BMRBj - BMREntryMaster

Found 1 Document (1.259 seconds)

BMRB: 7188

1ZNV

Im7, Immunity Protein of Colicin E7

Authors

Le Duff, C.S., Whittaker, S.B-M., Radford, S.E., Moore, G.R.

Assembly

Im7

Entity

1. Im7 (polymer, Thiol state: not present), 87 monomers, 9894.862 Da Detail

MELKNSISDY TEAEFVQLLK EIEKENVAAT DDVLDVLLEH FVKITEHPDG TDLIYYPSDN RDDSPEGIVK EIKEWRAANG KPGFKQG

Formula weight

9894.862 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 100.0 %, Completeness: 51.6 %, Completeness (bb): 93.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	51.6 % (526 of 1019)	34.5 % (183 of 531)	65.8 % (262 of 398)	90.0 % (81 of 90)
Backbone	93.4 % (480 of 514)	85.7 % (150 of 175)	97.3 % (249 of 256)	97.6 % (81 of 83)
Sidechain	21.8 % (128 of 587)	9.3 % (33 of 356)	42.4 % (95 of 224)	0.0 % (0 of 7)
Aromatic	2.7 % (2 of 74)	5.4 % (2 of 37)	0.0 % (0 of 36)	0.0 % (0 of 1)
Methyl	17.0 % (16 of 94)	12.8 % (6 of 47)	21.3 % (10 of 47)

1. Im7 native

MELKNSISDY TEAEFVQLLK EIEKENVAAT DDVLDVLLEH FVKITEHPDG TDLIYYPSDN RDDSPEGIVK EIKEWRAANG KPGFKQG

Show sample condition

Sample

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Im7	[U-15N; U-13C]		1 mM
2	Phosphate buffer

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 41.1 %, Completeness (bb): 73.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	41.1 % (837 of 2038)	21.8 % (232 of 1062)	64.1 % (510 of 796)	52.8 % (95 of 180)
Backbone	73.4 % (755 of 1028)	49.4 % (173 of 350)	95.1 % (487 of 512)	57.2 % (95 of 166)
Sidechain	21.0 % (246 of 1174)	8.3 % (59 of 712)	41.7 % (187 of 448)	0.0 % (0 of 14)
Aromatic	1.4 % (2 of 148)	2.7 % (2 of 74)	0.0 % (0 of 72)	0.0 % (0 of 2)
Methyl	17.0 % (32 of 188)	12.8 % (12 of 94)	21.3 % (20 of 94)

1. Im7 native

MELKNSISDY TEAEFVQLLK EIEKENVAAT DDVLDVLLEH FVKITEHPDG TDLIYYPSDN RDDSPEGIVK EIKEWRAANG KPGFKQG

Show sample condition

Sample

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Concentration
3	Im7	[U-15N; U-13C]	1 mM
4	Phosphate buffer		20 mM
5	Urea		6 M

Release date

2006-10-29

Citation

Characterisation of the conformational properties of urea-unfolded Im7: implications for the early stages of protein folding
Le Duff, C.S., Whittaker, S.B-M., Radford, S.E., Moore, G.R.
J. Mol. Biol. (2006), 364, 824-835, PubMed 17045607 , DOI 10.1016/j.jmb.2006.09.037 , Abstract

Related entities 1. Im7, : 1 : 9 : 3 : 44 entities Detail

Interaction partners 1. Im7, : 3 interactors Detail

More details for 3 interactors identified by 2 citations

Experiments performed 7 experiments Detail

1 2D 15N-1H HSQC

Instrument

Model Varian Unity Inova (500 MHz)

Sample #1

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Im7	[U-15N; U-13C]		1 mM
2	Phosphate buffer

Sample #2

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Concentration
3	Im7	[U-15N; U-13C]	1 mM
4	Phosphate buffer		20 mM
5	Urea		6 M

2 2D 15N-1H HSQC NH2 only

Instrument

Model Varian Unity Inova (500 MHz)

Sample #1

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Im7	[U-15N; U-13C]		1 mM
2	Phosphate buffer

Sample #2

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Concentration
3	Im7	[U-15N; U-13C]	1 mM
4	Phosphate buffer		20 mM
5	Urea		6 M

3 3D HNCO, 3D HNCA

Instrument

Model Varian Unity Inova (500 MHz)

Sample #1

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Im7	[U-15N; U-13C]		1 mM
2	Phosphate buffer

Sample #2

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Concentration
3	Im7	[U-15N; U-13C]	1 mM
4	Phosphate buffer		20 mM
5	Urea		6 M

4 3D HNCACB

Instrument

Model Varian Unity Inova (500 MHz)

Sample #1

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Im7	[U-15N; U-13C]		1 mM
2	Phosphate buffer

Sample #2

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Concentration
3	Im7	[U-15N; U-13C]	1 mM
4	Phosphate buffer		20 mM
5	Urea		6 M

5 3D CBCA(CO)NH

Instrument

Model Varian Unity Inova (500 MHz)

Sample #1

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Im7	[U-15N; U-13C]		1 mM
2	Phosphate buffer

Sample #2

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Concentration
3	Im7	[U-15N; U-13C]	1 mM
4	Phosphate buffer		20 mM
5	Urea		6 M

6 3D H(CCO)NH

Instrument

Model Varian Unity Inova (500 MHz)

Sample #1

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Im7	[U-15N; U-13C]		1 mM
2	Phosphate buffer

Sample #2

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Concentration
3	Im7	[U-15N; U-13C]	1 mM
4	Phosphate buffer		20 mM
5	Urea		6 M

7 3D HN(CA)CO

Instrument

Model Varian Unity Inova (500 MHz)

Sample #1

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Im7	[U-15N; U-13C]		1 mM
2	Phosphate buffer

Sample #2

Temperature 283 (±0.5) K, pH 7 (±0.1)

#	Name	Isotope labeling	Concentration
3	Im7	[U-15N; U-13C]	1 mM
4	Phosphate buffer		20 mM
5	Urea		6 M

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr7188_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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr7188_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	484	100.0 (chain: 1, length: 87)
2	Assigned chemical shifts	chem_shift_list_2	Warning	236	100.0 (chain: 1, length: 87)
1	Chemical shift references	chemical_shift_referencing	OK	4	No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 87, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 153
  - ¹³C chemical shifts: 250
  - ¹⁵N chemical shifts: 81
- 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
Saveframe: chem_shift_list_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 87, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 236
- 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	531	153	28.8
¹³C chemical shifts	398	250	62.8
¹⁵N chemical shifts	92	81	88.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	175	153	87.4
¹³C chemical shifts	174	168	96.6
¹⁵N chemical shifts	83	81	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	356	0	0.0
¹³C chemical shifts	224	82	36.6
¹⁵N chemical shifts	9	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	0	0.0
¹³C chemical shifts	48	5	10.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	37	0	0.0
¹³C chemical shifts	36	0	0.0
¹⁵N chemical shifts	1	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	398	236	59.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	174	155	89.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	224	81	36.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	48	5	10.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	36	0	0.0

Keywords Im7, NMR, protein folding, urea

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Found 1 Document (1.259 seconds)

BMRB: 7188

Sample

Sample

Related entities 1. Im7, : 1 : 9 : 3 : 44 entities Detail

Interaction partners 1. Im7, : 3 interactors Detail

Experiments performed 7 experiments Detail

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Chemical shift validation 4 contents Detail