BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	74.0 % (1088 of 1471)	70.4 % (534 of 758)	78.4 % (449 of 573)	75.0 % (105 of 140)
Backbone	86.2 % (614 of 712)	86.0 % (208 of 242)	85.8 % (302 of 352)	88.1 % (104 of 118)
Sidechain	65.6 % (573 of 873)	63.2 % (326 of 516)	73.4 % (246 of 335)	4.5 % (1 of 22)
Aromatic	62.2 % (112 of 180)	64.4 % (58 of 90)	59.6 % (53 of 89)	100.0 % (1 of 1)
Methyl	93.7 % (118 of 126)	93.7 % (59 of 63)	93.7 % (59 of 63)

1. entity 1

MFIGDSQVFI EKRSKDSKFV FSIVYNGFTL GVWVDVNQGL MYIDTAHDPS TKNVYTLTTD DLNENMMLIT NYKNNYHLRK LASAFMNGYL RFDNQVIRNI AYELFRKMRI QLEHHHHHH

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-15N] protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	protein	[U-15N]		1 uM
2	MES	natural abundance		50 mM

Sample #2

Solvent system 99.9% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-13C] protein, 99.9% D2O

#	Name	Isotope labeling	Type	Concentration
3	protein	[U-13C]		1 uM
4	MES	[U-2H]		50 mM

Sample #3

Solvent system 90% H2O/10% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM U-15N, U-13C protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein	U-15N, U-13C		1 uM
6	MES	natural abundance		50 mM

Protein Blocks Logo

Calculated from 15 models in PDB: 6V1W, Strand ID: A Detail

Release date

2019-11-25

Citation

Structure and dynamics of the P7 protein from the bacteriophage phi 12
Woodson, M., Pajak, J., Mahler, B.P., Zhao, W., Zhang, W., Arya, G., White, M.A., Jardine, P.J., Morais, M.C.
J. Mol. Biol. (2008), 382, 402-422, PubMed 18647606 , DOI 10.1016/j.jmb.2008.07.006 , Abstract

Related entities 1. DNA packaging protein (E.C.3.6.4.-), : 1 : 2 : 2 entities Detail

Experiments performed 12 experiments Detail

1 3D 15N NOESY-HSQC

Instrument

Bruker AVANCE III - 750 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-15N] protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	protein	[U-15N]		1 uM
2	MES	natural abundance		50 mM

2 3D 13C-edited NOESY-HSQC aliphatic

Instrument

Bruker AVANCE III - 750 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 99.9% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-13C] protein, 99.9% D2O

#	Name	Isotope labeling	Type	Concentration
3	protein	[U-13C]		1 uM
4	MES	[U-2H]		50 mM

3 3D 13C-editied NOESY-HSQC aromatic

Instrument

Bruker AVANCE III - 750 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 99.9% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-13C] protein, 99.9% D2O

#	Name	Isotope labeling	Type	Concentration
3	protein	[U-13C]		1 uM
4	MES	[U-2H]		50 mM

4 3D HSQC-NOESY-HSQC

Instrument

Bruker AVANCE III - 750 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 99.9% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-13C] protein, 99.9% D2O

#	Name	Isotope labeling	Type	Concentration
3	protein	[U-13C]		1 uM
4	MES	[U-2H]		50 mM

5 HD-exchange

Instrument

Bruker AVANCE III - 750 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-15N] protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	protein	[U-15N]		1 uM
2	MES	natural abundance		50 mM

6 3D HNCA

Instrument

Bruker AVANCE III - 600 MHz QCI cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM U-15N, U-13C protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein	U-15N, U-13C		1 uM
6	MES	natural abundance		50 mM

7 3D HNCACB

Instrument

Bruker AVANCE III - 600 MHz QCI cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM U-15N, U-13C protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein	U-15N, U-13C		1 uM
6	MES	natural abundance		50 mM

8 3D CBCA(CO)NH

Instrument

Bruker AVANCE III - 800 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM U-15N, U-13C protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein	U-15N, U-13C		1 uM
6	MES	natural abundance		50 mM

9 3D 1H-15N TOCSY

Instrument

Bruker AVANCE III - 750 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-15N] protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	protein	[U-15N]		1 uM
2	MES	natural abundance		50 mM

10 3D HCCH-TOCSY

Instrument

Bruker AVANCE III - 800 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 99.9% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-13C] protein, 99.9% D2O

#	Name	Isotope labeling	Type	Concentration
3	protein	[U-13C]		1 uM
4	MES	[U-2H]		50 mM

11 3D HCCH-TOCSY

Instrument

Bruker AVANCE III - 750 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 99.9% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM [U-13C] protein, 99.9% D2O

#	Name	Isotope labeling	Type	Concentration
3	protein	[U-13C]		1 uM
4	MES	[U-2H]		50 mM

12 3D HNCO

Instrument

Bruker AVANCE III - 800 MHz TCI cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1013 mbar, Temperature 303 K, pH 6.0, Details 1 uM U-15N, U-13C protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein	U-15N, U-13C		1 uM
6	MES	natural abundance		50 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30691_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: bmr30691_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1185		88.2 (chain: 1, length: 119)
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: 119, Sequence coverage: 88.2%
- Total number of assignments
  - ¹H chemical shifts: 641
  - ¹³C chemical shifts: 441
  - ¹⁵N chemical shifts: 103
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Tautomeric state of HIS
- 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	758	519	68.5
¹³C chemical shifts	573	441	77.0
¹⁵N chemical shifts	140	103	73.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	242	205	84.7
¹³C chemical shifts	238	199	83.6
¹⁵N chemical shifts	118	102	86.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	516	314	60.9
¹³C chemical shifts	335	242	72.2
¹⁵N chemical shifts	22	1	4.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	61	88.4
¹³C chemical shifts	69	61	88.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	57	63.3
¹³C chemical shifts	89	52	58.4
¹⁵N chemical shifts	1	1	100.0

Keywords RNase H fold, VIRAL PROTEIN, terminase, viral packaging motor

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Found 1 Document (0.558 seconds)

BMRB: 30691

Sample #1

Sample #2

Sample #3

Related entities 1. DNA packaging protein (E.C.3.6.4.-), : 1 : 2 : 2 entities Detail

Experiments performed 12 experiments Detail

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Chemical shift validation 3 contents Detail