BMRBj - BMREntryMaster

Found 1 Document (0.506 seconds)

BMRB: 15131

NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein

Authors

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

Assembly

MBP

Entity

1. MBP (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

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 93.8 %, Completeness: 53.6 %, Completeness (bb): 75.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	53.6 % (1074 of 2002)	46.4 % (491 of 1058)	56.3 % (432 of 768)	85.8 % (151 of 176)
Backbone	75.0 % (775 of 1034)	81.9 % (299 of 365)	64.7 % (326 of 504)	90.9 % (150 of 165)
Sidechain	39.3 % (440 of 1120)	27.7 % (192 of 693)	59.4 % (247 of 416)	9.1 % (1 of 11)
Aromatic	5.1 % (10 of 198)	5.1 % (5 of 99)	5.1 % (5 of 98)	0.0 % (0 of 1)
Methyl	47.2 % (50 of 106)	34.0 % (18 of 53)	60.4 % (32 of 53)

1. MBP

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

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 6.5, Details 1.47mM 15N-rmMBP/C1 in 100 mM KCl, pH 6.5, 10% D2O

#	Name	Isotope labeling	Concentration
1	MBP	[U-15N]	1.47 mM
2	potassium chloride	natural abundance	100 mM
3	D2O	[U-2H]	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 6.5, Details 2.0 mM 15N/13C-rmMBP/C1 in 100 mM KCl, pH 6.5, 10% D2O

#	Name	Isotope labeling	Concentration
4	MBP	[U-13C; U-15N]	2.0 mM
5	potassium chloride	natural abundance	100 mM
6	D2O	[U-2H]	10 %

Chem. Shift Complete2

Sequence coverage: 80.7 %, Completeness: 38.6 %, Completeness (bb): 55.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	38.6 % (1547 of 4004)	34.5 % (730 of 2116)	34.2 % (525 of 1536)	83.0 % (292 of 352)
Backbone	55.6 % (1150 of 2068)	63.7 % (465 of 730)	39.1 % (394 of 1008)	88.2 % (291 of 330)
Sidechain	25.0 % (559 of 2240)	19.1 % (265 of 1386)	35.2 % (293 of 832)	4.5 % (1 of 22)
Aromatic	3.5 % (14 of 396)	3.5 % (7 of 198)	3.6 % (7 of 196)	0.0 % (0 of 2)
Methyl	31.1 % (66 of 212)	24.5 % (26 of 106)	37.7 % (40 of 106)

1. MBP

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

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.5, Details 1.47mM 15N-rmMBP/C1 in 100 mM KCl, pH 6.5, 10% D2O

#	Name	Isotope labeling	Concentration
1	MBP	[U-15N]	1.47 mM
2	potassium chloride	natural abundance	100 mM
3	D2O	[U-2H]	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.5, Details 2.0 mM 15N/13C-rmMBP/C1 in 100 mM KCl, pH 6.5, 10% D2O

#	Name	Isotope labeling	Concentration
4	MBP	[U-13C; U-15N]	2.0 mM
5	potassium chloride	natural abundance	100 mM
6	D2O	[U-2H]	10 %

Release date

2007-06-25

Citation

NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein
Libich, D.S., Monette, M.M., Robertson, V.J., Harauz, G.
Biomol. NMR Assign. (2007), 1, 61-63, PubMed 19636827 , DOI 10.1007/s12104-007-9016-1 , Abstract

Related entities 1. MBP, : 16 entities Detail

Interaction partners 1. MBP, : 14 interactors Detail

More details for 14 interactors identified by 12 citations

Experiments performed 6 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr15131_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: bmr15131_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	979	93.2 (chain: 1, length: 176)
2	Assigned chemical shifts	assigned_chem_shift_list_2	OK	274	77.8 (chain: 1, length: 176)
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: 176, Sequence coverage: 93.2%
- Total number of assignments
  - ¹H chemical shifts: 434
  - ¹³C chemical shifts: 401
  - ¹⁵N chemical shifts: 144
- 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
Saveframe: assigned_chem_shift_list_2
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 176, Sequence coverage: 77.8%
- Total number of assignments
  - ¹H chemical shifts: 137
  - ¹⁵N chemical shifts: 137
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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	1058	414	39.1
¹³C chemical shifts	768	401	52.2
¹⁵N chemical shifts	195	144	73.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	365	287	78.6
¹³C chemical shifts	352	164	46.6
¹⁵N chemical shifts	165	144	87.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	693	127	18.3
¹³C chemical shifts	416	237	57.0
¹⁵N chemical shifts	30	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	10	18.2
¹³C chemical shifts	55	30	54.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	99	0	0.0
¹³C chemical shifts	98	0	0.0
¹⁵N chemical shifts	1	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1058	137	12.9
¹⁵N chemical shifts	195	137	70.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	365	137	37.5
¹⁵N chemical shifts	165	137	83.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	693	0	0.0
¹⁵N chemical shifts	30	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	99	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords calmodulin, multiple sclerosis, myelin basic protein, NMR

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Found 1 Document (0.506 seconds)

BMRB: 15131

Sample #1

Sample #2

Sample #1

Sample #2

Related entities 1. MBP, : 16 entities Detail

Interaction partners 1. MBP, : 14 interactors Detail

Experiments performed 6 experiments Detail

Instrument

Sample

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Chemical shift validation 4 contents Detail