BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	71.1 % (381 of 536)	82.4 % (229 of 278)	54.7 % (117 of 214)	79.5 % (35 of 44)
Backbone	73.0 % (187 of 256)	93.0 % (80 of 86)	57.8 % (74 of 128)	78.6 % (33 of 42)
Sidechain	70.5 % (227 of 322)	77.6 % (149 of 192)	59.4 % (76 of 128)	100.0 % (2 of 2)
Aromatic	32.6 % (15 of 46)	65.2 % (15 of 23)	0.0 % (0 of 23)
Methyl	79.3 % (46 of 58)	86.2 % (25 of 29)	72.4 % (21 of 29)

1. entity 1

MNKEHILAQK EVLTPIEYEH YVKHLFDIGE ITKELYIELS SDL

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Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.3, Details 20 mM potassium phosphate, 50 mM potassium chloride, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1		0.0 ~ 0.0 mM
2	potassium phosphate	natural abundance	20 mM
3	potassium chloride	natural abundance	50 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 6OBK, Strand ID: A Detail

Release date

2019-04-21

Citation

Structure determination of ORF47 from Lactococcus virus P2
Gagne, S.M.

Related entities 1. Uncharacterized protein ORF47, : 1 : 3 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30592_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	OK

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr30592_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	425		95.3 (chain: 1, length: 43)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 43, Sequence coverage: 95.3%
- Total number of assignments
  - ¹H chemical shifts: 276
  - ¹⁵N chemical shifts: 35
  - ¹³C chemical shifts: 114
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	278	228	82.0
¹⁵N chemical shifts	44	35	79.5
¹³C chemical shifts	214	114	53.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	86	80	93.0
¹⁵N chemical shifts	42	33	78.6
¹³C chemical shifts	86	39	45.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	192	148	77.1
¹⁵N chemical shifts	2	2	100.0
¹³C chemical shifts	128	75	58.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	30	24	80.0
¹³C chemical shifts	30	21	70.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	23	15	65.2
¹³C chemical shifts	23	0	0.0

Keywords VIRAL PROTEIN

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Found 1 Document (0.393 seconds)

BMRB: 30592

Sample

Related entities 1. Uncharacterized protein ORF47, : 1 : 3 entities Detail

Experiments performed 5 experiments Detail

Instrument

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Chemical shift validation 3 contents Detail