BMRB: 5390

1H,13C and 15N Chemical Shifts Assignments for the Oligomerization Domain of H-NS

Authors

Esposito, D., Petrovic, A., Harris, R., Shusuke, O., Eccleston, J., Mbabaali, A., Haq, I., Higgins, C.F., Hinton, J.C.D., Driscoll, P.C., Ladbury, J.E.

Assembly

DNA-binding Protein H-NS

Entity

1. DNA-binding Protein H-NS (polymer, Thiol state: not present), 61 monomers, 7008.812 × 2 Da Detail

GSHMSEALKI LNNIRTLRAQ ARESTLETLE EMLEKLEVVV NERREEESAA AAEVEERTRK L

Total weight

14017.624 Da

Max. entity weight

7008.812 Da

Source organism

Escherichia coli

Exptl. method

NMR

Refine. method

dynamical simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 93.4 %, Completeness: 77.9 %, Completeness (bb): 79.0 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	77.9 % (547 of 702)	78.3 % (289 of 369)	73.5 % (197 of 268)	93.8 % (61 of 65)
Backbone	79.0 % (289 of 366)	92.7 % (114 of 123)	64.8 % (118 of 182)	93.4 % (57 of 61)
Sidechain	79.5 % (315 of 396)	71.1 % (175 of 246)	93.2 % (136 of 146)	100.0 % (4 of 4)
Aromatic	0.0 % (0 of 4)	0.0 % (0 of 2)	0.0 % (0 of 2)
Methyl	100.0 % (78 of 78)	100.0 % (39 of 39)	100.0 % (39 of 39)

1. H-NS

GSHMSEALKI LNNIRTLRAQ ARESTLETLE EMLEKLEVVV NERREEESAA AAEVEERTRK L

Show sample condition

Sample #1

Pressure 1 atm, Temperature 298 (±1) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	H-NS	[U-15N]		1.5 mM
2	NaCl			300 mM
3	potassium phosphate			20 mM
4	EDTA			1 mM

Sample #2

Pressure 1 atm, Temperature 298 (±1) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
5	H-NS	[U-13C; U-15N]		1.5 mM
6	NaCl			300 mM
7	potassium phosphate			20 mM
8	EDTA			1 mM

Sample #3

Pressure 1 atm, Temperature 298 (±1) K, pH 7.0 (±0.1), Details 14N,12C/15N,13C 1:1 mixed labelled chains.

#	Name	Isotope labeling	Type	Concentration
9	H-NS	[U-13C; U-15N]		1.0 mM
10	H-NS			1.0 mM
11	NaCl			300 mM
12	potassium phosphate			20 mM
13	EDTA			1 mM

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LACS Plot; CA

Referencing offset: -0.25 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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LACS Plot; CB

Referencing offset: -0.25 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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LACS Plot; HA

Referencing offset: 0.05 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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Protein Blocks Logo

Calculated from 20 models in PDB: 1LR1, Strand ID: A, B Detail

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Release date

2003-02-24

Citation

H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein
Esposito, D., Petrovic, A., Harris, R., Ono, S., Eccleston, J.F., Mbabaali, A., Haq, I., Higgins, C.F., Hinton, J.C.D., Driscoll, P.C., Ladbury, J.E.
J. Mol. Biol. (2002), 324, 841-850, PubMed 12460581 , DOI 10.1016/s0022-2836(02)01141-5 , Abstract

Related entities 1. DNA-binding Protein H-NS, : 1 : 1 : 4 : 17 entities Detail

Interaction partners 1. DNA-binding Protein H-NS, : 3 interactors Detail

Experiments performed 3 experiments Detail