Header list of 1pjv.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 03-JUN-03 1PJV
TITLE COBATOXIN 1 FROM CENTRUROIDES NOXIUS SCORPION VENOM: CHEMICAL
TITLE 2 SYNTHESIS, 3-D STRUCTURE IN SOLUTION, PHARMACOLOGY AND DOCKING ON K+
TITLE 3 CHANNELS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COBATOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COTX1, GTIX;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PROTEIN IS NATURALLY FOUND IN CENTRUROIDES NOXIUS (MEXICAN
SOURCE 5 SCORPION)
KEYWDS COBATOXIN 1, SCORPION TOXIN, CENTUROIDES NOXIUS, K+ CHANNEL, CHEMICAL
KEYWDS 2 SYNTHESIS, 3-D STRUCTURE, 1H-NMR SPECTROSCOPY, CIRCULAR DICHROISM,
KEYWDS 3 MOLECULAR MODELING, DOCKING EXPERIMENT, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.MOSBAH,B.JOUIROU,V.VISAN,S.GRISSMER,M.EL AYEB,H.ROCHAT,M.DE WAARD,
AUTHOR 2 K.MABROUK,J.M.SABATIER
REVDAT 3 23-FEB-22 1PJV 1 REMARK
REVDAT 2 24-FEB-09 1PJV 1 VERSN
REVDAT 1 09-MAR-04 1PJV 0
JRNL AUTH B.JOUIROU,A.MOSBAH,V.VISAN,S.GRISSMER,S.M'BAREK,Z.FAJLOUN,
JRNL AUTH 2 J.VAN RIETSCHOTEN,C.DEVAUX,H.ROCHAT,G.LIPPENS,M.EL AYEB,
JRNL AUTH 3 M.DE WAARD,K.MABROUK,J.M.SABATIER
JRNL TITL COBATOXIN 1 FROM CENTRUROIDES NOXIUS SCORPION VENOM:
JRNL TITL 2 CHEMICAL SYNTHESIS, THREE-DIMENSIONAL STRUCTURE IN SOLUTION,
JRNL TITL 3 PHARMACOLOGY AND DOCKING ON K+ CHANNELS.
JRNL REF BIOCHEM.J. V. 377 37 2004
JRNL REFN ISSN 0264-6021
JRNL PMID 14498829
JRNL DOI 10.1042/BJ20030977
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PJV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019374.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 298
REMARK 210 PH : 3.1; 3.1
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM COBATOXIN 1; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
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 : NMRPIPE, XEASY, DIANA, TURBO
REMARK 210 -FRODO, MOLMOL
REMARK 210 METHOD USED : DISTANCE GEOMETRY CALCULATION
REMARK 210 AND CNS REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 2 ASN A 25 35.53 -152.84
REMARK 500 2 ALA A 26 111.58 -175.92
REMARK 500 2 PRO A 31 -78.43 -61.34
REMARK 500 3 ASN A 24 -30.57 -37.86
REMARK 500 3 ASN A 25 39.25 -155.60
REMARK 500 3 ALA A 26 109.67 -173.50
REMARK 500 4 ASN A 24 -27.67 -39.39
REMARK 500 4 ASN A 25 34.29 -153.51
REMARK 500 4 ALA A 26 119.47 -177.83
REMARK 500 5 ASN A 25 29.63 46.16
REMARK 500 6 ASN A 24 29.73 46.04
REMARK 500 6 PRO A 31 -168.00 -74.00
REMARK 500 7 ASN A 25 29.48 47.31
REMARK 500 8 ASN A 25 28.06 48.62
REMARK 500 8 PRO A 31 -168.02 -79.92
REMARK 500 9 ASN A 25 28.16 -149.97
REMARK 500 9 ALA A 26 123.02 -179.29
REMARK 500 10 ASN A 25 29.76 45.90
REMARK 500 15 ASN A 25 29.95 46.05
REMARK 500 15 PRO A 31 -169.55 -79.46
REMARK 500 16 ASN A 25 37.14 -153.31
REMARK 500 16 ALA A 26 111.16 -173.87
REMARK 500 17 ASN A 25 30.41 -150.90
REMARK 500 17 ALA A 26 121.24 -178.81
REMARK 500 19 ARG A 18 -64.75 -93.59
REMARK 500 19 LYS A 21 142.31 -176.21
REMARK 500 20 PRO A 31 -167.99 -74.59
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PJV A 1 32 UNP O46028 SCK1_CENNO 29 60
SEQRES 1 A 32 ALA VAL CYS VAL TYR ARG THR CYS ASP LYS ASP CYS LYS
SEQRES 2 A 32 ARG ARG GLY TYR ARG SER GLY LYS CYS ILE ASN ASN ALA
SEQRES 3 A 32 CYS LYS CYS TYR PRO TYR
HELIX 1 1 VAL A 4 ARG A 14 1 11
SHEET 1 A 2 SER A 19 ILE A 23 0
SHEET 2 A 2 ALA A 26 TYR A 30 -1 O LYS A 28 N LYS A 21
SSBOND 1 CYS A 3 CYS A 22 1555 1555 2.03
SSBOND 2 CYS A 8 CYS A 27 1555 1555 2.03
SSBOND 3 CYS A 12 CYS A 29 1555 1555 2.03
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