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BMRB: 6030


6030
2A29
1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli
Authors
Haupt, M., Coles, M., Truffault, V., Bramkamp, M., Altendorf, K., Kessler, H.
Assembly
Type IA potassium translocating ATPase B chain
Entity
1. potassium transporting ATPase (polymer, Thiol state: not present), 156 monomers, 17134.01 Da Detail

MGHHHHHHHH HHSSGHGGRH NRQASEFIPA QGVDEKTLAD AAQLASLADE TPEGRSIVIL AKQRFNLRER DVQSLHATFV PFTAQSRMSG INIDNRMIRK GSVDAIRRHV EANGGHFPTD VDQKVDQVAR QGATPLVVVE GSRVLGVIAL KDIVKG


2. ANP (non-polymer), 506.196 Da
Total weight
17640.205 Da
Max. entity weight
17134.01 Da
Source organism
Escherichia coli
Exptl. method
NMR
Refine. method
SIMULATED ANNEALING
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 89.7 %, Completeness: 76.5 %, Completeness (bb): 75.7 % Detail
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Polymer type: polypeptide(L)

Total1H13C15N
All76.5 % (1335 of 1744)82.5 % (746 of 904)66.1 % (446 of 675)86.7 % (143 of 165)
Backbone75.7 % (701 of 926)85.7 % (275 of 321)64.5 % (293 of 454)88.1 % (133 of 151)
Sidechain79.5 % (763 of 960)80.8 % (471 of 583)77.7 % (282 of 363)71.4 % (10 of 14)
Aromatic19.1 % (21 of 110)38.2 % (21 of 55) 0.0 % (0 of 55)
Methyl93.1 % (162 of 174)93.1 % (81 of 87)93.1 % (81 of 87)

1. potassium transporting ATPase

MGHHHHHHHH HHSSGHGGRH NRQASEFIPA QGVDEKTLAD AAQLASLADE TPEGRSIVIL AKQRFNLRER DVQSLHATFV PFTAQSRMSG INIDNRMIRK GSVDAIRRHV EANGGHFPTD VDQKVDQVAR QGATPLVVVE GSRVLGVIAL KDIVKG

Show sample condition
Sample

Temperature 300 (±0.1) K, pH 6.0 (±0.1)


#NameIsotope labelingTypeConcentration
1Type IA potassium translocating ATPase B chain[U-13C; U-15N]1.0 mM
2PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER0.5 ~ 15.0 mM

LACS Plot; CA
Referencing offset: 0.25 ppm, Outliers: 3 Detail
LACS Plot; CB
Referencing offset: 0.25 ppm, Outliers: 3 Detail
LACS Plot; HA
Referencing offset: -0.02 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 1 models in PDB: 2A29, Strand ID: A Detail

Release date
2004-07-05
Citation
1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli
Haupt, M., Coles, M., Truffault, V., Bramkamp, M., Altendorf, K., Kessler, H.
J. Biomol. NMR (2004), 29, 437-438, PubMed 15213457 , DOI 10.1023/B:JNMR.0000032512.08757.8b ,
Entries sharing articles BMRB: 1 entries Detail
  BMRB: 6029 released on 2004-07-05
    Title 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli
Related entities 1. potassium transporting ATPase, : 1 : 3 : 11 : 86 entities Detail
More details for 101 related entities
Interaction partners 1. potassium transporting ATPase, : 8 interactors Detail
More details for 8 interactors identified by 2 citations
Experiments performed 2 experiments Detail
nullKeywords ATP binding, KdpB, NMR assignment, nucleotide binding domain, P-type ATPase