Header list of 1wz5.pdb file
Complete list - 2 202 Bytes
HEADER TOXIN 24-FEB-05 1WZ5
TITLE SOLUTION STRUCTURE OF PI1-3P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM CHANNEL BLOCKING TOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PI1-3P, PI1, PI-1, PITX-K-GAMMA, ALPHA-KTX 6.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PANDINUS IMPERATOR;
SOURCE 3 ORGANISM_COMMON: EMPEROR SCORPION;
SOURCE 4 ORGANISM_TAXID: 55084
KEYWDS IONIC CHANNEL INHIBITOR, TOXIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR G.FERRAT
REVDAT 5 02-MAR-22 1WZ5 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1WZ5 1 VERSN
REVDAT 3 06-DEC-05 1WZ5 1 JRNL
REVDAT 2 01-NOV-05 1WZ5 1 JRNL
REVDAT 1 19-APR-05 1WZ5 0
JRNL AUTH L.CARREGA,A.MOSBAH,G.FERRAT,C.BEETON,N.ANDREOTTI,
JRNL AUTH 2 P.MANSUELLE,H.DARBON,M.DE WAARD,J.M.SABATIER
JRNL TITL THE IMPACT OF THE FOURTH DISULFIDE BRIDGE IN SCORPION TOXINS
JRNL TITL 2 OF THE ALPHA-KTX6 SUBFAMILY
JRNL REF PROTEINS V. 61 1010 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 16247791
JRNL DOI 10.1002/PROT.20681
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WZ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024176.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
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 : XWINNMR 2.1, DIANA 2.8
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 LYS A 3 60.57 -170.20
REMARK 500 CYS A 4 -94.42 46.21
REMARK 500 ARG A 5 9.69 52.77
REMARK 500 SER A 8 -23.36 169.47
REMARK 500 GLN A 17 -74.13 -71.30
REMARK 500 THR A 18 -148.79 -72.24
REMARK 500 SER A 23 136.42 -171.19
REMARK 500 LYS A 24 142.11 -170.09
REMARK 500 TYR A 33 70.79 43.76
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WZ5 A 1 35 UNP Q10726 SCKG_PANIM 1 35
SEQADV 1WZ5 ABA A 20 UNP Q10726 CYS 20 MODIFIED RESIDUE
SEQADV 1WZ5 ABA A 35 UNP Q10726 CYS 35 MODIFIED RESIDUE
SEQRES 1 A 35 LEU VAL LYS CYS ARG GLY THR SER ASP CYS GLY ARG PRO
SEQRES 2 A 35 CYS GLN GLN GLN THR GLY ABA PRO ASN SER LYS CYS ILE
SEQRES 3 A 35 ASN ARG MET CYS LYS CYS TYR GLY ABA
MODRES 1WZ5 ABA A 20 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 1WZ5 ABA A 35 ALA ALPHA-AMINOBUTYRIC ACID
HET ABA A 20 13
HET ABA A 35 14
HETNAM ABA ALPHA-AMINOBUTYRIC ACID
FORMUL 1 ABA 2(C4 H9 N O2)
HELIX 1 1 CYS A 10 THR A 18 1 9
SHEET 1 A 2 LYS A 24 ILE A 26 0
SHEET 2 A 2 MET A 29 LYS A 31 -1 O LYS A 31 N LYS A 24
SSBOND 1 CYS A 4 CYS A 25 1555 1555 2.03
SSBOND 2 CYS A 10 CYS A 30 1555 1555 2.03
SSBOND 3 CYS A 14 CYS A 32 1555 1555 2.03
LINK C GLY A 19 N ABA A 20 1555 1555 1.33
LINK C ABA A 20 N PRO A 21 1555 1555 1.35
LINK C GLY A 34 N ABA A 35 1555 1555 1.33
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