Header list of 2axk.pdb file
Complete list - 25 20 Bytes
HEADER TOXIN 05-SEP-05 2AXK
TITLE SOLUTION STRUCTURE OF DISCREPIN, A SCORPION VENOM TOXIN BLOCKING K+
TITLE 2 CHANNELS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISCREPIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN THE VENOM OF
SOURCE 4 SCORPION TITYUS DISCREPANS.
KEYWDS DISCREPIN, SCORPION TOXIN, A-CURRENT, K+-CHANNEL, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR A.PROCHNICKA-CHALUFOUR,G.CORZO,H.SATAKE,M.-F.MARTIN-EAUCLAIRE,
AUTHOR 2 A.R.MURGIA,G.PRESTIPINO,G.D'SUZE,L.D.POSSANI,M.DELEPIERRE
REVDAT 3 25-DEC-19 2AXK 1 REMARK SEQRES LINK
REVDAT 2 24-FEB-09 2AXK 1 VERSN
REVDAT 1 20-JUN-06 2AXK 0
JRNL AUTH A.PROCHNICKA-CHALUFOUR,G.CORZO,H.SATAKE,
JRNL AUTH 2 M.-F.MARTIN-EAUCLAIRE,A.R.MURGIA,G.PRESTIPINO,G.D'SUZE,
JRNL AUTH 3 L.D.POSSANI,M.DELEPIERRE
JRNL TITL SOLUTION STRUCTURE OF DISCREPIN, A NEW K+-CHANNEL BLOCKING
JRNL TITL 2 PEPTIDE FROM THE ALPHA-KTX15 SUBFAMILY.
JRNL REF BIOCHEMISTRY V. 45 1795 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16460026
JRNL DOI 10.1021/BI0519248
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.D'SUZE,C.V.F.BATISTA,A.FRAU,A.R.MURGIA,F.Z.ZAMUDIO,
REMARK 1 AUTH 2 C.SEVCIK,L.D.POSSANI,G.PRESTIPINO
REMARK 1 TITL DISCREPIN, A NEW PEPTIDE OF THE SUB-FAMILY ALPHA-KTX15,
REMARK 1 TITL 2 ISOLATED FROM THE SCORPION TITYUS DISCREPANS IRREVERSIBLY
REMARK 1 TITL 3 BLOCKS K+-CHANNELS (IA CURRENTS) OF CEREBELLUM GRANULAR
REMARK 1 TITL 4 CELLS.
REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 430 256 2004
REMARK 1 REFN ISSN 0003-9861
REMARK 1 PMID 15369825
REMARK 1 DOI 10.1016/J.ABB.2004.07.010
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CNS 1.1
REMARK 3 AUTHORS : VARIAN INC. (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES BASED ON TOTAL OF 565
REMARK 3 MEANINGFUL DISTANCE CONSTRAINTS, 22 DIHEDRAL ANGLE CONSTRAINTS
REMARK 3 AND THREE HYDROGEN BONDS. THREE DISULFIDE BRIDGES (8-29, 14-34,
REMARK 3 18-36) WERE ALSO INCLUDED IN CACLULATION.
REMARK 4
REMARK 4 2AXK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034433.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 4
REMARK 210 IONIC STRENGTH : 5
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3 MM DISCREPIN 10% D2O; 3 MM
REMARK 210 DISCREPIN 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2Q-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 3.1, ARIA 1.2, CNS 1.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY AND BEST SECONDARY
REMARK 210 STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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
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 SER A 9 32.91 -86.43
REMARK 500 1 TYR A 22 -94.35 -117.11
REMARK 500 1 ASN A 23 18.40 -160.08
REMARK 500 2 TYR A 22 -116.53 -124.27
REMARK 500 2 ASN A 23 101.95 -164.40
REMARK 500 3 ASN A 5 71.71 52.98
REMARK 500 3 SER A 11 -27.66 -164.38
REMARK 500 3 TYR A 22 -109.11 -115.10
REMARK 500 3 ASN A 23 15.57 -161.85
REMARK 500 3 ILE A 30 -71.88 -112.75
REMARK 500 3 ASN A 31 40.37 -98.27
REMARK 500 4 SER A 11 -37.64 71.46
REMARK 500 4 TYR A 22 -113.57 -111.93
REMARK 500 4 ASN A 23 19.73 -159.04
REMARK 500 4 ARG A 25 -1.35 -142.50
REMARK 500 5 TYR A 22 -111.71 -110.64
REMARK 500 5 ASN A 23 12.92 -161.59
REMARK 500 5 ILE A 30 -63.60 -99.07
REMARK 500 6 TYR A 22 -108.07 -108.54
REMARK 500 6 ASN A 23 18.18 -161.21
REMARK 500 6 ILE A 30 -66.09 -98.46
REMARK 500 6 ASN A 31 34.98 -96.64
REMARK 500 7 TYR A 22 -109.38 -123.07
REMARK 500 7 ASN A 23 4.62 -162.51
REMARK 500 7 ASN A 31 40.74 -95.18
REMARK 500 8 TYR A 22 -101.87 -109.37
REMARK 500 8 ASN A 23 -15.08 -160.39
REMARK 500 8 ILE A 30 -64.34 -127.97
REMARK 500 8 ASN A 31 33.71 -95.77
REMARK 500 9 SER A 9 43.21 -96.76
REMARK 500 9 SER A 11 -51.41 65.46
REMARK 500 9 TYR A 22 -114.09 -121.81
REMARK 500 9 ASN A 23 92.06 -161.73
REMARK 500 10 TYR A 22 -111.50 -110.05
REMARK 500 10 ASN A 23 6.41 -162.13
REMARK 500 10 ILE A 30 -55.79 -121.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NO SUITABLE SEQUENCE DATABASE REFERENCE WAS AVAILABLE AT
REMARK 999 THE TIME OF PROCESSING THIS FILE.
DBREF 2AXK A 1 38 UNP P84777 KA156_TITDI 1 38
SEQRES 1 A 38 PCA ILE ASP THR ASN VAL LYS CYS SER GLY SER SER LYS
SEQRES 2 A 38 CYS VAL LYS ILE CYS ILE ASP ARG TYR ASN THR ARG GLY
SEQRES 3 A 38 ALA LYS CYS ILE ASN GLY ARG CYS THR CYS TYR PRO
MODRES 2AXK PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 14
HETNAM PCA PYROGLUTAMIC ACID
FORMUL 1 PCA C5 H7 N O3
HELIX 1 1 GLY A 10 TYR A 22 1 13
SHEET 1 A 3 ILE A 2 LYS A 7 0
SHEET 2 A 3 ARG A 33 CYS A 36 -1 O CYS A 34 N VAL A 6
SHEET 3 A 3 ALA A 27 CYS A 29 -1 N LYS A 28 O THR A 35
SSBOND 1 CYS A 8 CYS A 29 1555 1555 2.03
SSBOND 2 CYS A 14 CYS A 34 1555 1555 2.02
SSBOND 3 CYS A 18 CYS A 36 1555 1555 2.03
LINK C PCA A 1 N ILE A 2 1555 1555 1.33
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 - 25 20 Bytes