Header list of 1cb9.pdb file
Complete list - v 29 2 Bytes
HEADER TOXIN 01-MAR-99 1CB9
TITLE NMR STRUCTURE WITH TIGHTLY BOUND WATER MOLECULES OF CYTOTOXIN II
TITLE 2 (CARDIOTOXIN) FROM NAJA NAJA OXIANA IN AQUEOUS SOLUTION (MAJOR FORM).
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CYTOTOXIN 2);
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 CYTOXIN (CARDIOTOXIN), MEMBRANE PERTURBATION, CIS/TRANS
KEYWDS 2 ISOMERIZATION, BOUND WATER, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.V.DEMENTIEVA,E.V.BOCHAROV,A.S.ARSENIEV
REVDAT 5 29-NOV-17 1CB9 1 REMARK HELIX
REVDAT 4 24-FEB-09 1CB9 1 VERSN
REVDAT 3 01-APR-03 1CB9 1 JRNL
REVDAT 2 12-MAY-00 1CB9 1 JRNL REMARK ATOM
REVDAT 1 29-JUN-99 1CB9 0
JRNL AUTH D.V.DEMENTIEVA,E.V.BOCHAROV,A.S.ARSENIEV
JRNL TITL TWO FORMS OF CYTOTOXIN II (CARDIOTOXIN) FROM NAJA NAJA
JRNL TITL 2 OXIANA IN AQUEOUS SOLUTION: SPATIAL STRUCTURES WITH TIGHTLY
JRNL TITL 3 BOUND WATER MOLECULES.
JRNL REF EUR.J.BIOCHEM. V. 263 152 1999
JRNL REFN ISSN 0014-2956
JRNL PMID 10429199
JRNL DOI 10.1046/J.1432-1327.1999.00478.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.V.DEMENTIEVA,N.UTKIN YU,A.S.ARSENIEV
REMARK 1 TITL SECONDARY STRUCTURE AND CONFORMATIONAL HETEROGENEITY OF
REMARK 1 TITL 2 CYTOTOXIN II FROM NAJA NAJA OXIANA
REMARK 1 REF RUSS.J.BIOORGANIC CHEM. V. 22 289 1996
REMARK 1 REFN ISSN 1068-1620
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FANTOM 4.0
REMARK 3 AUTHORS : FRACZKIEWICZ, MUMENTHALER, FREYBERG, SCHAUMANN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE RESTRAINED REFINMENT WAS MADE IN
REMARK 3 VACUUM AND ONLY FOR PROTEIN SIDE CHAINS.
REMARK 4
REMARK 4 1CB9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000569.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY; ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY-600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VARIAN VNMR VNMR, XEASY, DYANA
REMARK 210 METHOD USED : SIMULATED ANNEALING BY MOLECULAR
REMARK 210 DYNAMICS IN TORSION ANGLE SPACE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 220
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210 (TARGET FUNCTION VALUE)
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED BY HOMONUCLEAR NMR
REMARK 210 SPECTROSCOPY, USING GRADIENT TECHNIQUE. ROESY EXPERIMENTS WERE
REMARK 210 HELD AT 290 AND 318K.
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
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 LEU A 9 -45.58 -144.95
REMARK 500 1 VAL A 27 72.02 -66.85
REMARK 500 1 ALA A 28 -42.14 -169.38
REMARK 500 1 VAL A 34 -58.52 -130.21
REMARK 500 1 LEU A 48 -69.97 -97.66
REMARK 500 1 ASN A 55 51.19 -107.62
REMARK 500 2 LEU A 9 -46.56 -138.88
REMARK 500 2 VAL A 27 73.43 -66.19
REMARK 500 2 ALA A 28 -42.13 -167.44
REMARK 500 2 HIS A 31 -47.67 -152.09
REMARK 500 2 LEU A 48 -65.13 -90.69
REMARK 500 2 ASN A 55 49.96 -104.99
REMARK 500 3 LEU A 9 -46.45 -141.99
REMARK 500 3 ASN A 19 20.37 -144.00
REMARK 500 3 VAL A 27 74.42 -66.13
REMARK 500 3 ALA A 28 -42.05 -168.58
REMARK 500 3 HIS A 31 -46.18 -151.31
REMARK 500 3 VAL A 34 -55.58 -127.77
REMARK 500 3 LEU A 48 -67.28 -94.31
REMARK 500 3 ASN A 55 46.22 -98.55
REMARK 500 4 LEU A 9 -46.56 -144.42
REMARK 500 4 ASN A 19 25.60 -145.50
REMARK 500 4 VAL A 27 72.24 -65.66
REMARK 500 4 ALA A 28 -42.31 -164.61
REMARK 500 4 HIS A 31 -50.29 -148.65
REMARK 500 4 VAL A 34 -55.08 -124.98
REMARK 500 4 LEU A 48 -67.71 -90.89
REMARK 500 4 ASN A 55 49.27 -103.92
REMARK 500 4 LYS A 58 54.78 39.63
REMARK 500 5 LEU A 9 -46.20 -141.73
REMARK 500 5 ASN A 19 20.46 -141.04
REMARK 500 5 VAL A 27 72.52 -65.62
REMARK 500 5 ALA A 28 -42.40 -165.14
REMARK 500 5 HIS A 31 -49.06 -149.98
REMARK 500 5 VAL A 34 -59.97 -120.85
REMARK 500 5 LEU A 48 -67.15 -95.36
REMARK 500 5 ASN A 55 48.34 -102.34
REMARK 500 5 LYS A 58 51.95 39.85
REMARK 500 6 LEU A 9 -46.12 -143.50
REMARK 500 6 VAL A 27 73.09 -66.81
REMARK 500 6 ALA A 28 -42.11 -168.84
REMARK 500 6 ASN A 55 49.91 -105.26
REMARK 500 7 LEU A 9 -46.61 -145.26
REMARK 500 7 VAL A 27 74.15 -65.57
REMARK 500 7 ALA A 28 -42.32 -167.25
REMARK 500 7 HIS A 31 -46.98 -149.20
REMARK 500 7 VAL A 34 -59.15 -124.16
REMARK 500 7 LEU A 48 -64.59 -90.05
REMARK 500 7 ASN A 55 48.12 -102.76
REMARK 500 8 LEU A 9 -45.47 -145.71
REMARK 500
REMARK 500 THIS ENTRY HAS 145 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CB9 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 S1 2 LEU A 1 LYS A 5 0
SHEET 2 S1 2 PHE A 10 CYS A 14 -1 O PHE A 10 N LYS A 5
SHEET 1 S2 3 LYS A 35 ILE A 39 0
SHEET 2 S2 3 LEU A 20 MET A 26 -1 N LEU A 20 O ILE A 39
SHEET 3 S2 3 VAL A 49 ASN A 55 -1 N LYS A 50 O PHE A 25
SSBOND 1 CYS A 3 CYS A 21 1555 1555 1.96
SSBOND 2 CYS A 14 CYS A 38 1555 1555 1.98
SSBOND 3 CYS A 42 CYS A 53 1555 1555 2.01
SSBOND 4 CYS A 54 CYS A 59 1555 1555 1.99
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