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Found 1 Document (0.645 seconds)

BMRB: 19254

4CA4

NMR assignments and backbone amide relaxation data (T1-T2) for the complex of the Y48A mutant of the FimH adhesin carbohydrate-binding domain with heptyl-mannose

Authors

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

Assembly

FimH Y48A mutant - Heptyl-mannose complex

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

2. Heptyl Alpha-D-mannopyrannoside (non-polymer), 278.342 Da

Total weight

17093.982 Da

Max. entity weight

16815.64 Da

Entity Connection

disulfide 1 Detail

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: 93.0 %, Completeness: 34.1 %, Completeness (bb): 63.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	34.1 % (360 of 1055)	21.8 % (193 of 886)	98.8 % (167 of 169)
Backbone	63.2 % (295 of 467)	46.4 % (148 of 319)	99.3 % (147 of 148)
Sidechain	11.1 % (65 of 588)	7.9 % (45 of 567)	95.2 % (20 of 21)
Aromatic	4.9 % (4 of 82)	2.5 % (2 of 80)	100.0 % (2 of 2)
Methyl	2.9 % (3 of 103)	2.9 % (3 of 103)

1. FIMH Y48A mutant

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

Show sample condition

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	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	heptyl alpha-D-mannopyranoside (heptyl mannose)	natural abundance	1.3 mM
5	H2O	natural abundance	93 %
6	D2O	natural abundance	7 %

Heteronucl. T₁

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

Heteronucl. T₂

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

Heteronucl. T₁/T₂

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

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

More details for 4 interactors identified by 3 citations

Experiments performed 4 experiments Detail

1 2D 1H-15N HSQC

Instrument

Varian Direct-Drive - 600 MHz

Sample

State isotropic, 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	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	heptyl alpha-D-mannopyranoside (heptyl mannose)	natural abundance	1.3 mM
5	H2O	natural abundance	93 %
6	D2O	natural abundance	7 %

2 3D 1H-15N NOESY

Instrument

Varian Direct-Drive - 600 MHz

Sample

#	Name	Isotope labeling	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	heptyl alpha-D-mannopyranoside (heptyl mannose)	natural abundance	1.3 mM
5	H2O	natural abundance	93 %
6	D2O	natural abundance	7 %

3 2D 1H-15N HSQC (inverse recovery)

Instrument

Varian Direct-Drive - 600 MHz

Sample

#	Name	Isotope labeling	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	heptyl alpha-D-mannopyranoside (heptyl mannose)	natural abundance	1.3 mM
5	H2O	natural abundance	93 %
6	D2O	natural abundance	7 %

4 2D 1H-15N HSQC (CPMG)

Instrument

Varian Direct-Drive - 600 MHz

Sample

#	Name	Isotope labeling	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	heptyl alpha-D-mannopyranoside (heptyl mannose)	natural abundance	1.3 mM
5	H2O	natural abundance	93 %
6	D2O	natural abundance	7 %

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts, Heteronucl T1 relaxation data, Heteronucl T2 relaxation data	bmr19254_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:3:CYS:SG	1:44:CYS:SG	unknown	unknown	n/a

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr19254_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list	Warning	358		93.0 (chain: 1, length: 158)
1	Chemical shift references	chemical_shift_reference_1	Warning	1		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 158, Sequence coverage: 93.0%
- Total number of assignments
  - ¹H chemical shifts: 188
  - ¹⁵N chemical shifts: 170
- 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	886	188	21.2
¹⁵N chemical shifts	173	170	98.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	319	147	46.1
¹⁵N chemical shifts	148	147	99.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	567	41	7.2
¹⁵N chemical shifts	25	23	92.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	103	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	80	2	2.5
¹⁵N chemical shifts	2	2	100.0

Keywords CELL ADHESION, NMR, bacterial adhesin, carbohydrate, urinary tract infection

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Found 1 Document (0.645 seconds)

BMRB: 19254

Sample

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

Instrument

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Chemical shift validation 4 contents Detail