Header list of 1lqi.pdb file
Complete list - b 23 2 Bytes
HEADER NEUROTOXIN 17-JUN-96 1LQI
TITLE INSECTICIDAL ALPHA SCORPION TOXIN ISOLATED FROM THE VENOM OF SCORPION
TITLE 2 LEIURUS QUINQUESTRIATUS HEBRAEUS, NMR, 29 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSECT TOXIN ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NEUROTOXIN, INSECTOTOXIN, SCORPION TOXIN, LQHAIT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEIURUS QUINQUESTRIATUS HEBRAEUS;
SOURCE 3 ORGANISM_TAXID: 6884;
SOURCE 4 STRAIN: HEBRAEUS;
SOURCE 5 GENE: POTENTIAL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: T7
KEYWDS NEUROTOXIN, SODIUM CHANNEL INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 29
AUTHOR V.TUGARINOV,I.KUSTANOVICH,N.ZILBERBERG,M.GUREVITZ,J.ANGLISTER
REVDAT 3 23-FEB-22 1LQI 1 REMARK
REVDAT 2 24-FEB-09 1LQI 1 VERSN
REVDAT 1 12-MAR-97 1LQI 0
JRNL AUTH V.TUGARINOV,I.KUSTANOVICH,N.ZILBERBERG,M.GUREVITZ,
JRNL AUTH 2 J.ANGLISTER
JRNL TITL SOLUTION STRUCTURES OF A HIGHLY INSECTICIDAL RECOMBINANT
JRNL TITL 2 SCORPION ALPHA-TOXIN AND A MUTANT WITH INCREASED ACTIVITY.
JRNL REF BIOCHEMISTRY V. 36 2414 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9054546
JRNL DOI 10.1021/BI961497L
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.ZILBERBERG,D.GORDON,M.PELHATE,M.E.ADAMS,T.M.NORRIS,
REMARK 1 AUTH 2 E.ZLOTKIN,M.GUREVITZ
REMARK 1 TITL FUNCTIONAL EXPRESSION AND GENETIC ALTERATION OF AN ALPHA
REMARK 1 TITL 2 SCORPION NEUROTOXIN
REMARK 1 REF BIOCHEMISTRY V. 35 10215 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LQI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174801.
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 : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 29
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 1 ASN A 12 26.40 40.70
REMARK 500 1 GLU A 16 152.67 -47.42
REMARK 500 1 LEU A 26 -70.08 -65.12
REMARK 500 1 ALA A 40 -139.74 -172.57
REMARK 500 1 ALA A 46 -163.56 -116.10
REMARK 500 1 ILE A 58 -167.00 -112.78
REMARK 500 2 LYS A 9 -147.41 -112.42
REMARK 500 2 CYS A 13 -155.82 -89.09
REMARK 500 2 TYR A 22 -70.45 -51.90
REMARK 500 2 LEU A 26 -70.69 -70.16
REMARK 500 2 ALA A 32 -161.81 -103.25
REMARK 500 2 SER A 34 -165.29 -163.43
REMARK 500 2 ALA A 40 -127.73 -178.82
REMARK 500 2 ALA A 46 -143.89 -118.59
REMARK 500 3 LYS A 9 -157.19 -118.15
REMARK 500 3 TYR A 11 40.91 -97.58
REMARK 500 3 ASN A 12 29.39 36.85
REMARK 500 3 LEU A 26 -70.71 -65.53
REMARK 500 3 ALA A 40 129.39 69.26
REMARK 500 3 ASP A 54 -7.76 -59.48
REMARK 500 4 TYR A 11 34.61 -99.09
REMARK 500 4 ASN A 12 29.56 37.50
REMARK 500 4 ALA A 40 17.87 52.73
REMARK 500 4 ASN A 45 74.56 -111.96
REMARK 500 4 ALA A 46 -161.79 -79.30
REMARK 500 4 LYS A 63 -163.49 -161.70
REMARK 500 5 ILE A 7 134.76 -39.86
REMARK 500 5 LYS A 9 -150.65 -128.92
REMARK 500 5 ASN A 10 -100.81 15.69
REMARK 500 5 VAL A 14 -177.78 -69.06
REMARK 500 5 ALA A 40 131.34 70.48
REMARK 500 5 ALA A 46 -156.64 -115.97
REMARK 500 5 ILE A 58 -168.57 -113.29
REMARK 500 5 LYS A 63 -166.29 -164.67
REMARK 500 6 LYS A 9 -150.80 -115.35
REMARK 500 6 ASN A 10 -109.59 25.02
REMARK 500 6 TYR A 11 64.77 -113.23
REMARK 500 6 LEU A 26 -70.84 -70.92
REMARK 500 6 ALA A 40 116.25 68.16
REMARK 500 6 ALA A 46 -149.07 -79.97
REMARK 500 6 CYS A 47 117.05 -164.06
REMARK 500 6 LYS A 63 -165.78 -102.45
REMARK 500 7 TYR A 11 36.72 -98.87
REMARK 500 7 ASN A 12 29.30 37.49
REMARK 500 7 GLU A 16 153.13 -42.13
REMARK 500 7 LEU A 26 -71.01 -61.82
REMARK 500 7 ALA A 40 134.28 71.19
REMARK 500 7 ALA A 51 50.39 39.54
REMARK 500 8 LYS A 9 -147.01 -129.02
REMARK 500 8 ASN A 10 -85.80 -39.99
REMARK 500
REMARK 500 THIS ENTRY HAS 213 RAMACHANDRAN OUTLIERS.
