BMRB Entry 36514

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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/BMR36514
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
Solid-state NMR Structure of Aquaporin Z in its Native Cellular Membranes
Deposition date:
2022-10-02
Original release date:
2025-10-27
Authors:
Xie, H.; Zhao, Y.; Zhao, W.; Chen, Y.; Liu, M.; Yang, J.
Citation:

Citation: Xie, Huayong; Zhao, Yongxiang; Zhao, Weijing; Chen, Yanke; Liu, Maili; Yang, Jun. "Solid-state NMR structure determination of a membrane protein in E. coli cellular inner membrane."  Sci. Adv. 9, eadh4168-eadh4168 (2023).
PubMed: 37910616

Assembly members:

Assembly members:
Aquaporin Z, polymer, 243 residues, 25185.242 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 469008   Superkingdom: Bacteria   Kingdom: Pseudomonadati   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Aquaporin Z: MGSSHHHHHHEFMFRKLAAE CFGTFWLVFGGCGSAVLAAG FPELGIGFAGVALAFGLTVL TMAFAVGHISGGHFNPAVTI GLWAGGRFPAKEVVGYVIAQ VVGGIVAAALLYLIASGKTG FDAAASGFASNGYGEHSPGG YSMLSALVVELVLSAGFLLV IHGATDKFAPAGFAPIAIGL ALTLIHLISIPVTNTSVNPA RSTAVAIFQGGWALEQLWFF WVVPIVGGIIGGLIYRTLLE KRD

Data sets:
Data typeCount
13C chemical shifts847
15N chemical shifts227

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 243 residues - 25185.242 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   GLUPHEMETPHEARGLYSLEUALAALAGLU
3   CYSPHEGLYTHRPHETRPLEUVALPHEGLY
4   GLYCYSGLYSERALAVALLEUALAALAGLY
5   PHEPROGLULEUGLYILEGLYPHEALAGLY
6   VALALALEUALAPHEGLYLEUTHRVALLEU
7   THRMETALAPHEALAVALGLYHISILESER
8   GLYGLYHISPHEASNPROALAVALTHRILE
9   GLYLEUTRPALAGLYGLYARGPHEPROALA
10   LYSGLUVALVALGLYTYRVALILEALAGLN
11   VALVALGLYGLYILEVALALAALAALALEU
12   LEUTYRLEUILEALASERGLYLYSTHRGLY
13   PHEASPALAALAALASERGLYPHEALASER
14   ASNGLYTYRGLYGLUHISSERPROGLYGLY
15   TYRSERMETLEUSERALALEUVALVALGLU
16   LEUVALLEUSERALAGLYPHELEULEUVAL
17   ILEHISGLYALATHRASPLYSPHEALAPRO
18   ALAGLYPHEALAPROILEALAILEGLYLEU
19   ALALEUTHRLEUILEHISLEUILESERILE
20   PROVALTHRASNTHRSERVALASNPROALA
21   ARGSERTHRALAVALALAILEPHEGLNGLY
22   GLYTRPALALEUGLUGLNLEUTRPPHEPHE
23   TRPVALVALPROILEVALGLYGLYILEILE
24   GLYGLYLEUILETYRARGTHRLEULEUGLU
25   LYSARGASP

Samples:

13C_15N_sample: aquaporin Z, [U-13C; U-15N], 29.4 ± 2.4 % w/w; 5 mM Tris-Cl pH 8.0 100%

sample_conditions_1: ionic strength: 1 M; pH: 8.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 1 M; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D NCA13C_15N_sampleisotropicsample_conditions_1
2D DARR13C_15N_sampleisotropicsample_conditions_1
3D NCACX13C_15N_sampleisotropicsample_conditions_1
3D NCOCX13C_15N_sampleisotropicsample_conditions_1
3D CONCA13C_15N_sampleisotropicsample_conditions_1
2D 100ms CORD13C_15N_sampleisotropicsample_conditions_2
2D 500ms CORD13C_15N_sampleisotropicsample_conditions_2

Software:

NMRFAM-SPARKY v2.6, T. D. Goddard and D. G. Kneller - chemical shift assignment

X-PLOR NIH v2.47, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

TopSpin v3.6, Bruker Biospin - collection

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker AVANCE III 800 MHz