Search

Solution structure of the C-terminal domain of the FliK
Authors
Mizuno, S., Tate, S., Kobayashi, N., Amida, H.
Assembly
Flagellar hook-length control protein
Entity
1. Flagellar hook-length control protein (polymer, Thiol state: not present), 169 monomers, 17758.64 Da Detail

HMASDDRATG PALTPLVVAA AATSAKVEVD SPPAPVTHGA AMPTLSSATA QPLPVASAPV LSAPLGSHEW QQTFSQQVML FTRQGQQSAQ LRLHPEELGQ VHISLKLDDN QAQLQMVSPH SHVRAALEAA LPMLRTQLAE SGIQLGQSSI SSESFAGQQQ SSSQQQSSR


Formula weight
17758.64 Da
Source organism
Salmonella enterica subsp. enterica serovar Typhimurium
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.8 %, Completeness: 94.2 %, Completeness (bb): 96.9 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All94.2 % (1737 of 1843)93.8 % (894 of 953)95.6 % (679 of 710)91.1 % (164 of 180)
Backbone96.9 % (957 of 988)96.7 % (322 of 333)97.6 % (487 of 499)94.9 % (148 of 156)
Sidechain92.4 % (939 of 1016)92.3 % (572 of 620)94.4 % (351 of 372)66.7 % (16 of 24)
Aromatic74.3 % (52 of 70)80.0 % (28 of 35)67.6 % (23 of 34)100.0 % (1 of 1)
Methyl99.5 % (193 of 194)100.0 % (97 of 97)99.0 % (96 of 97)

1. UNP residues 204-370

HMASDDRATG PALTPLVVAA AATSAKVEVD SPPAPVTHGA AMPTLSSATA QPLPVASAPV LSAPLGSHEW QQTFSQQVML FTRQGQQSAQ LRLHPEELGQ VHISLKLDDN QAQLQMVSPH SHVRAALEAA LPMLRTQLAE SGIQLGQSSI SSESFAGQQQ SSSQQQSSR

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.4


#NameIsotope labelingTypeConcentration
1UNP residues 204-370[U-13C; U-15N]protein1 mM
2sodium phosphatenatural abundancebuffer50 mM
3EDTAnatural abundancebuffer1 mM
4H2Osolvent90 %
5D2Osolvent10 %
Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 303 K, pH 6.4


#NameIsotope labelingTypeConcentration
6UNP residues 204-370[U-13C; U-15N]protein1 mM
7sodium phosphatenatural abundancebuffer50 mM
8EDTAnatural abundancebuffer1 mM
9D2Osolvent100 %
Sample #3

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.4


#NameIsotope labelingTypeConcentration
10UNP residues 204-370[U-15N]protein1 mM
11sodium phosphatenatural abundancebuffer50 mM
12EDTAnatural abundancebuffer1 mM
13H2Osolvent90 %
14D2Osolvent10 %
Sample #4

Solvent system 100% D2O, Pressure 1 atm, Temperature 303 K, pH 6.4


#NameIsotope labelingTypeConcentration
15UNP residues 204-370[U-15N]protein0.5 mM
16sodium phosphatenatural abundancebuffer50 mM
17EDTAnatural abundancebuffer1 mM
18D2Osolvent100 %

LACS Plot; CA
Referencing offset: -0.09 ppm, Outliers: 2 Detail
LACS Plot; CB
Referencing offset: -0.09 ppm, Outliers: 2 Detail
LACS Plot; HA
Referencing offset: -0.02 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: 0.21 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 15 models in PDB: 2RRL, Strand ID: A Detail


Release date
2011-06-21
Citation
The NMR structure of FliK, the trigger for the switch of substrate specificity in the flagellar type III secretion apparatus
Mizuno, S., Amida, H., Kobayashi, N., Aizawa, S., Tate, S.
J. Mol. Biol. (2011), 409, 558-573, PubMed 21510958 , DOI 10.1016/j.jmb.2011.04.008 ,
Related entities 1. Flagellar hook-length control protein, : 1 : 1 : 10 entities Detail
Interaction partners 1. Flagellar hook-length control protein, : 1 interactors Detail
Experiments performed 27 experiments Detail
nullKeywords bacterial flagella motor, FlhB, FliK, hook-length control, NMR, protein transport