BMRBj - BMREntryMaster

Found 1 Document (1.264 seconds)

BMRB: 6051

3HCH

1H, 13C and 15N resonance assignments for methionine sulfoxide reductase B from Neisseria gonorroeae

Authors

Thureau, A., Olry, A., Coudevylle, N., Azza, S., Boshi-Muller, S., Branlant, G., Cung, M.

Assembly

methionine sulfoxide reductase B

Entity

1. methionine sulfoxide reductase B (polymer, Thiol state: all free), 146 monomers, 16373.96 Da Detail

TYKKPSDAEL KRTLTEEQYQ VTQNSATEYA FSHEYDHLFK PGIYVDVVSG EPLFSSADKY DSGCGWPSFT RPIDAKSVTE HDDFSYNMRR TEVRSHAADS HLGHVFPDGP RDKGGLRYCI NGASLKFIPL EQMDAAGYGA LKSKVK

Formula weight

16373.96 Da

Source organism

Neisseria meningitidis

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.9 %, Completeness: 72.2 %, Completeness (bb): 89.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	72.2 % (1208 of 1673)	70.5 % (613 of 869)	71.0 % (467 of 658)	87.7 % (128 of 146)
Backbone	89.9 % (773 of 860)	85.8 % (253 of 295)	92.7 % (396 of 427)	89.9 % (124 of 138)
Sidechain	58.8 % (557 of 948)	62.7 % (360 of 574)	52.7 % (193 of 366)	50.0 % (4 of 8)
Aromatic	0.0 % (0 of 178)	0.0 % (0 of 89)	0.0 % (0 of 88)	0.0 % (0 of 1)
Methyl	77.0 % (94 of 122)	86.9 % (53 of 61)	67.2 % (41 of 61)

1. methionine sulfoxide reductase B

TYKKPSDAEL KRTLTEEQYQ VTQNSATEYA FSHEYDHLFK PGIYVDVVSG EPLFSSADKY DSGCGWPSFT RPIDAKSVTE HDDFSYNMRR TEVRSHAADS HLGHVFPDGP RDKGGLRYCI NGASLKFIPL EQMDAAGYGA LKSKVK

Show sample condition

Sample

Temperature 298 (±0) K, pH 7.1 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	methionine sulfoxide reductase B	[U-13C; U-15N]		2 mM

LACS Plot; CA

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

Referencing offset: -0.62 ppm, Outliers: 2 Detail

LACS Plot; CB

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

Referencing offset: -0.62 ppm, Outliers: 2 Detail

LACS Plot; HA

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

Referencing offset: 0.07 ppm, Outliers: 4 Detail

LACS Plot; CO

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

Referencing offset: 0.78 ppm, Outliers: 3 Detail

Release date

2004-11-28

Citation 1

Letter to the Editor: 1H, 13C and 15N resonance assignments of the methionine sulfoxide reductase B from Neisseria meningitidis
Thureau, A., Olry, A., Coudevylle, N., Azza, S., Boschi-Muller, S., Branlant, G., Cung, M.
J. Biomol. NMR (2004), 30, 223-224, DOI 10.1023/b:jnmr.0000048851.95591.80

Show more 9 citaions

Citation 2

Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis
Antoine, M., Boschi-Muller, S., Branlant, G.
J. Biol. Chem. (2003), 278, 45352-45357, PubMed 12954610 , DOI 10.1074/jbc.M307471200 , Abstract

Citation 3

A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli
Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Van Dorsselear, A., Branlant, G.
J. Biol. Chem. (2000), 275, 35908-35913, PubMed 10964927 , DOI 10.1074/jbc.M006137200 , Abstract

Citation 4

Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., Bax, A.
J. Biomol. NMR (1999), 13, 289-302, PubMed 10212987 , Abstract

Citation 5

Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase
Grimaud, R., Ezraty, B., Mitchell, J.K., Lafitte, D., Briand, C., Derrick, P.J., Barras, F.
J. Biol. Chem. (2001), 276, 48915-48920, PubMed 11677230 , DOI 10.1074/jbc.M105509200 , Abstract

Citation 6

The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB
Lowther, W.T., Weissbach, H., Etienne, F., Brot, N., Matthews, B.W.
Nat. Struct. Biol. (2002), 9, 348-352, PubMed 11938352 , DOI 10.1038/nsb783 , Abstract

Citation 7

Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
Moskovitz, J., Poston, J.M., Berlett, B.S., Nosworthy, N.J., Szczepanowski, R., Stadtman, E.R.
J. Biol. Chem. (2000), 275, 14167-14172, PubMed 10799493 , DOI: , Abstract

Citation 8

Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis
Olry, A., Boschi-Muller, S., Marraud, M., Sanglier-Cianferani, S., Van Dorsselear, A., Branlant, G.
J. Biol. Chem. (2002), 277, 12016-12022, PubMed 11812798 , DOI 10.1074/jbc.M112350200 , Abstract

Citation 9

Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase
Sharov, V.S., Ferrington, D.A., Squier, T.C., Schneich, C.
FEBS Lett. (1999), 455, 247-250, PubMed 10437782 , DOI: , Abstract

Citation 10

1H, 13C and 15N resonance assignments for methionine sulfoxide reductase B from Bacillus subtilis
Zheng, D., Cort, J.R., Chiang, Y., Acton, T., Kennedy, M.A., Montelione, G.T.
J. Biomol. NMR (2003), 27, 183-184, PubMed 12913416 , Abstract

Hide non-primary 9 citaions

Related entities 1. methionine sulfoxide reductase B, : 1 : 1 : 2 : 157 entities Detail

Experiments performed 9 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6051_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: bmr6051_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1296		95.9 (chain: 1, length: 146)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 146, Sequence coverage: 95.9%
- Total number of assignments
  - ¹³C chemical shifts: 465
  - ¹H chemical shifts: 704
  - ¹⁵N chemical shifts: 127
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- 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	658	465	70.7
¹H chemical shifts	869	600	69.0
¹⁵N chemical shifts	153	127	83.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	292	275	94.2
¹H chemical shifts	295	252	85.4
¹⁵N chemical shifts	138	123	89.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	366	190	51.9
¹H chemical shifts	574	348	60.6
¹⁵N chemical shifts	15	4	26.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	63	40	63.5
¹H chemical shifts	63	52	82.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	88	0	0.0
¹H chemical shifts	89	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords methionine sulfoxyde reductase B, NMR assignment, Neisseria meningitidis

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (1.264 seconds)

BMRB: 6051

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. methionine sulfoxide reductase B, : 1 : 1 : 2 : 157 entities Detail

Experiments performed 9 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail