Header list of 1jlp.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 16-JUL-01 1JLP
TITLE SOLUTION STRUCTURE OF THE NONCOMPETITIVE SKELETAL MUSCLE NICOTINIC
TITLE 2 ACETYLCHOLINE RECEPTOR ANTAGONIST PSI-CONOTOXIN PIIIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PSI-CONOTOXIN PIIIF;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID PHASE CHEMICAL SYNTHESIS WAS USED. ONE SAMPLE
SOURCE 4 CONTAINED ONLY NATURAL ISOTOPIC ABUNDANCE RESIDUES. ANOTHER PEPTIDE
SOURCE 5 INCORPORATED 3-13C-LABELED CYSTEINE AT POSITION 4. THE THIRD PEPTIDE
SOURCE 6 INCORPORATED 3-13C-LABELED CYSTEINE AT POSITIONS 5, 10, 16, 21, AND
SOURCE 7 22. THE SEQUENCE FOR ALL PEPTIDES IS THE SAME AS THE NATIVE PEPTIDE
SOURCE 8 FROM CONUS PURPURASCENS (PURPLE CONE).
KEYWDS MULTIPLE DISULFIDE BONDS, AMIDATED C-TERMINUS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR R.M.VAN WAGONER,C.M.IRELAND
REVDAT 3 23-FEB-22 1JLP 1 REMARK LINK
REVDAT 2 24-FEB-09 1JLP 1 VERSN
REVDAT 1 24-JUN-03 1JLP 0
JRNL AUTH R.M.VAN WAGONER,C.M.IRELAND
JRNL TITL CHARACTERIZATION AND THREE-DIMENSIONAL STRUCTURE
JRNL TITL 2 DETERMINATION OF PSI-CONOTOXIN PIIIF, A NOVEL NONCOMPETITIVE
JRNL TITL 3 ANTAGONIST OF NICOTINIC ACETYLCHOLINE RECEPTORS
JRNL REF BIOCHEMISTRY V. 42 6353 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12767216
JRNL DOI 10.1021/BI0272757
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.S.MITCHELL,K.J.SHON,M.P.FOSTER,D.R.DAVIS,B.M.OLIVERA,
REMARK 1 AUTH 2 C.M.IRELAND
REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF CONOTOXIN PSI-PIIIE,
REMARK 1 TITL 2 AN ACETYLCHOLINE GATED ION CHANNEL ANTAGONIST
REMARK 1 REF BIOCHEMISTRY V. 37 1215 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI972186T
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.J.SHON,M.GRILLEY,R.JACOBSEN,G.E.CARTIER,C.HOPKINS,
REMARK 1 AUTH 2 W.R.GRAY,M.WATKINS,D.R.HILLYARD,J.RIVIER,J.TORRES,
REMARK 1 AUTH 3 D.YOSHIKAMI,B.M.OLIVERA
REMARK 1 TITL A NONCOMPETITIVE PEPTIDE INHIBITOR OF THE NICOTINIC
REMARK 1 TITL 2 ACETYLCHOLINE RECEPTOR FROM CONUS PURPURASCENS VENOM
REMARK 1 REF BIOCHEMISTRY V. 36 9581 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI970235W
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, DISCOVER 2.98
REMARK 3 AUTHORS : VARIAN, INC. (VNMR), MSI, INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THESE STRUCTURES ARE BASED ON 380 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINTS, 7 RESTRAINTS ON PHI DERIVED FROM J-
REMARK 3 COUPLING, AND 7 RESTRAINTS ON CHI1 DETERMINED FROM J-COUPLING
REMARK 3 AND NOE VOLUMES.
