BMRBj - BMREntryMaster

Found 1 Document (1.515 seconds)

BMRB: 6100

Backbone 1H, 13C and 15N chemical shift assignents of the 18.5kDa isoform of murine myelin basic protein (MBP)

Authors

Libich, D.S., Robertson, V.J., Monette, M.M., Harauz, G.

Assembly

rmMBP

Entity

1. rmMBP (polymer, Thiol state: not present), 176 monomers, 19449.34 Da Detail

ASQKRPSQRS KYLATASTMD HARHGFLPRH RDTGILDSIG RFFSGDRGAP KRGSGKDSHT RTTHYGSLPQ KSQHGRTQDE NPVVHFFKNI VTPRTPPPSQ GKGRGLSLSR FSWGAEGQRP GFGYGGRASD YKSAHKGFKG AYDAQGTLSK IFKLGGRDSR SGSPMARRLE HHHHHH

Formula weight

19449.34 Da

Source organism

Mus musculus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.6 %, Completeness: 58.2 %, Completeness (bb): 78.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	58.2 % (1166 of 2002)	52.2 % (552 of 1058)	59.6 % (458 of 768)	88.6 % (156 of 176)
Backbone	78.3 % (810 of 1034)	89.6 % (327 of 365)	65.1 % (328 of 504)	93.9 % (155 of 165)
Sidechain	44.6 % (500 of 1120)	32.5 % (225 of 693)	65.9 % (274 of 416)	9.1 % (1 of 11)
Aromatic	8.1 % (16 of 198)	8.1 % (8 of 99)	8.2 % (8 of 98)	0.0 % (0 of 1)
Methyl	56.6 % (60 of 106)	35.8 % (19 of 53)	77.4 % (41 of 53)

1. myelin basic protein

ASQKRPSQRS KYLATASTMD HARHGFLPRH RDTGILDSIG RFFSGDRGAP KRGSGKDSHT RTTHYGSLPQ KSQHGRTQDE NPVVHFFKNI VTPRTPPPSQ GKGRGLSLSR FSWGAEGQRP GFGYGGRASD YKSAHKGFKG AYDAQGTLSK IFKLGGRDSR SGSPMARRLE HHHHHH

Show sample condition

Sample

Temperature 298 (±0.1) K, pH 6.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	myelin basic protein	[U-15N; U-13C]		2 mM
2	2,2,2-trifluoroethanol-d2	[2H]		30 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl carbon	external	direct	1.0
¹H	TSP	methyl protons	external	direct	1.0
¹⁵N	liquid ammonia	nitrogen	external	indirect	1.0

Referencing offset: 0.06 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl carbon	external	direct	1.0
¹H	TSP	methyl protons	external	direct	1.0
¹⁵N	liquid ammonia	nitrogen	external	indirect	1.0

Referencing offset: 0.06 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl carbon	external	direct	1.0
¹H	TSP	methyl protons	external	direct	1.0
¹⁵N	liquid ammonia	nitrogen	external	indirect	1.0

Referencing offset: 0.06 ppm, Outliers: 2 Detail

Release date

2004-07-28

Citation

Backbone resonance assignments of the 18.5 kDa isoform of murine myelin basic protein (MBP)
Libich, D.S., Robertson, V.J., Monette, M.M., Harauz, G.
J. Biomol. NMR (2004), 29, 545-546, PubMed 15243191 , DOI 10.1023/B:JNMR.0000034348.99658.d7 , Abstract

Related entities 1. rmMBP, : 16 entities Detail

Interaction partners 1. rmMBP, : 14 interactors Detail

More details for 14 interactors identified by 12 citations

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6100_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: bmr6100_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_set_1	OK	1106		96.6 (chain: 1, length: 176)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: chemical_shift_set_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 176, Sequence coverage: 96.6%
- Total number of assignments
  - ¹³C chemical shifts: 436
  - ¹H chemical shifts: 516
  - ¹⁵N chemical shifts: 154
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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 (%)
¹³C chemical shifts	352	169	48.0
¹H chemical shifts	365	322	88.2
¹⁵N chemical shifts	165	154	93.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	768	436	56.8
¹H chemical shifts	1058	488	46.1
¹⁵N chemical shifts	195	154	79.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	416	267	64.2
¹H chemical shifts	693	166	24.0
¹⁵N chemical shifts	30	0	0.0

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Found 1 Document (1.515 seconds)

BMRB: 6100

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. rmMBP, : 16 entities Detail

Interaction partners 1. rmMBP, : 14 interactors Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

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Instrument

Sample

Chemical shift validation 3 contents Detail