Header list of 1jkz.pdb file
Complete list - b 23 2 Bytes
HEADER ANTIFUNGAL PROTEIN 13-JUL-01 1JKZ
TITLE NMR SOLUTION STRUCTURE OF PISUM SATIVUM DEFENSIN 1 (PSD1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEFENSE-RELATED PEPTIDE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PSD1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PISUM SATIVUM;
SOURCE 3 ORGANISM_COMMON: PEA;
SOURCE 4 ORGANISM_TAXID: 3888;
SOURCE 5 OTHER_DETAILS: ISOLATED FROM PEA SEEDS
KEYWDS PLANT DEFENSIN, CYS-RICH, ANTIFUNGAL, ANTIFUNGAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.S.ALMEIDA,K.M.S.CABRAL,E.KURTENBACH,F.C.L.ALMEIDA,A.P.VALENTE
REVDAT 4 23-FEB-22 1JKZ 1 REMARK
REVDAT 3 24-FEB-09 1JKZ 1 VERSN
REVDAT 2 01-APR-03 1JKZ 1 JRNL
REVDAT 1 06-FEB-02 1JKZ 0
JRNL AUTH M.S.ALMEIDA,K.M.CABRAL,E.KURTENBACH,F.C.ALMEIDA,A.P.VALENTE
JRNL TITL SOLUTION STRUCTURE OF PISUM SATIVUM DEFENSIN 1 BY HIGH
JRNL TITL 2 RESOLUTION NMR: PLANT DEFENSINS, IDENTICAL BACKBONE WITH
JRNL TITL 3 DIFFERENT MECHANISMS OF ACTION.
JRNL REF J.MOL.BIOL. V. 315 749 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11812144
JRNL DOI 10.1006/JMBI.2001.5252
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.S.ALMEIDA,K.M.S.CABRAL,L.N.MEDEIROS,A.P.VALENTE,
REMARK 1 AUTH 2 F.C.L.ALMEIDA,E.KURTENBACH
REMARK 1 TITL CDNA CLONING AND HETEROLOGOUS EXPRESSION OF FUNCTIONAL
REMARK 1 TITL 2 CYS-RICH ANTIFUNGAL PROTEIN PSD1 IN THE YEAST PICHIA
REMARK 1 TITL 3 PASTORIS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.S.ALMEIDA,K.M.CABRAL,R.B.ZINGALI,E.KURTENBACH
REMARK 1 TITL CHARACTERIZATION OF TWO NOVEL DEFENSE PEPTIDES FROM PEA
REMARK 1 TITL 2 (PISUM SATIVUM) SEEDS
REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 378 278 2000
REMARK 1 REFN ISSN 0003-9861
REMARK 1 DOI 10.1006/ABBI.2000.1824
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, CNS_SOLVE 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), AXEL BRUNGER (CNS_SOLVE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JKZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013892.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4
REMARK 210 IONIC STRENGTH : 10 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.8 MM PSD1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 1H/15N HMQC;
REMARK 210 1H/13C HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 400 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.2, CNS_SOLVE 1.0
REMARK 210 METHOD USED : THE STRUCTURE WAS CALCULATED
REMARK 210 USING TORSIONAL SIMULATED
REMARK 210 ANNEALING AND THEN MINIMIZED
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 18
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 OD2 ASP A 21 HZ2 LYS A 25 1.43
REMARK 500 O CYS A 20 H CYS A 24 1.50
