BMRBj - BMREntryMaster

Found 1 Document (0.614 seconds)

BMRB: 50188

6M78

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

Single Chain Pro-VPg

Entity

1. Single Chain Pro-VPg (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

Formula weight

32189.09 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

RDCs, assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 87.5 %, Completeness: 31.5 %, Completeness (bb): 55.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	31.5 % (1049 of 3334)	18.5 % (317 of 1715)	38.7 % (508 of 1312)	73.0 % (224 of 307)
Backbone	55.2 % (961 of 1742)	40.6 % (245 of 604)	57.5 % (494 of 859)	79.6 % (222 of 279)
Sidechain	16.4 % (304 of 1859)	6.5 % (72 of 1111)	31.9 % (230 of 720)	7.1 % (2 of 28)
Aromatic	1.4 % (4 of 286)	1.4 % (2 of 143)	0.0 % (0 of 135)	25.0 % (2 of 8)
Methyl	22.0 % (66 of 300)	29.3 % (44 of 150)	14.7 % (22 of 150)

1. entity 1

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	potassium phosphate buffer	natural abundance	20 mM
3	NaCl	natural abundance	50 mM
4	EDTA	natural abundance	1 mM
5	sodium azide	natural abundance	0.01 %

Protein Blocks Logo

Calculated from 4 models in PDB: 6M78, Strand ID: A, B Detail

RDC

111 RDC values in 1 lists
Field strength (¹H) 700 MHz, Pressure 1 atm, Temperature 298 K, pH 7 Detail

Release date

2020-02-06

Citation

Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein
Dixit, K., Karanth, M.N., Nair, S., 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: 50193 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. Single Chain Pro-VPg, : 1 : 7 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr50188_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: bmr50188_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1000		85.1 (chain: 1, length: 296)
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: 1, Chain length: 296, Sequence coverage: 85.1%
- Total number of assignments
  - ¹³C chemical shifts: 461
  - ¹H chemical shifts: 322
  - ¹⁵N chemical shifts: 217
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- 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 (%)
¹³C chemical shifts	859	461	53.7
¹H chemical shifts	604	215	35.6
¹⁵N chemical shifts	279	215	77.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	158	15	9.5
¹H chemical shifts	158	35	22.2

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Found 1 Document (0.614 seconds)

BMRB: 50188

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Single Chain Pro-VPg, : 1 : 7 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	1312	461	35.1
¹H chemical shifts	1715	252	14.7
¹⁵N chemical shifts	307	217	70.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	720	211	29.3
¹H chemical shifts	1111	37	3.3
¹⁵N chemical shifts	28	2	7.1