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HEADER NEUROTOXIN 25-NOV-96 1VIB TITLE NMR SOLUTION STRUCTURE OF THE NEUROTOXIN B-IV, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROTOXIN B-IV; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CEREBRATULUS LACTEUS; SOURCE 3 ORGANISM_COMMON: MILKY RIBBON WORM KEYWDS NEUROTOXIN, TOXIN, HYDROXYLATION EXPDTA NMR, 20 STRUCTURES AUTHOR K.J.BARNHAM,T.R.DYKE,W.R.KEM,R.S.NORTON REVDAT 1 15-MAY-97 1VIB 0 JRNL AUTH K.J.BARNHAM,T.R.DYKE,W.R.KEM,R.S.NORTON JRNL TITL STRUCTURE OF NEUROTOXIN B-IV FROM THE MARINE WORM JRNL TITL 2 CEREBRATULUS LACTEUS: A HELICAL HAIRPIN JRNL TITL 3 CROSS-LINKED BY DISULPHIDE BONDING. JRNL REF J.MOL.BIOL. V. 268 886 1997 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH P.E.HANSEN,W.R.KEM,A.L.BIEBER,R.S.NORTON REMARK 1 TITL 1H-NMR STUDY OF NEUROTOXIN B-IV FROM THE MARINE REMARK 1 TITL 2 WORM CEREBRATULUS LACTEUS. SOLUTION PROPERTIES, REMARK 1 TITL 3 SEQUENCE-SPECIFIC RESONANCE ASSIGNMENTS, SECONDARY REMARK 1 TITL 4 STRUCTURE AND GLOBAL FOLD REMARK 1 REF EUR.J.BIOCHEM. V. 210 231 1992 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 REMARK 1 REFERENCE 2 REMARK 1 AUTH W.R.KEM,C.K.TU,R.W.WILLIAMS,A.TOUMADJE, REMARK 1 AUTH 2 W.C.JOHNSON JUNIOR REMARK 1 TITL CIRCULAR DICHROISM AND LASER RAMAN SPECTROSCOPIC REMARK 1 TITL 2 ANALYSIS OF THE SECONDARY STRUCTURE OF REMARK 1 TITL 3 CEREBRATULUS LACTEUS TOXIN B-IV REMARK 1 REF J.PROTEIN CHEM. V. 9 433 1990 REMARK 1 REFN ASTM JPCHD2 UK ISSN 0277-8033 REMARK 1 REFERENCE 3 REMARK 1 AUTH K.M.BLUMENTHAL,P.S.KEIM,R.L.HEINRIKSON,W.R.KEM REMARK 1 TITL STRUCTURE AND ACTION OF HETERONEMERTINE REMARK 1 TITL 2 POLYPEPTIDE TOXINS. AMINO ACID SEQUENCE OF REMARK 1 TITL 3 CEREBRATULUS LACTEUS TOXIN B-II AND REVISED REMARK 1 TITL 4 STRUCTURE OF TOXIN B-IV REMARK 1 REF J.BIOL.CHEM. V. 256 9063 1981 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 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: NULL REMARK 4 REMARK 4 1VIB COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 295 REMARK 210 PH : 5.0 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 : 20 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 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 M RES CSSEQI PSI PHI REMARK 500 15 TRP A 5 178.59 108.35 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TYR A 9 HYP A 10 1 -148.82 REMARK 500 TYR A 9 HYP A 10 5 -145.65 REMARK 500 TYR A 9 HYP A 10 16 -144.89 DBREF 1VIB A 1 55 UNP P01525 NXB4_CERLA 1 55 SEQADV 1VIB HYP A 10 UNP P01525 PRO 10 CONFLICT SEQRES 1 A 55 ALA SER ALA THR TRP GLY ALA ALA TYR HYP ALA CYS GLU SEQRES 2 A 55 ASN ASN CYS ARG LYS LYS TYR ASP LEU CYS ILE ARG CYS SEQRES 3 A 55 GLN GLY LYS TRP ALA GLY LYS ARG GLY LYS CYS ALA ALA SEQRES 4 A 55 HIS CYS ILE ILE GLN LYS ASN ASN CYS LYS GLY LYS CYS SEQRES 5 A 55 LYS LYS GLU MODRES 1VIB HYP A 10 PRO 4-HYDROXYPROLINE HET HYP A 10 15 HETNAM HYP 4-HYDROXYPROLINE HETSYN HYP HYDROXYPROLINE FORMUL 1 HYP C5 H9 N O3 HELIX 1 1 ALA A 11 CYS A 23 1 13 HELIX 2 2 ARG A 34 LYS A 49 1 16 TURN 1 1 CYS A 23 ARG A 25 INVERSE GAMMA TURN 2 2 ILE A 24 CYS A 26 INVERSE GAMMA TURN 3 3 GLY A 28 ALA A 31 TYPE I TURN 4 4 TRP A 30 LYS A 33 TYPE II SSBOND 1 CYS A 12 CYS A 52 SSBOND 2 CYS A 16 CYS A 48 SSBOND 3 CYS A 23 CYS A 41 SSBOND 4 CYS A 26 CYS A 37 LINK N HYP A 10 C TYR A 9 LINK C HYP A 10 N ALA A 11 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