Header list of 1za8.pdb file
Complete list - 2 20 Bytes
HEADER ANTIVIRAL PROTEIN 05-APR-05 1ZA8
TITLE NMR SOLUTION STRUCTURE OF A LEAF-SPECIFIC-EXPRESSED CYCLOTIDE VHL-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VHL-1;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIOLA HEDERACEA;
SOURCE 3 ORGANISM_TAXID: 180952
KEYWDS CIRCULAR PROTEIN, CYCLIC CYSTINE KNOT MOTIF, ANTIVIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.CHEN,M.L.COLGRAVE,N.L.DALY,K.J.ROSENGREN,K.R.GUSTAFSON,D.J.CRAIK
REVDAT 4 02-MAR-22 1ZA8 1 REMARK LINK
REVDAT 3 24-FEB-09 1ZA8 1 VERSN
REVDAT 2 21-JUN-05 1ZA8 1 JRNL
REVDAT 1 12-APR-05 1ZA8 0
JRNL AUTH B.CHEN,M.L.COLGRAVE,N.L.DALY,K.J.ROSENGREN,K.R.GUSTAFSON,
JRNL AUTH 2 D.J.CRAIK
JRNL TITL ISOLATION AND CHARACTERIZATION OF NOVEL CYCLOTIDES FROM
JRNL TITL 2 VIOLA HEDERACEAE: SOLUTION STRUCTURE AND ANTI-HIV ACTIVITY
JRNL TITL 3 OF VHL-1, A LEAF-SPECIFIC EXPRESSED CYCLOTIDE.
JRNL REF J.BIOL.CHEM. V. 280 22395 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15824119
JRNL DOI 10.1074/JBC.M501737200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZA8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032493.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.3
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4MM VHL-1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; E
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.110, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: 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 CYS A 5 37.34 -94.59
REMARK 500 1 SER A 9 48.60 -75.79
REMARK 500 1 LYS A 23 -12.97 78.12
REMARK 500 2 CYS A 5 34.11 -92.44
REMARK 500 2 LYS A 23 -15.20 81.77
REMARK 500 3 CYS A 5 39.59 -92.78
REMARK 500 3 LYS A 23 -13.38 78.54
REMARK 500 3 SER A 29 -4.30 72.33
REMARK 500 4 CYS A 5 35.83 -91.26
REMARK 500 4 SER A 9 48.03 -75.41
REMARK 500 4 LYS A 23 -15.80 87.06
REMARK 500 4 SER A 29 -1.61 75.41
REMARK 500 5 CYS A 5 37.11 -96.19
REMARK 500 5 SER A 9 49.86 -76.45
REMARK 500 5 LYS A 23 -19.18 81.42
REMARK 500 5 SER A 29 -2.73 71.74
REMARK 500 6 CYS A 5 36.52 -98.05
REMARK 500 6 SER A 9 49.69 -77.43
REMARK 500 6 LYS A 23 -10.92 76.40
REMARK 500 6 SER A 29 -4.83 72.49
REMARK 500 7 SER A 9 49.04 -77.43
REMARK 500 7 LYS A 23 -11.70 79.85
REMARK 500 8 CYS A 5 37.56 -92.33
REMARK 500 8 SER A 9 48.69 -76.38
REMARK 500 8 LYS A 23 -19.35 84.95
REMARK 500 8 SER A 29 -6.59 72.92
REMARK 500 9 CYS A 5 36.90 -95.11
REMARK 500 9 LYS A 23 -16.79 79.51
REMARK 500 9 SER A 29 -8.52 73.63
REMARK 500 10 CYS A 5 37.97 -94.07
REMARK 500 10 SER A 9 47.99 -76.26
REMARK 500 10 LYS A 23 -15.83 80.30
REMARK 500 10 SER A 29 -0.07 72.92
REMARK 500 11 CYS A 5 35.50 -91.92
REMARK 500 11 LYS A 23 -12.10 77.50
REMARK 500 11 SER A 29 -1.98 74.70
REMARK 500 12 CYS A 5 37.02 -90.26
REMARK 500 12 SER A 9 47.55 -75.65
REMARK 500 12 LYS A 23 -16.32 81.42
REMARK 500 13 CYS A 5 37.26 -89.99
REMARK 500 13 LYS A 23 -10.93 76.89
REMARK 500 13 SER A 29 -6.14 73.79
REMARK 500 14 CYS A 5 36.10 -91.74
REMARK 500 14 LYS A 23 -11.67 77.75
REMARK 500 14 SER A 29 -7.95 72.00
REMARK 500 15 CYS A 5 37.58 -94.00
REMARK 500 15 SER A 9 49.94 -76.24
REMARK 500 15 LYS A 23 -12.26 79.14
REMARK 500 15 SER A 29 -5.70 73.20
REMARK 500 16 CYS A 5 38.46 -98.34
REMARK 500
REMARK 500 THIS ENTRY HAS 65 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZA8 A 1 28 UNP P84522 VHL1_VIOHE 4 31
SEQRES 1 A 31 CYS GLY GLU SER CYS ALA MET ILE SER PHE CYS PHE THR
SEQRES 2 A 31 GLU VAL ILE GLY CYS SER CYS LYS ASN LYS VAL CYS TYR
SEQRES 3 A 31 LEU ASN SER ILE SER
HELIX 1 1 CYS A 11 VAL A 15 5 5
SHEET 1 A 3 GLU A 3 SER A 4 0
SHEET 2 A 3 VAL A 24 TYR A 26 -1 O CYS A 25 N GLU A 3
SHEET 3 A 3 SER A 19 LYS A 21 -1 N SER A 19 O TYR A 26
SSBOND 1 CYS A 1 CYS A 18 1555 1555 2.03
SSBOND 2 CYS A 5 CYS A 20 1555 1555 2.03
SSBOND 3 CYS A 11 CYS A 25 1555 1555 2.02
LINK N CYS A 1 C SER A 31 1555 1555 1.33
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 - 2 20 Bytes