BMRB: 6495

Backbone 1H, 13C, and 15N Chemical Shift Assignments and relaxation data for Chorismate Mutase from Bacillus subtilis in complex with inhibitor

Authors

Eletsky, A., Kienhofer, A., Hilvert, D., Pervushin, K.

Assembly

BsCM trimer

Entity

1. BsCM (polymer, Thiol state: all free), 127 monomers, 14488.75 × 3 Da Detail

MMIRGIRGAT TVERDTEEEI LQKTKQLLEK IIEENHTKPE DVVQMLLSAT PDLHAVFPAK AVRELSGWQY VPVTCMQEMD VTGGLKKCIR VMMTVQTDVP QDQIRHVYLE KAVVLRPDLS LTKNTEL

2. na (non-polymer), 1 monomers, 228.199 × 3 Da

Total weight

44150.848 Da

Max. entity weight

14488.75 Da

Source organism

Bacillus subtilis

Exptl. method

NMR

Data set

assigned_chemical_shifts, heteronucl_NOEs, heteronucl_T1_relaxation, heteronucl_T2_relaxation

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 43.0 %, Completeness (bb): 80.7 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	43.0 % (646 of 1503)	31.8 % (249 of 784)	47.4 % (278 of 587)	90.2 % (119 of 132)
Backbone	80.7 % (605 of 750)	87.7 % (222 of 253)	70.2 % (264 of 376)	98.3 % (119 of 121)
Sidechain	6.6 % (58 of 875)	5.1 % (27 of 531)	9.3 % (31 of 333)	0.0 % (0 of 11)
Aromatic	0.0 % (0 of 50)	0.0 % (0 of 25)	0.0 % (0 of 24)	0.0 % (0 of 1)
Methyl	14.5 % (25 of 172)	14.0 % (12 of 86)	15.1 % (13 of 86)

1. BsCM

MMIRGIRGAT TVERDTEEEI LQKTKQLLEK IIEENHTKPE DVVQMLLSAT PDLHAVFPAK AVRELSGWQY VPVTCMQEMD VTGGLKKCIR VMMTVQTDVP QDQIRHVYLE KAVVLRPDLS LTKNTEL

Show sample condition

Sample #1

Temperature 293 (±0.1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	BsCM	[U-95% 15N]		0.0 ~ 0.0 mM
2	na			0.0 ~ 0.0 mM

Sample #2

Temperature 293 (±0.1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
3	BsCM	[U-50% 2H; U-95% 13C; U-95% 15N]		0.0 ~ 0.0 mM
4	na			0.0 ~ 0.0 mM

Sample #3

Temperature 293 (±0.1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
5	BsCM	[U-15N]		0.0 ~ 0.0 mM

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Heteronucl. T₁

232 T₁ values in 2 lists
Coherence Sz, Field strength (¹H) 600 MHz, 900 MHz, Temperature 293 (±0.1) K, pH 7.5 (±0.1) Detail

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Temperature 293 (±0.1) K, pH 7.5 (±0.1)

Heteronucl. T₂

230 T₂ values in 2 lists
Coherence S(+,-), Field strength (¹H) 600 MHz, 900 MHz, Temperature 293 (±0.1) K, pH 7.5 (±0.1) Detail

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Temperature 293 (±0.1) K, pH 7.5 (±0.1)

Heteronucl. NOE

115 NOE values in 1 lists
Value type relative intensities, Field strength (¹H) 600 MHz, Temperature 293 (±0.1) K, pH 7.5 (±0.1) Detail

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Temperature 293 (±0.1) K, pH 7.5 (±0.1)

Heteronucl. T₁/T₂

230 T₁/T₂ values in 2 lists
Field strength (¹H) 600 MHz, 900 MHz, Temperature 293 (±0.1) K, pH 7.5 (±0.1) Detail

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Temperature 293 (±0.1) K, pH 7.5 (±0.1)

Release date

2011-08-10

Citation

Investigation of ligand binding and protein dynamics in Bacillus subtilis chorismate mutase by transverse relaxation optimized spectroscopy-nuclear magnetic resonance
Eletsky, A., Kienhofer, A., Hilvert, D., Pervushin, K.
Biochemistry (2005), 44, 6788-6799, PubMed 15865424 , DOI 10.1021/bi0474259 , Abstract

Entries sharing articles BMRB: 2 entries Detail

Related entities 1. BsCM, : 1 : 4 : 2 : 19 entities Detail

Experiments performed 3 experiments Detail

Chemical shift validation 4 contents Detail