REMARK 500 O HIS A 23 H LYS A 27 1.56
REMARK 500 H HIS A 36 O LYS A 39 1.59
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 THR A 9 63.34 -107.41
REMARK 500 1 TYR A 10 -169.05 -107.20
REMARK 500 1 HIS A 29 72.03 -38.63
REMARK 500 2 THR A 9 60.41 -105.95
REMARK 500 2 TYR A 10 -164.66 -106.22
REMARK 500 2 ARG A 11 -150.29 -108.35
REMARK 500 2 HIS A 29 75.74 -27.35
REMARK 500 3 THR A 9 56.79 -105.62
REMARK 500 3 HIS A 29 74.02 -27.51
REMARK 500 3 ASN A 37 -76.11 62.63
REMARK 500 3 TRP A 38 20.73 -152.85
REMARK 500 4 THR A 9 58.44 -106.32
REMARK 500 4 TYR A 10 -168.05 -107.98
REMARK 500 4 HIS A 29 76.60 -28.24
REMARK 500 4 ASN A 37 -76.26 62.22
REMARK 500 4 TRP A 38 13.18 -148.83
REMARK 500 5 ASP A 8 33.83 -82.62
REMARK 500 5 HIS A 29 70.38 -38.03
REMARK 500 5 LEU A 30 -167.31 -109.28
REMARK 500 5 HIS A 36 76.36 -110.04
REMARK 500 5 ASN A 37 -76.46 75.03
REMARK 500 6 THR A 9 54.26 -107.14
REMARK 500 6 TYR A 10 -163.74 -106.36
REMARK 500 6 ARG A 11 -149.70 -107.56
REMARK 500 6 HIS A 29 75.18 -29.41
REMARK 500 7 THR A 9 70.96 -105.70
REMARK 500 7 TYR A 10 -169.40 -107.83
REMARK 500 7 PHE A 15 -59.03 73.31
REMARK 500 7 HIS A 29 73.11 -25.86
REMARK 500 8 THR A 9 56.39 -105.60
REMARK 500 8 HIS A 29 76.00 -29.45
REMARK 500 8 ASN A 37 -74.87 60.50
REMARK 500 8 TRP A 38 10.59 -145.35
REMARK 500 9 THR A 9 57.80 -108.07
REMARK 500 9 ASP A 21 -72.49 -45.42
REMARK 500 9 HIS A 29 76.48 -28.12
REMARK 500 9 ASN A 37 -75.34 63.28
REMARK 500 10 THR A 9 48.27 -107.87
REMARK 500 10 TYR A 10 -168.36 -107.08
REMARK 500 10 ARG A 11 -150.46 -106.73
REMARK 500 10 HIS A 29 71.93 -29.26
REMARK 500 10 ASN A 37 -78.26 46.92
REMARK 500 10 TRP A 38 30.60 -147.97
REMARK 500 11 THR A 9 -43.19 -145.11
REMARK 500 11 HIS A 29 69.99 -39.09
REMARK 500 11 HIS A 36 -155.03 -96.65
REMARK 500 11 ASN A 37 78.21 -56.97
REMARK 500 12 THR A 9 60.26 -107.62
REMARK 500 12 TYR A 10 -166.64 -107.33
REMARK 500 12 HIS A 29 73.38 -28.63
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE WAS NOT
REMARK 999 AVAILABLE AT THE TIME OF PROCESSING.
DBREF 1JKZ A 1 46 PDB 1JKZ 1JKZ 1 46
SEQRES 1 A 46 LYS THR CYS GLU HIS LEU ALA ASP THR TYR ARG GLY VAL
SEQRES 2 A 46 CYS PHE THR ASN ALA SER CYS ASP ASP HIS CYS LYS ASN
SEQRES 3 A 46 LYS ALA HIS LEU ILE SER GLY THR CYS HIS ASN TRP LYS
SEQRES 4 A 46 CYS PHE CYS THR GLN ASN CYS
HELIX 1 1 THR A 16 ALA A 28 1 13
SHEET 1 A 3 THR A 2 LEU A 6 0
SHEET 2 A 3 LYS A 39 ASN A 45 -1 N CYS A 42 O HIS A 5
SHEET 3 A 3 GLY A 33 HIS A 36 -1 O THR A 34 N PHE A 41
SSBOND 1 CYS A 3 CYS A 46 1555 1555 2.03
SSBOND 2 CYS A 14 CYS A 35 1555 1555 2.03
SSBOND 3 CYS A 20 CYS A 40 1555 1555 2.03
SSBOND 4 CYS A 24 CYS A 42 1555 1555 2.04
CRYST1 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