BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	74.9 % (460 of 614)	71.0 % (233 of 328)	76.3 % (177 of 232)	92.6 % (50 of 54)
Backbone	93.6 % (292 of 312)	90.5 % (95 of 105)	94.8 % (147 of 155)	96.2 % (50 of 52)
Sidechain	61.5 % (217 of 353)	61.9 % (138 of 223)	61.7 % (79 of 128)	0.0 % (0 of 2)
Aromatic	0.0 % (0 of 20)	0.0 % (0 of 10)	0.0 % (0 of 10)
Methyl	78.3 % (36 of 46)	87.0 % (20 of 23)	69.6 % (16 of 23)

1. entity 1

GSVEKLTADA ELQRLKNERH EEAELERLKS ERHDHDKKEA 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] VEK50, 1.5 mM Kringle 2, 2 ug/mL DSS, 20 mM [U-2H] Bis-Tris-d19, 2 ug/mL sodium azide, 93% H2O/7% D2O

#	Name	Isotope labeling	Concentration
1	VEK50	[U-99% 13C; U-99% 15N]	0.5 (±0.1) mM
2	Kringle 2	natural abundance	1.5 (±0.1) mM
3	DSS	natural abundance	2 ug/mL
4	Bis-Tris-d19	[U-2H]	20 mM
5	sodium azide	natural abundance	2 ug/mL

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl carbons	internal	indirect	0.2514495
¹H	DSS	protons	internal	direct	1.0
¹⁵N	DSS	nitrogen	internal	indirect	0.1013291

Referencing offset: -0.08 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl carbons	internal	indirect	0.2514495
¹H	DSS	protons	internal	direct	1.0
¹⁵N	DSS	nitrogen	internal	indirect	0.1013291

Referencing offset: -0.08 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl carbons	internal	indirect	0.2514495
¹H	DSS	protons	internal	direct	1.0
¹⁵N	DSS	nitrogen	internal	indirect	0.1013291

Referencing offset: 0.02 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl carbons	internal	indirect	0.2514495
¹H	DSS	protons	internal	direct	1.0
¹⁵N	DSS	nitrogen	internal	indirect	0.1013291

Referencing offset: 0.32 ppm, Outliers: 4 Detail

Protein Blocks Logo

Calculated from 15 models in PDB: 6OQ9, Strand ID: A Detail

Release date

2019-05-02

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

Entries sharing articles BMRB: 5 entries Detail

  BMRB: 30599 released on 2019-05-02
    Title Solution structure of VEK50RH1/AA
  BMRB: 30605 released on 2019-05-02
    Title SOLUTION STRUCTURE OF THE COMPLEX OF MUTANT VEK50[RH1/AA] AND PLASMINOGEN KRINGLE 2
  BMRB: 30606 released on 2019-05-02
    Title SOLUTION STRUCTURE OF THE COMPLEX OF MUTANT VEK50[RH2/AA] AND PLASMINOGEN KRINGLE 2
  BMRB: 30600 released on 2019-05-01
    Title Solution structure of truncated peptide from PAMap53
  BMRB: 30391 released on 2018-02-04
    Title Solution structure of VEK75

Related entities 1. M protein, : 1 : 1 : 7 : 14 entities Detail

Experiments performed 7 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 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] VEK50, 1.5 mM Kringle 2, 2 ug/mL DSS, 20 mM [U-2H] Bis-Tris-d19, 2 ug/mL sodium azide, 93% H2O/7% D2O

#	Name	Isotope labeling	Concentration
1	VEK50	[U-99% 13C; U-99% 15N]	0.5 (±0.1) mM
2	Kringle 2	natural abundance	1.5 (±0.1) mM
3	DSS	natural abundance	2 ug/mL
4	Bis-Tris-d19	[U-2H]	20 mM
5	sodium azide	natural abundance	2 ug/mL

2 3D CBCA(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	VEK50	[U-99% 13C; U-99% 15N]	0.5 (±0.1) mM
2	Kringle 2	natural abundance	1.5 (±0.1) mM
3	DSS	natural abundance	2 ug/mL
4	Bis-Tris-d19	[U-2H]	20 mM
5	sodium azide	natural abundance	2 ug/mL

3 3D C(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	VEK50	[U-99% 13C; U-99% 15N]	0.5 (±0.1) mM
2	Kringle 2	natural abundance	1.5 (±0.1) mM
3	DSS	natural abundance	2 ug/mL
4	Bis-Tris-d19	[U-2H]	20 mM
5	sodium azide	natural abundance	2 ug/mL

4 3D HNCO

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	VEK50	[U-99% 13C; U-99% 15N]	0.5 (±0.1) mM
2	Kringle 2	natural abundance	1.5 (±0.1) mM
3	DSS	natural abundance	2 ug/mL
4	Bis-Tris-d19	[U-2H]	20 mM
5	sodium azide	natural abundance	2 ug/mL

5 3D HNCA

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	VEK50	[U-99% 13C; U-99% 15N]	0.5 (±0.1) mM
2	Kringle 2	natural abundance	1.5 (±0.1) mM
3	DSS	natural abundance	2 ug/mL
4	Bis-Tris-d19	[U-2H]	20 mM
5	sodium azide	natural abundance	2 ug/mL

6 3D HNCACB

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	VEK50	[U-99% 13C; U-99% 15N]	0.5 (±0.1) mM
2	Kringle 2	natural abundance	1.5 (±0.1) mM
3	DSS	natural abundance	2 ug/mL
4	Bis-Tris-d19	[U-2H]	20 mM
5	sodium azide	natural abundance	2 ug/mL

7 3D HBHA(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	VEK50	[U-99% 13C; U-99% 15N]	0.5 (±0.1) mM
2	Kringle 2	natural abundance	1.5 (±0.1) mM
3	DSS	natural abundance	2 ug/mL
4	Bis-Tris-d19	[U-2H]	20 mM
5	sodium azide	natural abundance	2 ug/mL

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30603_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: bmr30603_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	491		98.1 (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: 98.1%
- Total number of assignments
  - ¹H chemical shifts: 268
  - ¹³C chemical shifts: 173
  - 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	328	228	69.5
¹³C chemical shifts	232	173	74.6
¹⁵N chemical shifts	59	50	84.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	105	94	89.5
¹³C chemical shifts	104	98	94.2
¹⁵N chemical shifts	52	50	96.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	223	134	60.1
¹³C chemical shifts	128	75	58.6
¹⁵N chemical shifts	7	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	23	20	87.0
¹³C chemical shifts	23	16	69.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	0	0.0
¹³C chemical shifts	10	0	0.0

Keywords PROTEIN BINDING, Plasminogen binding peptide, blood clotting

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Found 1 Document (0.597 seconds)

BMRB: 30603

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 5 entries Detail

Related entities 1. M protein, : 1 : 1 : 7 : 14 entities Detail

Experiments performed 7 experiments Detail

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Chemical shift validation 3 contents Detail