Header list of 1j5j.pdb file
Complete list - 23 202 Bytes
HEADER TOXIN 16-APR-02 1J5J TITLE SOLUTION STRUCTURE OF HERG-SPECIFIC SCORPION TOXIN BEKM-1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BEKM-1 TOXIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MESOBUTHUS EUPEUS; SOURCE 3 ORGANISM_COMMON: LESSER ASIAN SCORPION; SOURCE 4 ORGANISM_TAXID: 34648; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HB101; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PEZZ18 KEYWDS ALPHA-BETA MOTIF, CYSTEINE-KNOT MOTIF, TOXIN EXPDTA SOLUTION NMR AUTHOR Y.V.KOROLOKOVA,E.V.BOCHAROV,K.ANGELO,I.V.MASLENNIKOV,O.V.GRINENKO, AUTHOR 2 A.V.LIPKIN,E.D.NOSIREVA,K.A.PLUZHNIKOV,S.-P.OLESEN,A.S.ARSENIEV, AUTHOR 3 E.V.GRISHIN REVDAT 3 23-FEB-22 1J5J 1 REMARK REVDAT 2 24-FEB-09 1J5J 1 VERSN REVDAT 1 20-NOV-02 1J5J 0 JRNL AUTH Y.V.KOROLKOVA,E.V.BOCHAROV,K.ANGELO,I.V.MASLENNIKOV, JRNL AUTH 2 O.V.GRINENKO,A.V.LIPKIN,E.D.NOSYREVA,K.A.PLUZHNIKOV, JRNL AUTH 3 S.P.OLESEN,A.S.ARSENIEV,E.V.GRISHIN JRNL TITL NEW BINDING SITE ON COMMON MOLECULAR SCAFFOLD PROVIDES HERG JRNL TITL 2 CHANNEL SPECIFICITY OF SCORPION TOXIN BEKM-1. JRNL REF J.BIOL.CHEM. V. 277 43104 2002 JRNL REFN ISSN 0021-9258 JRNL PMID 12151390 JRNL DOI 10.1074/JBC.M204083200 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH Y.V.KOROLKOVA,S.A.KOZLOV,A.V.LIPKIN,K.A.PLUZHNIKOV, REMARK 1 AUTH 2 J.K.HADLEY,A.K.FILIPPOV,D.A.BROWN,K.ANGELO,D.STROBEK, REMARK 1 AUTH 3 T.JESPERSEN,S.P.OLESEN,B.S.JENSEN,E.V.GRISHIN REMARK 1 TITL AN ERG CHANNEL INHIBITOR FROM THE SCORPION BUTHUS EUPEUS REMARK 1 REF J.BIOL.CHEM. V. 276 9868 2001 REMARK 1 REFN ISSN 0021-9258 REMARK 1 DOI 10.1074/JBC.M005973200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 5.3B, FANTOM 4 REMARK 3 AUTHORS : VARIAN (VNMR), SCHAUMANN (FANTOM) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 653 RESTRAINTS: REMARK 3 326/67 ARE NOE-DERIVED UPPER/LOWER DISTANCE CONSTRAINTS, REMARK 3 68/46 BACKBONE/SIDECHAIN DIHEDRAL ANGLE RESTRAINTS, REMARK 3 64/64 UPPER/LOWER DISTANCE RESTRAINTS FROM 23 (18 BB-BB, 5 BB-SC) REMARK 3 HYDROGEN BONDS, REMARK 3 9/9 UPPER/LOWER DISTANCE RESTRAINTS FROM 3 SS-BONDS. REMARK 4 REMARK 4 1J5J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-02. REMARK 100 THE DEPOSITION ID IS D_1000001638. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 3.5 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM BEKM-1, 90% H2O, 10% D2O; 1 REMARK 210 MM BEKM-1, 99.9% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 5.3B, XEASY 1.2.11, DYANA REMARK 210 1.5 REMARK 210 METHOD USED : SIMULATED ANNEALING COMBINED REMARK 210 WITH TORSION ANGLE DYNAMICS 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 : NULL REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS 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 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5184 RELATED DB: BMRB REMARK 900 PROTON CHEMICAL SHIFTS AND COUPLING CONSTANTS OF BEKM-1 REMARK 900 RELATED ID: 1LGL RELATED DB: PDB REMARK 900 PDB-ID 1LGL REPRESENTS THE ENSEMBLE. DBREF 1J5J A 1 36 UNP Q9BKB7 SEKM_BUTEU 22 57 SEQRES 1 A 36 ARG PRO THR ASP ILE LYS CYS SER GLU SER TYR GLN CYS SEQRES 2 A 36 PHE PRO VAL CYS LYS SER ARG PHE GLY LYS THR ASN GLY SEQRES 3 A 36 ARG CYS VAL ASN GLY PHE CYS ASP CYS PHE HELIX 1 1 GLU A 9 GLN A 12 5 4 HELIX 2 2 CYS A 13 PHE A 21 1 9 SHEET 1 A 3 PRO A 2 LYS A 6 0 SHEET 2 A 3 PHE A 32 PHE A 36 -1 N CYS A 33 O ILE A 5 SHEET 3 A 3 ASN A 25 VAL A 29 -1 O ASN A 25 N PHE A 36 SSBOND 1 CYS A 7 CYS A 28 1555 1555 2.16 SSBOND 2 CYS A 13 CYS A 33 1555 1555 2.17 SSBOND 3 CYS A 17 CYS A 35 1555 1555 1.95 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 - 23 202 Bytes