BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	95.5 % (977 of 1023)	95.4 % (514 of 539)	97.7 % (385 of 394)	86.7 % (78 of 90)
Backbone	96.9 % (469 of 484)	95.1 % (156 of 164)	97.9 % (235 of 240)	97.5 % (78 of 80)
Sidechain	94.8 % (585 of 617)	95.5 % (358 of 375)	97.8 % (227 of 232)	0.0 % (0 of 10)
Aromatic	95.2 % (59 of 62)	90.3 % (28 of 31)	100.0 % (31 of 31)
Methyl	97.8 % (90 of 92)	97.8 % (45 of 46)	97.8 % (45 of 46)

1. entity 1

MAVNKNEYKI LIMLKENQCT TELKSFTYTK LCNISKLSMS TVRRSIKKFL ELQYVKEGCK QGISKTFYIT PNGIEKLKSI M

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Sample

Solvent system 90% H2O/10% D2O, Pressure 1 (±0.05) atm, Temperature 298 (±0.1) K, pH 6.4 (±0.1), Details 225 uM [U-15N] TubR, 25 mM potassium phosphate, 50 mM potassium chloride, 2 mM D-10 DTT, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

Protein Blocks Logo

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

Release date

2020-07-13

Citation

Structure of TubR protein fragment from Clostridium Botulinum's phage c-st
Valverde, P., Canada, F.J., Jimenez-Barbero, J., Oliva, M.A.

Related entities 1. DNA-binding protein TubR, : 1 : 1 : 4 entities Detail

Experiments performed 14 experiments Detail

1 3D HNCO

Instrument

Bruker AVANCE - 600 MHz crioprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 (±0.05) atm, Temperature 298 (±0.1) K, pH 6.4 (±0.1), Details 225 uM [U-15N] TubR, 25 mM potassium phosphate, 50 mM potassium chloride, 2 mM D-10 DTT, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

2 3D HN(CO)CA

Instrument

Bruker AVANCE - 600 MHz crioprobe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

3 3D HNCA

Instrument

Bruker AVANCE - 600 MHz crioprobe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

4 3D CBCA(CO)NH

Instrument

Bruker AVANCE - 600 MHz crioprobe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

5 3D HNCACB

Instrument

Bruker AVANCE - 600 MHz crioprobe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

6 3D H(CCO)NH

Instrument

Bruker AVANCE - 600 MHz PATXI probe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

7 2D 1H-1H NOESY

Instrument

Bruker AVANCE - 600 MHz PATXI probe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

8 2D 1H-13C HSQC

Instrument

Bruker AVANCE - 600 MHz PATXI probe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

9 2D 1H-15N HSQC

Instrument

Bruker AVANCE - 600 MHz crioprobe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

10 2D 1H-13C HSQC aromatic

Instrument

Bruker AVANCE - 600 MHz PATXI probe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

11 3D C(CO)NH

Instrument

Bruker AVANCE - 600 MHz PATXI probe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

12 3D HCCH-TOCSY

Instrument

Bruker AVANCE - 600 MHz PATXI probe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

13 3D HCCH-TOCSY

Instrument

Bruker AVANCE - 600 MHz PATXI probe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

14 3D 1H-15N NOESY

Instrument

Bruker AVANCE - 600 MHz crioprobe

Sample

#	Name	Isotope labeling	Concentration
1	TubR	[U-15N]	225 (±1.0) uM
2	potassium phosphate	natural abundance	25 (±0.1) mM
3	potassium chloride	natural abundance	50 (±0.1) mM
4	DTT	D-10	2 (±0.1) mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34449_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: bmr34449_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1071		97.5 (chain: 1, length: 81)
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: 81, Sequence coverage: 97.5%
- Total number of assignments
  - ¹H chemical shifts: 613
  - ¹³C chemical shifts: 381
  - ¹⁵N chemical shifts: 77
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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	539	523	97.0
¹³C chemical shifts	394	381	96.7
¹⁵N chemical shifts	90	77	85.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	164	159	97.0
¹³C chemical shifts	162	156	96.3
¹⁵N chemical shifts	80	77	96.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	375	364	97.1
¹³C chemical shifts	232	225	97.0
¹⁵N chemical shifts	10	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	45	90.0
¹³C chemical shifts	50	45	90.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	31	31	100.0
¹³C chemical shifts	31	31	100.0

Keywords DNA BINDING PROTEIN, DNA segregation, TubR, partition systems, winged helix-turn-helix

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Found 1 Document (0.589 seconds)

BMRB: 34449

Sample

Related entities 1. DNA-binding protein TubR, : 1 : 1 : 4 entities Detail

Experiments performed 14 experiments Detail

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Chemical shift validation 3 contents Detail