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Found 1 Document (1.392 seconds)

BMRB: 7236

4GKU

NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase Suggests Active-Site Dynamical Coupling

Authors

Doucet, N., Savard, P., Pelletier, J.N., Gagne, S.M.

Assembly

Mutants Y105W of TEM-1 beta-lactamase

Entity

1. Mutants Y105W of TEM-1 beta-lactamase (polymer, Thiol state: all disulfide bound), 263 monomers, 28929.70 Da Detail

HPETLVKVKD AEDQLGARVG YIELDLNSGK ILESFRPEER FPMMSTFKVL LCGAVLSRVD AGQEQLGRRI HYSQNDLVEW SPVTEKHLTD GMTVRELCSA AITMSDNTAA NLLLTTIGGP KELTAFLHNM GDHVTRLDRW EPELNEAIPN DERDTTMPAA MATTLRKLLT GELLTLASRQ QLIDWMEADK VAGPLLRSAL PAGWFIADKS GAGERGSRGI IAALGPDGKP SRIVVIYTTG SQATMDERNR QIAEIGASLI KHW

Formula weight

28929.7 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS52:SG	1:CYS98:SG

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.6 %, Completeness: 43.6 %, Completeness (bb): 78.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	43.6 % (1299 of 2980)	22.5 % (347 of 1543)	60.5 % (705 of 1165)	90.8 % (247 of 272)
Backbone	78.1 % (1213 of 1554)	53.1 % (284 of 535)	88.8 % (682 of 768)	98.4 % (247 of 251)
Sidechain	16.8 % (281 of 1668)	6.3 % (63 of 1008)	34.1 % (218 of 639)	0.0 % (0 of 21)
Aromatic	3.8 % (6 of 158)	6.3 % (5 of 79)	1.4 % (1 of 74)	0.0 % (0 of 5)
Methyl	16.0 % (52 of 326)	11.7 % (19 of 163)	20.2 % (33 of 163)

1. TEM-1

Show sample condition

Sample

Temperature 303 (±0.2) K, pH 6.6 (±0.2), Details 0.8 mM, pH 6.6 for all Y105X mutants

#	Name	Isotope labeling	Concentration
1	TEM-1 (Y105W)	[U-13C; U-15N]	0.8 mM
2	imidazole		4 mM
3	DSS		0.1 mM
4	H2O		90 %
5	D2O		10 %

LACS Plot; CA

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

Referencing offset: -0.32 ppm, Outliers: 2 Detail

LACS Plot; CB

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

Referencing offset: -0.32 ppm, Outliers: 2 Detail

LACS Plot; CO

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

Referencing offset: -0.12 ppm, Outliers: 2 Detail

Release date

2007-01-08

Citation

Backbone dynamics of TEM-1 determined by NMR: evidence for a highly ordered protein
Savard, P., Gagne, S.M.
Biochemistry (2006), 45, 11414-11424, PubMed 16981701 , DOI 10.1021/bi060414q , Abstract

Entries sharing articles BMRB: 4 entries Detail

  BMRB: 16392 released on 2009-07-09
    Title NMR relaxation data for the beta-lactamase TEM-1
  BMRB: 7237 released on 2007-01-08
    Title NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase Suggests Active-Site Dynamical Coupling
  BMRB: 7238 released on 2007-01-08
    Title NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase Suggests Active-Site Dynamical Coupling
  BMRB: 7239 released on 2007-01-08
    Title NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase Suggests Active-Site Dynamical Coupling

Related entities 1. Mutants Y105W of TEM-1 beta-lactamase, : 1 : 11 : 159 entities Detail

Interaction partners 1. Mutants Y105W of TEM-1 beta-lactamase, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr7236_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)
1:52:CYS:SG	1:98:CYS:SG	oxidized, CA 63.857, CB 44.875 ppm	oxidized, CA 62.348, CB 42.497 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr7236_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	1162		99.6 (chain: 1, length: 263)
1	Chemical shift references	chemical_shift_referencing	OK	3		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 263, Sequence coverage: 99.6%
- Total number of assignments
  - ¹³C chemical shifts: 668
  - ¹H chemical shifts: 247
  - ¹⁵N chemical shifts: 247
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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 (%)
¹³C chemical shifts	1165	668	57.3
¹H chemical shifts	1543	247	16.0
¹⁵N chemical shifts	290	247	85.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	526	481	91.4
¹H chemical shifts	535	247	46.2
¹⁵N chemical shifts	251	247	98.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	639	187	29.3
¹H chemical shifts	1008	0	0.0
¹⁵N chemical shifts	39	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	172	22	12.8
¹H chemical shifts	172	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	74	0	0.0
¹H chemical shifts	79	0	0.0
¹⁵N chemical shifts	5	0	0.0

Keywords 15N relaxation, Enzyme dynamics, NMR, TEM-1 beta-lactamase, Backbone assignment, Class A beta-lactamase, Mutant comparison, TEM-1, Tyr105

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Found 1 Document (1.392 seconds)

BMRB: 7236

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. Mutants Y105W of TEM-1 beta-lactamase, : 1 : 11 : 159 entities Detail

Interaction partners 1. Mutants Y105W of TEM-1 beta-lactamase, : 1 interactors Detail

Experiments performed 4 experiments Detail

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Instrument

Sample

Instrument

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Instrument

Sample

Chemical shift validation 3 contents Detail