Header list of 1ed0.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 26-JAN-00 1ED0
TITLE NMR STRUCTURAL DETERMINATION OF VISCOTOXIN A3 FROM VISCUM ALBUM L.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VISCOTOXIN A3;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VISCUM ALBUM;
SOURCE 3 ORGANISM_COMMON: EUROPEAN MISTLETOE;
SOURCE 4 ORGANISM_TAXID: 3972
KEYWDS THIONIN, CONCENTRIC MOTIF, HELIX-TURN-HELIX, ALPHA-BETA PROTEIN,
KEYWDS 2 AMPHIPATHIC HELIX, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.ROMAGNOLI,R.UGOLINI,F.FOGOLARI,G.SCHALLER,K.URECH,M.GIANNATTASIO,
AUTHOR 2 L.RAGONA,H.MOLINARI
REVDAT 4 16-FEB-22 1ED0 1 REMARK
REVDAT 3 24-FEB-09 1ED0 1 VERSN
REVDAT 2 05-APR-05 1ED0 3 ATOM JRNL
REVDAT 1 04-FEB-00 1ED0 0
JRNL AUTH S.ROMAGNOLI,R.UGOLINI,F.FOGOLARI,G.SCHALLER,K.URECH,
JRNL AUTH 2 M.GIANNATTASIO,L.RAGONA,H.MOLINARI
JRNL TITL NMR STRUCTURAL DETERMINATION OF VISCOTOXIN A3 FROM VISCUM
JRNL TITL 2 ALBUM L.
JRNL REF BIOCHEM.J. V. 350 569 2000
JRNL REFN ISSN 0264-6021
JRNL PMID 10947973
JRNL DOI 10.1042/0264-6021:3500569
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.4, DISCOVER 98
REMARK 3 AUTHORS : GUENTERT, WUETHRICH (DYANA), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1010 DISTANCE RESTRAINTS WERE
REMARK 3 CALCULATED REDUCED TO 734 (230 INTRARESIDUE, 172 SEQUENTIAL, 191
REMARK 3 MEDIUM RANGE, 141 LONG RANGE) AFTER REMOVAL OF IRRELEVANT
REMARK 3 RESTRAINTS. CALCULATION STARTED WITH 200 RANDOMIZED CONFORMERS
REMARK 3 AND CONSISTENTLY VIOLATED RESTRAINTS WERE CHECKED AND RELAXED
REMARK 3 WHERE NECESSARY. THIS PROCEDURE WAS REPEATED UNTIL NO CONSISTENT
REMARK 3 VIOLATIONS WERE FOUND IN HALF OR MORE OF THE STRUCTURES. 600 NEW
REMARK 3 CALCULATIONS WERE STARTED AND THE 20 STRUCTURES WITH LOWEST
REMARK 3 TARGET FUNCTION WERE ANALYZED. THE STRUCTURE WITH LOWEST TARGET
REMARK 3 FUNCTION AND THE STRUCTURE EXHIBITING THE LARGEST RMSD WITH IT
REMARK 3 WERE SUBJECTED TO RESTRAINED MOLECULAR DYNAMICS (20 CYCLES OF 15
REMARK 3 PS RESTRAINED MOLECULAR DYNAMICS FOLLOWED BY MINIMIZATION). ALL
REMARK 3 EVEN STRUCTURES FROM THE LAST 10 MINIMIZED STRUCTURES WERE
REMARK 3 RETAINED FROM BOTH SETS AND DEPOSITED.
REMARK 4
REMARK 4 1ED0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010459.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285
REMARK 210 PH : 3.6
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM VISCOTOXIN A3 1H; 50MM
REMARK 210 H3PO4/NAOH AQUEOUS BUFFER; 90%
REMARK 210 H2O, 10% D2O; 2MM VISCOTOXIN A3
REMARK 210 1H; 50MM H3PO4/NAOH AQUEOUS
REMARK 210 BUFFER; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY
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 1.2, XEASY 1.2
REMARK 210 METHOD USED : RESTRAINED SIMULATED ANNEALING
REMARK 210 IN TORSION ANGLE SPACE,
REMARK 210 ITERATIVE RESTRAINTS REFINEMENT,
REMARK 210 RESTRAINED MOLECULAR DYNAMICS IN
REMARK 210 CARTESIAN COORDINATE SPACE
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 600
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS 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: 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 THR A 19 27.41 -79.71
REMARK 500 2 THR A 19 30.29 -80.81
REMARK 500 3 THR A 19 30.16 -80.61
REMARK 500 5 THR A 19 30.64 -80.13
REMARK 500 6 THR A 19 30.11 -80.69
REMARK 500 8 THR A 19 29.17 -79.87
REMARK 500 10 THR A 19 29.43 -79.97
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 2 TYR A 13 0.09 SIDE CHAIN
REMARK 500 2 TYR A 44 0.12 SIDE CHAIN
REMARK 500 4 TYR A 44 0.07 SIDE CHAIN
REMARK 500 6 TYR A 44 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CBN RELATED DB: PDB
REMARK 900 CRAMBIN
REMARK 900 RELATED ID: 1CNR RELATED DB: PDB
REMARK 900 CRAMBIN
REMARK 900 RELATED ID: 1CCM RELATED DB: PDB
REMARK 900 CRAMBIN
REMARK 900 RELATED ID: 1AB1 RELATED DB: PDB
REMARK 900 CRAMBIN
REMARK 900 RELATED ID: 2PLH RELATED DB: PDB
REMARK 900 ALPHA-1-PUROTHIONIN
REMARK 900 RELATED ID: 1BHP RELATED DB: PDB
REMARK 900 BETA-PUROTHIONIN
DBREF 1ED0 A 1 46 UNP P01538 THN3_VISAL 27 72
SEQRES 1 A 46 LYS SER CYS CYS PRO ASN THR THR GLY ARG ASN ILE TYR
SEQRES 2 A 46 ASN ALA CYS ARG LEU THR GLY ALA PRO ARG PRO THR CYS
SEQRES 3 A 46 ALA LYS LEU SER GLY CYS LYS ILE ILE SER GLY SER THR
SEQRES 4 A 46 CYS PRO SER ASP TYR PRO LYS
HELIX 1 1 THR A 7 LEU A 18 1 12
HELIX 2 2 ARG A 23 SER A 30 1 8
SHEET 1 A 2 SER A 2 CYS A 3 0
SHEET 2 A 2 LYS A 33 ILE A 34 -1 O LYS A 33 N CYS A 3
SSBOND 1 CYS A 3 CYS A 40 1555 1555 2.04
SSBOND 2 CYS A 4 CYS A 32 1555 1555 2.03
SSBOND 3 CYS A 16 CYS A 26 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 - 16 20 Bytes