Header list of 1px9.pdb file
Complete list - 2 202 Bytes
HEADER TOXIN 03-JUL-03 1PX9
TITLE SOLUTION STRUCTURE OF THE NATIVE CNERG1 ERGTOXIN, A HIGHLY SPECIFIC
TITLE 2 INHIBITOR OF HERG CHANNEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERGTOXIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CENTRUROIDES NOXIUS;
SOURCE 3 ORGANISM_COMMON: MEXICAN SCORPION;
SOURCE 4 ORGANISM_TAXID: 6878;
SOURCE 5 SECRETION: VENOM
KEYWDS ALPHA/BETA MOLECULAR SCAFFOLD, TOXIN
EXPDTA SOLUTION NMR
AUTHOR K.FRENAL,K.WECKER,G.B.GURROLA,L.D.POSSANI,N.WOLFF,M.DELEPIERRE
REVDAT 3 02-MAR-22 1PX9 1 REMARK
REVDAT 2 24-FEB-09 1PX9 1 VERSN
REVDAT 1 22-JUN-04 1PX9 0
JRNL AUTH K.FRENAL,C.Q.XU,N.WOLFF,K.WECKER,G.B.GURROLA,S.Y.ZHU,
JRNL AUTH 2 C.W.CHI,L.D.POSSANI,J.TYTGAT,M.DELEPIERRE
JRNL TITL EXPLORING STRUCTURAL FEATURES OF THE INTERACTION BETWEEN THE
JRNL TITL 2 SCORPION TOXINCNERG1 AND ERG K+ CHANNELS.
JRNL REF PROTEINS V. 56 367 2004
JRNL REFN ISSN 0887-3585
JRNL PMID 15211519
JRNL DOI 10.1002/PROT.20102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER INSIGHTII 2000, DISCOVER INSIGHTII 2000
REMARK 3 AUTHORS : ACCELRYS TECHNOLOGIES (DISCOVER), ACCELRYS
REMARK 3 TECHNOLOGIES (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 452 DISTANCE CONSTRAINTS (252 ARE INTRARESIDUAL NOE-DERIVATED
REMARK 3 DISTANCE CONSTRAINTS, 200 ARE INTERRESIDUAL NOE-DERIVATED
REMARK 3 DISTANCE CONSTRAINTS INCLUDING 49 LONG RANGE), 13 3J AND 10
REMARK 3 HBONDS
REMARK 4
REMARK 4 1PX9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019663.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.55 MG OF LYOPHILIZED NATURAL
REMARK 210 ERGTX
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISCOVER INSIGHTII 2000
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : 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
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: SHIGEMI TUBE AND NANO-PROBE
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 LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A 42 C ALA A 42 OXT 0.136
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 34 CA - CB - SG ANGL. DEV. = 12.5 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 VAL A 6 -68.90 -131.15
REMARK 500 LYS A 8 48.64 -84.33
REMARK 500 TYR A 17 112.53 -166.13
REMARK 500 ASN A 30 -64.55 166.44
REMARK 500 MET A 35 141.22 163.57
REMARK 500 PHE A 37 36.04 -166.03
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PX9 A 1 42 UNP Q86QT3 SEK1_CENNO 1 42
SEQRES 1 A 42 ASP ARG ASP SER CYS VAL ASP LYS SER ARG CYS ALA LYS
SEQRES 2 A 42 TYR GLY TYR TYR GLN GLU CYS GLN ASP CYS CYS LYS ASN
SEQRES 3 A 42 ALA GLY HIS ASN GLY GLY THR CYS MET PHE PHE LYS CYS
SEQRES 4 A 42 LYS CYS ALA
HELIX 1 1 ARG A 2 VAL A 6 5 5
HELIX 2 2 TYR A 17 GLY A 28 1 12
SHEET 1 A 3 TYR A 14 GLY A 15 0
SHEET 2 A 3 GLY A 32 MET A 35 -1 O CYS A 34 N GLY A 15
SHEET 3 A 3 CYS A 39 CYS A 41 -1 O LYS A 40 N THR A 33
SSBOND 1 CYS A 5 CYS A 23 1555 1555 2.03
SSBOND 2 CYS A 11 CYS A 34 1555 1555 2.01
SSBOND 3 CYS A 20 CYS A 39 1555 1555 2.02
SSBOND 4 CYS A 24 CYS A 41 1555 1555 2.02
CISPEP 1 MET A 35 PHE A 36 0 -5.34
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 - 2 202 Bytes