Header list of 1v7f.pdb file
Complete list - b 12 2 Bytes
HEADER TOXIN 16-DEC-03 1V7F
TITLE SOLUTION STRUCTURE OF PHRIXOTOXIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHRIXOTOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PATX1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: PARAPHYSA SCROFA;
SOURCE 4 ORGANISM_TAXID: 269635;
SOURCE 5 OTHER_DETAILS: CHEMICALLY SYNTHETIZED
KEYWDS TOXIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR B.CHAGOT,P.ESCOUBAS,E.VILLEGAS,C.BERNARD,G.FERRAT,G.CORZO,
AUTHOR 2 M.LAZDUNSKI,H.DARBON
REVDAT 3 18-DEC-13 1V7F 1 SOURCE VERSN
REVDAT 2 24-FEB-09 1V7F 1 VERSN
REVDAT 1 23-NOV-04 1V7F 0
JRNL AUTH B.CHAGOT,P.ESCOUBAS,E.VILLEGAS,C.BERNARD,G.FERRAT,G.CORZO,
JRNL AUTH 2 M.LAZDUNSKI,H.DARBON
JRNL TITL SOLUTION STRUCTURE OF PHRIXOTOXIN 1, A SPECIFIC PEPTIDE
JRNL TITL 2 INHIBITOR OF KV4 POTASSIUM CHANNELS FROM THE VENOM OF THE
JRNL TITL 3 THERAPHOSID SPIDER PHRIXOTRICHUS AURATUS
JRNL REF PROTEIN SCI. V. 13 1197 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15096626
JRNL DOI 10.1110/PS.03584304
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,
REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V7F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-DEC-03.
REMARK 100 THE RCSB ID CODE IS RCSB006300.
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 : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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 CYS A 2 176.95 -51.05
REMARK 500 1 CYS A 9 112.70 -166.34
REMARK 500 1 ASP A 10 -169.39 -70.21
REMARK 500 1 ALA A 12 51.99 -166.70
REMARK 500 1 ARG A 13 -169.93 -69.09
REMARK 500 1 LEU A 23 -58.88 79.37
REMARK 500 1 CYS A 25 88.08 -59.89
REMARK 500 2 CYS A 2 -179.97 -52.64
REMARK 500 2 ASP A 10 -168.58 -63.86
REMARK 500 2 ALA A 12 48.84 -166.42
REMARK 500 2 CYS A 21 46.58 -88.76
REMARK 500 2 LEU A 23 -58.26 79.93
REMARK 500 2 CYS A 25 87.94 -60.49
REMARK 500 3 ASP A 10 -165.98 -60.21
REMARK 500 3 ALA A 12 49.79 -169.86
REMARK 500 3 LEU A 23 -62.86 75.83
REMARK 500 3 CYS A 25 93.27 -61.11
REMARK 500 3 ILE A 28 106.19 59.79
REMARK 500 4 MET A 6 -5.07 82.90
REMARK 500 4 ASP A 10 -167.60 -70.73
REMARK 500 4 ALA A 12 59.14 -165.89
REMARK 500 4 ARG A 13 -164.29 -68.71
REMARK 500 4 LYS A 14 65.26 -114.59
REMARK 500 4 ARG A 22 76.55 -170.47
REMARK 500 4 LEU A 23 -59.85 79.07
REMARK 500 4 ILE A 28 128.21 70.57
REMARK 500 5 MET A 6 -6.34 81.30
REMARK 500 5 ASP A 10 -167.99 -60.05
REMARK 500 5 ALA A 12 46.41 -173.88
REMARK 500 5 LEU A 23 -59.58 77.82
REMARK 500 5 CYS A 25 89.85 -57.68
REMARK 500 6 MET A 6 -11.66 88.03
REMARK 500 6 ASP A 10 -166.92 -70.13
REMARK 500 6 ALA A 12 57.43 -169.13
REMARK 500 6 LYS A 14 89.07 -68.57
REMARK 500 6 LEU A 23 -61.16 76.73
REMARK 500 6 CYS A 25 94.83 -57.78
REMARK 500 7 MET A 6 -11.98 84.19
REMARK 500 7 CYS A 9 104.95 -161.11
REMARK 500 7 ASP A 10 -165.02 -70.07
REMARK 500 7 ALA A 12 59.86 -173.26
REMARK 500 7 ARG A 22 77.62 -170.28
REMARK 500 7 LEU A 23 -57.31 80.93
REMARK 500 7 CYS A 25 92.57 -62.75
REMARK 500 8 ASP A 10 -167.89 -70.47
REMARK 500 8 ALA A 12 60.30 -169.03
REMARK 500 8 ARG A 13 -163.45 -68.88
REMARK 500 8 CYS A 21 56.41 -93.42
REMARK 500 8 ARG A 22 74.39 -103.75
REMARK 500 8 LEU A 23 -37.72 86.50
REMARK 500
REMARK 500 THIS ENTRY HAS 160 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 30
DBREF 1V7F A 1 29 UNP P61230 TXP1_PARSR 1 29
SEQADV 1V7F NH2 A 30 UNP P61230 AMIDATION
SEQRES 1 A 30 TYR CYS GLN LYS TRP MET TRP THR CYS ASP SER ALA ARG
SEQRES 2 A 30 LYS CYS CYS GLU GLY LEU VAL CYS ARG LEU TRP CYS LYS
SEQRES 3 A 30 LYS ILE ILE NH2
HET NH2 A 30 1
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
SHEET 1 A 2 VAL A 20 CYS A 21 0
SHEET 2 A 2 CYS A 25 LYS A 26 -1 O LYS A 26 N VAL A 20
SSBOND 1 CYS A 2 CYS A 16 1555 1555 2.03
SSBOND 2 CYS A 9 CYS A 21 1555 1555 2.03
SSBOND 3 CYS A 15 CYS A 25 1555 1555 2.03
LINK C ILE A 29 N NH2 A 30 1555 1555 1.25
SITE 1 AC1 1 ILE A 29
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 12 2 Bytes