Header list of 1emx.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 20-MAR-00 1EMX
TITLE SOLUTION STRUCTURE OF HPTX2, A TOXIN FROM HETEROPODA VENATORIA SPIDER
TITLE 2 VENOM THAT BLOCKS KV4.2 POTASSIUM CHANNEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HETEROPODATOXIN 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HPTX2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HETEROPODA VENATORIA;
SOURCE 3 ORGANISM_COMMON: GIANT CRAB SPIDER;
SOURCE 4 ORGANISM_TAXID: 152925;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 OTHER_DETAILS: VENOM OF SPIDER
KEYWDS TOXIN
EXPDTA SOLUTION NMR
NUMMDL 26
MDLTYP MINIMIZED AVERAGE
AUTHOR C.BERNARD,C.LEGROS,G.FERRAT,U.BISHOFF,A.MARQUARDT,O.PONGS,H.DARBON
REVDAT 4 16-FEB-22 1EMX 1 REMARK
REVDAT 3 24-FEB-09 1EMX 1 VERSN
REVDAT 2 01-APR-03 1EMX 1 JRNL
REVDAT 1 24-JAN-01 1EMX 0
JRNL AUTH C.BERNARD,C.LEGROS,G.FERRAT,U.BISCHOFF,A.MARQUARDT,O.PONGS,
JRNL AUTH 2 H.DARBON
JRNL TITL SOLUTION STRUCTURE OF HPTX2, A TOXIN FROM HETEROPODA
JRNL TITL 2 VENATORIA SPIDER THAT BLOCKS KV4.2 POTASSIUM CHANNEL.
JRNL REF PROTEIN SCI. V. 9 2059 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 11152117
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EMX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010734.
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 : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 26
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ALA A 14 H CYS A 16 1.60
REMARK 500 O ALA A 14 N CYS A 16 2.10
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 3 -174.86 41.97
REMARK 500 1 PHE A 7 -1.79 73.36
REMARK 500 1 THR A 12 -79.53 -70.04
REMARK 500 1 ASP A 15 66.92 -39.15
REMARK 500 1 CYS A 16 116.26 6.96
REMARK 500 1 CYS A 17 162.13 -39.71
REMARK 500 1 ARG A 23 -154.49 -70.42
REMARK 500 1 CYS A 26 47.06 -86.19
REMARK 500 1 ASP A 29 76.31 -56.86
REMARK 500 2 ASP A 2 -72.80 -65.80
REMARK 500 2 CYS A 3 172.00 44.01
REMARK 500 2 LEU A 6 98.40 -44.58
REMARK 500 2 CYS A 10 82.85 -153.36
REMARK 500 2 THR A 12 -85.77 -69.99
REMARK 500 2 ALA A 14 27.76 -71.23
REMARK 500 2 ASP A 15 55.80 -51.81
REMARK 500 2 CYS A 16 123.96 59.49
REMARK 500 2 ARG A 23 -155.97 -70.19
REMARK 500 2 ASP A 29 74.17 -61.60
REMARK 500 3 CYS A 3 -179.36 42.48
REMARK 500 3 ASP A 11 -156.34 -70.08
REMARK 500 3 THR A 12 -158.96 -57.67
REMARK 500 3 ALA A 14 25.67 -71.21
REMARK 500 3 CYS A 17 179.59 -56.40
REMARK 500 3 ARG A 23 -151.53 -70.46
REMARK 500 3 CYS A 26 47.51 -89.11
REMARK 500 3 ASP A 29 76.23 -56.62
REMARK 500 4 CYS A 3 172.61 43.90
REMARK 500 4 LEU A 6 100.79 -46.25
REMARK 500 4 THR A 12 -87.17 -69.16
REMARK 500 4 ALA A 14 28.72 -71.28
REMARK 500 4 ASP A 15 56.43 -51.46
REMARK 500 4 CYS A 16 125.00 59.86
REMARK 500 4 ARG A 23 -149.14 -70.14
REMARK 500 4 ASP A 29 73.68 -62.58
REMARK 500 5 ASP A 2 -72.18 -65.75
REMARK 500 5 CYS A 3 162.27 45.23
REMARK 500 5 LEU A 6 97.87 -43.23
REMARK 500 5 PHE A 7 -1.12 75.31
REMARK 500 5 CYS A 10 88.25 -155.39
REMARK 500 5 THR A 12 -85.24 -70.05
REMARK 500 5 ALA A 14 28.64 -71.17
REMARK 500 5 ASP A 15 55.80 -55.09
REMARK 500 5 CYS A 16 120.13 60.62
REMARK 500 5 CYS A 17 172.91 -59.97
REMARK 500 5 ARG A 23 -152.40 -70.37
REMARK 500 5 CYS A 26 57.80 -92.36
REMARK 500 5 ASP A 29 71.03 -67.69
REMARK 500 6 CYS A 3 163.69 44.67
REMARK 500 6 LEU A 6 95.35 -43.91
REMARK 500
REMARK 500 THIS ENTRY HAS 241 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EMX A 1 30 UNP P58426 TXHP2_HETVE 1 30
SEQRES 1 A 30 ASP ASP CYS GLY LYS LEU PHE SER GLY CYS ASP THR ASN
SEQRES 2 A 30 ALA ASP CYS CYS GLU GLY TYR VAL CYS ARG LEU TRP CYS
SEQRES 3 A 30 LYS LEU ASP TRP
SSBOND 1 CYS A 3 CYS A 17 1555 1555 2.03
SSBOND 2 CYS A 10 CYS A 22 1555 1555 2.03
SSBOND 3 CYS A 16 CYS A 26 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 - 16 20 Bytes