Header list of 1lgl.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 16-APR-02 1LGL
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
NUMMDL 20
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 1LGL 1 REMARK
REVDAT 2 24-FEB-09 1LGL 1 VERSN
REVDAT 1 20-NOV-02 1LGL 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 1LGL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015932.
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 : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
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 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 THR A 3 -161.28 -127.12
REMARK 500 2 THR A 3 -164.54 -126.95
REMARK 500 3 THR A 3 -164.29 -125.60
REMARK 500 6 THR A 3 -165.06 -126.54
REMARK 500 8 THR A 3 -164.67 -124.99
REMARK 500 10 THR A 3 -162.36 -126.41
REMARK 500 12 THR A 3 -162.14 -123.47
REMARK 500 15 THR A 3 -164.11 -126.62
REMARK 500 16 THR A 3 -164.44 -123.98
REMARK 500 18 THR A 3 -159.58 -126.98
REMARK 500 20 THR A 3 -159.61 -129.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 10 ARG A 27 0.10 SIDE CHAIN
REMARK 500 15 ARG A 27 0.11 SIDE CHAIN
REMARK 500 16 ARG A 1 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
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
DBREF 1LGL 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 2.01
SSBOND 2 CYS A 13 CYS A 33 1555 1555 2.18
SSBOND 3 CYS A 17 CYS A 35 1555 1555 1.93
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