Header list of 1i25.pdb file
Complete list - 29 20 Bytes
HEADER TOXIN 06-FEB-01 1I25
TITLE THREE DIMENSIONAL SOLUTION STRUCTURE OF HUWENTOXIN-II BY 2D 1H-NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUWENTOXIN-II;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HWTX-II
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORNITHOCTONUS HUWENA;
SOURCE 3 ORGANISM_COMMON: CHINESE EARTH TIGER;
SOURCE 4 ORGANISM_TAXID: 29017;
SOURCE 5 ORGAN: VENOM GLAND;
SOURCE 6 OTHER_DETAILS: VENOM
KEYWDS NEUROTOXIN, INSECTICIDAL TOXIN, DISULFIDE BONDS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Q.SHU,S.Y.LU,X.C.GU,S.P.LIANG
REVDAT 4 29-NOV-17 1I25 1 REMARK HELIX
REVDAT 3 24-FEB-09 1I25 1 VERSN
REVDAT 2 05-APR-05 1I25 1 JRNL
REVDAT 1 14-FEB-01 1I25 0
JRNL AUTH Q.SHU,S.Y.LU,X.C.GU,S.P.LIANG
JRNL TITL THE STRUCTURE OF SPIDER TOXIN HUWENTOXIN-II WITH UNIQUE
JRNL TITL 2 DISULFIDE LINKAGE: EVIDENCE FOR STRUCTURAL EVOLUTION.
JRNL REF PROTEIN SCI. V. 11 245 2002
JRNL REFN ISSN 0961-8368
JRNL PMID 11790834
JRNL DOI 10.1110/PS.30502
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Q.SHU,S.Y.LU,X.C.GU,S.P.LIANG
REMARK 1 TITL SEQUENCE-SPECIFIC ASSIGNMENT OF 1H-NMR RESONANCE AND
REMARK 1 TITL 2 DETERMINATION OF THE SECONDARY STRUCTURE OF HWTX-II
REMARK 1 REF ACTA BIOCHIM.BIOPHYS.SINICA V. 33 65 2001
REMARK 1 REFN ISSN 0582-9879
REMARK 1 REFERENCE 2
REMARK 1 AUTH Q.SHU,R.H.HUANG,S.P.LIANG
REMARK 1 TITL ASSIGNMENT OF DISULFIDE BONDS OF HUWENTOXIN-II BY EDMAN
REMARK 1 TITL 2 DEGRADATION SEQUENCING AND STEPWISE THIOL MODIFICATION
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 3
REMARK 1 AUTH Q.SHU,S.P.LIANG
REMARK 1 TITL PURIFICATION AND CHARACTERIZATION OF HUWENTOXIN-II, A
REMARK 1 TITL 2 NEUROTOXIC PEPTIDE FROM THE VENOM OF THE CHINESE BIRD SPIDER
REMARK 1 TITL 3 SELENOCOSMIA HUWENA
REMARK 1 REF J.PEPT.RES. V. 53 486 1999
REMARK 1 REFN ISSN 1397-002X
REMARK 1 DOI 10.1034/J.1399-3011.1999.00039.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98.0, X-PLOR 3.851
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS, INC. (FELIX), BRUNGER (X
REMARK 3 -PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 592 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 16 DIHEDRAL ANGEL RESTRAINTS AND
REMARK 3 9 FAKE DISTANCE RESTRAINTS FROM DISULFIDE BONDS.
REMARK 4
REMARK 4 1I25 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012808.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 290
REMARK 210 PH : 5.4; 5.4
REMARK 210 IONIC STRENGTH : 20; NULL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 4 MM HUWENTOXIN-II; 20 MMOL/L
REMARK 210 PHOSPHATE BUFFER; 90%H2O , 10%
REMARK 210 D2O; 4 MM HUWENTOXIN-II; 20 MMOL/
REMARK 210 L PHOSPHATE BUFFER; 100%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR 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: 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 GLU A 11 42.56 -91.93
REMARK 500 1 LYS A 30 -148.07 -102.77
REMARK 500 1 ASN A 32 32.87 -142.27
REMARK 500 2 MET A 33 -166.36 -161.14
REMARK 500 3 GLU A 11 49.09 -89.48
REMARK 500 3 LYS A 30 -152.75 -88.39
REMARK 500 3 ASN A 32 36.54 -146.48
REMARK 500 4 LYS A 30 -155.86 -80.86
REMARK 500 5 PHE A 6 -45.54 -147.14
REMARK 500 5 GLU A 11 32.47 -92.52
REMARK 500 5 LYS A 30 -152.58 -92.95
REMARK 500 5 ASN A 32 30.95 -149.66
REMARK 500 6 GLU A 11 48.59 -103.29
REMARK 500 6 ASP A 15 46.17 -140.09
REMARK 500 6 LYS A 30 -153.19 -83.43
REMARK 500 6 ASN A 32 33.35 -152.47
REMARK 500 7 GLU A 11 40.07 -97.71
REMARK 500 7 LYS A 30 -147.54 -92.42
REMARK 500 7 ASN A 32 37.67 -143.11
REMARK 500 8 CYS A 23 -167.49 -101.83
REMARK 500 8 LYS A 30 -118.08 -92.37
REMARK 500 8 ASN A 32 39.26 -146.99
REMARK 500 9 LYS A 30 -147.97 -104.59
REMARK 500 9 ASN A 32 33.96 -148.97
REMARK 500 10 PHE A 2 -138.82 -89.98
REMARK 500 10 GLU A 11 37.02 -92.65
REMARK 500 10 GLU A 13 38.86 -98.31
REMARK 500 10 LYS A 30 -148.47 -106.62
REMARK 500 10 ASN A 32 39.08 -154.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 750
REMARK 750 TURN
REMARK 750 DETERMINATION METHOD: AUTHOR-DETERMINED
DBREF 1I25 A 1 37 UNP P82959 TXH21_ORNHU 49 85
SEQRES 1 A 37 LEU PHE GLU CYS SER PHE SER CYS GLU ILE GLU LYS GLU
SEQRES 2 A 37 GLY ASP LYS PRO CYS LYS LYS LYS LYS CYS LYS GLY GLY
SEQRES 3 A 37 TRP LYS CYS LYS PHE ASN MET CYS VAL LYS VAL
SHEET 1 A 2 TRP A 27 CYS A 29 0
SHEET 2 A 2 CYS A 34 LYS A 36 -1 O VAL A 35 N LYS A 28
SSBOND 1 CYS A 4 CYS A 18 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 29 1555 1555 2.02
SSBOND 3 CYS A 23 CYS A 34 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 - 29 20 Bytes