BMRBj - BMREntryMaster

Found 1 Document (1.703 seconds)

BMRB: 5509

7Y1I

Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin

Authors

Liu, K., Kelly, J., Wemmer, D.

Assembly

Transthyretin

Entity

1. Transthyretin (polymer, Thiol state: all free), 128 monomers, 13924.48 × 4 Da Detail

MGPTGTGESK CPLMVKVLDA VRGSPAINVA MHVFRKAADD TWEPFASGKT SESGELHGLT TEEEFVEGIY KVEIDTKSYW KALGISPFHE HAEVVFTAND SGPRRYTIAA LLSPYSYSTT AVVTNPKE

Total weight

55697.92 Da

Max. entity weight

13924.48 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 30.7 %, Completeness (bb): 52.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	30.7 % (440 of 1431)	22.1 % (162 of 733)	27.2 % (156 of 573)	97.6 % (122 of 125)
Backbone	52.9 % (398 of 752)	51.2 % (132 of 258)	39.3 % (147 of 374)	99.2 % (119 of 120)
Sidechain	6.9 % (55 of 797)	6.7 % (32 of 475)	6.3 % (20 of 317)	60.0 % (3 of 5)
Aromatic	3.1 % (4 of 130)	3.1 % (2 of 65)	0.0 % (0 of 63)	100.0 % (2 of 2)
Methyl	9.3 % (13 of 140)	8.6 % (6 of 70)	10.0 % (7 of 70)

1. Transthyretin

MGPTGTGESK CPLMVKVLDA VRGSPAINVA MHVFRKAADD TWEPFASGKT SESGELHGLT TEEEFVEGIY KVEIDTKSYW KALGISPFHE HAEVVFTAND SGPRRYTIAA LLSPYSYSTT AVVTNPKE

Show sample condition

Sample

Temperature 298 (±1) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Transthyretin	[U-C13; U-N15]		0.3 ~ 1.5 mM
2	D2O			100 %

Release date

2003-01-26

Citation

Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin
Liu, K., Kelly, J., Wemmer, D.
J. Mol. Biol. (2002), 320, 821-832, PubMed 12095258 , DOI: , Abstract

Entries sharing articles BMRB: 3 entries Detail

  BMRB: 5507 released on 2003-01-26
    Title Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin
  BMRB: 5508 released on 2003-01-26
    Title Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin
  BMRB: 5510 released on 2003-01-26
    Title Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin

Related entities 1. Transthyretin, : 1 : 26 : 45 : 93 entities Detail

Interaction partners 1. Transthyretin, : 50 interactors Detail

More details for 50 interactors identified by 11 citations

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5509_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: bmr5509_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	TTR_V30M_cs	Warning	370		100.0 (chain: 1, length: 128)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: TTR_V30M_cs
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 128, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 128
  - ¹⁵N chemical shifts: 121
  - ¹H chemical shifts: 121
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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	573	128	22.3
¹⁵N chemical shifts	129	121	93.8
¹H chemical shifts	733	121	16.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	256	128	50.0
¹⁵N chemical shifts	120	119	99.2
¹H chemical shifts	258	119	46.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	317	0	0.0
¹⁵N chemical shifts	9	2	22.2
¹H chemical shifts	475	2	0.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	73	0	0.0
¹H chemical shifts	73	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	63	0	0.0
¹⁵N chemical shifts	2	2	100.0
¹H chemical shifts	65	2	3.1

Keywords transthyretin, amyloid, hydrogen exchange, NMR spectroscopy, protection factor

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Found 1 Document (1.703 seconds)

BMRB: 5509

Sample

Entries sharing articles BMRB: 3 entries Detail

Related entities 1. Transthyretin, : 1 : 26 : 45 : 93 entities Detail

Interaction partners 1. Transthyretin, : 50 interactors Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail