BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	86.2 % (518 of 601)	84.0 % (268 of 319)	87.3 % (199 of 228)	94.4 % (51 of 54)
Backbone	96.5 % (301 of 312)	97.1 % (102 of 105)	95.5 % (148 of 155)	98.1 % (51 of 52)
Sidechain	78.5 % (267 of 340)	77.6 % (166 of 214)	81.5 % (101 of 124)	0.0 % (0 of 2)
Aromatic	0.0 % (0 of 16)	0.0 % (0 of 8)	0.0 % (0 of 8)
Methyl	92.0 % (46 of 50)	92.0 % (23 of 25)	92.0 % (23 of 25)

1. entity 1

GSVEKLTADA ELQRLKNERH EEAELERLKS EAADHDKKEA ERKALEDKLA DY

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Sample

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8, Details 0.5 mM [U-99% 13C; U-99% 15N] Truncated peptide from PAMAP53, 20 mM [U-2H] Bis-Tris-d19, 2 ug/mL DSS, 1 ug/mL sodium azide, 93% H2O/7% D2O

#	Name	Isotope labeling	Concentration
1	Truncated peptide from PAMAP53	[U-99% 13C; U-99% 15N]	0.5 mM
2	Bis-Tris-d19	[U-2H]	20 mM
3	DSS	natural abundance	2 ug/mL
4	sodium azide	natural abundance	1 ug/mL

Protein Blocks Logo

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

Release date

2019-05-01

Citation

Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcus pyogenes
Yuan, Y., Ayinuola, Y.A., Singh, D., Ayinuola, O., Mayfield, J.A., Quek, A., Whisstock, J.C., Law, R., Lee, S.W., Ploplis, V.A., Castellino, F.J.
J. Struct. Biol. (2019), 208, 18-29, PubMed 31301349 , DOI 10.1016/j.jsb.2019.07.005 , Abstract

Related entities 1. M protein, : 1 : 1 : 7 : 5 entities Detail

Experiments performed 8 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AvanceII - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8, Details 0.5 mM [U-99% 13C; U-99% 15N] Truncated peptide from PAMAP53, 20 mM [U-2H] Bis-Tris-d19, 2 ug/mL DSS, 1 ug/mL sodium azide, 93% H2O/7% D2O

#	Name	Isotope labeling	Concentration
1	Truncated peptide from PAMAP53	[U-99% 13C; U-99% 15N]	0.5 mM
2	Bis-Tris-d19	[U-2H]	20 mM
3	DSS	natural abundance	2 ug/mL
4	sodium azide	natural abundance	1 ug/mL

2 2D NOESY

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Truncated peptide from PAMAP53	[U-99% 13C; U-99% 15N]	0.5 mM
2	Bis-Tris-d19	[U-2H]	20 mM
3	DSS	natural abundance	2 ug/mL
4	sodium azide	natural abundance	1 ug/mL

3 3D CBCA(CO)NH

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Truncated peptide from PAMAP53	[U-99% 13C; U-99% 15N]	0.5 mM
2	Bis-Tris-d19	[U-2H]	20 mM
3	DSS	natural abundance	2 ug/mL
4	sodium azide	natural abundance	1 ug/mL

4 3D C(CO)NH

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Truncated peptide from PAMAP53	[U-99% 13C; U-99% 15N]	0.5 mM
2	Bis-Tris-d19	[U-2H]	20 mM
3	DSS	natural abundance	2 ug/mL
4	sodium azide	natural abundance	1 ug/mL

5 3D HNCO

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Truncated peptide from PAMAP53	[U-99% 13C; U-99% 15N]	0.5 mM
2	Bis-Tris-d19	[U-2H]	20 mM
3	DSS	natural abundance	2 ug/mL
4	sodium azide	natural abundance	1 ug/mL

6 3D HN(CO)CA

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Truncated peptide from PAMAP53	[U-99% 13C; U-99% 15N]	0.5 mM
2	Bis-Tris-d19	[U-2H]	20 mM
3	DSS	natural abundance	2 ug/mL
4	sodium azide	natural abundance	1 ug/mL

7 3D HNCACB

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Truncated peptide from PAMAP53	[U-99% 13C; U-99% 15N]	0.5 mM
2	Bis-Tris-d19	[U-2H]	20 mM
3	DSS	natural abundance	2 ug/mL
4	sodium azide	natural abundance	1 ug/mL

8 3D HNCA

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Truncated peptide from PAMAP53	[U-99% 13C; U-99% 15N]	0.5 mM
2	Bis-Tris-d19	[U-2H]	20 mM
3	DSS	natural abundance	2 ug/mL
4	sodium azide	natural abundance	1 ug/mL

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30600_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: bmr30600_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	561		100.0 (chain: 1, length: 52)
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: 52, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 313
  - ¹³C chemical shifts: 198
  - ¹⁵N chemical shifts: 50
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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	319	267	83.7
¹³C chemical shifts	228	198	86.8
¹⁵N chemical shifts	58	50	86.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	105	101	96.2
¹³C chemical shifts	104	97	93.3
¹⁵N chemical shifts	52	50	96.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	214	166	77.6
¹³C chemical shifts	124	101	81.5
¹⁵N chemical shifts	6	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	25	23	92.0
¹³C chemical shifts	25	23	92.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	0	0.0
¹³C chemical shifts	8	0	0.0

Keywords PROTEIN BINDING, Plasminogen binding peptide

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Found 1 Document (0.462 seconds)

BMRB: 30600

Sample

Related entities 1. M protein, : 1 : 1 : 7 : 5 entities Detail

Experiments performed 8 experiments Detail

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Chemical shift validation 3 contents Detail