BMRBj - BMREntryMaster

Found 1 Document (0.794 seconds)

BMRB: 4106

1EZB

Solution Structure of the 30 Kda N-terminal Domain of Enzyme I of the Escherichia coli Phosphoenolpyruvate:Sugar Phosphotransferase System by Multidimensional NMR

Authors

Garrett, D.S., Seok, Y., Liao, D., Peterkofsky, A., Gronenborn, A.M., Clore, M.G.

Assembly

N-terminal Domain of Enzyme I

Entity

1. N-terminal Domain of Enzyme I (polymer), 259 monomers, 28345.97 Da Detail

MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA SAQLETIKTK AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QASALEELDD EYLKERAADV RDIGKRLLRN ILGLKIIDLS AIQDEVILVA ADLTPSETAQ LNLKKVLGFI TDAGGRTSHT SIMARSLELP AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR AVQEQVASEK AELAKLKDR

Formula weight

28345.97 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.6 %, Completeness: 71.5 %, Completeness (bb): 72.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	71.5 % (2110 of 2952)	78.7 % (1203 of 1528)	72.0 % (829 of 1151)	28.6 % (78 of 273)
Backbone	72.0 % (1113 of 1546)	96.0 % (508 of 529)	70.2 % (535 of 762)	27.5 % (70 of 255)
Sidechain	74.6 % (1231 of 1650)	69.3 % (692 of 999)	83.9 % (531 of 633)	44.4 % (8 of 18)
Aromatic	44.4 % (40 of 90)	64.4 % (29 of 45)	24.4 % (11 of 45)
Methyl	89.6 % (326 of 364)	91.8 % (167 of 182)	87.4 % (159 of 182)

1. N-terminal Domain of Enzyme I

Show sample condition

Sample #1

Temperature 313 (±2) K, pH 7.5 (±0.5)

#	Name	Isotope labeling	Type	Concentration
1	N-terminal Domain of Enzyme I	[U-95% 2H; U-99% 13C; U-99% 15N]		1.4 ~ 1.5 mM

Sample #2

Temperature 313 (±2) K, pH 7.5 (±0.5)

#	Name	Isotope labeling	Type	Concentration
2	N-terminal Domain of Enzyme I	[U-100% 1H; U-100% 12C; U-99%1 5N]		1.4 ~ 1.5 mM

Sample #3

Temperature 313 (±2) K, pH 7.5 (±0.5)

#	Name	Isotope labeling	Type	Concentration
3	N-terminal Domain of Enzyme I	[U-100% 2H; U-100% 12C; U-99% 15N]		1.4 ~ 1.5 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹³C	na	na	null	null
¹H	DSS	methyl protons	null	direct
¹⁵N	na	na	null	null

Referencing offset: -0.25 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹³C	na	na	null	null
¹H	DSS	methyl protons	null	direct
¹⁵N	na	na	null	null

Referencing offset: -0.25 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹³C	na	na	null	null
¹H	DSS	methyl protons	null	direct
¹⁵N	na	na	null	null

Referencing offset: 0.02 ppm, Outliers: 1 Detail

Release date

2000-06-18

Citation 1

Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR
Garrett, D.S., Seok, Y., Liao, D., Peterkofsky, A., Gronenborn, A.M., Clore, M.G.
Biochemistry (1997), 36, 2517-2530, PubMed 9054557 , DOI 10.1021/bi962924y , Abstract

Show more 1 citaion

Citation 2

1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140, PubMed 8589602 , DOI: , Abstract

Hide non-primary 1 citaion

Related entities 1. N-terminal Domain of Enzyme I, : 1 : 8 : 10 : 52 entities Detail

Interaction partners 1. N-terminal Domain of Enzyme I, : 11 interactors Detail

More details for 11 interactors identified by 5 citations

Experiments performed 3 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4106_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: bmr4106_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_EIN	Warning	2272		99.6 (chain: 1, length: 259)
1	Chemical shift references	chemical_shift_reference_one	OK	1		No information

Assigned chemical shifts

Saveframe: chemical_shift_assignment_EIN
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 259, Sequence coverage: 99.6%
- Total number of assignments
  - ¹³C chemical shifts: 769
  - ¹H chemical shifts: 1474
  - ¹⁵N chemical shifts: 29
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Tautomeric state of HIS
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
76	HIS	NE2	165.501
76	HIS	ND1	248.43
97	HIS	ND1	195.51
97	HIS	NE2	178.21
105	HIS	ND1	219.745
105	HIS	NE2	183.29
189	HIS	ND1	190.59
189	HIS	NE2	217.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	1151	769	66.8
¹H chemical shifts	1528	1140	74.6
¹⁵N chemical shifts	284	21	7.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	518	251	48.5
¹H chemical shifts	529	507	95.8
¹⁵N chemical shifts	255	10	3.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	633	518	81.8
¹H chemical shifts	999	633	63.4
¹⁵N chemical shifts	29	11	37.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	187	160	85.6
¹H chemical shifts	187	167	89.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	45	7	15.6
¹H chemical shifts	45	28	62.2

Keywords kinase, phosphotransferase, sugar transport

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Found 1 Document (0.794 seconds)

BMRB: 4106

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. N-terminal Domain of Enzyme I, : 1 : 8 : 10 : 52 entities Detail

Interaction partners 1. N-terminal Domain of Enzyme I, : 11 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample #1

Sample #2

Sample #3

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Sample #1

Sample #2

Sample #3

Instrument

Sample #1

Sample #2

Sample #3

Chemical shift validation 3 contents Detail