Header list of 1lup.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 23-MAY-02 1LUP
TITLE SOLUTION STRUCTURE OF A TOXIN (GSMTX2) FROM THE TARANTULA, GRAMMOSTOLA
TITLE 2 SPATULATA, WHICH INHIBITS MECHANOSENSITIVE ION CHANNELS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GSMTX2;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GRAMMOSTOLA ROSEA;
SOURCE 3 ORGANISM_TAXID: 432528;
SOURCE 4 SECRETION: VENOM
KEYWDS INHIBITOR CYSTEINE KNOT, BETA-SHEET, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.E.OSWALD,T.M.SUCHYNA,R.MCFEETERS,P.GOTTLIEB,F.SACHS
REVDAT 4 23-FEB-22 1LUP 1 REMARK
REVDAT 3 24-FEB-09 1LUP 1 VERSN
REVDAT 2 29-MAR-05 1LUP 1 JRNL
REVDAT 1 07-AUG-02 1LUP 0
JRNL AUTH R.E.OSWALD,T.M.SUCHYNA,R.MCFEETERS,P.GOTTLIEB,F.SACHS
JRNL TITL SOLUTION STRUCTURE OF PEPTIDE TOXINS THAT BLOCK
JRNL TITL 2 MECHANOSENSITIVE ION CHANNELS
JRNL REF J.BIOL.CHEM. V. 277 34443 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12082099
JRNL DOI 10.1074/JBC.M202715200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.M.SUCHYNA,J.H.JOHNSON,K.HAMER,J.F.LEYKAM,D.A.GAGE,
REMARK 1 AUTH 2 H.F.CLEMO,C.M.BAUMGARTEN,F.SACHS
REMARK 1 TITL IDENTIFICATION OF A PEPTIDE TOXIN FROM GRAMMOSTOLA SPATULATA
REMARK 1 TITL 2 SPIDER VENOM THAT BLOCKS STRETCH-ACTIVATED CHANNELS.
REMARK 1 REF J.GEN.PHYSIOL. V. 115 583 2000
REMARK 1 REFN ISSN 0022-1295
REMARK 1 DOI 10.1085/JGP.115.5.583
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2.2, CNS 1.1
REMARK 3 AUTHORS : ACCELRYS, INC. (FELIX), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LUP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016289.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278; 289; 293; 298; 308
REMARK 210 PH : 4.5; 4.5; 4.5; 4.5; 4.5
REMARK 210 IONIC STRENGTH : 1 MM NACL; 1 MM NACL; 1 MM NACL;
REMARK 210 1 MM NACL; 1 MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM NATURAL ABUNDANCE GSMTX2; 2
REMARK 210 MM NATURAL ABUNDANCE GSMTX2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D-TOCSY; 1H
REMARK 210 15N-HSQC; E-COSY; 1H 13C-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, SPARKY 3.95
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: H-D EXCHANGE USING 2D TOCSY FOLLOWING RESUSPENSION OF
REMARK 210 LYOPHILIZED PROTEIN IN 100% D2O
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 CYS A 2 134.20 178.01
REMARK 500 1 GLN A 3 -75.80 -105.14
REMARK 500 1 LYS A 4 54.55 170.36
REMARK 500 1 TRP A 5 158.56 56.75
REMARK 500 1 LYS A 14 -114.43 -62.22
REMARK 500 1 CYS A 15 135.89 60.62
REMARK 500 1 ARG A 22 99.13 -170.08
REMARK 500 1 LEU A 23 -62.39 69.88
REMARK 500 1 ARG A 27 -170.04 -65.79
REMARK 500 2 CYS A 2 90.57 82.87
REMARK 500 2 TRP A 5 168.23 -45.86
REMARK 500 2 MET A 6 -48.31 88.09
REMARK 500 2 TRP A 7 165.15 -43.44
REMARK 500 2 CYS A 16 155.09 -48.00
REMARK 500 2 VAL A 20 -177.09 -58.58
REMARK 500 2 ARG A 22 99.32 -168.84
REMARK 500 2 LEU A 23 -56.74 72.93
REMARK 500 2 CYS A 25 99.76 -41.91
REMARK 500 2 ASN A 30 -57.16 -146.08
REMARK 500 3 CYS A 2 110.43 64.73
REMARK 500 3 GLN A 3 -81.07 -58.84
REMARK 500 3 LYS A 4 59.18 172.89
REMARK 500 3 TRP A 5 161.79 56.26
REMARK 500 3 MET A 6 30.17 37.05
REMARK 500 3 ARG A 13 99.66 -68.38
REMARK 500 3 CYS A 15 150.51 -34.27
REMARK 500 3 ARG A 22 98.34 -170.39
REMARK 500 3 LEU A 23 -61.20 67.12
REMARK 500 3 ARG A 27 -174.43 -59.94
REMARK 500 3 ASN A 30 82.99 -165.03
REMARK 500 4 CYS A 2 125.06 60.99
REMARK 500 4 TRP A 5 172.93 53.67
REMARK 500 4 MET A 6 38.57 31.48
REMARK 500 4 ASP A 10 -159.30 -168.80
REMARK 500 4 GLU A 12 111.62 -164.06
REMARK 500 4 CYS A 15 150.70 -33.69
REMARK 500 4 ARG A 22 99.15 -170.12
REMARK 500 4 LEU A 23 -60.75 68.92
REMARK 500 4 ILE A 28 156.27 -45.22
REMARK 500 4 ASN A 30 37.37 -175.95
REMARK 500 5 CYS A 2 123.67 58.16
REMARK 500 5 GLN A 3 -80.45 -106.72
REMARK 500 5 LYS A 4 36.61 178.20
REMARK 500 5 TRP A 5 150.51 59.09
REMARK 500 5 MET A 6 -35.43 66.45
REMARK 500 5 TRP A 7 157.94 -39.68
REMARK 500 5 GLU A 12 99.81 -160.89
REMARK 500 5 LYS A 14 -107.90 -80.51
REMARK 500 5 CYS A 15 125.64 59.50
REMARK 500 5 ARG A 22 99.24 -170.35
REMARK 500
REMARK 500 THIS ENTRY HAS 193 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LQR RELATED DB: PDB
REMARK 900 STRUCTURE OF TOXIN GSMTX4 FROM THE TARANTULA, GRAMMOSTOLA SPATULATA
DBREF 1LUP A 1 31 PDB 1LUP 1LUP 1 31
SEQRES 1 A 31 TYR CYS GLN LYS TRP MET TRP THR CYS ASP GLU GLU ARG
SEQRES 2 A 31 LYS CYS CYS GLU GLY LEU VAL CYS ARG LEU TRP CYS LYS
SEQRES 3 A 31 ARG ILE ILE ASN MET
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
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 - 23 20 Bytes