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Found 1 Document (2.827 seconds)

BMRB: 5123

1C7P

Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy

Authors

Chamberlain, A.K., Receveur, V., Spencer, A., Redfield, C., Dobson, C.M.

Assembly

Human Lysozyme

Entity

1. Human Lysozyme (polymer, Thiol state: not reported), 130 monomers, 14700.53 Da Detail

KVFERCELAR TLKRLGMDGY RGISLANWMC LAKWESGYNT RATNYNAGDR STDYGIFQIN SRYWCNDGKT PGAVNACHLS CSALLQDNIA DAVACAKRVV RDPQGIRAWV AWRNRCQNRD VRQYVQGCGV

Formula weight

14700.53 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.6 %, Completeness: 29.2 %, Completeness (bb): 64.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	29.2 % (269 of 920)	18.9 % (146 of 771)	82.6 % (123 of 149)
Backbone	64.0 % (254 of 397)	48.7 % (131 of 269)	96.1 % (123 of 128)
Sidechain	2.9 % (15 of 523)	3.0 % (15 of 502)	0.0 % (0 of 21)
Aromatic	0.0 % (0 of 71)	0.0 % (0 of 66)	0.0 % (0 of 5)
Methyl	1.6 % (1 of 63)	1.6 % (1 of 63)

1. lysozyme

KVFERCELAR TLKRLGMDGY RGISLANWMC LAKWESGYNT RATNYNAGDR STDYGIFQIN SRYWCNDGKT PGAVNACHLS CSALLQDNIA DAVACAKRVV RDPQGIRAWV AWRNRCQNRD VRQYVQGCGV

Show sample condition

Sample

Temperature 310 (±1) K, pH 5.0 (±0.2)

#	Name	Concentration
1	lysozyme	0.8 ~ 1.2 mM
2	HCl	0.0 ~ 0.0 mM
3	H2O	100 %

Release date

2002-01-24

Citation

Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy
Chamberlain, A.K., Receveur, V., Spencer, A., Redfield, C., Dobson, C.M.
Protein Sci. (2001), 10, 2525-2530, PubMed 11714920 , DOI 10.1110/ps.28101 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 5124 released on 2002-01-24
    Title Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy
  BMRB: 5125 released on 2002-01-24
    Title Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy

Related entities 1. Human Lysozyme, : 1 : 39 : 39 : 25 : 144 entities Detail

Interaction partners 1. Human Lysozyme, : 41 interactors Detail

More details for 41 interactors identified by 13 citations

Experiments performed 3 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5123_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: bmr5123_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_set_1	Warning	246		94.6 (chain: 1, length: 130)
1	Chemical shift references	chemical_shift_reference	OK	1		No information

Assigned chemical shifts

Saveframe: chemical_shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 130, Sequence coverage: 94.6%
- Total number of assignments
  - ¹H chemical shifts: 123
  - ¹⁵N chemical shifts: 123
- 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	771	123	16.0
¹⁵N chemical shifts	163	123	75.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	269	123	45.7
¹⁵N chemical shifts	128	123	96.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	502	0	0.0
¹⁵N chemical shifts	35	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	65	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	66	0	0.0
¹⁵N chemical shifts	5	0	0.0

Keywords amyloid fibrils, backbone dynamics, lysozyme, mutant, NMR

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Found 1 Document (2.827 seconds)

BMRB: 5123

Sample

Entries sharing articles BMRB: 2 entries Detail

Related entities 1. Human Lysozyme, : 1 : 39 : 39 : 25 : 144 entities Detail

Interaction partners 1. Human Lysozyme, : 41 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail