BMRBj - BMREntryMaster

Found 1 Document (1.289 seconds)

BMRB: 3440

1CYE

1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein

Authors

Bruix, M., Pascual, J., Santoro, J., Serrano, L., Rico, M.

Assembly

che Y protein

Entity

1. che Y protein (polymer), 129 monomers, 14138.19 Da Detail

RSDKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG YGFVISDWNM PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL NKIFEKLGM

Formula weight

14138.19 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 91.4 %, Completeness (bb): 97.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	91.4 % (831 of 909)	90.5 % (699 of 772)	96.4 % (132 of 137)
Backbone	97.7 % (382 of 391)	98.1 % (260 of 265)	96.8 % (122 of 126)
Sidechain	86.7 % (449 of 518)	86.6 % (439 of 507)	90.9 % (10 of 11)
Aromatic	100.0 % (45 of 45)	100.0 % (44 of 44)	100.0 % (1 of 1)
Methyl	100.0 % (82 of 82)	100.0 % (82 of 82)

1. che Y protein

RSDKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG YGFVISDWNM PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL NKIFEKLGM

Show sample condition

Sample

Temperature 308 K, pH 7

Release date

1995-07-30

Citation

1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein
Bruix, M., Pascual, J., Santoro, J., Serrano, L., Rico, M.
Eur. J. Biochem. (1993), 215, 573-585, PubMed , DOI:

Related entities 1. che Y protein, : 1 : 8 : 288 entities Detail

Interaction partners 1. che Y protein, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr3440_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: bmr3440_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_data_set_one	Warning	995		100.0 (chain: 1, length: 129)

Assigned chemical shifts

Saveframe: chemical_shift_assignment_data_set_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 129, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 865
  - ¹⁵N chemical shifts: 130
- 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 (%)
¹H chemical shifts	772	688	89.1
¹⁵N chemical shifts	142	130	91.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	265	259	97.7
¹⁵N chemical shifts	126	119	94.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	507	429	84.6
¹⁵N chemical shifts	16	11	68.8

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Found 1 Document (1.289 seconds)

BMRB: 3440

Sample

Related entities 1. che Y protein, : 1 : 8 : 288 entities Detail

Interaction partners 1. che Y protein, : 1 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail