BMRB Entry 27396

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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/BMR27396
MolProbity Validation Chart

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Title:
NMR assignments of Rous sarcoma virus matrix protein (M domain)
Deposition date:
2018-02-06
Original release date:
2018-10-15
Authors:
Vlach, Jiri; Saad, Jamil; Eastep, Gunnar; Ghanam, Ruba
Citation:

Citation: Vlach, Jiri; Eastep, Gunnar; Ghanam, Ruba; Watanabe, Susan; Carter, Carol; Saad, Jamil. "Structural basis for targeting avian sarcoma virus Gag polyprotein to the plasma membrane for virus assembly"  J. Biol. Chem. 293, 18828-18840 (2018).
PubMed: 30309983

Assembly members:

Assembly members:
sRSV_MA, polymer, 87 residues, 9201.7769 Da.

Natural source:

Natural source:   Common Name: Rous sarcoma virus   Taxonomy ID: 11886   Superkingdom: Viruses   Kingdom: not available   Genus/species: Alpharetrovirus Rous sarcoma virus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
sRSV_MA: SEAVIKVISSACKTYCGKTS PSKKEIGAMLSLLQKEGLLM SPSDLYSPGSWDPITAALSQ RAMILGKSGELKTWGLVLGA LKAAREE

Data sets:
Data typeCount
13C chemical shifts390
15N chemical shifts89
1H chemical shifts622

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1sRSV MA1

Entities:

Entity 1, sRSV MA 87 residues - 9201.7769 Da.

1   SERGLUALAVALILELYSVALILESERSER
2   ALACYSLYSTHRTYRCYSGLYLYSTHRSER
3   PROSERLYSLYSGLUILEGLYALAMETLEU
4   SERLEULEUGLNLYSGLUGLYLEULEUMET
5   SERPROSERASPLEUTYRSERPROGLYSER
6   TRPASPPROILETHRALAALALEUSERGLN
7   ARGALAMETILELEUGLYLYSSERGLYGLU
8   LEULYSTHRTRPGLYLEUVALLEUGLYALA
9   LEULYSALAALAARGGLUGLU

Samples:

13C15N: sRSV MA, [U-95% 13C; U-90% 15N], .5 mM; sodium phosphate 50 mM; sodium chloride 50 mM; TCEP 2 mM

15N: sRSV MA, [U-95% 13C; U-90% 15N], .5 mM; sodium phosphate 50 mM; sodium chloride 50 mM; TCEP 2 mM

13C15ND2O: sRSV MA, [U-95% 13C; U-90% 15N], .5 mM; sodium phosphate 50 mM; potassium chloride 50 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 0.100 M; pH: 6.000; pressure: 1.000 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESY13C15Nisotropicsample_conditions_1
3D 1H-15N TOCSY13C15Nisotropicsample_conditions_1
2D 1H-15N HSQC/HMQC15Nisotropicsample_conditions_1
2D 1H-13C HSQC/HMQC13C15Nisotropicsample_conditions_1
3D HN(CO)CA13C15Nisotropicsample_conditions_1
3D HNCA13C15Nisotropicsample_conditions_1
3D HNCACB13C15Nisotropicsample_conditions_1
HNcoCACB (H[N[co[{CA|ca[C]}]]])13C15Nisotropicsample_conditions_1
3D HNCO13C15Nisotropicsample_conditions_1
hCCH (hC_CH.relayed)13C15Nisotropicsample_conditions_1
hCCH-aro (hC_CH.relayed)13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY13C15ND2Oisotropicsample_conditions_1

Software:

CcpNmr_Analysis v2.4, CCPN - spectral analysis

nmrDraw vany, Frank Delaglio - Spectrum analysis, Spectrum display

nmrPipe vany, Frank Delaglio - Spectrum processing

NMR spectrometers:

  • Bruker DMX 700 MHz

Related Database Links:

UniProt P03322
AlphaFold P03322

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