BMRB Entry 30297

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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/BMR30297
MolProbity Validation Chart

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Title:
1H, 13C, 15N chemical shift assignments of the HIV-1 gp41 cytoplasmic tail, residues 752-856
Deposition date:
2017-05-22
Original release date:
2017-11-02
Authors:
Saad, J.; Murphy, R.; Samal, A.; Vlach, J.
Citation:

Citation: Murphy, R Elliot; Samal, Alexandra; Vlach, Jiri; Saad, Jamil. "Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein"  Structure 0969-2126, 30301-30305 (2017).
PubMed: 29056482

Assembly members:

Assembly members:
entity_1, polymer, 105 residues, 12398.524 Da.

Natural source:

Natural source:   Common Name: HIV-1   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV-1

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SLALIWDDLRSLCLFSYHRL RDLLLIVTRIVELLGRRGWE ALKYWWNLLQYWSQELKNSA VNLLNATAIAVAEGTDRVIE VLQAAYRAIRHIPRRIRQGL ERILL

Data sets:
Data typeCount
13C chemical shifts462
15N chemical shifts107
1H chemical shifts680

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 105 residues - 12398.524 Da.

1   SERLEUALALEUILETRPASPASPLEUARG
2   SERLEUCYSLEUPHESERTYRHISARGLEU
3   ARGASPLEULEULEUILEVALTHRARGILE
4   VALGLULEULEUGLYARGARGGLYTRPGLU
5   ALALEULYSTYRTRPTRPASNLEULEUGLN
6   TYRTRPSERGLNGLULEULYSASNSERALA
7   VALASNLEULEUASNALATHRALAILEALA
8   VALALAGLUGLYTHRASPARGVALILEGLU
9   VALLEUGLNALAALATYRARGALAILEARG
10   HISILEPROARGARGILEARGGLNGLYLEU
11   GLUARGILELEULEU

Samples:

sample_1: DPC 25 mM; TCEP 1 mM; gp4CTc 500 uM; sodium chloride 50 mM; sodium phosphate 50 mM

sample_2: DPC 25 mM; TCEP 1 mM; gp4CTc, [U-99% 15N], 500 uM; sodium chloride 50 mM; sodium phosphate 50 mM

sample_3: DPC 25 mM; TCEP 1 mM; gp4CTc, [U-99% 13C; U-99% 15N], 500 uM; sodium chloride 50 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 324 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-13C HMQC NOESYsample_3isotropicsample_conditions_1

Software:

Analysis v2.4.2, CCPN - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

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

TOPSPIN, Bruker Biospin - collection

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