BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27634

Title: 1H, 13C, and 15N Chemical Shift Assignments of the C-terminal region of the Menangle virus Phosphoprotein   PubMed: 30680534

Deposition date: 2018-10-01 Original release date: 2019-09-12

Authors: Kingston, Richard; Herr, Nicole; Webby, Melissa; Bulloch, Esther; Schmitz, Michael

Citation: Herr, Nicole; Webby, Melissa; Bulloch, Esther; Schmitz, Michael; Kingston, Richard. "NMR chemical shift assignment of the C-terminal region of the Menangle virus phosphoprotein"  Biomol. NMR Assignments 13, 195-199 (2019).

Assembly members:
MenV_P_267_388, polymer, 122 residues, 13137.174 Da.

Natural source:   Common Name: Menangle rubulavirus   Taxonomy ID: 1979164   Superkingdom: Viruses   Kingdom: not available   Genus/species: Menangle rubulavirus

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

Entity Sequences (FASTA):
MenV_P_267_388: TTIKIMDPGVGDGATAAKSK RLFKEAPVVVSGPVIGDNPI VDADTIQLDELARPSLPKTK SQKSSAASPAALSGYKMTLL ALIKESIPNQAKRQKFEMQV GGIRNEQDFKNLRREIIRSA AQ

Data sets:
Data typeCount
13C chemical shifts513
15N chemical shifts127
1H chemical shifts855

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Menangle virus Phosphoprotein, C-terminal region1

Entities:

Entity 1, Menangle virus Phosphoprotein, C-terminal region 122 residues - 13137.174 Da.

1   THRTHRILELYSILEMETASPPROGLYVAL
2   GLYASPGLYALATHRALAALALYSSERLYS
3   ARGLEUPHELYSGLUALAPROVALVALVAL
4   SERGLYPROVALILEGLYASPASNPROILE
5   VALASPALAASPTHRILEGLNLEUASPGLU
6   LEUALAARGPROSERLEUPROLYSTHRLYS
7   SERGLNLYSSERSERALAALASERPROALA
8   ALALEUSERGLYTYRLYSMETTHRLEULEU
9   ALALEUILELYSGLUSERILEPROASNGLN
10   ALALYSARGGLNLYSPHEGLUMETGLNVAL
11   GLYGLYILEARGASNGLUGLNASPPHELYS
12   ASNLEUARGARGGLUILEILEARGSERALA
13   ALAGLN

Samples:

sample_1: MenV_P_267_388, [U-100% 13C; U-100% 15N], 0.7 – 1.2 mM; sodium phosphate 17.1 mM; sodium chloride 42.8 mM; sodium azide 0.43 mM; DSS 0.1 mM

sample_conditions_1: ionic strength: 42.8 mM; pH: 7.0; pressure: 1 atm; temperature: 283.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D (CT) HC-HSQCsample_1isotropicsample_conditions_1
2D fHSQCsample_1isotropicsample_conditions_1
3D 15N-edited NOESYsample_1isotropicsample_conditions_1
3D 15N-edited TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D (C)(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHACONHsample_1isotropicsample_conditions_1
3D (H)N(COCA)NHsample_1isotropicsample_conditions_1
3D HHC-NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D H2(C)Nsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment, collection

Biospin v2.4, Bruker Biospin - chemical shift assignment, collection

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

GenBank AF326114

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts