BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26805

Title: 13C,15N chemical shifts of human Aquaporin-1   PubMed: 27583975

Authors: Wang, Shenlin; Ing, Christopher; Emami, Sanaz; Jiang, Yunjiang; Liang, Hongjun; Pomes, Regis; Brown, Leonid; Ladizhansky, vladimir

Citation: Wang, Shenlin; Ing, Christopher; Emami, Sanaz; Jiang, Yunjiang; Liang, Hongjun; Pomes, Regis; Brown, Leonid; Ladizhansky, Vladimir. "Structure and Dynamics of Extracellular Loops in Human Aquaporin-1 from Solid-State NMR and Molecular Dynamics"  J Phys Chem B. 120, 9887-9902 (2016).

Assembly members:
human_aquaporin_1, polymer, 292 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris

Entity Sequences (FASTA):
human_aquaporin_1: masefkkklfwravvaefla ttlfvfisigsalgfkypvg nnqtavqdnvkvslafglsi atlaqsvghisgahlnpavt lglllscqisifralmyiia qcvgaivatailsgitsslt gnslgrndladgvnsgqglg ieiigtlqlvlcvlattdrr rrdlggsaplaiglsvalgh llaidytgcginparsfgsa vithnfsnhwifwvgpfigg alavliydfilaprssdltd rvkvwtsgqveeydldaddi nsrvemkpkaleqkliseed lnsavdhhhhhh

Data sets:
Data typeCount
13C chemical shifts744
15N chemical shifts207

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1human aquaporin 11

Entities:

Entity 1, human aquaporin 1 292 residues - Formula weight is not available

1   METALASERGLUPHELYSLYSLYSLEUPHE
2   TRPARGALAVALVALALAGLUPHELEUALA
3   THRTHRLEUPHEVALPHEILESERILEGLY
4   SERALALEUGLYPHELYSTYRPROVALGLY
5   ASNASNGLNTHRALAVALGLNASPASNVAL
6   LYSVALSERLEUALAPHEGLYLEUSERILE
7   ALATHRLEUALAGLNSERVALGLYHISILE
8   SERGLYALAHISLEUASNPROALAVALTHR
9   LEUGLYLEULEULEUSERCYSGLNILESER
10   ILEPHEARGALALEUMETTYRILEILEALA
11   GLNCYSVALGLYALAILEVALALATHRALA
12   ILELEUSERGLYILETHRSERSERLEUTHR
13   GLYASNSERLEUGLYARGASNASPLEUALA
14   ASPGLYVALASNSERGLYGLNGLYLEUGLY
15   ILEGLUILEILEGLYTHRLEUGLNLEUVAL
16   LEUCYSVALLEUALATHRTHRASPARGARG
17   ARGARGASPLEUGLYGLYSERALAPROLEU
18   ALAILEGLYLEUSERVALALALEUGLYHIS
19   LEULEUALAILEASPTYRTHRGLYCYSGLY
20   ILEASNPROALAARGSERPHEGLYSERALA
21   VALILETHRHISASNPHESERASNHISTRP
22   ILEPHETRPVALGLYPROPHEILEGLYGLY
23   ALALEUALAVALLEUILETYRASPPHEILE
24   LEUALAPROARGSERSERASPLEUTHRASP
25   ARGVALLYSVALTRPTHRSERGLYGLNVAL
26   GLUGLUTYRASPLEUASPALAASPASPILE
27   ASNSERARGVALGLUMETLYSPROLYSALA
28   LEUGLUGLNLYSLEUILESERGLUGLUASP
29   LEUASNSERALAVALASPHISHISHISHIS
30   HISHIS

Samples:

sample_1: human aquaporin 1, [U-100% 13C; U-100% 15N], 1:1 % w/w; Egg PC/Brain PS 1:1 % w/w; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
3D NCACXsample_1isotropicsample_conditions_1
3D NCOCXsample_1isotropicsample_conditions_1
3D CANCOsample_1isotropicsample_conditions_1
2D NCAsample_1isotropicsample_conditions_1
2D NCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection

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

CARA, Keller and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance III 800 MHz

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