BMRBj - BMREntryMaster

	Total	¹³C	¹⁵N
All	95.2 % (60 of 63)	98.1 % (52 of 53)	80.0 % (8 of 10)
Backbone	93.0 % (40 of 43)	97.0 % (32 of 33)	80.0 % (8 of 10)
Sidechain	96.8 % (30 of 31)	96.8 % (30 of 31)
Aromatic	100.0 % (8 of 8)	100.0 % (8 of 8)
Methyl	100.0 % (9 of 9)	100.0 % (9 of 9)

1. TTR(105-115)

YTIAALLSPY S

Show sample condition

Sample

Solvent system 10% acetonitrile/H2O, Pressure 1 atm, Temperature 298 K, pH 2

#	Name	Isotope labeling	Concentration
1	TTR(105-115)	[U-100% 13C; U-100% 15N]	15 mg/mL
2	acetonitrile	natural abundance	10 %
3	H2O	natural abundance	90 %

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Calculated from 1 models in PDB: 2M5M, Strand ID: A, B, C, D, E, F, G, H, I, J, K, L Detail

Release date

2013-10-29

Citation

Atomic structure and hierarchical assembly of a cross-β amyloid fibril
Fitzpatrick, A.W.P., Debelouchina, G.T., Bayro, M.J., Clare, D.K., Caporini, M.A., Bajaj, V.S., Jaroniec, C.P., Wang, L., Ladizhansky, V., Muller, S., MacPhee, C.E., Waudby, C.A., Mott, H.R., de Simone, A., Knowles, T.P.J., Saibil, H.R., Vendruscolo, M., Orlova, E.V., Griffin, R.G., Dobson, C.M.
Proc. Natl. Acad. Sci. U. S. A. (2013), 110, 5468-5473, PubMed 23513222 , DOI 10.1073/pnas.1219476110 , Abstract

Related entities 1. triplet cross-beta amyloid fibril, : 1 : 105 entities Detail

Experiments performed 4 experiments Detail

NMR combined restraints 2 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts	combined_19060_2m5m.nef
Input source #2: Coordindates	2m5m.cif
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	Error

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

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Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

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Entity_assembly_ID (NMR): C vs Auth_asym_ID (model): C

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Entity_assembly_ID (NMR): D vs Auth_asym_ID (model): D

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Entity_assembly_ID (NMR): E vs Auth_asym_ID (model): E

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Entity_assembly_ID (NMR): F vs Auth_asym_ID (model): F

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Entity_assembly_ID (NMR): G vs Auth_asym_ID (model): G

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Entity_assembly_ID (NMR): H vs Auth_asym_ID (model): H

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Entity_assembly_ID (NMR): I vs Auth_asym_ID (model): I

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Entity_assembly_ID (NMR): J vs Auth_asym_ID (model): J

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Entity_assembly_ID (NMR): K vs Auth_asym_ID (model): K

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Entity_assembly_ID (NMR): L vs Auth_asym_ID (model): L

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Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Sequence coverage (%)
A	A	11	100.0
B	B	11	100.0
C	C	11	100.0
D	D	11	100.0
E	E	11	100.0
F	F	11	100.0
G	G	11	100.0
H	H	11	100.0
I	I	11	100.0
J	J	11	100.0
K	K	11	100.0
L	L	11	100.0

Content subtype: combined_19060_2m5m.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	66		100.0 (chain: A, length: 11)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 11, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 56
  - ¹⁵N chemical shifts: 10
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
1	TYR	CG	124.5
1	TYR	CZ	160.0
9	PRO	N	135.8
10	TYR	CG	128.7
10	TYR	CZ	157.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	53	52	98.1
¹⁵N chemical shifts	10	9	90.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	22	22	100.0
¹⁵N chemical shifts	10	9	90.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	31	30	96.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	9	9	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	8	8	100.0

Keywords Amyloid fibril, Cross-beta structure

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Found 1 Document (0.48 seconds)

BMRB: 19060

Sample

Related entities 1. triplet cross-beta amyloid fibril, : 1 : 105 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 2 contents Detail