 10 CYS A 4 151.25 -48.30
REMARK 500 11 THR A 3 -48.59 -134.54
REMARK 500 11 ARG A 35 -169.68 -112.36
REMARK 500 12 THR A 3 -152.15 -148.22
REMARK 500 12 CYS A 4 150.83 -47.54
REMARK 500 13 THR A 3 -153.61 -153.11
REMARK 500 13 CYS A 4 150.84 -44.81
REMARK 500 15 THR A 3 -154.05 -141.74
REMARK 500 15 ASN A 27 -169.38 -105.95
REMARK 500 16 THR A 3 -154.87 -130.71
REMARK 500 16 ARG A 35 -169.14 -120.04
REMARK 500 17 THR A 3 -155.42 -133.89
REMARK 500 18 THR A 3 -49.94 -157.45
REMARK 500 19 THR A 3 -153.55 -81.94
REMARK 500 19 CYS A 4 154.07 -46.95
REMARK 500 20 THR A 3 -156.37 -126.59
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 2 ARG A 35 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AXH A 1 37 UNP P56207 TOT1A_HADVE 1 37
SEQRES 1 A 37 SER PRO THR CYS ILE PRO SER GLY GLN PRO CYS PRO TYR
SEQRES 2 A 37 ASN GLU ASN CYS CYS SER GLN SER CYS THR PHE LYS GLU
SEQRES 3 A 37 ASN GLU ASN GLY ASN THR VAL LYS ARG CYS ASP
HELIX 1 1 TYR A 13 ASN A 16 5 4
SHEET 1 B1 2 CYS A 22 GLU A 26 0
SHEET 2 B1 2 THR A 32 CYS A 36 -1
SSBOND 1 CYS A 4 CYS A 18 1555 1555 2.02
SSBOND 2 CYS A 11 CYS A 22 1555 1555 2.02
SSBOND 3 CYS A 17 CYS A 36 1555 1555 2.02
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 - 3 20 Bytes