BMRB Entry 5577

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5577
MolProbity Validation Chart

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Title:
Sodium/potassium-transporting ATPase alpha-1 chain
Deposition date:
2002-11-06
Original release date:
2003-08-01
Authors:
Hilge, M.; Siegal, G.; Vuister, G.; Guentert, P.; Gloor, S.; Abrahams, J.
Citation:

Citation: Hilge, M.; Siegal, G.; Vuister, G.; Guntert, P.; Gloor, S.; Abrahams, J.. "ATP-induced Conformational Changes of the Nucleotide-binding Domain of Na, K-ATPase"  Nat. Struct. Biol. 10, 468-474 (2003).
PubMed: 12730684

Assembly members:

Assembly members:
SODIUM/POTASSIUM-TRANSPORTING ATPASE ALPHA-1, polymer, 213 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET23b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SODIUM/POTASSIUM-TRANSPORTING ATPASE ALPHA-1: QNPMTVAHMWFDNQIHEADT TENQSGVSFDKTSATWFALS RIAGLCNRAVFQANQENLPI LKRAVAGDASESALLKCIEV CCGSVMEMREKYTKIVEIPF NSTNKYQLSIHKNPNASEPK HLLVMKGAPERILDRCSSIL LHGKEQPLDEELKDAFQNAY LELGGLGERVLGFCHLLLPD EQFPEGFQFDTDEVNFPVDN LCFVGLISMIDPP

Data sets:
Data typeCount
1H chemical shifts1313
13C chemical shifts659
15N chemical shifts187

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Sodium/Potassium-Transporting ATPase alpha-11

Entities:

Entity 1, Sodium/Potassium-Transporting ATPase alpha-1 213 residues - Formula weight is not available

1   GLNASNPROMETTHRVALALAHISMETTRP
2   PHEASPASNGLNILEHISGLUALAASPTHR
3   THRGLUASNGLNSERGLYVALSERPHEASP
4   LYSTHRSERALATHRTRPPHEALALEUSER
5   ARGILEALAGLYLEUCYSASNARGALAVAL
6   PHEGLNALAASNGLNGLUASNLEUPROILE
7   LEULYSARGALAVALALAGLYASPALASER
8   GLUSERALALEULEULYSCYSILEGLUVAL
9   CYSCYSGLYSERVALMETGLUMETARGGLU
10   LYSTYRTHRLYSILEVALGLUILEPROPHE
11   ASNSERTHRASNLYSTYRGLNLEUSERILE
12   HISLYSASNPROASNALASERGLUPROLYS
13   HISLEULEUVALMETLYSGLYALAPROGLU
14   ARGILELEUASPARGCYSSERSERILELEU
15   LEUHISGLYLYSGLUGLNPROLEUASPGLU
16   GLULEULYSASPALAPHEGLNASNALATYR
17   LEUGLULEUGLYGLYLEUGLYGLUARGVAL
18   LEUGLYPHECYSHISLEULEULEUPROASP
19   GLUGLNPHEPROGLUGLYPHEGLNPHEASP
20   THRASPGLUVALASNPHEPROVALASPASN
21   LEUCYSPHEVALGLYLEUILESERMETILE
22   ASPPROPRO

Samples:

sample_1: SODIUM/POTASSIUM-TRANSPORTING ATPASE ALPHA-1, [U-13C; U-15N], 2 mM; Tris-HCl 20 mM; NaN3 0.02%; H2O 95%; D2O 5%

sample_cond_1: pH: 8.6; temperature: 296 K; ionic strength: 20 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available

Software:

NMRPipe v1.0 - processing

XEASY v1.3.11 - data analysis

CYANA v1.0.5 - structure solution

OPALp v1.0 - refinement

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 5576
PDB
DBJ BAE29635 BAE34957
EMBL CAA29306
GB AAA40775 AAA41670 AAA41671 AAH10319 AAH21496
PRF 1309271A
REF NP_036636 NP_659149 XP_005076578 XP_005076579 XP_005357163
SP P06685 Q8VDN2
AlphaFold P06685 Q8VDN2

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