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BMRB: 4802

3NR7

1H, 13C, and 15N sequential assignment of the triple labelled N-terminal domain of the Histone like Nucleoid Structuring protein (H-NS) from Salmonella typhimurium (first 64 residues of the protein)

Authors

Renzoni, D., Esposito, D., Pfuhl, M., Higgins, C.F., Driscoll, P.C., Ladbury, J.E.

Assembly

N-terminal domain of H-NS

Entity

1. N-terminal domain of H-NS (polymer, Thiol state: not present), 64 monomers, 7545.432 × 3 Da Detail

SEALKILNNI RTLRAQARES TLETLEEMLE KLEVVVNERR EEESAAAAEV EERTRKLQQY REML

Total weight

22636.297 Da

Max. entity weight

7545.432 Da

Source organism

Salmonella enterica subsp. enterica serovar Typhimurium

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 49.1 %, Completeness (bb): 92.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	49.1 % (373 of 760)	34.3 % (138 of 402)	60.1 % (173 of 288)	88.6 % (62 of 70)
Backbone	92.4 % (355 of 384)	96.9 % (124 of 128)	88.0 % (169 of 192)	96.9 % (62 of 64)
Sidechain	15.7 % (69 of 440)	5.8 % (16 of 274)	33.1 % (53 of 160)	0.0 % (0 of 6)
Aromatic	0.0 % (0 of 8)	0.0 % (0 of 4)	0.0 % (0 of 4)
Methyl	17.1 % (14 of 82)	14.6 % (6 of 41)	19.5 % (8 of 41)

1. Oligomerisation domain of the 'histone' like nucleoid structuring protein

SEALKILNNI RTLRAQARES TLETLEEMLE KLEVVVNERR EEESAAAAEV EERTRKLQQY REML

Show sample condition

Sample

Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

Release date

2001-01-22

Citation 1

Structural Insight to the Oligomerisation of the Bacterial Chromatin-Structuring Protein H-N
Renzoni, D., Esposito, D., Pfuhl, M., Higgins, C.F., Driscoll, P.C., Ladbury, J.E.

Show more 2 citaions

Citation 2

Oligomerization of the chromatin-structuring protein H-NS
Smyth, C.P., Lundback, T., Renzoni, D., Siligardi, G., Beavil, R., Layton, M., Sidebotham, J.M., Hinton, J.C., Driscoll, P.C., Higgins, C.F., Ladbury, J.E.
Mol. Microbiol. (2000), 36, 962-972, PubMed 10844682 , DOI: , Abstract

Citation 3

NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , Abstract

Hide non-primary 2 citaions

Related entities 1. N-terminal domain of H-NS, : 1 : 5 : 18 entities Detail

Interaction partners 1. N-terminal domain of H-NS, : 3 interactors Detail

More details for 3 interactors identified by 1 citations

Experiments performed 17 experiments Detail

1 1H-1H NOESY

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

2 1H-1H TOCSY

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

3 1H-15N HSQC

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

4 15N NOESY-HSQC

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

5 15N TOCSY-HSQC

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

6 15N-15N HSQC-NOESY-HSQC

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

7 HNHA

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

8 13C NOESY-HSQC

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

9 13C HCCH-TOCSY

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

10 HNCA

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

11 HNCO

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

12 HNCOCA

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

13 HNCACO

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

14 HNCACB

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

15 HNCOCACB

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

16 HCCH 13C-13C NOE

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

17 The triple resonance experiments were recorded on triple labelled samples (2H/15N/13C).

Instrument

Varian UNITYplus - 500 MHz

Sample

State isotropic, Temperature 298 (±0.4) K, pH 7.0 (±0)

#	Name	Isotope labeling	Type	Concentration
1	Oligomerisation domain of the 'histone' like nucleoid structuring protein	[U-13C; U-15N; U-2H]		1.5 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4802_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	OK

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr4802_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set1	OK	353		100.0 (chain: 1, length: 64)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 64, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 123
  - ¹³C chemical shifts: 168
  - ¹⁵N chemical shifts: 62
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Keywords nuclear magnetic resonance, secondary structure, coiled-coil, general topology