BMRBj - BMREntryMaster

Found 1 Document (0.556 seconds)

BMRB: 26715

beta-endorphin

Authors

Seuring, C., Gath, J., Verasdonck, J., Nespovitaya, N., Cadalbert, R., Rivier, J., Boeckmann, A., Meier, B.H., Riek, R.

Assembly

beta-endorphin

Entity

1. beta-endorphin (polymer, Thiol state: not present), 31 monomers, 3464.980 Da Detail

YGGFMTSEKS QTPLVTLFKN AIIKNAYKKG E

Formula weight

3464.98 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.8 %, Completeness: 52.4 %, Completeness (bb): 64.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	52.4 % (198 of 378)	15.7 % (31 of 198)	93.2 % (137 of 147)	90.9 % (30 of 33)
Backbone	64.7 % (119 of 184)	9.4 % (6 of 64)	94.4 % (85 of 90)	93.3 % (28 of 30)
Sidechain	47.7 % (106 of 222)	18.7 % (25 of 134)	92.9 % (79 of 85)	66.7 % (2 of 3)
Aromatic	38.9 % (14 of 36)	0.0 % (0 of 18)	77.8 % (14 of 18)
Methyl	93.3 % (28 of 30)	86.7 % (13 of 15)	100.0 % (15 of 15)

1. beta-endorphin

YGGFMTSEKS QTPLVTLFKN AIIKNAYKKG E

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5.5

#	Name	Isotope labeling	Concentration
1	beta-endorphin	[U-100% 13C; U-100% 15N]	25 mg
2	H2O	natural abundance	10 %
3	D2O	natural abundance	90 %

Release date

2016-07-13

Citation

Solid-state NMR sequential assignment of the β-endorphin peptide in its amyloid form
Seuring, C., Gath, J., Verasdonck, J., Nespovitaya, N., Cadalbert, R., Rivier, J., Boeckmann, A., Meier, B.H., Riek, R.
Biomol. NMR Assign. (2016), 10, 259-268, PubMed 27165576 , DOI 10.1007/s12104-016-9681-z , Abstract

Related entities 1. beta-endorphin, : 2 : 9 : 1 : 22 entities Detail

Experiments performed 7 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr26715_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: bmr26715_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	230		93.5 (chain: 1, length: 31)
1	Chemical shift references	chemical_shift_reference_1	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: 1, Chain length: 31, Sequence coverage: 93.5%

--------10--------20--------30-
YGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE
  |||||||||||||||||||||||||||||
..GFMTSEKSQTPLVTLFKNAIIKNAYKKGE

Total number of assignments
- ¹³C chemical shifts: 146
- ¹⁵N chemical shifts: 32
- ¹H chemical shifts: 52

Completeness of assignments

Entity_assemble_ID: 1

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
4	PHE	CG	137.412
8	GLU	CD	175.338
11	GLN	CD	179.363
13	PRO	N	140.66
18	PHE	CG	137.486
20	ASN	CG	178.187
24	LYS	NZ	33.216
25	ASN	CG	179.353
27	TYR	CG	129.229
27	TYR	CZ	156.258
28	LYS	NZ	33.57
31	GLU	CD	180.63

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	147	137	93.2
¹⁵N chemical shifts	33	29	87.9
¹H chemical shifts	198	26	13.1

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	62	58	93.5
¹⁵N chemical shifts	30	27	90.0
¹H chemical shifts	64	1	1.6

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	85	79	92.9
¹⁵N chemical shifts	3	2	66.7
¹H chemical shifts	134	25	18.7

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	16	15	93.8
¹H chemical shifts	16	13	81.2

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	18	14	77.8
¹H chemical shifts	18	0	0.0

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

Keywords assignment, beta-endorphin fibrils, beta-strand, functional amyloids, secondary structure, solid-state NMR

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Found 1 Document (0.556 seconds)

BMRB: 26715

Sample

Related entities 1. beta-endorphin, : 2 : 9 : 1 : 22 entities Detail

Experiments performed 7 experiments Detail

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Chemical shift validation 3 contents Detail