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Backbone and sidechain 1H, 13C, and 15N chemical shifts for Sda
Authors
Rowland, S.L., Maciejewski, M.W., King, G.F.
Assembly
Sda
Entity
1. Sda (polymer, Thiol state: not present), 46 monomers, 5440.214 Da Detail

MRKLSDELLI ESYFKATEMN LNRDFIELIE NEIKRRSLGH IISVSS


Formula weight
5440.214 Da
Source organism
Bacillus subtilis
Exptl. method
NMR
Refine. method
torsion angle dynamics followed by simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 95.6 %, Completeness (bb): 98.6 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All95.6 % (540 of 565)99.0 % (294 of 297)90.4 % (198 of 219)98.0 % (48 of 49)
Backbone98.6 % (272 of 276)98.9 % (92 of 93)98.5 % (135 of 137)97.8 % (45 of 46)
Sidechain93.7 % (313 of 334)99.0 % (202 of 204)85.0 % (108 of 127)100.0 % (3 of 3)
Aromatic50.0 % (16 of 32)100.0 % (16 of 16) 0.0 % (0 of 16)
Methyl100.0 % (56 of 56)100.0 % (28 of 28)100.0 % (28 of 28)

1. Sda

MRKLSDELLI ESYFKATEMN LNRDFIELIE NEIKRRSLGH IISVSS

Sample

Temperature 298 (±0.5) K, pH 6.85 (±0.1)


#NameIsotope labelingTypeConcentration
1Sda[U-13C; U-15N]1.0 mM

Protein Blocks Logo
Calculated from 25 models in PDB: 1PV0, Strand ID: A Detail


Release date
2003-09-15
Citation
Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis
Rowland, S.L., Burkholder, W.F., Cunningham, K.A., Maciejewski, M.W., Grossman, A.D., King, G.F.
Mol. Cell (2004), 13, 689-701, PubMed 15023339 , DOI 10.1016/s1097-2765(04)00084-x ,
Related entities 1. Sda, : 1 : 1 : 1 : 15 entities Detail
Interaction partners 1. Sda, : 1 interactors Detail
Experiments performed 13 experiments Detail
nullKeywords Sda, KinA, antikinase, histidine kinase, sporulation phosphorelay