Header list of 1mb6.pdb file
Complete list - 29 20 Bytes
HEADER TOXIN 02-AUG-02 1MB6
TITLE THREE DIMENSIONAL SOLUTION STRUCTURE OF HUWENTOXIN-IV BY 2D 1H-NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUWENTOXIN-IV;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORNITHOCTONUS HUWENA;
SOURCE 3 ORGANISM_COMMON: CHINESE EARTH TIGER;
SOURCE 4 ORGANISM_TAXID: 29017;
SOURCE 5 SECRETION: VENOM
KEYWDS CONTAINING A DOUBLE-STRANDED BETA-SHEET AND FOUR BETA-TURNS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.PENG,Q.SHU,S.P.LIANG
REVDAT 4 29-NOV-17 1MB6 1 REMARK HELIX
REVDAT 3 24-FEB-09 1MB6 1 VERSN
REVDAT 2 05-APR-05 1MB6 1 JRNL
REVDAT 1 21-AUG-02 1MB6 0
JRNL AUTH K.PENG,Q.SHU,Z.LIU,S.P.LIANG
JRNL TITL FUNCTION AND SOLUTION STRUCTURE OF HUWENTOXIN-IV, A POTENT
JRNL TITL 2 NEURONAL TETRODOTOXIN (TTX)-SENSITIVE SODIUM CHANNEL
JRNL TITL 3 ANTAGONIST FROM CHINESE BIRD SPIDER SELENOCOSMIA HUWENA
JRNL REF J.BIOL.CHEM. V. 277 47564 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12228241
JRNL DOI 10.1074/JBC.M204063200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 527 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 14 DIHEDRAL ANGEL RESTRAINTS AND
REMARK 3 9 FAKE DISTANCE RESTRAINTS FROM DISULFIDE BONDS.
REMARK 4
REMARK 4 1MB6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016799.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300.00
REMARK 210 PH : 4.50
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 5MM HUWENTOXIN-IV MMOL/L
REMARK 210 PHOSPHATE BUFFER; 90%H2O, 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 2 GLU A 4 -176.99 -69.90
REMARK 500 4 GLU A 4 -172.27 -68.29
REMARK 500 4 ASN A 13 79.12 -105.78
REMARK 500 4 GLN A 15 46.43 -107.71
REMARK 500 9 ASP A 14 99.00 -69.56
REMARK 500 11 GLN A 34 56.53 -91.46
REMARK 500 12 GLU A 4 -174.72 -66.95
REMARK 500 12 LYS A 21 74.66 52.04
REMARK 500 13 ASN A 13 78.57 -110.49
REMARK 500 13 LYS A 21 74.32 55.36
REMARK 500 14 GLU A 4 -178.07 -68.49
REMARK 500 17 ARG A 29 -4.27 72.21
REMARK 500 18 GLU A 4 -171.84 -65.36
REMARK 500 18 ASN A 13 65.37 -100.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 26 0.31 SIDE CHAIN
REMARK 500 1 ARG A 29 0.30 SIDE CHAIN
REMARK 500 2 ARG A 26 0.30 SIDE CHAIN
REMARK 500 2 ARG A 29 0.31 SIDE CHAIN
REMARK 500 3 ARG A 26 0.30 SIDE CHAIN
REMARK 500 3 ARG A 29 0.30 SIDE CHAIN
REMARK 500 4 ARG A 26 0.30 SIDE CHAIN
REMARK 500 4 ARG A 29 0.31 SIDE CHAIN
REMARK 500 5 ARG A 26 0.32 SIDE CHAIN
REMARK 500 5 ARG A 29 0.28 SIDE CHAIN
REMARK 500 6 ARG A 26 0.28 SIDE CHAIN
REMARK 500 6 ARG A 29 0.30 SIDE CHAIN
REMARK 500 7 ARG A 26 0.32 SIDE CHAIN
REMARK 500 7 ARG A 29 0.30 SIDE CHAIN
REMARK 500 8 ARG A 26 0.30 SIDE CHAIN
REMARK 500 8 ARG A 29 0.30 SIDE CHAIN
REMARK 500 9 ARG A 26 0.31 SIDE CHAIN
REMARK 500 9 ARG A 29 0.32 SIDE CHAIN
REMARK 500 10 ARG A 26 0.32 SIDE CHAIN
REMARK 500 10 ARG A 29 0.27 SIDE CHAIN
REMARK 500 11 ARG A 26 0.31 SIDE CHAIN
REMARK 500 11 ARG A 29 0.30 SIDE CHAIN
REMARK 500 12 ARG A 26 0.26 SIDE CHAIN
REMARK 500 12 ARG A 29 0.31 SIDE CHAIN
REMARK 500 13 ARG A 26 0.31 SIDE CHAIN
REMARK 500 13 ARG A 29 0.28 SIDE CHAIN
REMARK 500 14 ARG A 26 0.28 SIDE CHAIN
REMARK 500 14 ARG A 29 0.29 SIDE CHAIN
REMARK 500 15 ARG A 26 0.31 SIDE CHAIN
REMARK 500 15 ARG A 29 0.32 SIDE CHAIN
REMARK 500 16 ARG A 26 0.32 SIDE CHAIN
REMARK 500 16 ARG A 29 0.32 SIDE CHAIN
REMARK 500 17 ARG A 26 0.29 SIDE CHAIN
REMARK 500 17 ARG A 29 0.31 SIDE CHAIN
REMARK 500 18 ARG A 26 0.24 SIDE CHAIN
REMARK 500 18 ARG A 29 0.32 SIDE CHAIN
REMARK 500 19 ARG A 26 0.31 SIDE CHAIN
REMARK 500 19 ARG A 29 0.31 SIDE CHAIN
REMARK 500 20 ARG A 26 0.32 SIDE CHAIN
REMARK 500 20 ARG A 29 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MB6 A 1 35 UNP P83303 TXH4_ORNHU 1 35
SEQRES 1 A 35 GLU CYS LEU GLU ILE PHE LYS ALA CYS ASN PRO SER ASN
SEQRES 2 A 35 ASP GLN CYS CYS LYS SER SER LYS LEU VAL CYS SER ARG
SEQRES 3 A 35 LYS THR ARG TRP CYS LYS TYR GLN ILE
SHEET 1 A 2 LEU A 22 SER A 25 0
SHEET 2 A 2 TRP A 30 TYR A 33 -1 O LYS A 32 N VAL A 23
SSBOND 1 CYS A 2 CYS A 17 1555 1555 2.02
SSBOND 2 CYS A 9 CYS A 24 1555 1555 2.02
SSBOND 3 CYS A 16 CYS A 31 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 - 29 20 Bytes