BMRB Entry 27498

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27498

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Title:
1H, 15N and 13C resonance assignments of the C-terminal domain of the P protein of the Nishigahara strain of rabies virus
Deposition date:
2018-05-30
Original release date:
2018-10-03
Authors:
Zhan, Jingyu; Gooley, Paul
Citation:

Citation: Zhan, Jingyu; Hossain, Md Alamgir; Sethi, Ashish; Ose, Toyoyuki; Moseley, Gregory; Gooley, Paul. "1H, 15N and 13C resonance assignments of the C-terminal domain of the P protein of the Nishigahara strain of rabies virus"  Biomol. NMR Assign. 13, 5-8 (2019).
PubMed: 30238347

Assembly members:

Assembly members:
RABV_P-protein_CTD, polymer, 115 residues, 13000.82 Da.

Natural source:

Natural source:   Common Name: Lyssavirus genus   Taxonomy ID: 11286   Superkingdom: viruses   Kingdom: ssRNA2   Genus/species: Lyssavirus genus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RABV_P-protein_CTD: GHMWSATNEEDDLSVEAEIA HQIAESFSKKYKFPSRSSGI FLYNFEQLKMNLDDIVKEAK NVPGVTRLAHDGSKLPLRCV LGWVALANSKKFQLLVEANK LNKIMQDDLNRYASS

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts121
1H chemical shifts760

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RABV P-protein CTD1

Entities:

Entity 1, RABV P-protein CTD 115 residues - 13000.82 Da.

The first 3 residues GHM represent a non-native part introduced from cloning.

1   GLYHISMETTRPSERALATHRASNGLUGLU
2   ASPASPLEUSERVALGLUALAGLUILEALA
3   HISGLNILEALAGLUSERPHESERLYSLYS
4   TYRLYSPHEPROSERARGSERSERGLYILE
5   PHELEUTYRASNPHEGLUGLNLEULYSMET
6   ASNLEUASPASPILEVALLYSGLUALALYS
7   ASNVALPROGLYVALTHRARGLEUALAHIS
8   ASPGLYSERLYSLEUPROLEUARGCYSVAL
9   LEUGLYTRPVALALALEUALAASNSERLYS
10   LYSPHEGLNLEULEUVALGLUALAASNLYS
11   LEUASNLYSILEMETGLNASPASPLEUASN
12   ARGTYRALASERSER

Samples:

15N: sodium phosphate 50 mM; DTT 1 mM; sodium chloride 100 mM; sodium azide 0.02%; NIP-CTD, [U-99% 15N], 0.6 mM

unlabelled: sodium phosphate 50 mM; DTT 1 mM; sodium chloride 100 mM; sodium azide 0.02%; NIP-CTD 0.6 mM; DSS 50 uM

13C-D2O: sodium phosphate 50 mM; DTT 1 mM; sodium chloride 100 mM; sodium azide 0.02%; NIP-CTD, [U-98% 13C; U-98% 15N], 0.3 mM

13C-H2O: sodium phosphate 50 mM; DTT 1 mM; sodium chloride 100 mM; sodium azide 0.02%; NIP-CTD, [U-98% 13C; U-98% 15N], 0.3 mM

10_13C: sodium phosphate 50 mM; DTT 1 mM; sodium chloride 100 mM; sodium azide 0.02%; NIP-CTD, [U-10% 13C; U-99% 15N], 0.32 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic13C-D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aromatic13C-D2Oisotropicsample_conditions_1
2D 1H-1H TOCSYunlabelledisotropicsample_conditions_1
2D 1H-1H NOESYunlabelledisotropicsample_conditions_1
3D CBCA(CO)NH13C-H2Oisotropicsample_conditions_1
3D HNCACB13C-H2Oisotropicsample_conditions_1
3D C(CO)NH13C-H2Oisotropicsample_conditions_1
3D HNCO13C-H2Oisotropicsample_conditions_1
3D HN(CA)CO13C-H2Oisotropicsample_conditions_1
3D H(CCO)NH13C-H2Oisotropicsample_conditions_1
3D HBHA(CO)NH13C-H2Oisotropicsample_conditions_1
3D HCCH-TOCSY13C-D2Oisotropicsample_conditions_1
3D 1H-13C NOESY aromatic13C-D2Oisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic13C-D2Oisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic10_13Cisotropicsample_conditions_1

Software:

NMRFAM-SPARKY vv 1.3, Lee W, Tonelli M, Markley JL - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA vv 2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

MddNMR, V. Orekhov, V. Jaravine, M. Mayzel, K. Kazimierczuk - processing

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP Q9IPJ8
AlphaFold Q75T11

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