Header list of 1shi.pdb file
Complete list - v 29 2 Bytes
HEADER NEUROTOXIN 07-DEC-94 1SHI
TITLE REFINED STRUCTURE IN SOLUTION OF THE SEA ANEMONE NEUROTOXIN SHI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROTOXIN I;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STICHODACTYLA HELIANTHUS;
SOURCE 3 ORGANISM_TAXID: 6123
KEYWDS NEUROTOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.K.PALLAGHY,T.R.DYKE,R.S.NORTON
REVDAT 3 29-NOV-17 1SHI 1 REMARK HELIX
REVDAT 2 24-FEB-09 1SHI 1 VERSN
REVDAT 1 07-FEB-95 1SHI 0
JRNL AUTH G.R.WILCOX,R.H.FOGH,R.S.NORTON
JRNL TITL REFINED STRUCTURE IN SOLUTION OF THE SEA ANEMONE NEUROTOXIN
JRNL TITL 2 SHI.
JRNL REF J.BIOL.CHEM. V. 268 24707 1993
JRNL REFN ISSN 0021-9258
JRNL PMID 7901218
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.MANOLERAS,R.S.NORTON
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF NEUROTOXIN III
REMARK 1 TITL 2 FROM THE SEA ANEMONE ANEMONIA SULCATA
REMARK 1 REF BIOCHEMISTRY V. 33 11051 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.S.NORTON
REMARK 1 TITL STRUCTURE AND STRUCTURE-FUNCTION RELATIONSHIPS OF SEA
REMARK 1 TITL 2 ANEMONE PROTEINS THAT INTERACT WITH THE SODIUM CHANNEL
REMARK 1 REF TOXICON V. 29 1051 1991
REMARK 1 REFN ISSN 0041-0101
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.H.FOGH,W.R.KEM,R.S.NORTON
REMARK 1 TITL SOLUTION STRUCTURE OF NEUROTOXIN I FROM THE SEA ANEMONE
REMARK 1 TITL 2 STICHODACTYLA HELIANTHUS. A NUCLEAR MAGNETIC RESONANCE,
REMARK 1 TITL 3 DISTANCE GEOMETRY, AND RESTRAINED MOLECULAR DYNAMICS STUDY
REMARK 1 REF J.BIOL.CHEM. V. 265 13016 1990
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SHI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176375.
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 : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 3 10.52 -141.55
REMARK 500 1 LYS A 4 172.43 59.11
REMARK 500 1 ASP A 7 69.73 -165.73
REMARK 500 1 PRO A 10 -91.09 -80.52
REMARK 500 1 ASP A 11 -155.81 43.23
REMARK 500 1 ILE A 12 -52.22 171.77
REMARK 500 1 ALA A 15 146.91 166.95
REMARK 500 1 TYR A 36 -146.00 -155.21
REMARK 500 1 TYR A 37 -91.34 -177.52
REMARK 500 1 ASP A 42 -151.84 -116.35
REMARK 500 1 CYS A 43 98.09 -163.98
REMARK 500 1 LYS A 46 89.00 -53.51
REMARK 500 1 LYS A 47 87.69 41.89
REMARK 500 2 ALA A 2 163.43 -43.99
REMARK 500 2 CYS A 3 144.13 178.75
REMARK 500 2 LYS A 4 -173.49 -67.25
REMARK 500 2 ASP A 7 81.84 -150.15
REMARK 500 2 ASP A 11 -178.64 60.89
REMARK 500 2 ILE A 12 -43.03 -142.36
REMARK 500 2 THR A 14 -87.67 -138.37
REMARK 500 2 SER A 25 141.64 163.91
REMARK 500 2 LYS A 32 151.45 -41.99
REMARK 500 2 SER A 35 96.01 -45.08
REMARK 500 2 TYR A 36 70.57 58.79
REMARK 500 2 TYR A 37 -92.63 -39.75
REMARK 500 2 THR A 38 -127.53 -93.62
REMARK 500 2 ILE A 40 13.58 -144.27
REMARK 500 2 ASP A 42 19.43 -140.23
REMARK 500 2 CYS A 43 89.32 43.09
REMARK 500 2 LYS A 46 104.16 -53.38
REMARK 500 2 LYS A 47 103.13 -43.65
REMARK 500 3 CYS A 5 -175.26 -58.85
REMARK 500 3 ASP A 7 57.51 -142.98
REMARK 500 3 ASP A 11 -147.83 -101.55
REMARK 500 3 ALA A 15 104.32 -43.50
REMARK 500 3 LEU A 17 76.42 62.30
REMARK 500 3 CYS A 26 -172.25 -67.27
REMARK 500 3 TYR A 36 -141.59 -153.55
REMARK 500 3 TYR A 37 -76.34 -174.53
REMARK 500 3 THR A 38 -131.08 -126.33
REMARK 500 3 ILE A 40 10.40 -140.65
REMARK 500 3 ASP A 42 -151.03 -131.18
REMARK 500 3 CYS A 43 94.85 -164.51
REMARK 500 3 LYS A 46 153.63 -43.98
REMARK 500 3 LYS A 47 95.42 -64.07
REMARK 500 4 CYS A 3 144.70 -175.16
REMARK 500 4 ILE A 12 -91.25 57.05
REMARK 500 4 ARG A 13 -71.12 -88.38
REMARK 500 4 THR A 14 -91.19 -140.66
REMARK 500 4 LEU A 23 96.77 -43.98
REMARK 500
REMARK 500 THIS ENTRY HAS 238 RAMACHANDRAN OUTLIERS.
