Header list of 1ijc.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 25-APR-01 1IJC
TITLE SOLUTION STRUCTURE OF BUCANDIN, A NEUROTOXIN FROM THE VENOM OF THE
TITLE 2 MALAYAN KRAIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BUCANDIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BUNGARUS CANDIDUS;
SOURCE 3 ORGANISM_TAXID: 92438;
SOURCE 4 SECRETION: VENOM
KEYWDS THREE-FINGER MOTIF, TWO ANTIPARALLEL BETA-SHEETS, TWO AND FOUR
KEYWDS 2 STRANDED BETA-SHEETS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.M.TORRES,R.M.KINI,S.NIRTHANAN,P.W.KUCHEL
REVDAT 3 23-FEB-22 1IJC 1 REMARK
REVDAT 2 24-FEB-09 1IJC 1 VERSN
REVDAT 1 21-DEC-01 1IJC 0
JRNL AUTH A.M.TORRES,R.M.KINI,N.SELVANAYAGAM,P.W.KUCHEL
JRNL TITL NMR STRUCTURE OF BUCANDIN, A NEUROTOXIN FROM THE VENOM OF
JRNL TITL 2 THE MALAYAN KRAIT (BUNGARUS CANDIDUS).
JRNL REF BIOCHEM.J. V. 360 539 2001
JRNL REFN ISSN 0264-6021
JRNL PMID 11736642
JRNL DOI 10.1042/0264-6021:3600539
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.KUHN,A.M.DEACON,S.COMOSO,G.RAJASEGER,R.M.KINI,I.USON,
REMARK 1 AUTH 2 P.R.KOLATKAR
REMARK 1 TITL THE ATOMIC RESOLUTION STRUCTURE OF BUCANDIN, A NOVEL TOXIN
REMARK 1 TITL 2 ISOLATED FROM THE MALAYAN KRAIT, DETERMINED BY DIRECT
REMARK 1 TITL 3 METHODS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 1401 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444900011501
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.843
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1363 RESTRAINTS, 1258 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 61
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 44 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1IJC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013328.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NO SALT ADDED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.7 MM BUCANDIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, INFIT, NOAH, DYANA
REMARK 210 1.5, X-PLOR 3.843
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 6000
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 : 10
REMARK 210
REMARK 210 REMARK: THE STRUCTURES WERE 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: 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 HE1 TRP A 27 HG13 VAL A 51 1.21
REMARK 500 HH TYR A 52 HE2 LYS A 54 1.22
REMARK 500 HG2 ARG A 5 HG21 ILE A 15 1.23
REMARK 500 HD21 ASN A 50 H VAL A 51 1.28
REMARK 500 HG12 ILE A 15 H THR A 16 1.29
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 -16.18 -142.90
REMARK 500 1 SER A 18 165.36 -48.20
REMARK 500 1 ALA A 19 -8.88 -55.83
REMARK 500 1 LYS A 30 19.21 -64.89
REMARK 500 1 ASN A 33 30.93 37.38
REMARK 500 1 GLU A 45 132.80 -35.80
REMARK 500 1 THR A 48 -132.81 -99.80
REMARK 500 1 THR A 58 -161.90 -107.18
REMARK 500 1 LEU A 60 51.49 13.27
REMARK 500 1 ASN A 62 70.90 -117.19
REMARK 500 2 CYS A 17 -152.27 -72.80
REMARK 500 2 LYS A 30 36.89 -75.50
REMARK 500 2 CYS A 43 153.25 -44.42
REMARK 500 2 THR A 44 23.62 -140.14
REMARK 500 2 GLU A 45 132.31 -34.65
REMARK 500 2 THR A 48 -138.14 -126.64
REMARK 500 2 LEU A 60 60.60 20.07
REMARK 500 3 SER A 9 -4.68 -150.08
REMARK 500 3 CYS A 17 170.96 -58.58
REMARK 500 3 ALA A 19 -26.74 -35.29
REMARK 500 3 ASN A 33 27.39 36.25
REMARK 500 3 THR A 48 -139.47 -100.20
REMARK 500 3 ASN A 59 159.11 -39.17
REMARK 500 3 LEU A 60 55.94 13.10
REMARK 500 3 ASN A 62 75.85 -111.68
REMARK 500 4 CYS A 3 -168.57 -108.82
REMARK 500 4 VAL A 8 -58.91 74.17
REMARK 500 4 ALA A 19 -36.74 85.64
REMARK 500 4 GLU A 20 -67.71 -95.52
REMARK 500 4 ILE A 31 -62.54 -133.10
REMARK 500 4 ASN A 33 22.04 37.95
REMARK 500 4 GLU A 45 139.63 -34.76
REMARK 500 4 ASP A 47 77.90 -101.41
REMARK 500 4 THR A 48 -124.68 -100.04
REMARK 500 4 LEU A 60 54.52 13.99
REMARK 500 5 HIS A 12 50.64 -117.20
REMARK 500 5 ILE A 31 -61.20 -103.89
REMARK 500 5 ASN A 33 16.73 87.98
REMARK 500 5 THR A 42 -158.55 -102.64
REMARK 500 5 GLU A 45 123.68 -38.75
REMARK 500 5 THR A 48 -132.45 -109.28
REMARK 500 5 LEU A 60 51.23 16.09
REMARK 500 6 ALA A 19 -37.07 -29.88
REMARK 500 6 THR A 22 -1.14 -140.11
REMARK 500 6 ASN A 33 14.55 48.44
REMARK 500 6 THR A 48 -129.22 -120.57
REMARK 500 6 LEU A 60 51.53 13.92
REMARK 500 7 ALA A 19 -31.12 72.04
REMARK 500 7 GLU A 20 -62.37 -108.17
REMARK 500 7 ILE A 31 -60.40 -100.70
REMARK 500
REMARK 500 THIS ENTRY HAS 139 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F94 RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF BUCANDIN
DBREF 1IJC A 1 63 UNP P81782 BUCA_BUNCA 1 63
SEQRES 1 A 63 MET GLU CYS TYR ARG CYS GLY VAL SER GLY CYS HIS LEU
SEQRES 2 A 63 LYS ILE THR CYS SER ALA GLU GLU THR PHE CYS TYR LYS
SEQRES 3 A 63 TRP LEU ASN LYS ILE SER ASN GLU ARG TRP LEU GLY CYS
SEQRES 4 A 63 ALA LYS THR CYS THR GLU ILE ASP THR TRP ASN VAL TYR
SEQRES 5 A 63 ASN LYS CYS CYS THR THR ASN LEU CYS ASN THR
SHEET 1 A 2 GLU A 2 ARG A 5 0
SHEET 2 A 2 LEU A 13 THR A 16 -1 N LEU A 13 O ARG A 5
SHEET 1 B 4 GLU A 34 ALA A 40 0
SHEET 2 B 4 PHE A 23 ASN A 29 -1 N PHE A 23 O ALA A 40
SHEET 3 B 4 VAL A 51 CYS A 56 -1 N TYR A 52 O LEU A 28
SHEET 4 B 4 ILE A 46 ASP A 47 -1 N ILE A 46 O ASN A 53
SSBOND 1 CYS A 3 CYS A 24 1555 1555 2.03
SSBOND 2 CYS A 6 CYS A 11 1555 1555 2.03
SSBOND 3 CYS A 17 CYS A 39 1555 1555 2.03
SSBOND 4 CYS A 43 CYS A 55 1555 1555 2.03
SSBOND 5 CYS A 56 CYS A 61 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 - b 23 2 Bytes