BMRBj - BMREntryMaster

Found 1 Document (1.258 seconds)

BMRB: 7149

4O9S

Characterization of the Molten Globule of Human Serum Retinol-Binding Protein using NMR Spectroscopy

Authors

Greene, L.H., Wijesinha-Bettoni, R., Redfield, C.

Assembly

RBP

Entity

1. RBP (polymer, Thiol state: all disulfide bound), 182 monomers, 20958.21 Da Detail

ERDCRVSSFR VKENFDKARF SGTWYAMAKK DPEGLFLQDN IVAEFSVDET GQMSATAKGR VRLLNNWDVC ADMVGTFTDT EDPAKFKMKY WGVASFLQKG NDDHWIVDTD YDTYAVQYSC RLLNLDGTCA DSYSFVFSRD PNGLPPEAQK IVRQRQEELC LARQYRLIVH NGYCDGRSER NL

Formula weight

20958.21 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS4:SG	1:CYS160:SG
2	disulfide	sing	1:CYS70:SG	1:CYS174:SG
3	disulfide	sing	1:CYS120:SG	1:CYS129:SG

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.6 %, Completeness: 29.8 %, Completeness (bb): 66.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	29.8 % (388 of 1303)	19.4 % (214 of 1105)	87.9 % (174 of 198)
Backbone	66.0 % (361 of 547)	50.5 % (187 of 370)	98.3 % (174 of 177)
Sidechain	3.6 % (27 of 756)	3.7 % (27 of 735)	0.0 % (0 of 21)
Aromatic	0.0 % (0 of 114)	0.0 % (0 of 110)	0.0 % (0 of 4)
Methyl	2.4 % (2 of 82)	2.4 % (2 of 82)

1. human serum retinol-binding protein

Show sample condition

Sample

Temperature 293 (±2) K, pH 2 (±0.05), Details 0.16mM 15N,2H-labeled RBP in 5mM sodium phosphate and 8M urea at pH 2 and 20C

#	Name	Isotope labeling	Type	Concentration
1	human serum retinol-binding protein	[U-15N; U-2H]	protein	0.16 mM
2	sodium phosphate			5 mM
3	urea			8 M

Release date

2006-10-29

Citation

Characterization of the molten globule of human serum retinol-binding protein using NMR spectroscopy
Greene, L.H., Wijesinha-Bettoni, R., Redfield, C.
Biochemistry (2006), 45, 9475-9484, PubMed 16878982 , DOI 10.1021/bi060229c , Abstract

Related entities 1. RBP, : 1 : 17 : 6 : 45 entities Detail

Interaction partners 1. RBP, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr7149_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	OK

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:4:CYS:SG	1:160:CYS:SG	unknown	unknown	n/a
1:70:CYS:SG	1:174:CYS:SG	unknown	unknown	n/a
1:120:CYS:SG	1:129: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: bmr7149_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	OK	348		95.6 (chain: 1, length: 182)
1	Chemical shift references	chemical_shift_referencing	OK	2		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 182, Sequence coverage: 95.6%
- Total number of assignments
  - ¹H chemical shifts: 174
  - ¹⁵N chemical shifts: 174
- 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	1105	174	15.7
¹⁵N chemical shifts	212	174	82.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	370	174	47.0
¹⁵N chemical shifts	177	174	98.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	735	0	0.0
¹⁵N chemical shifts	35	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	86	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	110	0	0.0
¹⁵N chemical shifts	4	0	0.0

Keywords monomeric RBP, molten globule, retinol-binding protein, RBP in 8M urea

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Found 1 Document (1.258 seconds)

BMRB: 7149

Sample

Related entities 1. RBP, : 1 : 17 : 6 : 45 entities Detail

Interaction partners 1. RBP, : 1 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail