BMRB Entry 27663

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27663

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Title:
HKU4 NSP3 C Domain
Deposition date:
2018-10-26
Original release date:
2021-07-21
Authors:
Staup, Andrew; De Silva, Ivon; Catt, Justin; Tan, Xuan; Hammond, Robert; Ahmadvand, Parvaneh; Cowan, Jaden; Crisp, Eric; Cuny, Zachary; Konutham, Amareshwari; Mushimiyimana, Anne; Parker, Candace; Prasannakumar, Geethika; Rojas, Edwin; Subedi, Ashok; Zaharias, Steve; Jablonsky, Michael; Shin, Ronald; Johnson, Margaret
Citation:

Citation: Staup, Andrew; De Silva, Ivon; Catt, Justin; Tan, Xuan; Hammond, Robert; Johnson, Margaret. "Structure of the SARS-Unique Domain C From the Bat Coronavirus HKU4"  Nat. Prod. Commun. 14, .-. (2019).
PubMed: 32395093

Assembly members:

Assembly members:
HKU4C, polymer, 81 residues, 9111.31 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 694007   Superkingdom: virus   Kingdom: ssRNA virus   Genus/species: betacoronavirus Tylonycteris bat coronavirus HKU4

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HKU4C: SHMQTPETAFINNVTSNGGY HSWHLVSGDLIVKDVCYKKL LHWSGQTICYADNKFYVVKN DVALPFSDLEACRAYLTSRA A

Data sets:
Data typeCount
13C chemical shifts324
15N chemical shifts85
1H chemical shifts535

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HKU4C1

Entities:

Entity 1, HKU4C 81 residues - 9111.31 Da.

First three residues (-3 to -1) are remnants of a non-native affinity tag. Residues Q 1445 through A 1522 are native to non-structural protein 3 of HKU4 and are numbered based on the beginning of nsp3.

1   SERHISMETGLNTHRPROGLUTHRALAPHE
2   ILEASNASNVALTHRSERASNGLYGLYTYR
3   HISSERTRPHISLEUVALSERGLYASPLEU
4   ILEVALLYSASPVALCYSTYRLYSLYSLEU
5   LEUHISTRPSERGLYGLNTHRILECYSTYR
6   ALAASPASNLYSPHETYRVALVALLYSASN
7   ASPVALALALEUPROPHESERASPLEUGLU
8   ALACYSARGALATYRLEUTHRSERARGALA
9   ALA

Samples:

sample_1: HKU4C, [U-99% 13C; U-99% 15N], 2 mM; sodium chloride 150 mM; DTT, [U-99% 2H], 3 mM; sodium phosphate 20 mM; sodium azide 1 mM

sample_2: HKU4C, [U-99% 15N], 2 mM; sodium chloride 150 mM; DTT, [U-99% 2H], 3 mM; sodium phosphate 20 mM; sodium azide 1 mM

sample_conditions_1: ionic strength: 0.17 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2anisotropicsample_conditions_1
2D 1H-13C HSQCsample_1anisotropicsample_conditions_1
3D CBCA(CO)NHsample_1anisotropicsample_conditions_1
3D HCCH-TOCSYsample_1anisotropicsample_conditions_1
3D HNCOsample_1anisotropicsample_conditions_1
3D HNCAsample_1anisotropicsample_conditions_1
3D HNCACBsample_1anisotropicsample_conditions_1
3D HBHA(CO)NHsample_1anisotropicsample_conditions_1
3D HN(CO)CAsample_1anisotropicsample_conditions_1
3D 1H-15N NOESYsample_2anisotropicsample_conditions_1
3D 1H-15N TOCSYsample_2anisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1anisotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

TOPSPIN v3.5pI7, Bruker Biospin - collection

CARA v1.9.1.7, Keller and Wuthrich - chemical shift assignment, data analysis

UNIO'10 v2.0.2, Hermann and Wuthrich - peak picking

ATNOS/CANDID, Hermann and Wuthrich - peak picking, structure solution

NMR spectrometers:

  • Bruker Avance III 850 MHz
  • Bruker Avance II 700 MHz
  • Bruker Avance III 600 MHz

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