BMRBj - BMREntryMaster

Found 1 Document (0.402 seconds)

BMRB: 15522

2KN8

Solution structure of pUL89(580-600) from Human Cytomegalovirus at pH 6.8.

Authors

Couvreux, A., Champier, G., Marquant, R., Hantz, S., Alain, S., Morellet, N., Bouaziz, S.

Assembly

pUL89(580-600)

Entity

1. pUL89(580-600) (polymer, Thiol state: not present), 21 monomers, 2399.703 Da Detail

GRDKALAVEQ FISRFNSGYI K

Formula weight

2399.703 Da

Source organism

Human betaherpesvirus 5

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 95.2 %, Completeness: 96.3 %, Completeness (bb): 90.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	96.3 % (129 of 134)	96.3 % (129 of 134)
Backbone	90.9 % (40 of 44)	90.9 % (40 of 44)
Sidechain	98.9 % (89 of 90)	98.9 % (89 of 90)
Aromatic	100.0 % (14 of 14)	100.0 % (14 of 14)
Methyl	100.0 % (10 of 10)	100.0 % (10 of 10)

1. pUL89(580-600)

GRDKALAVEQ FISRFNSGYI K

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 280 K, pH 6.8 (±0.25), Details TFE was used to allow folding of the peptide

#	Name	Isotope labeling	Type	Concentration
1	pUL89(580-600)	natural abundance		1.4 mM
2	TFE	[U-99% 2H]		30 %

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 97.0 %, Completeness (bb): 94.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	97.0 % (260 of 268)	97.0 % (260 of 268)
Backbone	94.3 % (83 of 88)	94.3 % (83 of 88)
Sidechain	98.3 % (177 of 180)	98.3 % (177 of 180)
Aromatic	92.9 % (26 of 28)	92.9 % (26 of 28)
Methyl	100.0 % (20 of 20)	100.0 % (20 of 20)

1. pUL89(580-600)

GRDKALAVEQ FISRFNSGYI K

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 280 K, pH 2.8 (±0.25), Details TFE was used to allow folding of the peptide

#	Name	Isotope labeling	Type	Concentration
1	pUL89(580-600)	natural abundance		1.4 mM
2	TFE	[U-99% 2H]		30 %

Release date

2007-10-16

Citation

Solution structure of the small terminase subunit interaction domain of pUL89 within the Human Cytomegalovirus terminase complex
Couvreux, A., Champier, G., Marquant, R., Hantz, S., Alain, S., Morellet, N., Bouaziz, S.
Biochem. J.

Related entities 1. pUL89(580-600), : 1 : 4 : 4 entities Detail

Experiments performed 2 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr15522_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: bmr15522_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	149	95.2 (chain: 1, length: 21)
2	Assigned chemical shifts	assigned_chem_shift_list_2	OK	151	100.0 (chain: 1, length: 21)
1	Chemical shift references	chemical_shift_reference_1	OK	1	No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 21, Sequence coverage: 95.2%
- Total number of assignments
  - ¹H chemical shifts: 149
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: assigned_chem_shift_list_2
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 21, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 151
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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	134	129	96.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	44	40	90.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	89	98.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	10	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	14	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	134	131	97.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	44	43	97.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	88	97.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	10	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	12	85.7

Keywords 21 amino acids, amphipatic, helix, peptide

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Found 1 Document (0.402 seconds)

BMRB: 15522

Sample

Sample

Related entities 1. pUL89(580-600), : 1 : 4 : 4 entities Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

Chemical shift validation 4 contents Detail