BMRBj - BMREntryMaster

Found 1 Document (1.289 seconds)

BMRB: 2371

1POH

Three-Dimensional 15N-1H-1H and 15N-13C-1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli

Authors

van Nuland, N.A.J., van Dijk, A.A., Dijkstra, K., van Hoesel, F.H.J., Scheek, R.M., Robillard, G.T.

Assembly

phosphocarrier protein HPr

Entity

1. phosphocarrier protein HPr (polymer), 85 monomers, 9119.249 Da Detail

MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL QTLGLTQGTV VTISAEGEDE QKAVEHLVKL MAELE

Formula weight

9119.249 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 39.8 %, Completeness (bb): 69.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	39.8 % (382 of 961)	39.7 % (196 of 494)	27.7 % (104 of 376)	90.1 % (82 of 91)
Backbone	69.2 % (350 of 506)	99.4 % (173 of 174)	38.2 % (95 of 249)	98.8 % (82 of 83)
Sidechain	6.9 % (37 of 534)	7.2 % (23 of 320)	6.8 % (14 of 206)	0.0 % (0 of 8)
Aromatic	0.0 % (0 of 48)	0.0 % (0 of 24)	0.0 % (0 of 24)
Methyl	8.2 % (9 of 110)	7.3 % (4 of 55)	9.1 % (5 of 55)

1. phosphocarrier protein HPr

MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL QTLGLTQGTV VTISAEGEDE QKAVEHLVKL MAELE

Show sample condition

Sample

Temperature 303 K, pH 6.5

Release date

1995-07-30

Citation

Three-dimensional 15N-1H-1H and 15N-13C-1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli. Assignment of backbone resonances
van Nuland, N.A.J., van Dijk, A.A., Dijkstra, K., van Hoesel, F.H.J., Scheek, R.M., Robillard, G.T.
Eur. J. Biochem. (1992), 203, 483-491, PubMed 1735433 , DOI: , Abstract

Related entities 1. phosphocarrier protein HPr, : 1 : 17 : 1 : 4 : 93 entities Detail

Interaction partners 1. phosphocarrier protein HPr, : 10 interactors Detail

More details for 10 interactors identified by 5 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr2371_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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr2371_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_data_set_one	Warning	340		100.0 (chain: 1, length: 85)

Assigned chemical shifts

Saveframe: chemical_shift_assignment_data_set_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 85, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 85
  - ¹H chemical shifts: 173
  - ¹⁵N chemical shifts: 82
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	57	0	0.0
¹H chemical shifts	57	0	0.0

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Found 1 Document (1.289 seconds)

BMRB: 2371

Sample

Related entities 1. phosphocarrier protein HPr, : 1 : 17 : 1 : 4 : 93 entities Detail

Interaction partners 1. phosphocarrier protein HPr, : 10 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	376	85	22.6
¹H chemical shifts	494	173	35.0
¹⁵N chemical shifts	92	82	89.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	170	85	50.0
¹H chemical shifts	174	173	99.4
¹⁵N chemical shifts	83	82	98.8