BMRBj - BMREntryMaster

Found 1 Document (0.523 seconds)

BMRB: 15201

2M06

Sequence-specific resonance assignments for OmpX in 8 M urea aqueous solution

Authors

Tafer, H., Hiller, S., Hilty, C., Fernandez, C., Wuthrich, K.

Assembly

denatured OmpX

Entity

1. denatured OmpX (polymer, Thiol state: all free), 148 monomers, 16382.69 Da Detail

ATSTVTGGYA QSDAQGQMNK MGGFNLKYRY EEDNSPLGVI GSFTYTEKSR TASSGDYNKN QYYGITAGPA YRINDWASIY GVVGVGYGKF QTTEYPTYKH DTSDYGFSYG AGLQFNPMEN VALDFSYEQS RIRSVDVGTW IAGVGYRF

Formula weight

16382.69 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 86.6 %, Completeness (bb): 99.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.6 % (1446 of 1670)	86.7 % (743 of 857)	85.4 % (557 of 652)	90.7 % (146 of 161)
Backbone	99.3 % (874 of 880)	98.7 % (308 of 312)	99.5 % (422 of 424)	100.0 % (144 of 144)
Sidechain	76.3 % (700 of 918)	79.8 % (435 of 545)	73.9 % (263 of 356)	11.8 % (2 of 17)
Aromatic	23.0 % (52 of 226)	25.7 % (29 of 113)	18.9 % (21 of 111)	100.0 % (2 of 2)
Methyl	100.0 % (120 of 120)	100.0 % (60 of 60)	100.0 % (60 of 60)

1. Outer membrane protein X

ATSTVTGGYA QSDAQGQMNK MGGFNLKYRY EEDNSPLGVI GSFTYTEKSR TASSGDYNKN QYYGITAGPA YRINDWASIY GVVGVGYGKF QTTEYPTYKH DTSDYGFSYG AGLQFNPMEN VALDFSYEQS RIRSVDVGTW IAGVGYRF

Show sample condition

Sample

Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	Outer membrane protein X	[U-100% 13C; U-100% 15N]	3 mM
2	urea	natural abundance	8 M
3	D2O	[U-100% 2H]	5 %
4	sodium phosphate	natural abundance	20 mM
5	sodium azide	natural abundance	0.1 mM

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: -0.05 ppm, Outliers: 1 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: -0.05 ppm, Outliers: 1 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: 0.07 ppm, Outliers: 2 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: 0.11 ppm, Outliers: 1 Detail

Release date

2007-04-25

Citation

Nonrandom structure in the urea-unfolded Escherichia coli outer membrane protein X (OmpX)
Tafer, H., Hiller, S., Hilty, C., Fernandez, C., Wuthrich, K.
Biochemistry (2004), 43, 860-869, PubMed 14744128 , DOI 10.1021/bi0356606 , Abstract

Related entities 1. denatured OmpX, : 1 : 3 : 6 : 10 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr15201_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: bmr15201_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1565		100.0 (chain: 1, length: 148)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 148, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 869
  - ¹³C chemical shifts: 550
  - ¹⁵N chemical shifts: 146
- 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

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Found 1 Document (0.523 seconds)

BMRB: 15201

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. denatured OmpX, : 1 : 3 : 6 : 10 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	857	743	86.7
¹³C chemical shifts	652	550	84.4
¹⁵N chemical shifts	167	146	87.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	312	312	100.0
¹³C chemical shifts	296	296	100.0
¹⁵N chemical shifts	144	144	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	545	431	79.1
¹³C chemical shifts	356	254	71.3
¹⁵N chemical shifts	23	2	8.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	113	14	12.4
¹³C chemical shifts	111	12	10.8
¹⁵N chemical shifts	2	2	100.0