BMRB Entry 31039

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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/BMR31039
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
VPS37A_21-148
Deposition date:
2022-08-12
Original release date:
2023-08-03
Authors:
Tian, F.; Ye, Y.
Citation:

Citation: Ye, Yansheng; Liang, Xinwen; Wang, Guifang; Bewley, Maria; Hamamoto, Kouta; Liu, Xiaoming; Flanagan, John; Wang, Hong-Gang; Takahashi, Yoshinori; Tian, Fang. "Identification of membrane curvature sensing motifs essential for VPS37A phagophore recruitment and autophagosome closure"  Commun. Biol. 7, 334-334 (2024).
PubMed: 38491121

Assembly members:

Assembly members:
entity_1, polymer, 128 residues, 14571.687 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: GLTSLQQQKQRLIESLRNSH SSIAEIQKDVEYRLPFTINN LTININILLPPQFPQEKPVI SVYPPIRHHLMDKQGVYVTS PLVNNFTMHSDLGKIIQSLL DEFWKNPPVLAPTSTAFPYL YSNPSGMS

Data typeCount
13C chemical shifts573
15N chemical shifts113
1H chemical shifts794

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 128 residues - 14571.687 Da.

1   GLYLEUTHRSERLEUGLNGLNGLNLYSGLN
2   ARGLEUILEGLUSERLEUARGASNSERHIS
3   SERSERILEALAGLUILEGLNLYSASPVAL
4   GLUTYRARGLEUPROPHETHRILEASNASN
5   LEUTHRILEASNILEASNILELEULEUPRO
6   PROGLNPHEPROGLNGLULYSPROVALILE
7   SERVALTYRPROPROILEARGHISHISLEU
8   METASPLYSGLNGLYVALTYRVALTHRSER
9   PROLEUVALASNASNPHETHRMETHISSER
10   ASPLEUGLYLYSILEILEGLNSERLEULEU
11   ASPGLUPHETRPLYSASNPROPROVALLEU
12   ALAPROTHRSERTHRALAPHEPROTYRLEU
13   TYRSERASNPROSERGLYMETSER

Samples:

sample_1: VPS37A_21-148, [U-13C; U-15N], 0.5 ± 0.05 mM; HEPES 50 mM; NaCl 250 mM; phage Pf1 6.5 mg/mL

sample_2: VPS37A_21-148, [U-13C; U-15N], 0.5 mM; HEPES 25 mM; NaCl 150 mM; bicelles (DMPC:DMPG:DHPC = 4:1:10, molar ratio, q=0.5)30 12 % w/v

sample_3: VPS37A_21-148, [U-13C; U-15N], 0.5 mM; NaCl 150 mM; PBS 20 mM; NaN3 0.02%

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

Experiments:

NameSampleSample stateSample conditions
2D TROSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D IPAP-HSQCsample_1anisotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, CYANA by Guntert, P. - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE II 600 MHz
  • Bruker AVANCE III HD 850 MHz

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