BMRB Entry 30736

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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/BMR30736
MolProbity Validation Chart

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Title:
Solution structure of the FYVE domain of ALFY
Deposition date:
2020-03-23
Original release date:
2020-12-18
Authors:
Reinhart, E.; Pellegrini, M.; Ragusa, M.
Citation:

Citation: Reinhart, Erin; Litt, Nicole; Katzenell, Sarah; Pellegrini, Maria; Yamamoto, Ai; Ragusa, Michael. "A highly conserved glutamic acid in ALFY inhibits membrane binding to aid in aggregate clearance"  Traffic 22, 23-37 (2021).
PubMed: 33225481

Assembly members:

Assembly members:
entity_1, polymer, 78 residues, 8940.072 Da.
entity_ZN, non-polymer, 65.409 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SNAGRSAADHWVKDEGGDSC SGCSVRFSLTERRHHCRNCG QLFCQKCSRFQSEIKRLKIS SPVRVCQNCYYNLQHERG

Data sets:
Data typeCount
13C chemical shifts290
15N chemical shifts75
1H chemical shifts467

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2, 12
3entity_2, 22

Entities:

Entity 1, entity_1 78 residues - 8940.072 Da.

1   SERASNALAGLYARGSERALAALAASPHIS
2   TRPVALLYSASPGLUGLYGLYASPSERCYS
3   SERGLYCYSSERVALARGPHESERLEUTHR
4   GLUARGARGHISHISCYSARGASNCYSGLY
5   GLNLEUPHECYSGLNLYSCYSSERARGPHE
6   GLNSERGLUILELYSARGLEULYSILESER
7   SERPROVALARGVALCYSGLNASNCYSTYR
8   TYRASNLEUGLNHISGLUARGGLY

Entity 2, entity_2, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: The FYVE domain of ALFY, [U-99% 13C; U-99% 15N], 768 uM; sodium phosphate 20 mM; sodium chloride 150 mM; TCEP 0.2 mM

sample_2: The FYVE domain of ALFY, [U-99% 15N], 583 uM; sodium phosphate 20 mM; sodium chloride 150 mM; TCEP 0.2 mM

sample_3: The FYVE domain of ALFY 589 uM; sodium phosphate 20 mM; sodium chloride 150 mM; TCEP 0.2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_2
2D 1H-1H NOESYsample_3isotropicsample_conditions_3
2D 1H-1H COSYsample_3isotropicsample_conditions_3
2D 1H-1H TOCSYsample_3isotropicsample_conditions_3
3D HN(CO)CAsample_1isotropicsample_conditions_2
3D HNCAsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_2
3D HCCH-TOCSYsample_1isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_2
3D HCCH-COSYsample_1isotropicsample_conditions_2
3D HN(CA)COsample_1isotropicsample_conditions_2
3D (H)C(CCO)NHsample_1isotropicsample_conditions_2
3D HBHA(CBCACO)NHsample_1isotropicsample_conditions_2
3D H(CCCO)NHsample_1isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_2

Software:

TopSpin, Bruker Biospin - processing

CARA, Keller and Wuthrich - chemical shift assignment

CANDID, Herrmann, Guntert and Wuthrich - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AVANCE 700 MHz

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