Header list of 1acw.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 10-FEB-97 1ACW
TITLE SOLUTION NMR STRUCTURE OF P01, A NATURAL SCORPION PEPTIDE STRUCTURALLY
TITLE 2 ANALOGOUS TO SCORPION TOXINS SPECIFIC FOR APAMIN-SENSITIVE POTASSIUM
TITLE 3 CHANNEL, 25 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NATURAL SCORPION PEPTIDE P01;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANDROCTONUS MAURETANICUS MAURETANICUS;
SOURCE 3 ORGANISM_TAXID: 6860;
SOURCE 4 STRAIN: MAURETANICUS
KEYWDS SCORPION TOXIN, ANDROCTONUS MAURETANICUS MAURETANICUS, POTASSIUM
KEYWDS 2 CHANNEL, P01, NEUROTOXIN, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR E.BLANC,V.FREMONT,P.SIZUN,S.MEUNIER,J.VAN RIETSCHOTEN,A.THEVAND,
AUTHOR 2 J.M.BERNASSAU,H.DARBON
REVDAT 3 16-FEB-22 1ACW 1 REMARK
REVDAT 2 24-FEB-09 1ACW 1 VERSN
REVDAT 1 01-APR-97 1ACW 0
JRNL AUTH E.BLANC,V.FREMONT,P.SIZUN,S.MEUNIER,J.VAN RIETSCHOTEN,
JRNL AUTH 2 A.THEVAND,J.M.BERNASSAU,H.DARBON
JRNL TITL SOLUTION STRUCTURE OF P01, A NATURAL SCORPION PEPTIDE
JRNL TITL 2 STRUCTURALLY ANALOGOUS TO SCORPION TOXINS SPECIFIC FOR
JRNL TITL 3 APAMIN-SENSITIVE POTASSIUM CHANNEL.
JRNL REF PROTEINS V. 24 359 1996
JRNL REFN ISSN 0887-3585
JRNL PMID 8778783
JRNL DOI 10.1002/(SICI)1097-0134(199603)24:3<359::AID-PROT9>3.0.CO;2-
JRNL DOI 2 B
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE CALCULATED WITH THE
REMARK 3 DISTANCE GEOMETRY SOFTWARE DIANA-1.1 AND THEN MINIMIZED USING
REMARK 3 THE POWELL ALGORITHM OF THE X-PLOR SOFTWARE.
REMARK 4
REMARK 4 1ACW 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_1000170662.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 3.
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX400
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, XPLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : OVERALL ENERGY
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 GLU A 4 -50.58 -139.35
REMARK 500 2 GLU A 4 -51.27 -138.33
REMARK 500 3 GLU A 4 -53.73 -132.04
REMARK 500 4 GLU A 4 -62.76 -135.41
REMARK 500 5 CYS A 3 31.33 -96.66
REMARK 500 5 GLU A 4 -56.54 -127.19
REMARK 500 6 GLU A 4 -59.61 -138.20
REMARK 500 7 GLU A 4 -42.41 -134.45
REMARK 500 8 GLU A 4 -59.79 -142.50
REMARK 500 9 GLU A 4 -59.26 -140.40
REMARK 500 10 CYS A 3 31.15 -96.90
REMARK 500 10 GLU A 4 -55.81 -132.60
REMARK 500 10 GLN A 13 51.68 -112.75
REMARK 500 11 GLU A 4 -57.18 -138.96
REMARK 500 12 GLU A 4 -61.04 -135.73
REMARK 500 13 GLU A 4 -56.72 -139.07
REMARK 500 14 GLU A 4 -49.43 -140.98
REMARK 500 14 GLN A 13 52.54 -110.71
REMARK 500 15 GLU A 4 -56.29 -123.96
REMARK 500 16 CYS A 3 30.97 -97.16
REMARK 500 16 GLU A 4 -56.72 -130.53
REMARK 500 17 GLU A 4 -59.07 -130.55
REMARK 500 18 GLU A 4 -53.79 -141.56
REMARK 500 18 GLN A 13 52.93 -114.44
REMARK 500 19 GLU A 4 -58.16 -130.63
REMARK 500 20 GLU A 4 -57.65 -138.18
REMARK 500 20 GLN A 13 52.99 -113.38
REMARK 500 21 GLU A 4 -60.24 -133.17
REMARK 500 21 GLN A 13 50.26 -111.41
REMARK 500 22 GLU A 4 -63.06 -133.56
REMARK 500 23 CYS A 3 31.70 -97.11
REMARK 500 23 GLU A 4 -54.86 -131.66
REMARK 500 24 GLU A 4 -52.31 -138.69
REMARK 500 25 GLU A 4 -61.02 -132.48
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ACW A 1 29 UNP P56215 SCX1_ANDMA 1 29
SEQRES 1 A 29 VAL SER CYS GLU ASP CYS PRO GLU HIS CYS SER THR GLN
SEQRES 2 A 29 LYS ALA GLN ALA LYS CYS ASP ASN ASP LYS CYS VAL CYS
SEQRES 3 A 29 GLU PRO ILE
HELIX 1 1 ASP A 5 GLN A 13 1 9
SHEET 1 A 2 GLN A 16 ASP A 20 0
SHEET 2 A 2 LYS A 23 GLU A 27 -1 N GLU A 27 O GLN A 16
SSBOND 1 CYS A 3 CYS A 19 1555 1555 2.02
SSBOND 2 CYS A 6 CYS A 24 1555 1555 2.02
SSBOND 3 CYS A 10 CYS A 26 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 - 16 20 Bytes