BMRBj - BMREntryMaster

Found 1 Document (3.383 seconds)

BMRB: 30734

2MSD

NMR-driven structure of KRAS4B-GTP homodimer on a lipid bilayer nanodisc

Authors

Lee, K., Fang, Z., Enomoto, M., Gasmi-Seabrook, G.M., Zheng, L., Marshall, C.B., Ikura, M.

Assembly

Apolipoprotein A-I, GTPase KRas

Entity

1. Apolipoprotein A-I, GTPase KRas, entity 1 (polymer, Thiol state: not present), 200 monomers, 23196.96 × 2 Da Detail

GPLKLLDNWD SVTSTFSKLR EQLGPVTQEF WDNLEKETEG LRQEMSKDLE EVKAKVQPYL DDFQKKWQEE MELYRQKVEP LRAELQEGAR QKLHELQEKL SPLGEEMRDR ARAHVDALRT HLAPYSDELR QRLAARLEAL KENGGARLAE YHAKATEHLS TLSEKAKPAL EDLRQGLLPV LESFKVSFLS ALEEYTKKLN

2. Apolipoprotein A-I, GTPase KRas, entity 2 (polymer), 185 monomers, 21094.72 × 2 Da Detail

STEYKLVVVG ADGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL PSRTVDTKQA QDLARSYGIP FIETSAKTRQ GVDDAFYTLV REIRKHKEKM SKDGKKKKKK SKTKC

3. Apolipoprotein A-I, GTPase KRas, entity PCW (non-polymer), 787.121 × 64 Da
4. Apolipoprotein A-I, GTPase KRas, entity 17F (non-polymer), 788.043 × 16 Da
5. Apolipoprotein A-I, GTPase KRas, entity GSP (non-polymer), 539.246 × 2 Da
6. Apolipoprotein A-I, GTPase KRas, entity MG (non-polymer), 24.305 × 2 Da

Total weight

152694.88 Da

Max. entity weight

23196.96 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 16.6 %, Completeness: 6.2 %, Completeness (bb): 5.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	6.2 % (283 of 4597)	6.0 % (146 of 2419)	5.8 % (103 of 1773)	8.4 % (34 of 405)
Backbone	5.6 % (127 of 2286)	6.2 % (48 of 777)	4.1 % (47 of 1136)	8.6 % (32 of 373)
Sidechain	6.5 % (175 of 2677)	6.2 % (102 of 1642)	7.0 % (70 of 1003)	9.4 % (3 of 32)
Aromatic	4.2 % (12 of 286)	4.2 % (6 of 143)	4.3 % (6 of 140)	0.0 % (0 of 3)
Methyl	21.2 % (86 of 406)	22.2 % (45 of 203)	20.2 % (41 of 203)

1. entity 1

2. entity 2

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 7.4, Details 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	KRAS4B	[ILV 13C-methyl; Lys 15N-amide]		80 uM

Protein Blocks Logo

Calculated from 20 models in PDB: 6W4E, Strand ID: A, B, C, D Detail

Release date

2020-04-07

Citation

Two Distinct Structures of Membrane-Associated Homodimers of GTP- and GDP-Bound KRAS4B Revealed by Paramagnetic Relaxation Enhancement
Lee, K.Y., Fang, Z., Enomoto, M., Seabrook, G.G., Zheng, L., Koide, S., Ikura, M., Marshall, C.B.
Angew. Chem Int Ed Engl. (2020), 59, 11037-11045, PubMed 32227412 , DOI 10.1002/anie.202001758 , Abstract

Related entities 1. Apolipoprotein A-I, GTPase KRas, entity 1, : 1 : 9 : 11 : 109 entities Detail

Related entities 2. Apolipoprotein A-I, GTPase KRas, entity 2, : 100 entities Detail

Interaction partners 1. Apolipoprotein A-I, GTPase KRas, entity 1, : 37 interactors Detail

More details for 37 interactors identified by 22 citations

Experiments performed 2 experiments Detail

Chemical shift validation 8 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30734_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: bmr30734_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	154		23.8 (chain: 2, length: 185)
1	Chemical shift references	chem_shift_reference_1	OK	1		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 2, Chain length: 185, Sequence coverage: 23.8%
- Total number of assignments
  - ¹H chemical shifts: 108
  - ¹⁵N chemical shifts: 15
  - ¹³C chemical shifts: 31
- Completeness of assignments
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 2

Keywords GTPase, ONCOPROTEIN, nanodisc

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Found 1 Document (3.383 seconds)

BMRB: 30734

Sample

Related entities 1. Apolipoprotein A-I, GTPase KRas, entity 1, : 1 : 9 : 11 : 109 entities Detail

Related entities 2. Apolipoprotein A-I, GTPase KRas, entity 2, : 100 entities Detail

Interaction partners 1. Apolipoprotein A-I, GTPase KRas, entity 1, : 37 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

Chemical shift validation 8 contents Detail