BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	69.3 % (282 of 407)	95.9 % (209 of 218)	27.0 % (43 of 159)	100.0 % (30 of 30)
Backbone	62.9 % (122 of 194)	100.0 % (64 of 64)	28.7 % (29 of 101)	100.0 % (29 of 29)
Sidechain	68.3 % (168 of 246)	94.2 % (145 of 154)	24.2 % (22 of 91)	100.0 % (1 of 1)
Aromatic	83.3 % (20 of 24)	100.0 % (12 of 12)	66.7 % (8 of 12)
Methyl	57.1 % (16 of 28)	100.0 % (14 of 14)	14.3 % (2 of 14)

1. entity 1

XPPKKPKKPG DNATPEKLAA YEKELAAYEK ELAAYX

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 278 K, pH 7.4, Details 1 mM Optimised PPa-TYR, 8.2 mM Na2HPO4, 1.8 mM KH2PO4, 2.7 mM KCL, 137 mM NaCl, 10 % [U-99% 2H] D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	Optimised PPa-TYR	natural abundance	1 (±0.1) mM
2	Na2HPO4	natural abundance	8.2 (±0.1) mM
3	KH2PO4	natural abundance	1.8 (±0.1) mM
4	KCL	natural abundance	2.7 (±0.1) mM
5	NaCl	natural abundance	137 (±0.1) mM
6	D2O	[U-99% 2H]	10 (±0.1) %

Protein Blocks Logo

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

Release date

2019-06-30

Citation

Stabilizing and Understanding a Miniprotein by Rational Redesign
Porter Goff, K.L., Nicol, D., Williams, C., Crump, M.P., Zieleniewski, F., Samphire, J., Baker, E.G., Woolfson, D.N.
Biochemistry (2019), 58, 3060-3064, PubMed 31251570 , DOI 10.1021/acs.biochem.9b00067 , Abstract

Related entities 1. PPaTyr, : 36 entities Detail

Experiments performed 8 experiments Detail

1 2D 100ms NOESY

Instrument

Bruker AvanceIII - 700 MHz 1.7mm TCI cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 278 K, pH 7.4, Details 1 mM Optimised PPa-TYR, 8.2 mM Na2HPO4, 1.8 mM KH2PO4, 2.7 mM KCL, 137 mM NaCl, 10 % [U-99% 2H] D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	Optimised PPa-TYR	natural abundance	1 (±0.1) mM
2	Na2HPO4	natural abundance	8.2 (±0.1) mM
3	KH2PO4	natural abundance	1.8 (±0.1) mM
4	KCL	natural abundance	2.7 (±0.1) mM
5	NaCl	natural abundance	137 (±0.1) mM
6	D2O	[U-99% 2H]	10 (±0.1) %

2 2D 100ms NOESY

Instrument

Varian VNMRS - 600 MHz 5mm cryoprobe

Sample

#	Name	Isotope labeling	Concentration
1	Optimised PPa-TYR	natural abundance	1 (±0.1) mM
2	Na2HPO4	natural abundance	8.2 (±0.1) mM
3	KH2PO4	natural abundance	1.8 (±0.1) mM
4	KCL	natural abundance	2.7 (±0.1) mM
5	NaCl	natural abundance	137 (±0.1) mM
6	D2O	[U-99% 2H]	10 (±0.1) %

3 2D 1H-1H TOCSY

Instrument

Bruker AvanceIII - 700 MHz 1.7mm TCI cryoprobe

Sample

#	Name	Isotope labeling	Concentration
1	Optimised PPa-TYR	natural abundance	1 (±0.1) mM
2	Na2HPO4	natural abundance	8.2 (±0.1) mM
3	KH2PO4	natural abundance	1.8 (±0.1) mM
4	KCL	natural abundance	2.7 (±0.1) mM
5	NaCl	natural abundance	137 (±0.1) mM
6	D2O	[U-99% 2H]	10 (±0.1) %

