BMRB Entry 30880

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30880
MolProbity Validation Chart

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Title:
NMR structure of the Human T-cell leukemia virus 1 matrix protein
Deposition date:
2021-03-15
Original release date:
2021-09-17
Authors:
Herrmann, D.; Saad, J.
Citation:

Citation: Herrmann, Dominik; Zhou, Lynne; Hanson, Heather; Willkomm, Nora; Mansky, Louis; Saad, Jamil. "Structural Insights into the Mechanism of Human T-cell Leukemia Virus Type 1 Gag Targeting to the Plasma Membrane for Assembly"  J. Mol. Biol. 433, 167161-167161 (2021).
PubMed: 34298060

Assembly members:

Assembly members:
entity_1, polymer, 105 residues, 12026.986 Da.

Natural source:

Natural source:   Common Name: HTLV-1   Taxonomy ID: 11908   Superkingdom: Viruses   Kingdom: not available   Genus/species: Deltaretrovirus HTLV-1

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGRIFSRSASPIPRPPRGLA AHHWLNFLQAAYRLEPGPSS YDFHQLKKFLKIALETPVWI CPINYSLLASLLPKGYPGRV NEILHILIQTQAQIPSRPAH HHHHH

Data sets:
Data typeCount
13C chemical shifts439
15N chemical shifts95
1H chemical shifts698

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 105 residues - 12026.986 Da.

1   METGLYARGILEPHESERARGSERALASER
2   PROILEPROARGPROPROARGGLYLEUALA
3   ALAHISHISTRPLEUASNPHELEUGLNALA
4   ALATYRARGLEUGLUPROGLYPROSERSER
5   TYRASPPHEHISGLNLEULYSLYSPHELEU
6   LYSILEALALEUGLUTHRPROVALTRPILE
7   CYSPROILEASNTYRSERLEULEUALASER
8   LEULEUPROLYSGLYTYRPROGLYARGVAL
9   ASNGLUILELEUHISILELEUILEGLNTHR
10   GLNALAGLNILEPROSERARGPROALAHIS
11   HISHISHISHISHIS

Samples:

sample_1: sodium chloride 100 mM; sodium phosphate 50 mM; TCEP 2 mM; HTLV-1 Matrix, [U-99% 13C; U-99% 15N], 400 uM

sample_2: sodium chloride 100 mM; sodium phosphate 50 mM; TCEP 2 mM; HTLV-1 Matrix, [U-99% 13C; U-99% 15N], 320 uM

sample_3: sodium chloride 100 mM; sodium phosphate 50 mM; TCEP 2 mM; HTLV-1 Matrix, [U-99% 15N], 500 uM

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_3isotropicsample_conditions_1
3D 13C-separated NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSY arom.sample_2isotropicsample_conditions_1
3D HCCH-TOCSY ali.sample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 15N-separated TOCSYsample_3isotropicsample_conditions_1

Software:

CYANA, Guntert P. - refinement

CcpNmr Analysis v2.4, CCPN - chemical shift assignment

CARA v1.9.1.2, Keller and Wuthrich - processing

UNIO v10, Torsten Herrmann - chemical shift assignment

TopSpin, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker AVANCE II 700 MHz

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