BMRBj - BMREntryMaster

Found 1 Document (0.365 seconds)

BMRB: 50193

6LXF

Structures of the free and bound forms of the intrinsically disordered plant viral genome-linked protein

Authors

Dixit, K., Karanth, M.N., Nair, S., Kumari, K., Chakraborti, K.S., Savitri, H.S., Sarma, S.P.

Assembly

VPg in bound state

Entity

1. VPg in bound state, entity 1 (polymer, Thiol state: all free), 296 monomers, 32189.09 Da Detail

MRGSHHHHHH GMASSLKLNV GDASNESAVL GSFYSPVKAG DEPASLVAIK SGPTTIGFGC RTKIDGEDCL LTAHHVWCNS MRPTGLAKAG KQVSVEDWEI SMSSSDKMLD FAIVRVPTHV WSKLGVKSTP LVCPSSKDVI TCYGGSSSDC LMSGVGSSST SEFTWKLTHT CPTAAGWAGT PLYSSRGVVG MHVGFEEIGK LNRGVNMFYV ANYLLRSNET LPPELSIIEI PFDDVETRSY EFIEVEIKGR GKAKLGKREF AWIPESGKYW ADEDEDELPP PPKLVGGKLV WENAQE

2. VPg in bound state, entity 2 (polymer, Thiol state: all free), 57 monomers, 6560.352 Da Detail

GSMTLPPELS IIEIPFDDVE TRSYEFIEVE IKGRGKAKLG KREFAWIPES GKYWADE

Total weight

38749.44 Da

Max. entity weight

32189.09 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 16.7 %, Completeness: 7.4 %, Completeness (bb): 12.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	7.4 % (297 of 4026)	3.9 % (82 of 2077)	10.2 % (162 of 1584)	14.5 % (53 of 365)
Backbone	12.0 % (250 of 2076)	7.5 % (54 of 719)	14.1 % (145 of 1025)	15.4 % (51 of 332)
Sidechain	4.0 % (91 of 2269)	2.1 % (28 of 1358)	6.9 % (61 of 878)	6.1 % (2 of 33)
Aromatic	1.1 % (4 of 356)	1.1 % (2 of 178)	0.0 % (0 of 168)	20.0 % (2 of 10)
Methyl	9.9 % (35 of 354)	9.6 % (17 of 177)	10.2 % (18 of 177)

1. entity 1

2. entity 2

GSMTLPPELS IIEIPFDDVE TRSYEFIEVE IKGRGKAKLG KREFAWIPES GKYWADE

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7, Details U-2H, 15N, 13C-provpg selectively labeled ILV

#	Name	Isotope labeling	Concentration
1	entity_1	[U-100% 13C; U-100% 15N; U-80% 2H]	0.3 (±0.02) mM
2	entity_2	[U-100% 13C; U-100% 15N; U-80% 2H]	0.3 (±0.01) mM
3	potassium phosphate buffer	natural abundance	20 mM
4	NaCl	natural abundance	50 mM
5	EDTA	natural abundance	1 mM
6	sodium azide	natural abundance	0.01 %

Release date

2020-02-06

Citation

Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein
Nair, S., Dixit, K., Karanth, M.N., Kumari, K., Chakraborti, K.S., Savitri, H.S., Sarma, S.P.
Biochemistry (2020), 59, 4663-4680, PubMed 33269926 , DOI 10.1021/acs.biochem.0c00721 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 50188 released on 2020-02-06
Title Structures of the free and bound forms of the intrinsically disordered plant viral genome-linked protein

Related entities 1. VPg in bound state, entity 1, : 7 entities Detail

Related entities 2. VPg in bound state, entity 2, : 1 : 1 : 1 : 4 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr50193_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: bmr50193_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	286		94.7 (chain: 2, length: 57)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 2, Chain length: 57, Sequence coverage: 94.7%
- Total number of assignments
  - ¹³C chemical shifts: 152
  - ¹H chemical shifts: 85
  - ¹⁵N chemical shifts: 49
- Completeness of assignments
  - Entity_assemble_ID: 2
- Peptide bond of PRO
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	272	152	55.9
¹H chemical shifts	362	61	16.9
¹⁵N chemical shifts	58	49	84.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	166	140	84.3
¹H chemical shifts	115	47	40.9
¹⁵N chemical shifts	53	47	88.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	158	54	34.2
¹H chemical shifts	247	14	5.7
¹⁵N chemical shifts	5	2	40.0

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.365 seconds)

BMRB: 50193

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. VPg in bound state, entity 1, : 7 entities Detail

Related entities 2. VPg in bound state, entity 2, : 1 : 1 : 1 : 4 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 4 contents Detail