Header list of 1i26.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 06-FEB-01 1I26
TITLE SOLUTION STRUCTURE OF PTU-1, A TOXIN FROM THE ASSASSIN BUGS PEIRATES
TITLE 2 TURPIS THAT BLOCKS THE VOLTAGE SENSITIVE CALCIUM CHANNEL N-TYPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTU-1;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PEIRATES TURPIS;
SOURCE 3 ORGANISM_TAXID: 181095
KEYWDS CA CHANNEL, ASSASSIN BUG, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 26
AUTHOR C.BERNARD,G.CORZO,A.MOSBAH,T.NAKAJIMA,H.DARBON
REVDAT 4 23-FEB-22 1I26 1 REMARK
REVDAT 3 24-FEB-09 1I26 1 VERSN
REVDAT 2 01-APR-03 1I26 1 JRNL
REVDAT 1 21-NOV-01 1I26 0
JRNL AUTH C.BERNARD,G.CORZO,A.MOSBAH,T.NAKAJIMA,H.DARBON
JRNL TITL SOLUTION STRUCTURE OF PTU1, A TOXIN FROM THE ASSASSIN BUG
JRNL TITL 2 PEIRATES TURPIS THAT BLOCKS THE VOLTAGE-SENSITIVE CALCIUM
JRNL TITL 3 CHANNEL N-TYPE.
JRNL REF BIOCHEMISTRY V. 40 12795 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11669615
JRNL DOI 10.1021/BI015537J
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA, X-PLOR
REMARK 3 AUTHORS : GUNTERT, P. ET AL. (DYANA), BRUNGER, A.T. ET AL.
REMARK 3 (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I26 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012809.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : WATER
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 26
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
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 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 PRO A 11 88.70 -60.30
REMARK 500 1 PHE A 13 109.09 -58.15
REMARK 500 1 ASP A 16 25.95 43.59
REMARK 500 1 SER A 27 77.00 -119.39
REMARK 500 1 ASN A 31 82.59 45.82
REMARK 500 1 LYS A 32 154.78 178.75
REMARK 500 2 GLU A 2 -174.66 -60.83
REMARK 500 2 LYS A 3 -173.04 -60.47
REMARK 500 2 PRO A 11 89.34 -67.03
REMARK 500 2 ASP A 16 23.88 45.12
REMARK 500 2 ASN A 31 87.41 44.69
REMARK 500 2 LYS A 32 153.43 168.44
REMARK 500 3 LYS A 3 -169.78 -70.05
REMARK 500 3 PRO A 11 87.57 -63.26
REMARK 500 3 PHE A 13 110.34 -17.88
REMARK 500 3 THR A 15 -11.95 78.77
REMARK 500 3 LYS A 17 86.94 -170.56
REMARK 500 3 PRO A 18 -175.71 -69.14
REMARK 500 3 SER A 27 75.59 -119.88
REMARK 500 3 ASN A 31 74.31 45.72
REMARK 500 4 LYS A 3 -175.50 -59.93
REMARK 500 4 PRO A 11 88.16 -68.33
REMARK 500 4 ASP A 16 25.11 44.38
REMARK 500 4 ASN A 31 88.26 45.59
REMARK 500 4 LYS A 32 156.12 168.43
REMARK 500 5 GLU A 2 -178.58 -60.09
REMARK 500 5 LYS A 3 -167.26 -63.44
REMARK 500 5 PRO A 11 88.06 -52.89
REMARK 500 5 PHE A 13 112.47 -22.16
REMARK 500 5 THR A 15 -16.01 80.63
REMARK 500 5 LYS A 17 76.68 -170.54
REMARK 500 5 PRO A 18 -173.29 -62.57
REMARK 500 5 ASN A 31 81.44 46.72
REMARK 500 5 LYS A 32 162.76 168.00
REMARK 500 6 LYS A 3 -170.21 -60.26
REMARK 500 6 PRO A 11 90.44 -66.18
REMARK 500 6 ASP A 16 25.88 43.72
REMARK 500 6 PRO A 18 -167.74 -66.96
REMARK 500 6 ASN A 31 89.32 43.64
REMARK 500 6 LYS A 32 174.81 164.70
REMARK 500 7 GLU A 2 -174.56 -62.10
REMARK 500 7 LYS A 3 -174.58 -60.39
REMARK 500 7 PRO A 11 86.66 -69.50
REMARK 500 7 PHE A 13 102.27 -30.14
REMARK 500 7 THR A 15 -13.92 79.28
REMARK 500 7 LYS A 17 90.42 -170.56
REMARK 500 7 PRO A 22 4.36 -69.51
REMARK 500 7 ASN A 31 85.88 45.13
REMARK 500 7 LYS A 32 149.08 168.90
REMARK 500 8 GLU A 2 -174.62 -67.08
REMARK 500
REMARK 500 THIS ENTRY HAS 177 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1I26 A 1 34 UNP P58606 PTU1_PEITU 1 34
SEQRES 1 A 34 ALA GLU LYS ASP CYS ILE ALA PRO GLY ALA PRO CYS PHE
SEQRES 2 A 34 GLY THR ASP LYS PRO CYS CYS ASN PRO ARG ALA TRP CYS
SEQRES 3 A 34 SER SER TYR ALA ASN LYS CYS LEU
SHEET 1 A 2 CYS A 26 SER A 27 0
SHEET 2 A 2 LYS A 32 CYS A 33 -1 O LYS A 32 N SER A 27
SSBOND 1 CYS A 5 CYS A 20 1555 1555 2.03
SSBOND 2 CYS A 12 CYS A 26 1555 1555 2.03
SSBOND 3 CYS A 19 CYS A 33 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 - b 23 2 Bytes