BMRB: 19255

Backbone amide chemical shifts and relaxation data (T1-T2) for the Y48A mutant of the FimH adhesin carbohydrate-binding domain

Authors

Vanwetswinkel, S., Van Nuland, N.A.

Assembly

FimH Y48A mutant

Entity

1. FimH Y48A mutant (polymer, Thiol state: all disulfide bound), 158 monomers, 16815.64 Da Detail

FACKTANGTA IPIGGGSANV YVNLAPVVNV GQNLVVDLST QIFCHNDAPE TITDYVTLQR GSAYGGVLSN FSGTVKYSGS SYPFPTTSET PRVVYNSRTD KPWPVALYLT PVSSAGGVAI KAGSLIAVLI LRQTNNYNSD DFQFVWNIYA NNDVVVPT

Formula weight

16815.64 Da

Entity Connection

disulfide 1 Detail

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ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS3:SG	1:CYS44:SG

Source organism

Escherichia coli

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, heteronucl_T1_relaxation, heteronucl_T2_relaxation

Chem. Shift Complete

Sequence coverage: 93.7 %, Completeness: 37.9 %, Completeness (bb): 66.8 % Detail

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Polymer type: polypeptide(L)

	Total	1H	15N
All	37.9 % (400 of 1055)	26.3 % (233 of 886)	98.8 % (167 of 169)
Backbone	66.8 % (312 of 467)	51.7 % (165 of 319)	99.3 % (147 of 148)
Sidechain	15.0 % (88 of 588)	12.0 % (68 of 567)	95.2 % (20 of 21)
Aromatic	4.9 % (4 of 82)	2.5 % (2 of 80)	100.0 % (2 of 2)
Methyl	9.7 % (10 of 103)	9.7 % (10 of 103)

1. FIMH Y48A mutant

FACKTANGTA IPIGGGSANV YVNLAPVVNV GQNLVVDLST QIFCHNDAPE TITDYVTLQR GSAYGGVLSN FSGTVKYSGS SYPFPTTSET PRVVYNSRTD KPWPVALYLT PVSSAGGVAI KAGSLIAVLI LRQTNNYNSD DFQFVWNIYA NNDVVVPT

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Sample

Solvent system 93% H2O/7% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.000, Details FimH_Y48A 0.0011 M, sodium phosphate 0.020000 M, sodium chloride 0.100000 M

#	Name	Isotope labeling	Type	Concentration
1	FIMH Y48A mutant	[U-100% 15N]		0.0011 M
2	sodium phosphate	natural abundance		0.02 M
3	sodium chloride	natural abundance		0.1 M
4	H2O	natural abundance		93 %
5	D2O	natural abundance		7 %

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Heteronucl. T₁

132 T₁ values in 1 lists
Coherence Sz, Field strength (¹H) 600 MHz, Pressure 1.000 atm, Temperature 298.000 K, pH 6.000 Detail

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Pressure 1.000 atm, Temperature 298.000 K, pH 6.000

Experiment name 2D 1H-15N HSQC (inverse recovery)

Heteronucl. T₂

132 T₂ values in 1 lists
Coherence S(+,-), Field strength (¹H) 600 MHz, Pressure 1.000 atm, Temperature 298.000 K, pH 6.000 Detail

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Pressure 1.000 atm, Temperature 298.000 K, pH 6.000

Experiment name 2D 1H-15N HSQC (CPMG)

Heteronucl. T₁/T₂

131 T₁/T₂ values in 1 lists
Field strength (¹H) 600 MHz, Pressure 1.000 atm, Temperature 298.000 K, pH 6.000 Detail

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Pressure 1.000 atm, Temperature 298.000 K, pH 6.000

Release date

2013-05-21

Citation

Study of the structural and dynamic effects in the FimH adhesin upon α-d-heptyl mannose binding
Vanwetswinkel, S., Volkov, A.N., Sterckx, Y.G.J., Garcia-Pino, A., Buts, L., Vranken, W.F., Bouckaert, J., Roy, R., Wyns, L., van Nuland, N.A.J.
J. Med. Chem. (2014), 57, 1416-1427, PubMed 24476493 , DOI 10.1021/jm401666c , Abstract

Related entities 1. FimH Y48A mutant, : 1 : 69 : 29 entities Detail

Interaction partners 1. FimH Y48A mutant, : 4 interactors Detail

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail