Header list of 1zad.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 06-APR-05 1ZAD
TITLE STRUCTURE OF CYTOTOXIN I (CTI) FROM NAJA OXIANA IN COMPLEX WITH DPC
TITLE 2 MICELLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOTOXIN 1;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NAJA OXIANA;
SOURCE 3 ORGANISM_COMMON: CENTRAL ASIAN COBRA;
SOURCE 4 ORGANISM_TAXID: 8657;
SOURCE 5 SECRETION: VENOM
KEYWDS ANTIPARALLEL BETA-SHEET, BETA-TURN TYPE I, BETA-TURN TYPE II, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.A.DUBINNYI,Y.E.PUSTOVALOVA,P.V.DUBOVSKII,Y.N.UTKIN,A.G.KONSHINA,
AUTHOR 2 R.G.EFREMOV,A.S.ARSENIEV
REVDAT 3 02-MAR-22 1ZAD 1 REMARK
REVDAT 2 24-FEB-09 1ZAD 1 VERSN
REVDAT 1 20-JUN-06 1ZAD 0
JRNL AUTH P.V.DUBOVSKII,D.M.LESOVOY,M.A.DUBINNYI,A.G.KONSHINA,
JRNL AUTH 2 Y.N.UTKIN,R.G.EFREMOV,A.S.ARSENIEV
JRNL TITL INTERACTION OF THREE-FINGER TOXINS WITH PHOSPHOLIPID
JRNL TITL 2 MEMBRANES: COMPARISON OF S- AND P-TYPE CYTOTOXINS
JRNL REF BIOCHEM.J. V. 387 807 2005
JRNL REFN ISSN 0264-6021
JRNL PMID 15584897
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.V.FEOFANOV,G.V.SHARONOV,M.A.DUBINNYI,M.V.ASTAPOVA,
REMARK 1 AUTH 2 I.A.KUDELINA,P.V.DUBOVSKII,D.I.RODIONOV,Y.N.UTKIN,
REMARK 1 AUTH 3 A.S.ARSENIEV
REMARK 1 TITL COMPARATIVE STUDY OF STRUCTURE AND ACTIVITY OF CYTOTOXINS
REMARK 1 TITL 2 FROM VENOM OF THE COBRAS NAJA OXIANA, NAJA KAOUTHIA, AND
REMARK 1 TITL 3 NAJA HAJE
REMARK 1 REF BIOCHEMISTRY V. 69 1148 2004
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 15527416
REMARK 1 DOI 10.1023/B:BIRY.0000046890.46901.7E
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.6
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT P. ET. AL. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FLEXIBLE PROLINE RESIDUES WERE USED TO
REMARK 3 DISTINGUISH UP/DOWN CONFORMATION OF PROLINE RINGS.
REMARK 4
REMARK 4 1ZAD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032496.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 323
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 1 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10MG CYTOTOXIN I, 35 MG D38
REMARK 210 -DODECYLPHOSPHOCHOLINE, 90% H2O,
REMARK 210 10% D2O; 10MG CYTOTOXIN I, 35 MG
REMARK 210 D38-DODECYLPHOSPHOCHOLINE, 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY
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 3.1.A, XEASY 1.2.11,
REMARK 210 CYANA 1.0.6, NMRPIPE, ACME
REMARK 210 2001.085.20.47
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 SG CYS A 3 SG CYS A 14 1.62
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 LYS A 5 -156.17 -92.70
REMARK 500 1 PRO A 8 55.33 -60.63
