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1H, 13C and 15N Chemical Shift Assignments of the Colicin E9 Immunity Protein from Escherichia coli
Authors
Boetzel, R., Czisch, M., MacDonald, C.J., Kaptein, R., Hemmings, A.M., James, R., Kleanthous, C., Moore, G.R.
Assembly
Im9 immunity protein
Entity
1. Im9 immunity protein (polymer), 86 monomers, 9582.414 Da Detail

MELKHSISDY TEAEFLQLVT TICNADTSSE EELVKLVTHF EEMTEHPSGS DLIYYPKEGD DDSPSGIVNT VKQWRAANGK SGFKQG


Formula weight
9582.414 Da
Source organism
Escherichia coli
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 97.7 %, Completeness: 77.8 %, Completeness (bb): 79.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All77.8 % (757 of 973)86.3 % (433 of 502)62.9 % (239 of 380)93.4 % (85 of 91)
Backbone79.2 % (399 of 504)95.3 % (161 of 169)62.7 % (158 of 252)96.4 % (80 of 83)
Sidechain79.1 % (434 of 549)81.7 % (272 of 333)75.5 % (157 of 208)62.5 % (5 of 8)
Aromatic30.8 % (24 of 78)61.5 % (24 of 39) 0.0 % (0 of 38) 0.0 % (0 of 1)
Methyl100.0 % (82 of 82)100.0 % (41 of 41)100.0 % (41 of 41)

1. Im9 immunity protein

MELKHSISDY TEAEFLQLVT TICNADTSSE EELVKLVTHF EEMTEHPSGS DLIYYPKEGD DDSPSGIVNT VKQWRAANGK SGFKQG

Sample

Temperature 298 K, pH 6.2


#NameIsotope labelingTypeConcentration
1Im9 immunity protein[U-100%15N; U-100%13C]4.0 mM
2H2O90 %
3D2O10 %

LACS Plot; CA
Referencing offset: 1.81 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: 1.81 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.01 ppm, Outliers: 1 Detail
Release date
1999-02-23
Citation
Assignment of 1H, 13C and 15N signals of the inhibitor protein Im9 bound to the DNase domain of colicin E9
Boetzel, R., Czisch, M., MacDonald, C.J., Kaptein, R., Hemmings, A.M., James, R., Kleanthous, C., Moore, G.R.
J. Biomol. NMR (1998), 12, 567-568, PubMed 9917143 , DOI: ,
Related entities 1. Im9 immunity protein, : 1 : 11 : 2 : 5 : 31 entities Detail
Interaction partners 1. Im9 immunity protein, : 2 interactors Detail
Experiments performed 1 experiments Detail
Keywords colicin, immunity protein, NMR, nuclear magnetic resonance, protein, protein-protein interaction, resonance assignments, secondary structure