BMRB Entry 17523

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17523
MolProbity Validation Chart

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Title:
Backbone and side-chain 1H, 15N, and 13C resonance assignments of Norwalk virus protease
Deposition date:
2011-03-11
Original release date:
2011-06-08
Authors:
Takahashi, Daisuke; Kim, Yunjeong; Chang, Kyeong-Ok; Anbanandam, Asokan; Prakash, Om
Citation:

Citation: Takahashi, Daisuke; Kim, Yunjeong; Chang, Kyeong-Ok; Anbanandam, Asokan; Prakash, Om. "Backbone and side-chain (1)H, (15)N, and (13)C resonance assignments of Norwalk virus protease."  Biomol. NMR Assignments 6, 19-21 (2012).
PubMed: 21647610

Assembly members:

Assembly members:
NVpro, polymer, 188 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Nowwalk virus   Taxonomy ID: 11983   Superkingdom: Viruses   Kingdom: not available   Genus/species: Norovirus Nowwalk virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NVpro: MHHHHHHAPPTLWSRVTKFG SGWGFWVSPTVFITTTHVVP TGVKEFFGEPLSSIAIHQAG EFTQFRFSKKMRPDLTGMVL EEGCPEGTVCSVLIKRDSGE LLPLAVRMGAIASMRIQGRL VHGQSGMLLTGANAKGMDLG TIPGDCGAPYVHKRGNDWVV CGVHAAATKSGNTVVCAVQA GEGETALE

Data sets:
Data typeCount
13C chemical shifts683
15N chemical shifts177
1H chemical shifts1123

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Norwalk virus protease1

Entities:

Entity 1, Norwalk virus protease 188 residues - Formula weight is not available

1   METHISHISHISHISHISHISALAPROPRO
2   THRLEUTRPSERARGVALTHRLYSPHEGLY
3   SERGLYTRPGLYPHETRPVALSERPROTHR
4   VALPHEILETHRTHRTHRHISVALVALPRO
5   THRGLYVALLYSGLUPHEPHEGLYGLUPRO
6   LEUSERSERILEALAILEHISGLNALAGLY
7   GLUPHETHRGLNPHEARGPHESERLYSLYS
8   METARGPROASPLEUTHRGLYMETVALLEU
9   GLUGLUGLYCYSPROGLUGLYTHRVALCYS
10   SERVALLEUILELYSARGASPSERGLYGLU
11   LEULEUPROLEUALAVALARGMETGLYALA
12   ILEALASERMETARGILEGLNGLYARGLEU
13   VALHISGLYGLNSERGLYMETLEULEUTHR
14   GLYALAASNALALYSGLYMETASPLEUGLY
15   THRILEPROGLYASPCYSGLYALAPROTYR
16   VALHISLYSARGGLYASNASPTRPVALVAL
17   CYSGLYVALHISALAALAALATHRLYSSER
18   GLYASNTHRVALVALCYSALAVALGLNALA
19   GLYGLUGLYGLUTHRALALEUGLU

Samples:

NVpro_15N_labeled: NVpro, [U-99% 15N], 0.7-0.8 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 3 mM; D2O 5 mM

NVpro_13C15N_labeled: NVpro, [U-99% 13C; U-99% 15N], 0.7-0.8 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 3 mM; D2O, [U-99% 2H], 5 mM

NVpro_13C15N_labeled_D2O: NVpro, [U-99% 13C; U-99% 15N], 0.7-0.8 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 3 mM; D2O 5 mM

NVpro_15N_Val: NVpro, [U-15N]-Val, 0.7 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 3 mM; D2O 5 mM

NVpro_15N_Ala: NVpro, [U-15N]-Ala, 0.7 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 3 mM; D2O 5 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNVpro_15N_labeledisotropicsample_conditions_1
2D 1H-15N HSQCNVpro_13C15N_labeledisotropicsample_conditions_1
2D 1H-15N HSQCNVpro_13C15N_labeledisotropicsample_conditions_1
3D HNCONVpro_13C15N_labeledisotropicsample_conditions_1
3D HNCONVpro_13C15N_labeledisotropicsample_conditions_1
3D HN(CA)CONVpro_13C15N_labeledisotropicsample_conditions_1
3D HNCANVpro_13C15N_labeledisotropicsample_conditions_1
3D HN(CO)CANVpro_13C15N_labeledisotropicsample_conditions_1
3D HNCANVpro_13C15N_labeledisotropicsample_conditions_1
3D HNCACBNVpro_13C15N_labeledisotropicsample_conditions_1
3D CBCA(CO)NHNVpro_13C15N_labeledisotropicsample_conditions_1
3D HBHA(CO)NHNVpro_13C15N_labeledisotropicsample_conditions_1
3D H(CCO)NHNVpro_13C15N_labeledisotropicsample_conditions_1
3D C(CO)NHNVpro_13C15N_labeledisotropicsample_conditions_1
3D HNCACBNVpro_13C15N_labeledisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNVpro_13C15N_labeled_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNVpro_13C15N_labeledisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticNVpro_13C15N_labeledisotropicsample_conditions_1
3D 1H-15N NOESYNVpro_15N_labeledisotropicsample_conditions_1
3D hCCH-TOCSYNVpro_13C15N_labeled_D2Oisotropicsample_conditions_1
3D HCCH-TOCSYNVpro_13C15N_labeled_D2Oisotropicsample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment

SPARKY, Goddard - chemical shift assignment

VNMRJ, Varian - collection

TALOS, Cornilescu, Delaglio and Bax - Dihedral angle analysis, Secondary structure prediction

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Varian UnityPlus 500 MHz

Related Database Links:

PDB
GB AAB50465 AFJ38515 AGM33207 AGM33210 AGM33213
REF NP_056820 NP_786949
SP Q83883
AlphaFold Q83883

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