BMRBj - BMREntryMaster

Found 1 Document (1.169 seconds)

BMRB: 7318

4F37

Backbone 1HN, 15N, and 13C Chemical Shift Assignments for wt Im7* (* denotes his-tag) and its variants, Im7*L53AI54A and Im7*YY

Authors

Whittaker, S.B.-M., Spence, G.R., Grossmann, G.J., Radford, S.E., Moore, G.R.

Assembly

Monomer

Entity

1. Monomer (polymer, Thiol state: not present), 94 monomers, 10632.51 Da Detail

MEHHHHHHEL KNSISDYTEA EFVQLLKEIE KENVAATDDV LDVLLEHFVK ITEHPDGGGG GYYPSDNRDD SPEGIVKEIK EWRAANGKPG FKQG

Formula weight

10632.51 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 81.9 %, Completeness: 37.5 %, Completeness (bb): 68.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	37.5 % (405 of 1081)	22.4 % (126 of 563)	50.1 % (211 of 421)	70.1 % (68 of 97)
Backbone	68.7 % (382 of 556)	56.0 % (108 of 193)	75.5 % (206 of 273)	75.6 % (68 of 90)
Sidechain	13.9 % (85 of 610)	4.9 % (18 of 370)	28.8 % (67 of 233)	0.0 % (0 of 7)
Aromatic	0.0 % (0 of 98)	0.0 % (0 of 49)	0.0 % (0 of 48)	0.0 % (0 of 1)
Methyl	15.5 % (13 of 84)	14.3 % (6 of 42)	16.7 % (7 of 42)

1. YY

MEHHHHHHEL KNSISDYTEA EFVQLLKEIE KENVAATDDV LDVLLEHFVK ITEHPDGGGG GYYPSDNRDD SPEGIVKEIK EWRAANGKPG FKQG

Show sample condition

Sample #1

Temperature 298 (±0.1) K, pH 7 (±0.2), Details doubly-labelled (13C/15N) Im7*YY sample for backbone resonance assignments.

#	Name	Isotope labeling	Type	Concentration
1	Im7*	[U-13C; U-15N]	protein	1 (±0.2) mM
2	potassium phosphate buffer			50 mM
3	sodium sulphate			400 mM
4	H2O			90 %
5	D2O			10 %

Sample #2

Temperature 298 (±0.1) K, pH 7 (±0.2), Details singly-labelled (15N) Im7* sample for relaxation data measurement and 15N-edited NOESY experiment.

#	Name	Isotope labeling	Type	Concentration
6	Im7*	[U-99% 15N]	protein	1 (±0.2) mM
7	potassium phosphate buffer			50 mM
8	sodium sulphate			400 mM
9	H2O			90 %
10	D2O			10 %

LACS Plot; CA

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

Referencing offset: -0.09 ppm, Outliers: 5 Detail

LACS Plot; CB

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

Referencing offset: -0.09 ppm, Outliers: 5 Detail

LACS Plot; HA

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

Referencing offset: 0.03 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: 0.19 ppm, Outliers: 1 Detail

Release date

2007-05-03

Citation

NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7
Whittaker, S.B.-M., Spence, G.R., Grossmann, G.J., Radford, S.E., Moore, G.R.
J. Mol. Biol. (2007), 366, 1001-1015, PubMed 17188712 , DOI 10.1016/j.jmb.2006.11.012 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 7316 released on 2007-05-03
    Title Backbone 1HN, 15N, and 13C Chemical Shift Assignments for wt Im7* (* denotes his-tag) and its variants, Im7*L53AI54A and Im7*YY
  BMRB: 7317 released on 2007-05-03
    Title Backbone 1HN, 15N, and 13C Chemical Shift Assignments for wt Im7* (* denotes his-tag) and its variants, Im7*L53AI54A and Im7*YY

Related entities 1. Monomer, : 1 : 12 : 39 entities Detail

Interaction partners 1. Monomer, : 3 interactors Detail

More details for 3 interactors identified by 2 citations

Experiments performed 7 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr7318_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	OK

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr7318_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	Im7*_YY_chemical_shifts	OK	371		81.9 (chain: 1, length: 94)
1	Chemical shift references	chemical_shift_referencing	OK	3		No information

Assigned chemical shifts

Saveframe: Im7*_YY_chemical_shifts
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 94, Sequence coverage: 81.9%
- Total number of assignments
  - ¹H chemical shifts: 101
  - ¹³C chemical shifts: 202
  - ¹⁵N chemical shifts: 68
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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 (%)
¹H chemical shifts	563	101	17.9
¹³C chemical shifts	421	202	48.0
¹⁵N chemical shifts	99	68	68.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	193	101	52.3
¹³C chemical shifts	188	141	75.0
¹⁵N chemical shifts	90	68	75.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	370	0	0.0
¹³C chemical shifts	233	61	26.2
¹⁵N chemical shifts	9	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	0	0.0
¹³C chemical shifts	43	5	11.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	0	0.0
¹³C chemical shifts	48	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords Im7, intermediate, NMR, partially folded, Protein folding, SAXS, conformational properties, protein folding

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Found 1 Document (1.169 seconds)

BMRB: 7318

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 2 entries Detail

Related entities 1. Monomer, : 1 : 12 : 39 entities Detail

Interaction partners 1. Monomer, : 3 interactors Detail

Experiments performed 7 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail