BMRBj - BMREntryMaster

Found 1 Document (0.355 seconds)

BMRB: 17985

2LK9

Structure of BST-2/Tetherin Transmembrane Domain

Authors

Skasko, M., Wang, Y., Tian, Y., Tokarev, A., Munguia, J., Ruiz, A., Stephens, E., Opella, S., Guatelli, J.

Assembly

BST-2

Entity

1. BST-2 (polymer, Thiol state: not present), 24 monomers, 2529.321 Da Detail

LLLGIGILVL LIIVILGVPL IIFT

Formula weight

2529.321 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 23.3 %, Completeness (bb): 49.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	23.3 % (70 of 300)	15.4 % (23 of 149)	18.8 % (24 of 128)	100.0 % (23 of 23)
Backbone	49.3 % (70 of 142)	46.0 % (23 of 50)	34.8 % (24 of 69)	100.0 % (23 of 23)
Sidechain	0.0 % (0 of 179)	0.0 % (0 of 99)	0.0 % (0 of 80)
Aromatic	0.0 % (0 of 10)	0.0 % (0 of 5)	0.0 % (0 of 5)
Methyl	0.0 % (0 of 74)	0.0 % (0 of 37)	0.0 % (0 of 37)

1. BST-2

LLLGIGILVL LIIVILGVPL IIFT

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 7.4

#	Name	Isotope labeling	Concentration
1	BST-2	[U-100% 15N]	0.5 mM
2	H2O	[U-100% 15N]	90 %
3	D2O	[U-100% 15N]	10 %

Protein Blocks Logo

Calculated from 1 models in PDB: 2LK9, Strand ID: A Detail

Release date

2011-12-11

Citation

HIV-1 Vpu protein antagonizes innate restriction factor BST-2 via lipid-embedded helix-helix interactions
Skasko, M., Wang, Y., Tian, Y., Tokarev, A., Munguia, J., Ruiz, A., Stephens, E.B., Opella, S.J., Guatelli, J.
J. Biol. Chem. (2012), 287, 58-67, PubMed 22072710 , DOI 10.1074/jbc.M111.296772 , Abstract

Experiments performed 2 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, RDC restraints	combined_17985_2lk9.nef
Input source #2: Coordindates	2lk9.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	Warning

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

--20-------30--------40--------50--
KRSKLLLGIGILVLLIIVILGVPLIIFTIKKKKKK
|||||||||||||||||||||||||||||||||||
KRSKLLLGIGILVLLIIVILGVPLIIFTIKKKKKK
--------10--------20--------30-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	35	0	0	100.0

Content subtype: combined_17985_2lk9.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	70		68.6 (chain: A, length: 35)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_2	OK	23 (23)	.	65.7 (chain: A, length: 35)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 68.6%
- Total number of assignments
  - ¹H chemical shifts: 23
  - ¹³C chemical shifts: 24
  - ¹⁵N chemical shifts: 23
- Completeness of assignments
  - Entity_assemble_ID: A
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	249	23	9.2
¹³C chemical shifts	190	24	12.6
¹⁵N chemical shifts	35	23	65.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	72	23	31.9
¹³C chemical shifts	70	24	34.3
¹⁵N chemical shifts	34	23	67.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	177	0	0.0
¹³C chemical shifts	120	0	0.0
¹⁵N chemical shifts	1	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	0	0.0
¹³C chemical shifts	39	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	0	0.0
¹³C chemical shifts	5	0	0.0

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 65.7%
- Total number of restraints: 23
- Potential type of restraints: undefined (23)
- Range of observed RDC values: 100.0, -100.0 (Hz)
- RDC restraints per residue
  - Chain_ID: A
    None

Keywords BST-2, Membrane, Micelle, NMR, Vpu

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Found 1 Document (0.355 seconds)

BMRB: 17985

Sample

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail