Header list of 1n8m.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 21-NOV-02 1N8M TITLE SOLUTION STRUCTURE OF PI4, A FOUR DISULFIDE BRIDGED SCORPION TOXIN TITLE 2 ACTIVE ON POTASSIUM CHANNELS COMPND MOL_ID: 1; COMPND 2 MOLECULE: POTASSIUM CHANNEL BLOCKING TOXIN 4; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PI4; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN THE VENOM OF SOURCE 4 PANDINUS IMPERATOR SCORPIONS, WITH AN AMIDATED C-TERMINUS. IT WAS SOURCE 5 ESTABLISHED BY NMR THAT THE STRUCTURE OF THE NATURAL TOXIN EXTRACTED SOURCE 6 FROM SCORPION VENOM IS EFFECTIVELY IDENTICAL TO THE STRUCTURE OF THE SOURCE 7 SYNTHETIC TOXIN, WHICH HAS A CARBOXYLATED C-TERMINUS. KEYWDS POTASSIUM CHANNEL BLOCKER, DISULFIDE BRIDGE STABILIZED ALPHA BETA KEYWDS 2 MOTIF, TOXIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR J.I.GUIJARRO,S.M'BAREK,T.OLAMENDI-PORTUGAL,F.GOMEZ-LAGUNAS,D.GARNIER, AUTHOR 2 H.ROCHAT,L.D.POSSANI,J.M.SABATIER,M.DELEPIERRE REVDAT 3 23-FEB-22 1N8M 1 REMARK REVDAT 2 24-FEB-09 1N8M 1 VERSN REVDAT 1 02-SEP-03 1N8M 0 JRNL AUTH J.I.GUIJARRO,S.M'BAREK,F.GOMEZ-LAGUNAS,D.GARNIER,H.ROCHAT, JRNL AUTH 2 J.M.SABATIER,L.D.POSSANI,M.DELEPIERRE JRNL TITL SOLUTION STRUCTURE OF PI4, A SHORT FOUR-DISULFIDE-BRIDGED JRNL TITL 2 SCORPION TOXIN SPECIFIC OF POTASSIUM CHANNELS. JRNL REF PROTEIN SCI. V. 12 1844 2003 JRNL REFN ISSN 0961-8368 JRNL PMID 12930984 JRNL DOI 10.1110/PS.03186703 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.OLAMENDI-PORTUGAL,F.GOMEZ-LAGUNAS,G.B.GURROLA,L.D.POSSANI REMARK 1 TITL TWO SIMILAR PEPTIDES FROM THE VENOM OF THE SCORPION PANDINUS REMARK 1 TITL 2 IMPERATOR, ONE HIGHLY EFFECTIVE BLOCKER AND THE OTHER REMARK 1 TITL 3 INACTIVE ON K+ CHANNELS REMARK 1 REF TOXICON V. 36 759 1998 REMARK 1 REFN ISSN 0041-0101 REMARK 1 DOI 10.1016/S0041-0101(97)00163-3 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CNS 1.1 REMARK 3 AUTHORS : VARIAN INC. (VNMR), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON A TOTAL OF 705 REMARK 3 CONSTRAINTS, 679 ARE MEANINGFUL NOE DERIVED CONSTRAINTS (642 REMARK 3 UNAMBIGUOUS, 37 AMBIGUOUS), 16 ARE DIHEDRAL (PHI) ANGLE REMARK 3 CONSTRAINTS AND 10 ARE HYDROGEN BONDS. THE FOUR DISULFIDE REMARK 3 BRIDGES (CYS 6-27, 12-32, 16-34, 22-37) WERE INCLUDED IN THE REMARK 3 TOPOLOGY FILE USED FOR THE CALCULATIONS. REMARK 4 REMARK 4 1N8M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-02. REMARK 100 THE DEPOSITION ID IS D_1000017655. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : 5 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2.5 MM PI4, 5 MM CD3COONA, PH REMARK 210 4.0, 10% D2O; 3.2 MM PI4, 5 MM REMARK 210 CD3COONA, PD 4.0, 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; P-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.03, ARIA 1.2, CNS 1.1 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: REMARK 210 DISULFIDE BRIDGES WERE DETERMINED BY NMR AND BY N-TERMINAL REMARK 210 SEQUENCING OF PROTEOLYSIS PEPTIDES. REMARK 210 DISTANCE CONSTRAINTS WERE DERIVED FROM INITIAL NOE BUILD UP RATES REMARK 210 USING 2D NOESY EXPERIMENTS WITH MIXING TIMES OF 70, 100, 150, 200 REMARK 210 AND 250 MS IN H2O AND D2O. 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 ASN A 24 104.58 -54.74 REMARK 500 1 CYS A 37 69.02 -117.69 REMARK 500 2 ALA A 3 77.64 51.45 REMARK 500 2 CYS A 34 98.19 -69.00 REMARK 500 2 CYS A 37 54.30 -93.45 REMARK 500 3 GLU A 2 48.00 -108.47 REMARK 500 3 ALA A 3 76.36 56.21 REMARK 500 3 ASN A 24 96.25 -66.28 REMARK 500 4 ASN A 24 98.75 -61.66 REMARK 500 5 ASN A 24 100.84 -58.01 REMARK 500 6 ASN A 24 99.37 -62.05 REMARK 500 8 ALA A 3 76.18 52.43 REMARK 500 10 ASN A 24 98.46 -63.63 REMARK 500 REMARK 500 REMARK: NULL DBREF 1N8M A 1 38 UNP P58498 SCK4_PANIM 1 38 SEQRES 1 A 38 ILE GLU ALA ILE ARG CYS GLY GLY SER ARG ASP CYS TYR SEQRES 2 A 38 ARG PRO CYS GLN LYS ARG THR GLY CYS PRO ASN ALA LYS SEQRES 3 A 38 CYS ILE ASN LYS THR CYS LYS CYS TYR GLY CYS SER HELIX 1 1 SER A 9 GLY A 21 1 13 SHEET 1 A 2 ALA A 25 ILE A 28 0 SHEET 2 A 2 THR A 31 CYS A 34 -1 O LYS A 33 N LYS A 26 SSBOND 1 CYS A 6 CYS A 27 1555 1555 2.03 SSBOND 2 CYS A 12 CYS A 32 1555 1555 2.03 SSBOND 3 CYS A 16 CYS A 34 1555 1555 2.02 SSBOND 4 CYS A 22 CYS A 37 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