BMRBj - BMREntryMaster

Found 1 Document (0.636 seconds)

BMRB: 16067

2KC8

Backbone assignment of RelB antitoxin C-terminal peptide (RelBc) in the RelE-free state

Authors

Li, G., Zhang, Y., Inouye, M., Ikura, M.

Assembly

RelBc

Entity

1. RelBc (polymer, Thiol state: not present), 36 monomers, 4128.639 Da Detail

GSHKQTLLSD EDAELVEIVK ERLRNPKPVR VTLDEL

Formula weight

4128.639 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.7 %, Completeness: 31.3 %, Completeness (bb): 60.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	31.3 % (133 of 425)	16.1 % (36 of 224)	40.0 % (66 of 165)	86.1 % (31 of 36)
Backbone	60.8 % (129 of 212)	45.1 % (32 of 71)	61.7 % (66 of 107)	91.2 % (31 of 34)
Sidechain	14.9 % (37 of 248)	2.6 % (4 of 153)	35.5 % (33 of 93)	0.0 % (0 of 2)
Aromatic	0.0 % (0 of 4)	0.0 % (0 of 2)	0.0 % (0 of 2)
Methyl	4.0 % (2 of 50)	4.0 % (1 of 25)	4.0 % (1 of 25)

1. RelBc

GSHKQTLLSD EDAELVEIVK ERLRNPKPVR VTLDEL

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 296.5 (±0.1) K, pH 6.5 (±0.05)

#	Name	Isotope labeling	Concentration
1	RelBc	[U-13C; U-15N]	1 (±0.2) mM
2	sodium phosphate	natural abundance	25 mM
3	sodium chloride	natural abundance	300 mM
4	DTT	natural abundance	1 mM
5	sodium azide	natural abundance	0.5 mM

LACS Plot; CA

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

Referencing offset: 0.02 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.02 ppm, Outliers: 1 Detail

Release date

2009-04-21

Citation

Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site
Li, G., Zhang, Y., Inouye, M., Ikura, M.
J. Biol. Chem. (2009), 284, 14628-14636, PubMed 19297318 , DOI 10.1074/jbc.M809656200 , Abstract

Related entities 1. RelBc, : 1 : 3 : 4 entities Detail

Interaction partners 1. RelBc, : 2 interactors Detail

More details for 2 interactors identified by 2 citations

Experiments performed 3 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr16067_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: bmr16067_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	128		91.7 (chain: 1, length: 36)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 36, Sequence coverage: 91.7%
- Total number of assignments
  - ¹H chemical shifts: 31
  - ¹³C chemical shifts: 66
  - ¹⁵N chemical shifts: 31
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- 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	224	31	13.8
¹³C chemical shifts	165	66	40.0
¹⁵N chemical shifts	39	31	79.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	71	31	43.7
¹³C chemical shifts	72	33	45.8
¹⁵N chemical shifts	34	31	91.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	153	0	0.0
¹³C chemical shifts	93	33	35.5
¹⁵N chemical shifts	5	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	25	0	0.0
¹³C chemical shifts	25	1	4.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	2	0	0.0
¹³C chemical shifts	2	0	0.0

Keywords Antitoxin, RelB

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Found 1 Document (0.636 seconds)

BMRB: 16067

Sample

Chemical shift reference

Chemical shift reference

Related entities 1. RelBc, : 1 : 3 : 4 entities Detail

Interaction partners 1. RelBc, : 2 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail