BMRBj - BMREntryMaster

Found 1 Document (1.128 seconds)

BMRB: 4115

1IMP

Assignment of 1H, 13C and 15N Signals of the Inhibitor Protein Im9 Bound to the DNase Domain of Colicin E9

Authors

Boetzel, R., Czisch, M., MacDonald, C.J., Kaptein, R., Hemmings, A., James, R., Kleanthous, C., Moore, G.R.

Assembly

IM9 E9-complex

Entity

1. IM9 (polymer), 86 monomers, 9582.414 Da Detail

MELKHSISDY TEAEFLQLVT TICNADTSSE EELVKLVTHF EEMTEHPSGS DLIYYPKEGD DDSPSGIVNT VKQWRAANGK SGFKQG

2. E9 (polymer), na Da

Formula weight

9582.414 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 83.6 %, Completeness (bb): 85.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	83.6 % (813 of 972)	91.4 % (459 of 502)	71.6 % (272 of 380)	91.1 % (82 of 90)
Backbone	85.5 % (436 of 510)	98.3 % (172 of 175)	72.6 % (183 of 252)	97.6 % (81 of 83)
Sidechain	84.3 % (457 of 542)	87.8 % (287 of 327)	81.3 % (169 of 208)	14.3 % (1 of 7)
Aromatic	34.6 % (27 of 78)	59.0 % (23 of 39)	10.5 % (4 of 38)	0.0 % (0 of 1)
Methyl	95.1 % (78 of 82)	95.1 % (39 of 41)	95.1 % (39 of 41)

1. IM9

MELKHSISDY TEAEFLQLVT TICNADTSSE EELVKLVTHF EEMTEHPSGS DLIYYPKEGD DDSPSGIVNT VKQWRAANGK SGFKQG

Show sample condition

Sample

Temperature 298 K, pH 6.2

#	Name	Isotope labeling	Concentration
1	IM9	[U-100% 15N; U-100% 13C]	1.2 mM
2	E9	[U-100% 15N; U-100% 13C]	1.3 mM
3	H2O		90 %
4	D2O		10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	na	na	0.0 na	null	null	0.0
¹H	dioxane	methylene protons	3.77 ppm	internal	direct	0.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: 1.08 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	na	na	0.0 na	null	null	0.0
¹H	dioxane	methylene protons	3.77 ppm	internal	direct	0.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: 1.08 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	na	na	0.0 na	null	null	0.0
¹H	dioxane	methylene protons	3.77 ppm	internal	direct	0.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: 0.02 ppm, Outliers: 1 Detail

Release date

1999-02-23

Citation

Assignment of 1H, 13C and 15N signals of the inhibitor protein Im9 bound to the DNase domain of colicin E9
Boetzel, R., Czisch, M., MacDonald, C.J., Kaptein, R., Hemmings, A., James, R., Kleanthous, C., Moore, G.R.
J. Biomol. NMR (1998), 12, 567-568, PubMed 9917143 , DOI: , Abstract

Related entities 1. IM9, : 1 : 11 : 2 : 5 : 32 entities Detail

Interaction partners 1. IM9, : 2 interactors Detail

More details for 2 interactors identified by 2 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4115_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: bmr4115_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_one	Warning	864		100.0 (chain: 1, length: 86)
1	Chemical shift references	chemical_shift_reference	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 86, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 529
  - ¹³C chemical shifts: 254
  - ¹⁵N chemical shifts: 81
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- 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	502	449	89.4
¹³C chemical shifts	380	254	66.8
¹⁵N chemical shifts	91	81	89.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	175	172	98.3
¹³C chemical shifts	172	86	50.0
¹⁵N chemical shifts	83	81	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	327	277	84.7
¹³C chemical shifts	208	168	80.8
¹⁵N chemical shifts	8	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	40	93.0
¹³C chemical shifts	43	40	93.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	22	56.4
¹³C chemical shifts	38	4	10.5
¹⁵N chemical shifts	1	0	0.0

Keywords colicin, immunity protein, NMR, nuclear magnetic resonance, protein, protein-protein interaction, resonance assignments, secondary structure

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Found 1 Document (1.128 seconds)

BMRB: 4115

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. IM9, : 1 : 11 : 2 : 5 : 32 entities Detail

Interaction partners 1. IM9, : 2 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail