BMRBj - BMREntryMaster

Found 1 Document (1.07 seconds)

BMRB: 4773

1OSP

Backbone assignments for OspA N-terminal fragment[27-163]

Authors

Huang, X., Nakagawa, T., Tamura, A., Link, K., Koide, A., Koide, S.

Assembly

OspA N-terminal fragment

Entity

1. OspA N-terminal fragment (polymer, Thiol state: not present), 141 monomers, 15252.09 Da Detail

GSHMKNSVSV DLPGEMKVLV SKEKNKDGKY DLIATVDKLE LKGTSDKNNG SGVLEGVKAD KSKVKLTISD DLGQTTLEVF KEDGKTLVSK KVTSKDKSST EEKFNEKGEV SEKIITRADG TRLEYTGIKS DGSGKAKEVL K

Formula weight

15252.09 Da

Source organism

Borreliella burgdorferi

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.3 %, Completeness: 46.1 %, Completeness (bb): 81.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	46.1 % (743 of 1610)	21.8 % (184 of 845)	68.2 % (422 of 619)	93.8 % (137 of 146)
Backbone	81.5 % (688 of 844)	50.2 % (148 of 295)	98.5 % (403 of 409)	97.9 % (137 of 140)
Sidechain	20.3 % (181 of 893)	6.5 % (36 of 550)	43.0 % (145 of 337)	0.0 % (0 of 6)
Aromatic	0.0 % (0 of 40)	0.0 % (0 of 20)	0.0 % (0 of 20)
Methyl	8.0 % (12 of 150)	4.0 % (3 of 75)	12.0 % (9 of 75)

1. outer surface protein A

GSHMKNSVSV DLPGEMKVLV SKEKNKDGKY DLIATVDKLE LKGTSDKNNG SGVLEGVKAD KSKVKLTISD DLGQTTLEVF KEDGKTLVSK KVTSKDKSST EEKFNEKGEV SEKIITRADG TRLEYTGIKS DGSGKAKEVL K

Show sample condition

Sample

Temperature 308 (±0.5) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	outer surface protein A	[U-13C; U-15N]	1.5 mM
2	sodium phosphate		10 mM
3	sodium chloride		50 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl protons	external	indirect	0.2514495
¹⁵N	ammonia	nitrogen	external	indirect	0.101329
¹H	DSS	methyl protons	internal	direct	0.0

Referencing offset: -0.2 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl protons	external	indirect	0.2514495
¹⁵N	ammonia	nitrogen	external	indirect	0.101329
¹H	DSS	methyl protons	internal	direct	0.0

Referencing offset: -0.2 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl protons	external	indirect	0.2514495
¹⁵N	ammonia	nitrogen	external	indirect	0.101329
¹H	DSS	methyl protons	internal	direct	0.0

Referencing offset: 0.63 ppm, Outliers: 2 Detail

Release date

2001-08-08

Citation

Formation of the single-layer beta-sheet of Borrelia burgdorferi OspA in the absence of the C-terminal capping globular domain
Huang, X., Nakagawa, T., Tamura, A., Link, K., Koide, A., Koide, S.
J. Mol. Biol. (2001), 308, 367-375, PubMed 11327773 , DOI 10.1006/jmbi.2001.4579 , Abstract

Related entities 1. OspA N-terminal fragment, : 1 : 12 : 27 entities Detail

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4773_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: bmr4773_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	backbone	OK	682		100.0 (chain: 1, length: 141)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: backbone
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 141, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 406
  - ¹⁵N chemical shifts: 138
  - ¹H chemical shifts: 138
- 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 (%)
¹³C chemical shifts	619	406	65.6
¹⁵N chemical shifts	148	138	93.2
¹H chemical shifts	845	138	16.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	282	279	98.9
¹⁵N chemical shifts	140	138	98.6
¹H chemical shifts	295	138	46.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	337	127	37.7
¹⁵N chemical shifts	8	0	0.0
¹H chemical shifts	550	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	77	4	5.2
¹H chemical shifts	77	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	20	0	0.0
¹H chemical shifts	20	0	0.0

Keywords outer surface protein A, protein folding, protein stability, Lyme disease

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Found 1 Document (1.07 seconds)

BMRB: 4773

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. OspA N-terminal fragment, : 1 : 12 : 27 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail