Header list of 1ffj.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 25-JUL-00 1FFJ
TITLE NMR STRUCTURE OF CARDIOTOXIN IN DPC-MICELLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOTOXIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 1;
COMPND 5 SYNONYM: CARDIOTOXIN
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 ALL-BETA SHEET PROTEIN, MEMBRANE PERTURBATION, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.V.DUBOVSKII,D.V.DEMENTIEVA,E.V.BOCHAROV,Y.N.UTKIN,A.S.ARSENIEV
REVDAT 4 23-FEB-22 1FFJ 1 REMARK
REVDAT 3 24-FEB-09 1FFJ 1 VERSN
REVDAT 2 01-APR-03 1FFJ 1 JRNL
REVDAT 1 17-JAN-01 1FFJ 0
JRNL AUTH P.V.DUBOVSKII,D.V.DEMENTIEVA,E.V.BOCHAROV,Y.N.UTKIN,
JRNL AUTH 2 A.S.ARSENIEV
JRNL TITL MEMBRANE BINDING MOTIF OF THE P-TYPE CARDIOTOXIN.
JRNL REF J.MOL.BIOL. V. 305 137 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11114253
JRNL DOI 10.1006/JMBI.2000.4283
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.V.DEMENTIEVA,E.V.BOCHAROV,A.S.ARSENIEV
REMARK 1 TITL TWO FORMS OF CYTOTOXIN II (CARDIOTOXIN) FROM NAJA NAJA
REMARK 1 TITL 2 OXIANA IN AQUEOUS SOLUTION. SPATIAL STRUCTURES WITH TIGHTLY
REMARK 1 TITL 3 BOUND WATER MOLECULES
REMARK 1 REF EUR.J.BIOCHEM. V. 263 152 1999
REMARK 1 REFN ISSN 0014-2956
REMARK 1 DOI 10.1046/J.1432-1327.1999.00478.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1A, DYANA 1.5
REMARK 3 AUTHORS : VARIAN SOFTWARE (VNMR), GUENTERT, P. &
REMARK 3 MUMENTHALER, C. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON A TOTAL OF 368
REMARK 3 NOE-DERIVED CONSTRAINTS, 154 DIHEDRAL ANGLE RESTRAINTS, 248
REMARK 3 DISTANCE RESTRAINTS FROM HYDROGEN BONDS AND DISULFIDES
REMARK 4
REMARK 4 1FFJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011541.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318; 303
REMARK 210 PH : 5.5; 5.5
REMARK 210 IONIC STRENGTH : 0M NACL; 0M NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM CARDIOTOXIN (CYTOTOXIN II);
REMARK 210 120 MM PERDEUTERATED
REMARK 210 DODECYLPHOSPHOCHOLINE; 3MM
REMARK 210 CARDIOTOXIN (CYTOTOXIN II); 120
REMARK 210 MM PERDEUTERATED
REMARK 210 DODECYLPHOSPHOCHOLINE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; TOCSY; DQF-COSY; ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.2.11, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 220
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES. SITES OF TIGHTLY BOUND WATER MOLECULES
REMARK 210 WERE DETERMINED AS IN DEMENTIEVA ET AL., EUR.J.BIOCHEM.1999,263,
REMARK 210 152-162.