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 13 0.18 SIDE CHAIN
REMARK 500 1 ARG A 45 0.26 SIDE CHAIN
REMARK 500 2 ARG A 13 0.23 SIDE CHAIN
REMARK 500 2 ARG A 45 0.27 SIDE CHAIN
REMARK 500 3 ARG A 13 0.17 SIDE CHAIN
REMARK 500 3 ARG A 45 0.29 SIDE CHAIN
REMARK 500 4 ARG A 13 0.26 SIDE CHAIN
REMARK 500 4 ARG A 45 0.31 SIDE CHAIN
REMARK 500 5 ARG A 13 0.28 SIDE CHAIN
REMARK 500 5 ARG A 45 0.13 SIDE CHAIN
REMARK 500 6 ARG A 13 0.23 SIDE CHAIN
REMARK 500 6 ARG A 45 0.29 SIDE CHAIN
REMARK 500 7 ARG A 13 0.23 SIDE CHAIN
REMARK 500 7 ARG A 45 0.28 SIDE CHAIN
REMARK 500 8 ARG A 13 0.29 SIDE CHAIN
REMARK 500 8 ARG A 45 0.30 SIDE CHAIN
REMARK 500 9 ARG A 13 0.23 SIDE CHAIN
REMARK 500 9 ARG A 45 0.29 SIDE CHAIN
REMARK 500 10 ARG A 13 0.29 SIDE CHAIN
REMARK 500 10 ARG A 45 0.32 SIDE CHAIN
REMARK 500 11 ARG A 13 0.16 SIDE CHAIN
REMARK 500 11 ARG A 45 0.28 SIDE CHAIN
REMARK 500 12 ARG A 13 0.24 SIDE CHAIN
REMARK 500 12 ARG A 45 0.32 SIDE CHAIN
REMARK 500 13 ARG A 13 0.16 SIDE CHAIN
REMARK 500 13 ARG A 45 0.23 SIDE CHAIN
REMARK 500 14 ARG A 13 0.23 SIDE CHAIN
REMARK 500 14 ARG A 45 0.31 SIDE CHAIN
REMARK 500 15 ARG A 13 0.21 SIDE CHAIN
REMARK 500 15 ARG A 45 0.28 SIDE CHAIN
REMARK 500 16 ARG A 13 0.21 SIDE CHAIN
REMARK 500 16 ARG A 45 0.20 SIDE CHAIN
REMARK 500 17 ARG A 13 0.31 SIDE CHAIN
REMARK 500 17 ARG A 45 0.14 SIDE CHAIN
REMARK 500 18 ARG A 13 0.32 SIDE CHAIN
REMARK 500 18 ARG A 45 0.27 SIDE CHAIN
REMARK 500 19 ARG A 13 0.31 SIDE CHAIN
REMARK 500 19 ARG A 45 0.30 SIDE CHAIN
REMARK 500 20 ARG A 13 0.28 SIDE CHAIN
REMARK 500 20 ARG A 45 0.08 SIDE CHAIN
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 49
DBREF 1SHI A 1 48 UNP P19651 TXA1_STOHE 1 48
SEQRES 1 A 49 ALA ALA CYS LYS CYS ASP ASP GLU GLY PRO ASP ILE ARG
SEQRES 2 A 49 THR ALA PRO LEU THR GLY THR VAL ASP LEU GLY SER CYS
SEQRES 3 A 49 ASN ALA GLY TRP GLU LYS CYS ALA SER TYR TYR THR ILE
SEQRES 4 A 49 ILE ALA ASP CYS CYS ARG LYS LYS LYS NH2
HET NH2 A 49 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
SHEET 1 A 4 ALA A 1 CYS A 3 0
SHEET 2 A 4 GLY A 19 GLY A 24 -1 N VAL A 21 O ALA A 1
SHEET 3 A 4 ILE A 40 LYS A 47 -1 N CYS A 44 O THR A 20
SHEET 4 A 4 GLY A 29 ALA A 34 -1 N GLU A 31 O ARG A 45
SSBOND 1 CYS A 3 CYS A 43 1555 1555 2.02
SSBOND 2 CYS A 5 CYS A 33 1555 1555 2.02
SSBOND 3 CYS A 26 CYS A 44 1555 1555 2.03
LINK C LYS A 48 N NH2 A 49 1555 1555 1.31
SITE 1 AC1 2 LYS A 47 LYS A 48
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 - v 29 2 Bytes