REMARK 500 1 ILE A 9 -47.13 -134.87
REMARK 500 1 PRO A 15 -174.83 -59.59
REMARK 500 1 MET A 27 -67.07 62.89
REMARK 500 1 THR A 31 -154.05 -89.99
REMARK 500 1 PRO A 33 -173.10 -63.12
REMARK 500 1 ARG A 58 38.54 70.52
REMARK 500 2 LYS A 5 -156.82 -87.19
REMARK 500 2 PRO A 8 55.05 -60.51
REMARK 500 2 ILE A 9 -51.25 -143.08
REMARK 500 2 PRO A 15 -174.88 -58.26
REMARK 500 2 MET A 27 -80.46 57.23
REMARK 500 2 PRO A 33 -172.04 -65.54
REMARK 500 2 ARG A 58 40.32 72.94
REMARK 500 3 LYS A 5 -159.19 -87.46
REMARK 500 3 PRO A 8 41.07 -60.15
REMARK 500 3 PRO A 15 -175.08 -58.88
REMARK 500 3 MET A 27 -69.55 62.05
REMARK 500 3 THR A 31 -157.10 -101.62
REMARK 500 3 PRO A 33 -173.52 -64.66
REMARK 500 3 ARG A 58 35.26 77.24
REMARK 500 4 PRO A 8 48.62 -60.67
REMARK 500 4 ILE A 9 -46.21 -131.65
REMARK 500 4 PRO A 15 -174.78 -59.41
REMARK 500 4 MET A 27 -72.99 61.39
REMARK 500 4 PRO A 33 -166.30 -65.26
REMARK 500 5 LYS A 5 -158.26 -92.17
REMARK 500 5 PRO A 8 58.93 -61.68
REMARK 500 5 ILE A 9 -44.44 -133.84
REMARK 500 5 PRO A 15 -174.85 -59.89
REMARK 500 5 MET A 27 -78.48 57.30
REMARK 500 5 PRO A 33 -172.36 -65.16
REMARK 500 5 SER A 46 -167.55 -122.99
REMARK 500 5 ARG A 58 36.33 74.00
REMARK 500 6 PRO A 8 52.77 -59.94
REMARK 500 6 ILE A 9 -46.95 -137.71
REMARK 500 6 PRO A 15 -174.92 -59.26
REMARK 500 6 MET A 27 -82.99 55.08
REMARK 500 6 THR A 31 -168.76 -106.31
REMARK 500 6 PRO A 33 -171.68 -65.95
REMARK 500 6 ARG A 58 37.11 75.86
REMARK 500 7 LYS A 5 -154.42 -91.52
REMARK 500 7 PRO A 8 49.70 -60.75
REMARK 500 7 PRO A 15 -174.84 -59.04
REMARK 500 7 MET A 27 -67.60 63.08
REMARK 500 7 PRO A 33 -172.97 -64.46
REMARK 500 7 ARG A 58 36.60 76.39
REMARK 500 8 PRO A 8 47.56 -57.51
REMARK 500 8 PRO A 15 -174.75 -61.92
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RL5 RELATED DB: PDB
REMARK 900 STRUCTURE OF CYTOTOXIN I IN AQUEOUS SOLUTION (MAJOR FORM)
DBREF 1ZAD A 1 60 UNP P01451 CX1_NAJOX 1 60
SEQRES 1 A 60 LEU LYS CYS ASN LYS LEU VAL PRO ILE ALA TYR LYS THR
SEQRES 2 A 60 CYS PRO GLU GLY LYS ASN LEU CYS TYR LYS MET PHE MET
SEQRES 3 A 60 MET SER ASP LEU THR ILE PRO VAL LYS ARG GLY CYS ILE
SEQRES 4 A 60 ASP VAL CYS PRO LYS ASN SER LEU LEU VAL LYS TYR VAL
SEQRES 5 A 60 CYS CYS ASN THR ASP ARG CYS ASN
SHEET 1 A 2 LYS A 2 ASN A 4 0
SHEET 2 A 2 TYR A 11 THR A 13 -1 O LYS A 12 N CYS A 3
SHEET 1 B 3 LYS A 35 ILE A 39 0
SHEET 2 B 3 LEU A 20 MET A 26 -1 N TYR A 22 O GLY A 37
SHEET 3 B 3 VAL A 49 CYS A 54 -1 O LYS A 50 N PHE A 25
SSBOND 1 CYS A 3 CYS A 21 1555 1555 1.99
SSBOND 2 CYS A 14 CYS A 38 1555 1555 2.08
SSBOND 3 CYS A 42 CYS A 53 1555 1555 2.10
SSBOND 4 CYS A 54 CYS A 59 1555 1555 2.00
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