Header list of 1tch.pdb file
Complete list - 29 201 Bytes
HEADER NEUROTOXIN 12-DEC-92 1TCH
TITLE STRUCTURE-ACTIVITY RELATIONSHIPS OF MU-CONOTOXIN GIIIA: STRUCTURE
TITLE 2 DETERMINATION OF ACTIVE AND INACTIVE SODIUM CHANNEL BLOCKER PEPTIDES
TITLE 3 BY NMR AND SIMULATED ANNEALING CALCULATIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MU-CONOTOXIN GIIIA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1
KEYWDS NEUROTOXIN
EXPDTA SOLUTION NMR
AUTHOR J.-M.LANCELIN,D.KOHDA,F.INAGAKI
REVDAT 4 29-NOV-17 1TCH 1 REMARK HELIX
REVDAT 3 24-FEB-09 1TCH 1 VERSN
REVDAT 2 01-APR-03 1TCH 1 JRNL
REVDAT 1 31-JAN-94 1TCH 0
JRNL AUTH K.WAKAMATSU,D.KOHDA,H.HATANAKA,J.M.LANCELIN,Y.ISHIDA,M.OYA,
JRNL AUTH 2 H.NAKAMURA,F.INAGAKI,K.SATO
JRNL TITL STRUCTURE-ACTIVITY RELATIONSHIPS OF MU-CONOTOXIN GIIIA:
JRNL TITL 2 STRUCTURE DETERMINATION OF ACTIVE AND INACTIVE SODIUM
JRNL TITL 3 CHANNEL BLOCKER PEPTIDES BY NMR AND SIMULATED ANNEALING
JRNL TITL 4 CALCULATIONS.
JRNL REF BIOCHEMISTRY V. 31 12577 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1335283
JRNL DOI 10.1021/BI00165A006
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.-M.LANCELIN,D.KOHDA,S.-I.TATE,Y.YANAGAWA,T.ABE,M.SATAKE,
REMARK 1 AUTH 2 F.INAGAKI
REMARK 1 TITL TERTIARY STRUCTURE OF CONOTOXIN GIIIA IN AQUEOUS SOLUTION
REMARK 1 REF BIOCHEMISTRY V. 30 6908 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.SATO,Y.ISHIDA,K.WAKAMATSU,R.KATO,H.HONDA,Y.OHIZUMI,
REMARK 1 AUTH 2 H.NAKAMURA,M.OHYA,J.-M.LANCELIN,D.KOHDA,F.INAGAKI
REMARK 1 TITL ACTIVE SITE OF MU-CONOTOXIN GIIIA, A PEPTIDE BLOCKER OF
REMARK 1 TITL 2 MUSCLE SODIUM CHANNELS
REMARK 1 REF J.BIOL.CHEM. V. 266 16989 1991
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 2.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TCH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176614.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : 1
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 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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 9 CB - CG - CD ANGL. DEV. = 17.6 DEGREES
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 ASP A 12 -178.70 -67.85
REMARK 500 GLN A 14 -1.35 -54.58
REMARK 500 CYS A 21 -56.99 -152.00
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 ARG A 1 0.26 SIDE CHAIN
REMARK 500 ARG A 19 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 23
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TCK RELATED DB: PDB
DBREF 1TCH A 1 22 UNP P01523 CXM1_CONGE 1 22
SEQADV 1TCH HYP A 6 UNP P01523 PRO 6 CONFLICT
SEQADV 1TCH HYP A 7 UNP P01523 PRO 7 CONFLICT
SEQADV 1TCH ALA A 13 UNP P01523 ARG 13 CONFLICT
SEQADV 1TCH HYP A 17 UNP P01523 PRO 17 CONFLICT
SEQRES 1 A 23 ARG ASP CYS CYS THR HYP HYP LYS LYS CYS LYS ASP ALA
SEQRES 2 A 23 GLN CYS LYS HYP GLN ARG CYS CYS ALA NH2
MODRES 1TCH HYP A 6 PRO 4-HYDROXYPROLINE
MODRES 1TCH HYP A 7 PRO 4-HYDROXYPROLINE
MODRES 1TCH HYP A 17 PRO 4-HYDROXYPROLINE
HET HYP A 6 15
HET HYP A 7 15
HET HYP A 17 15
HET NH2 A 23 3
HETNAM HYP 4-HYDROXYPROLINE
HETNAM NH2 AMINO GROUP
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP 3(C5 H9 N O3)
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 3 CYS A 15 1555 1555 2.02
SSBOND 2 CYS A 4 CYS A 20 1555 1555 2.02
SSBOND 3 CYS A 10 CYS A 21 1555 1555 2.02
LINK C ALA A 22 N NH2 A 23 1555 1555 1.31
LINK C THR A 5 N HYP A 6 1555 1555 1.32
LINK C HYP A 6 N HYP A 7 1555 1555 1.33
LINK C HYP A 7 N LYS A 8 1555 1555 1.30
LINK C LYS A 16 N HYP A 17 1555 1555 1.32
LINK C HYP A 17 N GLN A 18 1555 1555 1.30
CISPEP 1 HYP A 6 HYP A 7 0 -1.65
SITE 1 AC1 1 ALA A 22
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
Complete list - 29 201 Bytes