REMARK 4
REMARK 4 1JLP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013915.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277; 295
REMARK 210 PH : 3.5; 3.5
REMARK 210 IONIC STRENGTH : 12 MM; TETRA-TFA SALT; 12 MM;
REMARK 210 TETRA-TFA SALT
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 12 MM PSI-CONOTOXIN PIIIF; TFA
REMARK 210 ADDED TO PH 3.5; 12 MM PSI-
REMARK 210 CONOTOXIN PIIIF; 14 MM OF PSI-
REMARK 210 CONOTOXIN PIIIF [5,10,16,21,22]
REMARK 210 3-13C-CYS; TFA ADDED TO PH 3.5;
REMARK 210 16 MM OF PSI-CONOTOXIN PIIIF [4]
REMARK 210 3-13C-CYS; TFA ADDED TO PH 3.5;
REMARK 210 16 MM OF PSI-CONOTOXIN PIIIF [4]
REMARK 210 3-13C-CYS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; PE-COSY; 13C
REMARK 210 -SELECTED 2D NOESY; DOUBLE HALF-
REMARK 210 FILTERED 2D NOESY; DOUBLE HALF-
REMARK 210 FILTERED 2D PE-COSY; 13C-
REMARK 210 SELECTED 1D 1H NMR
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 97.0, IRMA 97.0, DGII
REMARK 210 97.0, DISCOVER 2.98
REMARK 210 METHOD USED : DISTANCE GEOMETRY MOLECULAR
REMARK 210 DYNAMICS RELAXATION MATRIX
REMARK 210 DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING ISOTOPIC FILTRATION
REMARK 210 AND ISOTOPE-SELECTED 1H OBSERVATION IN ADDITION TO STANDARD
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: 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 1 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 SER A 9 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 6 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 6 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 SER A 9 N - CA - CB ANGL. DEV. = -9.7 DEGREES
REMARK 500 7 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 7 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 8 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 8 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 9 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 10 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 11 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 12 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 12 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 13 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 13 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 14 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 14 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 15 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 15 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 16 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 16 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 17 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 17 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 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 1 CYS A 22 68.91 -103.10
REMARK 500 2 SER A 9 -155.08 -90.62
REMARK 500 3 SER A 9 -122.03 -89.08
REMARK 500 3 ARG A 11 103.18 -160.55
REMARK 500 4 SER A 9 -140.91 -81.89
REMARK 500 4 CYS A 22 59.02 -113.80
REMARK 500 5 SER A 9 -149.00 -87.87
REMARK 500 6 SER A 9 -163.31 -79.39
REMARK 500 7 TYR A 7 42.74 70.58
REMARK 500 7 SER A 9 -168.46 -79.88
REMARK 500 8 SER A 9 -122.58 -88.87
REMARK 500 8 CYS A 22 73.91 -100.18
REMARK 500 9 SER A 9 -143.32 -92.26
REMARK 500 9 CYS A 22 68.46 -103.21
REMARK 500 10 SER A 9 -154.43 -87.54
REMARK 500 10 CYS A 22 70.55 -110.19
REMARK 500 11 SER A 9 -130.43 -87.19
REMARK 500 12 SER A 9 -134.21 -88.40
REMARK 500 12 CYS A 22 67.68 -103.48
REMARK 500 13 SER A 9 -134.86 -86.38
REMARK 500 13 CYS A 22 77.39 -101.20
REMARK 500 15 CYS A 22 76.52 -102.62
REMARK 500 16 SER A 9 -132.79 -89.09
REMARK 500 17 SER A 9 -148.69 -90.87
REMARK 500
REMARK 500 REMARK: NULL
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 ALA A 19 LEU A 20 4 -148.67
REMARK 500 SER A 9 CYS A 10 7 149.02
REMARK 500 ALA A 19 LEU A 20 9 -149.97
REMARK 500 ALA A 19 LEU A 20 10 -147.73
REMARK 500 ALA A 19 LEU A 20 14 -147.81
REMARK 500 ALA A 19 LEU A 20 16 -149.81
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 25
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AS5 RELATED DB: PDB
REMARK 900 1AS5 CONTAINS THE ORIGINAL STRUCTURES CALCULATED FOR PSI-CONOTOXIN
REMARK 900 PIIIE.
REMARK 900 RELATED ID: 1JLO RELATED DB: PDB
REMARK 900 1JLO CONTAINS THE REVISED STRUCTURES CALCULATED FOR PSI-CONOTOXIN
REMARK 900 PIIIE.
DBREF 1JLP A 1 24 UNP P60245 CXP3F_CONPU 1 24
SEQRES 1 A 25 GLY HYP HYP CYS CYS LEU TYR GLY SER CYS ARG HYP PHE
SEQRES 2 A 25 HYP GLY CYS TYR ASN ALA LEU CYS CYS ARG LYS NH2
MODRES 1JLP HYP A 2 PRO 4-HYDROXYPROLINE
MODRES 1JLP HYP A 3 PRO 4-HYDROXYPROLINE
MODRES 1JLP HYP A 12 PRO 4-HYDROXYPROLINE
MODRES 1JLP HYP A 14 PRO 4-HYDROXYPROLINE
HET HYP A 2 15
HET HYP A 3 15
HET HYP A 12 15
HET HYP A 14 15
HET NH2 A 25 3
HETNAM HYP 4-HYDROXYPROLINE
HETNAM NH2 AMINO GROUP
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP 4(C5 H9 N O3)
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 4 CYS A 16 1555 1555 1.99
SSBOND 2 CYS A 5 CYS A 21 1555 1555 1.99
SSBOND 3 CYS A 10 CYS A 22 1555 1555 2.01
LINK C GLY A 1 N HYP A 2 1555 1555 1.37
LINK C HYP A 2 N HYP A 3 1555 1555 1.37
LINK C HYP A 3 N CYS A 4 1555 1555 1.32
LINK C ARG A 11 N HYP A 12 1555 1555 1.37
LINK C HYP A 12 N PHE A 13 1555 1555 1.34
LINK C PHE A 13 N HYP A 14 1555 1555 1.36
LINK C HYP A 14 N GLY A 15 1555 1555 1.32
LINK C LYS A 24 N NH2 A 25 1555 1555 1.32
SITE 1 AC1 1 LYS A 24
CRYST1 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