BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	68.1 % (327 of 480)	60.4 % (154 of 255)	74.7 % (136 of 182)	86.0 % (37 of 43)
Backbone	95.0 % (228 of 240)	95.1 % (77 of 81)	95.8 % (114 of 119)	92.5 % (37 of 40)
Sidechain	48.7 % (136 of 279)	44.3 % (77 of 174)	57.8 % (59 of 102)	0.0 % (0 of 3)
Aromatic	0.0 % (0 of 24)	0.0 % (0 of 12)	0.0 % (0 of 12)
Methyl	63.2 % (24 of 38)	68.4 % (13 of 19)	57.9 % (11 of 19)

1. M protein

GSVKKLNDEV ALERLKNERH VHDEEVELER LKNERHDHDY

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7, Details 1.0 mM [U-13C; U-15N] VKK38, 2.5 mM Kringle2, 20 mM [U-100% 2H] BisTris-d19, 0.2 mM DSS, 2 mM EDTA, 3 mM sodium azide, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-100% 2H]	20 mM
2	DSS	natural abundance	0.2 mM
3	EDTA	natural abundance	2 mM
4	Kringle2	natural abundance	2.5 mM
5	VKK38	[U-13C; U-15N]	1.0 mM
6	sodium azide	natural abundance	3 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 5V4U, Strand ID: A Detail

Release date

2017-06-19

Citation

Conformationally Organized Lysine Isosteres in Streptococcus Pyogenes M Protein Mediate Direct High-Affinity Binding to Human Plasminogen
Yuan, Y., Zajicek, J., Qiu, C., Chandrahas, V., Lee, S.W., Ploplis, V.A., Castellino, F.J.
J. Biol. Chem. (2017), 292, 15016-15027, PubMed 28724633 , DOI 10.1074/jbc.M117.794198 , Abstract

Related entities 1. M protein, : 1 : 39 entities Detail

Experiments performed 7 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7, Details 1.0 mM [U-13C; U-15N] VKK38, 2.5 mM Kringle2, 20 mM [U-100% 2H] BisTris-d19, 0.2 mM DSS, 2 mM EDTA, 3 mM sodium azide, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-100% 2H]	20 mM
2	DSS	natural abundance	0.2 mM
3	EDTA	natural abundance	2 mM
4	Kringle2	natural abundance	2.5 mM
5	VKK38	[U-13C; U-15N]	1.0 mM
6	sodium azide	natural abundance	3 mM

2 3D HNCO

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-100% 2H]	20 mM
2	DSS	natural abundance	0.2 mM
3	EDTA	natural abundance	2 mM
4	Kringle2	natural abundance	2.5 mM
5	VKK38	[U-13C; U-15N]	1.0 mM
6	sodium azide	natural abundance	3 mM

3 3D C(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-100% 2H]	20 mM
2	DSS	natural abundance	0.2 mM
3	EDTA	natural abundance	2 mM
4	Kringle2	natural abundance	2.5 mM
5	VKK38	[U-13C; U-15N]	1.0 mM
6	sodium azide	natural abundance	3 mM

4 3D CBCA(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-100% 2H]	20 mM
2	DSS	natural abundance	0.2 mM
3	EDTA	natural abundance	2 mM
4	Kringle2	natural abundance	2.5 mM
5	VKK38	[U-13C; U-15N]	1.0 mM
6	sodium azide	natural abundance	3 mM

5 3D HNCA

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-100% 2H]	20 mM
2	DSS	natural abundance	0.2 mM
3	EDTA	natural abundance	2 mM
4	Kringle2	natural abundance	2.5 mM
5	VKK38	[U-13C; U-15N]	1.0 mM
6	sodium azide	natural abundance	3 mM

6 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-100% 2H]	20 mM
2	DSS	natural abundance	0.2 mM
3	EDTA	natural abundance	2 mM
4	Kringle2	natural abundance	2.5 mM
5	VKK38	[U-13C; U-15N]	1.0 mM
6	sodium azide	natural abundance	3 mM

7 3D 15N HSQC-NOESY

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-100% 2H]	20 mM
2	DSS	natural abundance	0.2 mM
3	EDTA	natural abundance	2 mM
4	Kringle2	natural abundance	2.5 mM
5	VKK38	[U-13C; U-15N]	1.0 mM
6	sodium azide	natural abundance	3 mM

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_30271_5v4u.nef
Input source #2: Coordindates	5v4u.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40
GSVKKLNDEVALERLKNERHVHDEEVELERLKNERHDHDY
||||||||||||||||||||||||||||||||||||||||
GSVKKLNDEVALERLKNERHVHDEEVELERLKNERHDHDY

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	40	0	0	100.0

Content subtype: combined_30271_5v4u.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	314		100.0 (chain: A, length: 40)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	224 (1)	noe	92.5 (chain: A, length: 40)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 40, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 144
  - ¹³C chemical shifts: 133
  - ¹⁵N chemical shifts: 37
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	255	144	56.5
¹³C chemical shifts	182	133	73.1
¹⁵N chemical shifts	47	37	78.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	81	77	95.1
¹³C chemical shifts	80	77	96.3
¹⁵N chemical shifts	40	37	92.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	174	67	38.5
¹³C chemical shifts	102	56	54.9
¹⁵N chemical shifts	7	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	13	68.4
¹³C chemical shifts	19	11	57.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	12	0	0.0
¹³C chemical shifts	12	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 40, Sequence coverage: 92.5%
- Total number of restraints: 223
- Weight of restraints: 1.0 (223)
- Potential type of restraints: square-well-parabolic (223)
- Range of distance target values: 2.5, 4.4 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords BLOOD CLOTTING, PROTEIN/PEPTIDE

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Found 1 Document (0.562 seconds)

BMRB: 30271

Sample

Related entities 1. M protein, : 1 : 39 entities Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 3 contents Detail