BMRB Entry 50370

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50370

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Nipah Virus Phosphoprotein N-terminal Region (1-406)
Deposition date:
2020-06-30
Original release date:
2021-07-27
Authors:
Schiavina, Marco; Salladini, Edoardo; Murrali, Maria Grazia; Tria, Giancarlo; Felli, Isabella C.; Pierattelli, Roberta; Longhi, Sonia
Citation:

Citation: Schiavina, Marco; Salladini, Edoardo; Murrali, Maria Grazia; Tria, Giancarlo; Felli, Isabella C.; Pierattelli, Roberta; Longhi, Sonia. "Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS"  Sci. Rep. 10, 19574-19574 (2020).
PubMed: 33177626

Assembly members:

Assembly members:
entity_1, polymer, 406 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Nipah henipavirus   Taxonomy ID: 121791   Superkingdom: Viruses   Kingdom: not available   Genus/species: Nipah henipavirus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDest14

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDKLELVNDGLNIIDFIQKN QKEIQKTYGRSSIQQPSIKD QTKAWEDFLQCTSGESEQVE GGMSKDDGDVERRNLEDLSS TSPTDGTIGKRVSNTRDWAE GSDDIQLDPVVTDVVYHDHG GECTGYGFTSSPERGWSDYT SGANNGNVCLVSDAKMLSYA PEIAVSKEDRETDLVHLENK LSTTGLNPTAVPFTLRNLSD PAKDSPVIAEHYYGLGVKEQ NVGPQTSRNVNLDSIKLYTS DDEEADQLEFEDEFAGSSSE VIVGISPEDEEPSSVGGKPN ESIGRTIEGQSIRDNLQAKD NKSTDVPGAGPKDSAVKEEP PQKRLPMLAEEFECSGSEDP IIRELLKENSLINCQQGKDA QPPYHWSIERSISPDKTEIV NGAVQTADRQRPGTPMPKSR GIPIKK

Data sets:
Data typeCount
13C chemical shifts1066
15N chemical shifts360
1H chemical shifts307

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NiV_PNT1

Entities:

Entity 1, NiV_PNT 406 residues - Formula weight is not available

1   METASPLYSLEUGLULEUVALASNASPGLY
2   LEUASNILEILEASPPHEILEGLNLYSASN
3   GLNLYSGLUILEGLNLYSTHRTYRGLYARG
4   SERSERILEGLNGLNPROSERILELYSASP
5   GLNTHRLYSALATRPGLUASPPHELEUGLN
6   CYSTHRSERGLYGLUSERGLUGLNVALGLU
7   GLYGLYMETSERLYSASPASPGLYASPVAL
8   GLUARGARGASNLEUGLUASPLEUSERSER
9   THRSERPROTHRASPGLYTHRILEGLYLYS
10   ARGVALSERASNTHRARGASPTRPALAGLU
11   GLYSERASPASPILEGLNLEUASPPROVAL
12   VALTHRASPVALVALTYRHISASPHISGLY
13   GLYGLUCYSTHRGLYTYRGLYPHETHRSER
14   SERPROGLUARGGLYTRPSERASPTYRTHR
15   SERGLYALAASNASNGLYASNVALCYSLEU
16   VALSERASPALALYSMETLEUSERTYRALA
17   PROGLUILEALAVALSERLYSGLUASPARG
18   GLUTHRASPLEUVALHISLEUGLUASNLYS
19   LEUSERTHRTHRGLYLEUASNPROTHRALA
20   VALPROPHETHRLEUARGASNLEUSERASP
21   PROALALYSASPSERPROVALILEALAGLU
22   HISTYRTYRGLYLEUGLYVALLYSGLUGLN
23   ASNVALGLYPROGLNTHRSERARGASNVAL
24   ASNLEUASPSERILELYSLEUTYRTHRSER
25   ASPASPGLUGLUALAASPGLNLEUGLUPHE
26   GLUASPGLUPHEALAGLYSERSERSERGLU
27   VALILEVALGLYILESERPROGLUASPGLU
28   GLUPROSERSERVALGLYGLYLYSPROASN
29   GLUSERILEGLYARGTHRILEGLUGLYGLN
30   SERILEARGASPASNLEUGLNALALYSASP
31   ASNLYSSERTHRASPVALPROGLYALAGLY
32   PROLYSASPSERALAVALLYSGLUGLUPRO
33   PROGLNLYSARGLEUPROMETLEUALAGLU
34   GLUPHEGLUCYSSERGLYSERGLUASPPRO
35   ILEILEARGGLULEULEULYSGLUASNSER
36   LEUILEASNCYSGLNGLNGLYLYSASPALA
37   GLNPROPROTYRHISTRPSERILEGLUARG
38   SERILESERPROASPLYSTHRGLUILEVAL
39   ASNGLYALAVALGLNTHRALAASPARGGLN
40   ARGPROGLYTHRPROMETPROLYSSERARG
41   GLYILEPROILELYSLYS

Samples:

sample_1: N-terminal domain of Phosphoprotein of Nipah Virus, [U-100% 13C; U-100% 15N], 150 uM

sample_conditions_1: ionic strength: 0.06 M; pH: 6.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N BEST TROSYsample_1isotropicsample_conditions_1
2D 13C-CONsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D (H)H(COCA)NNHsample_1isotropicsample_conditions_1
3D (H)N(CA)NNHsample_1isotropicsample_conditions_1
3D (H)CBCACONsample_1isotropicsample_conditions_1
3D (H)CBCANCOsample_1isotropicsample_conditions_1
3D (HCA)COCONsample_1isotropicsample_conditions_1
5D (HACA)CONCACONsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1
1D 13Csample_1isotropicsample_conditions_1

Software:

TOPSPIN; Dynamic Centre; Xeasy v4.0.8; 2.0; - chemical shift assignment, collection, data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz
  • Bruker AVANCE NEO 700 MHz
  • Bruker AVANCE III 950 MHz

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