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Found 1 Document (1.314 seconds)

BMRB: 7239

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 Y105D of TEM-1 beta-lactamase

Entity

1. Mutants Y105D of TEM-1 beta-lactamase (polymer, Thiol state: all disulfide bound), 263 monomers, 28858.57 Da Detail

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

Formula weight

28858.57 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: 31.3 %, Completeness (bb): 54.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	31.3 % (930 of 2968)	21.7 % (334 of 1537)	30.0 % (348 of 1160)	91.5 % (248 of 271)
Backbone	54.2 % (843 of 1554)	51.4 % (275 of 535)	41.7 % (320 of 768)	98.8 % (248 of 251)
Sidechain	7.1 % (118 of 1656)	5.9 % (59 of 1002)	9.3 % (59 of 634)	0.0 % (0 of 20)
Aromatic	5.5 % (8 of 146)	5.5 % (4 of 73)	5.8 % (4 of 69)	0.0 % (0 of 4)
Methyl	7.7 % (25 of 326)	6.7 % (11 of 163)	8.6 % (14 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 (Y105D)	[U-13C; U-15N]	0.8 mM
2	imidazole		4 mM
3	DSS		0.1 mM
4	H2O		90 %
5	D2O		10 %

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: 7236 released on 2007-01-08
    Title NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase Suggests Active-Site Dynamical Coupling
  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

Related entities 1. Mutants Y105D of TEM-1 beta-lactamase, : 1 : 48 : 122 entities Detail

Interaction partners 1. Mutants Y105D 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	bmr7239_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	unknown	unknown	n/a

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

None

Non-standard residues

None

Content subtype: bmr7239_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	744		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: 248
  - ¹H chemical shifts: 248
  - ¹⁵N chemical shifts: 248
- 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 (%)
¹³C chemical shifts	1160	248	21.4
¹H chemical shifts	1537	248	16.1
¹⁵N chemical shifts	289	248	85.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	526	248	47.1
¹H chemical shifts	535	248	46.4
¹⁵N chemical shifts	251	248	98.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	634	0	0.0
¹H chemical shifts	1002	0	0.0
¹⁵N chemical shifts	38	0	0.0

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	69	0	0.0
¹H chemical shifts	73	0	0.0
¹⁵N chemical shifts	4	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 (1.314 seconds)

BMRB: 7239

Sample

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. Mutants Y105D of TEM-1 beta-lactamase, : 1 : 48 : 122 entities Detail

Interaction partners 1. Mutants Y105D of TEM-1 beta-lactamase, : 1 interactors Detail

Experiments performed 4 experiments Detail

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Chemical shift validation 3 contents Detail