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 H MET A 26 O HOH A 61 1.52
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 VAL A 32 87.22 -155.90
REMARK 500 1 ASN A 55 63.75 -105.26
REMARK 500 2 ALA A 28 -38.49 -37.03
REMARK 500 2 VAL A 32 78.58 -157.11
REMARK 500 2 ASN A 55 70.35 -108.13
REMARK 500 3 LEU A 6 -71.70 -40.69
REMARK 500 3 VAL A 32 78.46 -157.41
REMARK 500 3 ASN A 55 63.61 -107.53
REMARK 500 4 VAL A 32 84.04 -153.07
REMARK 500 4 ASN A 55 70.59 -113.87
REMARK 500 5 ALA A 16 155.02 -40.18
REMARK 500 5 ALA A 28 -39.17 -37.14
REMARK 500 5 VAL A 32 84.94 -158.75
REMARK 500 5 ASN A 55 63.38 -118.81
REMARK 500 6 LEU A 6 -70.23 -42.81
REMARK 500 6 ALA A 16 156.07 -48.35
REMARK 500 6 VAL A 32 85.45 -152.21
REMARK 500 7 VAL A 32 74.41 -156.59
REMARK 500 7 ASN A 55 69.03 -103.27
REMARK 500 8 LEU A 6 -73.30 -39.77
REMARK 500 8 ALA A 16 157.77 -42.30
REMARK 500 8 VAL A 32 81.26 -158.35
REMARK 500 9 ALA A 16 157.36 -40.31
REMARK 500 9 HIS A 31 57.54 -142.21
REMARK 500 9 ASN A 55 65.90 -109.77
REMARK 500 10 LEU A 6 -72.13 -40.75
REMARK 500 10 VAL A 32 87.29 -151.68
REMARK 500 10 ASN A 55 66.10 -110.81
REMARK 500 11 ALA A 16 158.74 -44.69
REMARK 500 11 VAL A 32 83.94 -155.12
REMARK 500 12 LYS A 5 -167.04 -75.59
REMARK 500 12 VAL A 32 80.75 -156.59
REMARK 500 12 CYS A 54 143.27 -171.41
REMARK 500 12 ASN A 55 62.12 -103.61
REMARK 500 13 ALA A 16 163.41 -43.49
REMARK 500 13 ASN A 55 66.27 -110.87
REMARK 500 14 VAL A 32 84.02 -157.54
REMARK 500 15 HIS A 31 48.19 -140.28
REMARK 500 15 ASN A 55 66.34 -112.65
REMARK 500 16 ALA A 16 158.07 -40.01
REMARK 500 16 ASN A 55 69.38 -105.70
REMARK 500 17 ALA A 16 151.80 -41.10
REMARK 500 17 ASN A 55 60.88 -108.18
REMARK 500 18 LEU A 6 -73.32 -42.25
REMARK 500 18 ALA A 16 156.09 -43.78
REMARK 500 18 VAL A 32 85.31 -156.95
REMARK 500 18 CYS A 54 139.03 -170.62
REMARK 500 18 ASN A 55 58.01 -101.73
REMARK 500 19 ALA A 16 151.21 -45.88
REMARK 500 19 ALA A 28 -36.95 -36.90
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CB9 RELATED DB: PDB
REMARK 900 1CB9 IS THE SOLUTION STRUCTURE OF CARDIOTOXIN FROM NAJA OXIANA
REMARK 900 (MAJOR FORM)
DBREF 1FFJ A 1 60 UNP P01441 CX2_NAJOX 1 60
SEQRES 1 A 60 LEU LYS CYS LYS LYS LEU VAL PRO LEU PHE SER LYS THR
SEQRES 2 A 60 CYS PRO ALA GLY LYS ASN LEU CYS TYR LYS MET PHE MET
SEQRES 3 A 60 VAL ALA ALA PRO HIS VAL PRO VAL LYS ARG GLY CYS ILE
SEQRES 4 A 60 ASP VAL CYS PRO LYS SER SER LEU LEU VAL LYS TYR VAL
SEQRES 5 A 60 CYS CYS ASN THR ASP LYS CYS ASN
FORMUL 2 HOH *2(H2 O)
SHEET 1 A 2 LYS A 2 LYS A 4 0
SHEET 2 A 2 SER A 11 THR A 13 -1 N LYS A 12 O CYS A 3
SHEET 1 B 3 PRO A 33 ILE A 39 0
SHEET 2 B 3 LEU A 20 MET A 26 -1 O LEU A 20 N ILE A 39
SHEET 3 B 3 VAL A 49 CYS A 54 -1 N LYS A 50 O PHE A 25
SSBOND 1 CYS A 3 CYS A 21 1555 1555 2.03
SSBOND 2 CYS A 14 CYS A 38 1555 1555 1.98
SSBOND 3 CYS A 42 CYS A 53 1555 1555 2.08
SSBOND 4 CYS A 54 CYS A 59 1555 1555 2.09
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