BMRB: 5847

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

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	95.6 % (540 of 565)	99.0 % (294 of 297)	90.4 % (198 of 219)	98.0 % (48 of 49)
Backbone	98.6 % (272 of 276)	98.9 % (92 of 93)	98.5 % (135 of 137)	97.8 % (45 of 46)
Sidechain	93.7 % (313 of 334)	99.0 % (202 of 204)	85.0 % (108 of 127)	100.0 % (3 of 3)
Aromatic	50.0 % (16 of 32)	100.0 % (16 of 16)	0.0 % (0 of 16)
Methyl	100.0 % (56 of 56)	100.0 % (28 of 28)	100.0 % (28 of 28)

1. Sda

MRKLSDELLI ESYFKATEMN LNRDFIELIE NEIKRRSLGH IISVSS

Show sample condition

Sample

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

#	Name	Isotope labeling	Type	Concentration
1	Sda	[U-13C; U-15N]		1.0 mM

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

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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 , Abstract

Entries sharing articles Swiss-Prot: 1 entries Detail

Related entities 1. Sda, : 1 : 1 : 1 : 15 entities Detail

Interaction partners 1. Sda, : 1 interactors Detail

Experiments performed 13 experiments Detail