Header list of 1wt7.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 16-NOV-04 1WT7
TITLE SOLUTION STRUCTURE OF BUTX-MTX: A BUTANTOXIN-MAUROTOXIN CHIMERA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BUTX-MTX;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BUTANTOXIN-MAUROTOXIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: BUTANTOXIN-MAUROTOXIN CHIMERA (BUTANTOXIN: TOXIN FROM
SOURCE 4 THE BRAZILIAN SCORPION TITYUS SERRULATUS, MAUROTOXIN: TOXIN FROM THE
SOURCE 5 SCORPION S. MAURUS PALMATUS)
KEYWDS MAUROTOXIN, BUTANTOXIN, SCORPION TOXIN, K+ CHANNELS, MOLECULAR
KEYWDS 2 CONTACTS, TOXIN AFFINITY, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR S.M'BAREK,B.CHAGOT,N.ANDREOTTI,V.VISAN,P.MANSUELLE,S.GRISSMER,
AUTHOR 2 M.MARRAKCHI,M.EL AYEB,F.SAMPIERI,H.DARBON,Z.FAJLOUN,M.DE WAARD,J.-
AUTHOR 3 M.SABATIER
REVDAT 4 02-MAR-22 1WT7 1 REMARK
REVDAT 3 24-FEB-09 1WT7 1 VERSN
REVDAT 2 02-AUG-05 1WT7 1 JRNL
REVDAT 1 30-NOV-04 1WT7 0
JRNL AUTH S.M'BAREK,B.CHAGOT,N.ANDREOTTI,V.VISAN,P.MANSUELLE,
JRNL AUTH 2 S.GRISSMER,M.MARRAKCHI,M.EL AYEB,F.SAMPIERI,H.DARBON,
JRNL AUTH 3 Z.FAJLOUN,M.DE WAARD,J.M.SABATIER
JRNL TITL INCREASING THE MOLECULAR CONTACTS BETWEEN MAUROTOXIN AND
JRNL TITL 2 KV1.2 CHANNEL AUGMENTS LIGAND AFFINITY.
JRNL REF PROTEINS V. 60 401 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 15971207
JRNL DOI 10.1002/PROT.20509
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WT7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000023971.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290
REMARK 210 PH : 3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
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 : XWINNMR 2.1, XEASY 1.13, ARIA
REMARK 210 1.2
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY, STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS
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: 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 LEU A 6 -71.25 -109.49
REMARK 500 1 LEU A 8 43.95 -101.68
REMARK 500 1 ALA A 9 83.68 -55.68
REMARK 500 2 ALA A 9 81.10 -53.90
REMARK 500 2 LYS A 34 -15.07 73.25
REMARK 500 3 THR A 4 -95.28 -108.61
REMARK 500 3 LEU A 8 31.30 -89.76
REMARK 500 3 ALA A 9 85.41 -55.17
REMARK 500 3 ASN A 33 97.96 -53.77
REMARK 500 4 ALA A 9 83.82 -56.34
REMARK 500 4 ASN A 28 103.96 -58.73
REMARK 500 5 THR A 4 37.46 -150.66
REMARK 500 5 ALA A 9 79.43 -58.67
REMARK 500 5 THR A 11 32.18 -89.50
REMARK 500 5 TYR A 39 22.51 -79.62
REMARK 500 6 ALA A 9 81.06 -56.44
REMARK 500 7 SER A 3 44.76 -77.63
REMARK 500 7 THR A 4 -21.31 -148.04
REMARK 500 7 ALA A 9 83.34 -57.69
REMARK 500 8 ALA A 9 84.13 -49.91
REMARK 500 9 THR A 4 39.76 -149.98
REMARK 500 9 ALA A 9 81.76 -52.97
REMARK 500 9 ASN A 28 105.48 -58.99
REMARK 500 10 SER A 3 -70.45 -73.36
REMARK 500 10 ALA A 9 81.41 -58.21
REMARK 500 10 ASN A 33 17.98 43.15
REMARK 500 10 LYS A 34 -56.43 169.85
REMARK 500 10 TYR A 39 23.21 -79.82
REMARK 500 11 ALA A 9 82.59 -54.53
REMARK 500 11 ASN A 33 80.99 -19.04
REMARK 500 11 LYS A 34 -52.16 157.31
REMARK 500 12 LEU A 8 31.43 -84.37
REMARK 500 12 ALA A 9 83.67 -53.84
REMARK 500 12 ASN A 33 79.55 -67.31
REMARK 500 12 LYS A 34 -46.69 169.01
REMARK 500 13 SER A 3 34.97 -90.92
REMARK 500 13 THR A 4 -135.29 -161.42
REMARK 500 13 CYS A 5 82.03 77.90
REMARK 500 13 LEU A 6 -61.27 -90.07
REMARK 500 13 ASP A 7 90.35 -160.53
REMARK 500 13 ALA A 9 79.71 -55.68
REMARK 500 14 LEU A 6 -70.45 -103.93
REMARK 500 14 ALA A 9 82.34 -53.20
REMARK 500 14 ASN A 33 54.89 -63.51
REMARK 500 14 LYS A 34 -27.51 174.26
REMARK 500 15 ALA A 9 82.22 -59.23
REMARK 500 16 THR A 4 -80.54 -123.76
REMARK 500 16 LEU A 8 47.54 -93.43
REMARK 500 16 ALA A 9 83.82 -53.19
REMARK 500 17 THR A 4 53.76 -117.36
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WT7 A 1 9 UNP P59936 SCK4_TITSE 1 9
DBREF 1WT7 A 10 41 UNP P80719 SCXM_SCOMA 3 34
SEQRES 1 A 41 TRP CYS SER THR CYS LEU ASP LEU ALA CYS THR GLY SER
SEQRES 2 A 41 LYS ASP CYS TYR ALA PRO CYS ARG LYS GLN THR GLY CYS
SEQRES 3 A 41 PRO ASN ALA LYS CYS ILE ASN LYS SER CYS LYS CYS TYR
SEQRES 4 A 41 GLY CYS
HELIX 1 1 GLY A 12 GLY A 25 1 14
SHEET 1 A 2 ALA A 29 ILE A 32 0
SHEET 2 A 2 SER A 35 CYS A 38 -1 O SER A 35 N ILE A 32
SSBOND 1 CYS A 2 CYS A 5 1555 1555 2.03
SSBOND 2 CYS A 10 CYS A 31 1555 1555 2.04
SSBOND 3 CYS A 16 CYS A 36 1555 1555 2.03
SSBOND 4 CYS A 20 CYS A 38 1555 1555 2.03
SSBOND 5 CYS A 26 CYS A 41 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 - r 2 2 Bytes