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 1 ARG A 3 0.25 SIDE CHAIN
REMARK 500 1 ARG A 19 0.24 SIDE CHAIN
REMARK 500 1 ARG A 59 0.27 SIDE CHAIN
REMARK 500 1 ARG A 65 0.29 SIDE CHAIN
REMARK 500 2 ARG A 3 0.28 SIDE CHAIN
REMARK 500 2 ARG A 19 0.25 SIDE CHAIN
REMARK 500 2 ARG A 59 0.17 SIDE CHAIN
REMARK 500 2 ARG A 65 0.30 SIDE CHAIN
REMARK 500 3 ARG A 3 0.32 SIDE CHAIN
REMARK 500 3 ARG A 19 0.23 SIDE CHAIN
REMARK 500 3 ARG A 59 0.32 SIDE CHAIN
REMARK 500 3 ARG A 65 0.30 SIDE CHAIN
REMARK 500 4 ARG A 3 0.08 SIDE CHAIN
REMARK 500 4 ARG A 19 0.30 SIDE CHAIN
REMARK 500 4 ARG A 65 0.20 SIDE CHAIN
REMARK 500 5 ARG A 3 0.20 SIDE CHAIN
REMARK 500 5 ARG A 19 0.17 SIDE CHAIN
REMARK 500 5 ARG A 59 0.17 SIDE CHAIN
REMARK 500 5 ARG A 65 0.22 SIDE CHAIN
REMARK 500 6 ARG A 3 0.23 SIDE CHAIN
REMARK 500 6 ARG A 19 0.24 SIDE CHAIN
REMARK 500 6 ARG A 59 0.19 SIDE CHAIN
REMARK 500 6 ARG A 65 0.28 SIDE CHAIN
REMARK 500 7 ARG A 3 0.18 SIDE CHAIN
REMARK 500 7 ARG A 59 0.30 SIDE CHAIN
REMARK 500 7 ARG A 65 0.32 SIDE CHAIN
REMARK 500 8 ARG A 3 0.32 SIDE CHAIN
REMARK 500 8 ARG A 19 0.32 SIDE CHAIN
REMARK 500 8 ARG A 59 0.27 SIDE CHAIN
REMARK 500 8 ARG A 65 0.28 SIDE CHAIN
REMARK 500 9 ARG A 3 0.23 SIDE CHAIN
REMARK 500 9 ARG A 19 0.24 SIDE CHAIN
REMARK 500 9 ARG A 59 0.21 SIDE CHAIN
REMARK 500 10 ARG A 3 0.31 SIDE CHAIN
REMARK 500 10 ARG A 19 0.22 SIDE CHAIN
REMARK 500 10 ARG A 59 0.32 SIDE CHAIN
REMARK 500 10 ARG A 65 0.24 SIDE CHAIN
REMARK 500 11 ARG A 3 0.32 SIDE CHAIN
REMARK 500 11 ARG A 19 0.19 SIDE CHAIN
REMARK 500 11 ARG A 59 0.32 SIDE CHAIN
REMARK 500 11 ARG A 65 0.27 SIDE CHAIN
REMARK 500 12 ARG A 3 0.31 SIDE CHAIN
REMARK 500 12 ARG A 19 0.15 SIDE CHAIN
REMARK 500 12 ARG A 59 0.25 SIDE CHAIN
REMARK 500 12 ARG A 65 0.30 SIDE CHAIN
REMARK 500 13 ARG A 3 0.11 SIDE CHAIN
REMARK 500 13 ARG A 19 0.14 SIDE CHAIN
REMARK 500 13 ARG A 59 0.17 SIDE CHAIN
REMARK 500 13 ARG A 65 0.28 SIDE CHAIN
REMARK 500 14 ARG A 3 0.16 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 110 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LQH RELATED DB: PDB
DBREF 1LQI A 2 64 UNP P17728 SCXA_LEIQH 20 82
SEQRES 1 A 65 MET VAL ARG ASP ALA TYR ILE ALA LYS ASN TYR ASN CYS
SEQRES 2 A 65 VAL TYR GLU CYS PHE ARG ASP ALA TYR CYS ASN GLU LEU
SEQRES 3 A 65 CYS THR LYS ASN GLY ALA SER SER GLY TYR CYS GLN TRP
SEQRES 4 A 65 ALA GLY LYS TYR GLY ASN ALA CYS TRP CYS TYR ALA LEU
SEQRES 5 A 65 PRO ASP ASN VAL PRO ILE ARG VAL PRO GLY LYS CYS ARG
HELIX 1 1 ASP A 20 ASN A 30 1 11
SHEET 1 A 2 SER A 34 TRP A 39 0
SHEET 2 A 2 ASN A 45 TYR A 50 -1 N TYR A 50 O SER A 34
SSBOND 1 CYS A 13 CYS A 64 1555 1555 2.02
SSBOND 2 CYS A 17 CYS A 37 1555 1555 2.02
SSBOND 3 CYS A 23 CYS A 47 1555 1555 2.02
SSBOND 4 CYS A 27 CYS A 49 1555 1555 2.02
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