BMRB Entry 4403

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4403

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Title:
1H, 13C and 15N Resonance Assignment and Secondary Structure of the J Domain of Murine Polyomavirus T Antigens
Deposition date:
1999-09-13
Original release date:
2001-02-15
Authors:
Berjanskii, Mark; Riley, Michael; Xie, Anyong; Semenchenko, Valentyna; Folk, William; Van Doren, Steven
Citation:

Citation: Berjanskii, Mark; Riley, Michael; Xie, Anyong; Semenchenko, Valentyna; Folk, William; Van Doren, Steven. "NMR Structure of the N-terminal J Domain of Murine Polyomavirus T Antigens: Implications for DnaJ-like Domains and for Mutations of T Antigens"  J. Biol. Chem. 275, 36094-36103 (2000).

Assembly members:

Assembly members:
Polyomavirus J domain, polymer, 85 residues, 9985 Da.

Natural source:

Natural source:   Common Name: Polyomavirus   Taxonomy ID: 10624   Superkingdom: Virus   Kingdom: not available   Genus/species: Polyomavirus not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Polyomavirus J domain: MDRVLSRADKERLLELLKLP RQLWGDFGRMQQAYKQQSLL LHPDKGGSHALMQELNSLWG TFKTEVYNLRMNLGGTGFQH HHHHH

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts81
1H chemical shifts568

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Py J1

Entities:

Entity 1, Py J 85 residues - 9985 Da.

1   METASPARGVALLEUSERARGALAASPLYS
2   GLUARGLEULEUGLULEULEULYSLEUPRO
3   ARGGLNLEUTRPGLYASPPHEGLYARGMET
4   GLNGLNALATYRLYSGLNGLNSERLEULEU
5   LEUHISPROASPLYSGLYGLYSERHISALA
6   LEUMETGLNGLULEUASNSERLEUTRPGLY
7   THRPHELYSTHRGLUVALTYRASNLEUARG
8   METASNLEUGLYGLYTHRGLYPHEGLNHIS
9   HISHISHISHISHIS

Samples:

sample_1: Polyomavirus J domain, [95% 13C; 95% 15N], 0.5 – 1.5 mM; sodium phosphate 10 mM; KCl 10 mM; glycine 100 mM

sample_conditions_set_1: pH*: 6; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
HNCAsample_1not availablesample_conditions_set_1
HN(CO)CAsample_1not availablesample_conditions_set_1
HN(CA)HAsample_1not availablesample_conditions_set_1
HA(CACO)NHsample_1not availablesample_conditions_set_1
CBCA(CO)NHsample_1not availablesample_conditions_set_1
(H)CCA(CO)NHsample_1not availablesample_conditions_set_1
HACACOsample_1not availablesample_conditions_set_1
HCCH-COSYsample_1not availablesample_conditions_set_1
HCCH-TOCSY, 15N-separatedsample_1not availablesample_conditions_set_1
NOESY-HSQC, 13N-separatedsample_1not availablesample_conditions_set_1
FSCT-HSMQC-NOESYsample_1not availablesample_conditions_set_1

Software:

Sybyl Triad v6.3 - spectra processing and viewing

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 16044
PDB
EMBL CAA42510
GB AAA46872 AAA93241 AAA93245 AAB59901 AAL35609
REF YP_009111413
SP P03073 P03074 P12905
AlphaFold P03073 P03074 P12905

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks