Header list of 1im1.pdb file
Complete list - 23 20 Bytes
HEADER PEPTIDE TOXIN 18-NOV-98 1IM1
TITLE NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CONOTOXIN IM1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: NEUROTOXIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS IMPERIALIS;
SOURCE 3 ORGANISM_TAXID: 35631
KEYWDS PEPTIDE TOXIN, NEUROTOXIN, NICOTINIC ACETYLCHOLINE RECEPTOR
KEYWDS 2 ANTAGONIST, ALPHA-CONOTOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.P.ROGERS,P.LUGINBUHL,G.S.SHEN,R.T.MCCABE,R.C.STEVENS,D.E.WEMMER
REVDAT 4 23-FEB-22 1IM1 1 REMARK
REVDAT 3 24-FEB-09 1IM1 1 VERSN
REVDAT 2 01-APR-03 1IM1 1 JRNL
REVDAT 1 15-JUN-99 1IM1 0
JRNL AUTH J.P.ROGERS,P.LUGINBUHL,G.S.SHEN,R.T.MCCABE,R.C.STEVENS,
JRNL AUTH 2 D.E.WEMMER
JRNL TITL NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IMI AND COMPARISON
JRNL TITL 2 TO OTHER CONOTOXINS SPECIFIC FOR NEURONAL NICOTINIC
JRNL TITL 3 ACETYLCHOLINE RECEPTORS.
JRNL REF BIOCHEMISTRY V. 38 3874 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10194298
JRNL DOI 10.1021/BI9826254
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.S.JOHNSON,J.MARTINEZ,A.B.ELGOYHEN,S.F.HEINEMANN,
REMARK 1 AUTH 2 J.M.MCINTOSH
REMARK 1 TITL ALPHA-CONOTOXIN IMI EXHIBITS SUBTYPE-SPECIFIC NICOTINIC
REMARK 1 TITL 2 ACETYLCHOLINE RECEPTOR BLOCKADE: PREFERENTIAL INHIBITION OF
REMARK 1 TITL 3 HOMOMERIC ALPHA 7 AND ALPHA 9 RECEPTORS
REMARK 1 REF MOL.PHARMACOL. V. 48 194 1995
REMARK 1 REFN ISSN 0026-895X
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.M.MCINTOSH,D.YOSHIKAMI,E.MAHE,D.B.NIELSEN,J.E.RIVIER,
REMARK 1 AUTH 2 W.R.GRAY,B.M.OLIVERA
REMARK 1 TITL A NICOTINIC ACETYLCHOLINE RECEPTOR LIGAND OF UNIQUE
REMARK 1 TITL 2 SPECIFICITY, ALPHA-CONOTOXIN IMI
REMARK 1 REF J.BIOL.CHEM. V. 269 16733 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : LUGINBUHL,GUNTERT,BILLETER, WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FOR THE PRESENT STRUCTURES THE NMR
REMARK 3 DISTANCE CONSTRAINTS WERE WEIGHTED SUCH THAT A VIOLATION OF AN
REMARK 3 UPPER DISTANCE LIMIT OF 0.1 ANGSTROM CORRESPONDS TO AN ENERGY OF
REMARK 3 KT/2. THE CONSTRAINTS ON DIHEDRAL ANGLES RESULTING FROM
REMARK 3 MEASUREMENTS OF VICINAL COUPLING CONSTANTS WERE WEIGHTED SUCH
REMARK 3 THAT A VIOLATION OF 2.5 DEGREES CORRESPONDS TO AN ENERGY OF KT/2.
REMARK 4
REMARK 4 1IM1 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_1000174190.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O OR 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; ROESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 300 MHZ
REMARK 210 SPECTROMETER MODEL : DRX500; DRX300
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, OPAL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, RESTRAINED
REMARK 210 ENERGY REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESIDUAL TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
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 ARG A 11 -15.83 45.88
REMARK 500 2 ARG A 11 10.12 46.39
REMARK 500 3 ARG A 11 26.87 45.92
REMARK 500 4 ARG A 11 -11.54 46.79
REMARK 500 5 CYS A 3 -33.33 -39.27
REMARK 500 5 CYS A 8 22.93 -147.64
REMARK 500 5 ARG A 11 -9.50 73.51
REMARK 500 6 ARG A 11 -12.44 73.53
REMARK 500 7 CYS A 3 -0.48 -54.83
REMARK 500 7 ARG A 11 -17.06 73.87
REMARK 500 8 ARG A 11 -7.14 73.14
REMARK 500 9 TRP A 10 -155.33 -65.16
REMARK 500 9 ARG A 11 54.04 -68.26
REMARK 500 10 ARG A 11 -19.68 74.52
REMARK 500 11 ARG A 11 26.02 45.68
REMARK 500 13 ARG A 11 -8.06 73.40
REMARK 500 14 CYS A 3 9.77 -65.76
REMARK 500 14 ARG A 11 -17.75 73.11
REMARK 500 15 ARG A 11 -25.47 75.42
REMARK 500 16 ARG A 11 17.90 46.20
REMARK 500 17 ARG A 11 -8.85 73.05
REMARK 500 18 TRP A 10 -144.12 -66.12
REMARK 500 18 ARG A 11 32.02 -63.95
REMARK 500 19 ARG A 11 27.94 45.77
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 13 ARG A 11 0.09 SIDE CHAIN
REMARK 500 18 ARG A 7 0.09 SIDE CHAIN
REMARK 500 18 ARG A 11 0.10 SIDE CHAIN
REMARK 500 19 ARG A 7 0.10 SIDE CHAIN
REMARK 500 19 ARG A 11 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IM1 A 1 12 UNP P50983 CXA1_CONIM 1 12
SEQRES 1 A 12 GLY CYS CYS SER ASP PRO ARG CYS ALA TRP ARG CYS
HELIX 1 1 CYS A 2 SER A 4 5 3
HELIX 2 2 PRO A 6 CYS A 8 5 3
SSBOND 1 CYS A 2 CYS A 8 1555 1555 2.04
SSBOND 2 CYS A 3 CYS A 12 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 - 23 20 Bytes