Header list of 1ne5.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 10-DEC-02 1NE5
TITLE SOLUTION STRUCTURE OF HERG SPECIFIC SCORPION TOXIN CNERG1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERGTOXIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CNERG1, ERGTX;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN CENTRUROIDES NOXIUS
KEYWDS ALPHA-HELIX, TRIPLE-STRANDED BETA-SHEET, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.M.TORRES,B.PARAMJIT,P.ALEWOOD,P.W.KUCHEL,J.I.VANDENBERG
REVDAT 4 23-FEB-22 1NE5 1 REMARK
REVDAT 3 17-NOV-09 1NE5 1 REMARK TITLE
REVDAT 2 24-FEB-09 1NE5 1 VERSN
REVDAT 1 01-APR-03 1NE5 0
JRNL AUTH A.M.TORRES,P.BANSAL,P.F.ALEWOOD,J.A.BURSILL,P.W.KUCHEL,
JRNL AUTH 2 J.I.VANDENBERG
JRNL TITL SOLUTION STRUCTURE OF CNERG1 (ERGTOXIN), A HERG SPECIFIC
JRNL TITL 2 SCORPION TOXIN
JRNL REF FEBS LETT. V. 539 138 2003
JRNL REFN ISSN 0014-5793
JRNL PMID 12650941
JRNL DOI 10.1016/S0014-5793(03)00216-3
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.B.GURROLA,B.ROSATI,M.ROCCHETTI,G.PIMIENTA,A.ZAZA,
REMARK 1 AUTH 2 A.ARCANGELI,M.OLIVOTTO,L.D.POSSANI,E.WANKE
REMARK 1 TITL A TOXIN TO NERVOUS, CARDIAC, AND ENDOCRINE ERG K+ CHANNELS
REMARK 1 TITL 2 ISOLATED FROM CENTRUROIDES NOXIUS SCORPION VENOM.
REMARK 1 REF FASEB J. V. 13 953 1999
REMARK 1 REFN ISSN 0892-6638
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.SCALONI,C.BOTTIGLIERI,L.FERRARA,M.CORONA,G.B.GURROLA,
REMARK 1 AUTH 2 C.BATISTA,E.WANKE,L.D.POSSANI
REMARK 1 TITL DISULFIDE BRIDGES OF ERGTOXIN, A MEMBER OF A NEW SUB-FAMILY
REMARK 1 TITL 2 OF PEPTIDE BLOCKERS OF THE ETHER-A-GO-GO-RELATED K+ CHANNEL
REMARK 1 REF FEBS LETT. V. 479 156 2000
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(00)01891-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 578 RESTRAINTS, 535 ARE NOE-
REMARK 3 DERIVED DISTANCE RESTRAINTS, 11 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS, 32 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1NE5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017798.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.2
REMARK 210 IONIC STRENGTH : NO SALT ADDED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.7MM CNERG1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, INFIT, NOAH, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, DISTANCE GEOMETRY,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 4000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WERE DETERMINED USING STANDARD 2D
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: 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 2 47.63 -148.45
REMARK 500 1 ASP A 3 -74.52 -66.59
REMARK 500 1 SER A 4 95.52 57.93
REMARK 500 1 LYS A 8 -53.62 -131.53
REMARK 500 1 ARG A 10 -165.25 -64.89
REMARK 500 1 TYR A 14 161.41 176.78
REMARK 500 1 HIS A 29 -151.88 -139.04
REMARK 500 1 PHE A 37 18.97 58.93
REMARK 500 2 ARG A 2 107.78 -178.53
REMARK 500 2 ASP A 3 -71.05 -69.48
REMARK 500 2 SER A 4 93.72 58.27
REMARK 500 2 TYR A 14 156.84 174.35
REMARK 500 2 HIS A 29 -150.64 -141.47
REMARK 500 3 ARG A 2 107.33 -177.97
REMARK 500 3 ASP A 3 -71.55 -133.91
REMARK 500 3 SER A 4 100.54 56.86
REMARK 500 3 TYR A 14 166.54 174.52
REMARK 500 3 HIS A 29 -148.34 -134.95
REMARK 500 4 SER A 4 103.36 62.03
REMARK 500 4 LYS A 8 -51.75 -130.00
REMARK 500 4 ARG A 10 -164.63 -59.02
REMARK 500 4 TYR A 14 160.47 171.54
REMARK 500 4 HIS A 29 -150.94 -140.34
REMARK 500 5 ARG A 2 60.93 -116.65
REMARK 500 5 TYR A 14 162.83 176.68
REMARK 500 5 HIS A 29 -150.98 -140.24
REMARK 500 6 ARG A 2 107.75 -179.24
REMARK 500 6 ASP A 3 -79.27 -121.24
REMARK 500 6 SER A 4 91.67 51.23
REMARK 500 6 LYS A 8 -50.75 -125.75
REMARK 500 6 TYR A 14 165.26 171.42
REMARK 500 6 HIS A 29 -147.49 -102.71
REMARK 500 6 PHE A 36 71.75 45.37
REMARK 500 7 ASP A 3 -71.64 -85.07
REMARK 500 7 SER A 4 84.94 50.03
REMARK 500 7 LYS A 8 -55.50 -132.62
REMARK 500 7 TYR A 14 153.68 172.59
REMARK 500 7 HIS A 29 -151.11 -140.69
REMARK 500 8 ARG A 2 93.42 52.99
REMARK 500 8 ASP A 3 -73.37 -81.57
REMARK 500 8 SER A 4 82.39 54.39
REMARK 500 8 LYS A 8 -65.58 -126.09
REMARK 500 8 ARG A 10 -165.09 -77.23
REMARK 500 8 TYR A 14 153.32 176.21
REMARK 500 8 HIS A 29 -150.27 -140.03
REMARK 500 9 ASP A 3 -70.06 -59.07
REMARK 500 9 SER A 4 99.54 55.63
REMARK 500 9 LYS A 8 -58.64 -137.39
REMARK 500 9 ARG A 10 -164.87 -58.19
REMARK 500 9 TYR A 14 168.34 178.76
REMARK 500
REMARK 500 THIS ENTRY HAS 111 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NE5 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 SER A 4 LYS A 8 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 2.03
SSBOND 3 CYS A 20 CYS A 39 1555 1555 2.03
SSBOND 4 CYS A 24 CYS A 41 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 - b 23 2 Bytes