4 2D 1H-1H TOCSY

Instrument

Varian VNMRS - 600 MHz 5mm cryoprobe

Sample

#	Name	Isotope labeling	Concentration
1	Optimised PPa-TYR	natural abundance	1 (±0.1) mM
2	Na2HPO4	natural abundance	8.2 (±0.1) mM
3	KH2PO4	natural abundance	1.8 (±0.1) mM
4	KCL	natural abundance	2.7 (±0.1) mM
5	NaCl	natural abundance	137 (±0.1) mM
6	D2O	[U-99% 2H]	10 (±0.1) %

5 1H-15N HSQC

Instrument

Bruker AvanceIII - 700 MHz 1.7mm TCI cryoprobe

Sample

#	Name	Isotope labeling	Concentration
1	Optimised PPa-TYR	natural abundance	1 (±0.1) mM
2	Na2HPO4	natural abundance	8.2 (±0.1) mM
3	KH2PO4	natural abundance	1.8 (±0.1) mM
4	KCL	natural abundance	2.7 (±0.1) mM
5	NaCl	natural abundance	137 (±0.1) mM
6	D2O	[U-99% 2H]	10 (±0.1) %

6 2D 1H-1H 250ms NOESY

Instrument

Varian VNMRS - 600 MHz 5mm cryoprobe

Sample

#	Name	Isotope labeling	Concentration
1	Optimised PPa-TYR	natural abundance	1 (±0.1) mM
2	Na2HPO4	natural abundance	8.2 (±0.1) mM
3	KH2PO4	natural abundance	1.8 (±0.1) mM
4	KCL	natural abundance	2.7 (±0.1) mM
5	NaCl	natural abundance	137 (±0.1) mM
6	D2O	[U-99% 2H]	10 (±0.1) %

7 2D 1H-1H 250ms NOESY

Instrument

Bruker AvanceIII - 700 MHz 1.7mm TCI cryoprobe

Sample

#	Name	Isotope labeling	Concentration
1	Optimised PPa-TYR	natural abundance	1 (±0.1) mM
2	Na2HPO4	natural abundance	8.2 (±0.1) mM
3	KH2PO4	natural abundance	1.8 (±0.1) mM
4	KCL	natural abundance	2.7 (±0.1) mM
5	NaCl	natural abundance	137 (±0.1) mM
6	D2O	[U-99% 2H]	10 (±0.1) %

8 1H-13N HSQC

Instrument

Bruker AvanceIII - 700 MHz 1.7mm TCI cryoprobe

Sample

#	Name	Isotope labeling	Concentration
1	Optimised PPa-TYR	natural abundance	1 (±0.1) mM
2	Na2HPO4	natural abundance	8.2 (±0.1) mM
3	KH2PO4	natural abundance	1.8 (±0.1) mM
4	KCL	natural abundance	2.7 (±0.1) mM
5	NaCl	natural abundance	137 (±0.1) mM
6	D2O	[U-99% 2H]	10 (±0.1) %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34295_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

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
1	1	ACE	ACETYL GROUP	Assigned chemical shifts
1	36	NH2	AMINO GROUP	None

Content subtype: bmr34295_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	306		97.2 (chain: 1, length: 36)
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: 36, Sequence coverage: 97.2%
- Total number of assignments
  - ¹H chemical shifts: 241
  - ¹³C chemical shifts: 35
  - ¹⁵N chemical shifts: 30
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
14	THR	HG1	5.767

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	222	209	94.1
¹³C chemical shifts	161	35	21.7
¹⁵N chemical shifts	31	30	96.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	65	65	100.0
¹³C chemical shifts	68	18	26.5
¹⁵N chemical shifts	30	29	96.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	157	144	91.7
¹³C chemical shifts	93	17	18.3
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	15	15	100.0
¹³C chemical shifts	15	1	6.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	12	12	100.0
¹³C chemical shifts	12	8	66.7

Keywords Designed miniprotein CH-pi interactions, STRUCTURAL PROTEIN, weak non-covalent interactions in proteins solution structure proline-tyrosine interactions

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Found 1 Document (0.468 seconds)

BMRB: 34295

Sample

Related entities 1. PPaTyr, : 36 entities Detail

Experiments performed 8 experiments Detail

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Chemical shift validation 3 contents Detail