BMRB Entry 30858

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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/BMR30858
MolProbity Validation Chart

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Title:
Structure of Nedd4L WW3 domain
Deposition date:
2021-02-11
Original release date:
2021-07-15
Authors:
Alam, S.; Alian, A.; Thompson, T.; Rheinemann, L.; Sundquist, W.
Citation:

Citation: Rheinemann, Lara; Thompson, Tuscan; Mercenne, Gaelle; Paine, Elliott; Peterson, Francis; Volkman, Brian; Alam, Steven; Alian, Akram; Sundquist, Wesley. "Interactions between AMOT PPxY motifs and NEDD4L WW domains function in HIV-1 release"  J. Biol. Chem. 297, 100975-100975 (2021).
PubMed: 34284061

Assembly members:

Assembly members:
entity_1, polymer, 68 residues, 7756.744 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQNNEELPTYEEAKVGGGGG SKVTQSFLPPGWEMRIAPNG RPFFIDHNTKTTTWEDPRLK FPVHMRSK

Data sets:
Data typeCount
13C chemical shifts276
15N chemical shifts66
1H chemical shifts444

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 68 residues - 7756.744 Da.

1   METGLNASNASNGLUGLULEUPROTHRTYR
2   GLUGLUALALYSVALGLYGLYGLYGLYGLY
3   SERLYSVALTHRGLNSERPHELEUPROPRO
4   GLYTRPGLUMETARGILEALAPROASNGLY
5   ARGPROPHEPHEILEASPHISASNTHRLYS
6   THRTHRTHRTRPGLUASPPROARGLEULYS
7   PHEPROVALHISMETARGSERLYS

Samples:

sample_1: Angiomotin,E3 ubiquitin-protein ligase NEDD4-like fusion, [U-100% 13C; U-100% 15N], mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_2: Angiomotin,E3 ubiquitin-protein ligase NEDD4-like fusion, [U-100% 15N], mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

Felix v2007, Accelrys Software Inc. - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 900 MHz
  • Varian INOVA 800 MHz

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