BMRBj - BMREntryMaster

Found 1 Document (1.953 seconds)

BMRB: 5783

2YXF

1H chemical shift assignments for a mutant of human beta2-microglobulin where ARG 3 is replaced by Ala

Authors

Corazza, A., Pettirossi, F., Verdone, G., Viglino, P., Esposito, G.

Assembly

Arg3Ala beta2-microglobulin

Entity

1. Arg3Ala beta2-microglobulin (polymer, Thiol state: all disulfide bound), 100 monomers, 11777.11 Da Detail

MIQATPKIQV YSRHPAENGK SNFLNCYVSG FHPSDIEVDL LKNGERIEKV EHSDLSFSKD WSFYLLYYTE FTPTEKDEYA CRVNHVTLSQ PKIVKWDRDM

Formula weight

11777.11 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS26:SG	1:CYS81:SG

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.0 %, Completeness: 78.0 %, Completeness (bb): 93.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	78.0 % (494 of 633)	78.0 % (494 of 633)
Backbone	93.9 % (186 of 198)	93.9 % (186 of 198)
Sidechain	70.8 % (308 of 435)	70.8 % (308 of 435)
Aromatic	58.0 % (40 of 69)	58.0 % (40 of 69)
Methyl	91.3 % (42 of 46)	91.3 % (42 of 46)

1. beta2-microglobulin

MIQATPKIQV YSRHPAENGK SNFLNCYVSG FHPSDIEVDL LKNGERIEKV EHSDLSFSKD WSFYLLYYTE FTPTEKDEYA CRVNHVTLSQ PKIVKWDRDM

Show sample condition

Sample

Temperature 310 (±0.1) K, pH 6.5 (±0.1)

#	Name	Concentration
1	beta2-microglobulin	0.7 mM
2	sodium phosphate	70 mM
3	sodium chloride	100 mM
4	H2O	100 %

Release date

2003-04-23

Citation 1

Properties of some variants of human beta2-microglobulin and amyloidogenesis
Corazza, A., Pettirossi, F., Viglino, P., Verdone, G., Garcia, J., Dumy, P., Giorgetti, S., Mangione, P., Andreola, A., Stoppini, M., Bellotti, V., Esposito, G.
J. Biol. Chem. (2004), 279, 9176-9189, PubMed 14660575 , DOI 10.1074/jbc.M310779200 , Abstract

Show more 2 citaions

Citation 2

The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition
Verdone, G., Corazza, A., Viglino, P., Pettirossi, F., Giorgetti, S., Mangione, P., Andreola, A., Stoppini, M., Bellotti, V., Esposito, G.
Protein Sci. (2002), 11, 487-499, PubMed 11847272 , DOI 10.1110/ps.29002 , Abstract

Citation 3

Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation
Esposito, G., Michelutti, R., Verdone, G., Viglino, P., Hernandez, H., Robinson, C.V., Amoresano, A., Dal Piaz, F., Monti, M., Pucci, P., Mangione, P., Stoppini, M., Merlini, G., Ferri, G., Bellotti, V.
Protein Sci. (2000), 9, 831-845, PubMed 10850793 , DOI 10.1110/ps.9.5.831 , Abstract

Hide non-primary 2 citaions

Entries sharing articles BMRB: 3 entries Detail

  BMRB: 5782 released on 2003-04-23
    Title 1H chemical shift assignment for the truncated form of the human beta2-microglobulin lacking of the first 3 residues
  BMRB: 5784 released on 2003-04-23
    Title 1H assignment of a human variant of beta2-microglobulin where His 31 was replaced by a Tyr
  BMRB: 5169 released on 2002-05-05
    Title NMR solution structure of the human beta2-microglobulin

Related entities 1. Arg3Ala beta2-microglobulin, : 1 : 103 : 184 entities Detail

Interaction partners 1. Arg3Ala beta2-microglobulin, : 121 interactors Detail

More details for 121 interactors identified by 43 citations

Experiments performed 2 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5783_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:26:CYS:SG	1:81:CYS:SG	unknown	unknown	n/a

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

None

Non-standard residues

None

Content subtype: bmr5783_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	587		98.0 (chain: 1, length: 100)
1	Chemical shift references	chemical_shift_reference	OK	1		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 100, Sequence coverage: 98.0%
- Total number of assignments
  - ¹H chemical shifts: 587
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
85	HIS	HD1	7.554

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	633	502	79.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	198	191	96.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	435	311	71.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	42	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	39	56.5

Keywords amyloidosis, beta2-microglobulin

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Found 1 Document (1.953 seconds)

BMRB: 5783

Sample

Entries sharing articles BMRB: 3 entries Detail

Related entities 1. Arg3Ala beta2-microglobulin, : 1 : 103 : 184 entities Detail

Interaction partners 1. Arg3Ala beta2-microglobulin, : 121 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail