BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	86.8 % (799 of 920)	83.6 % (414 of 495)	90.4 % (309 of 342)	91.6 % (76 of 83)
Backbone	98.9 % (457 of 462)	99.4 % (155 of 156)	98.7 % (226 of 229)	98.7 % (76 of 77)
Sidechain	78.2 % (417 of 533)	76.4 % (259 of 339)	84.0 % (158 of 188)	0.0 % (0 of 6)
Aromatic	0.0 % (0 of 24)	0.0 % (0 of 12)	0.0 % (0 of 12)
Methyl	96.9 % (62 of 64)	96.9 % (31 of 32)	96.9 % (31 of 32)

1. entity 1

GSVEKLTADA ELQRLKNERH EEAELERLKS ERHDHDKKEA ERKALEDKLA DKQEHLNGAL RYINEKEAER KEKEAEQ

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7, Details 20 mM [U-99% 2H] BisTris-d19, 1 mM DSS, 1 mM sodium azide, 1 mM EDTA, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

LACS Plot; CA

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

Referencing offset: -0.24 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -0.24 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.16 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: -0.01 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 6BZL, Strand ID: A Detail

Release date

2018-02-04

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 : 2 : 4 entities Detail

Experiments performed 9 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AvanceII - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7, Details 20 mM [U-99% 2H] BisTris-d19, 1 mM DSS, 1 mM sodium azide, 1 mM EDTA, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

2 3D HNCO

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

3 3D HNCA

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

4 3D HNCACB

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

5 3D CBCA(CO)NH

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

6 3D C(CO)NH

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

7 3D H(CCO)NH

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

8 3D HBHA(CO)NH

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

9 3D NOESY-HSQC

Instrument

Bruker AvanceII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	BisTris-d19	[U-99% 2H]	20 mM
2	DSS	natural abundance	1 mM
3	sodium azide	natural abundance	1 mM
4	EDTA	natural abundance	1 mM

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30391_6bzl.nef
Input source #2: Coordindates	6bzl.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--------50--------60--------70-------
GSVEKLTADAELQRLKNERHEEAELERLKSERHDHDKKEAERKALEDKLADKQEHLNGALRYINEKEAERKEKEAEQ
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSVEKLTADAELQRLKNERHEEAELERLKSERHDHDKKEAERKALEDKLADKQEHLNGALRYINEKEAERKEKEAEQ

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	77	0	0	100.0

Content subtype: combined_30391_6bzl.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	797		100.0 (chain: A, length: 77)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	301 (1)	noe	97.4 (chain: A, length: 77)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	69 (69)	.	50.6 (chain: A, length: 77)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 412
  - ¹³C chemical shifts: 309
  - ¹⁵N chemical shifts: 76
- 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	495	412	83.2
¹³C chemical shifts	342	309	90.4
¹⁵N chemical shifts	90	76	84.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	156	155	99.4
¹³C chemical shifts	154	151	98.1
¹⁵N chemical shifts	77	76	98.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	339	257	75.8
¹³C chemical shifts	188	158	84.0
¹⁵N chemical shifts	13	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	32	31	96.9
¹³C chemical shifts	32	31	96.9

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: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 97.4%
- Total number of restraints: 301
- Weight of restraints: 1.0 (301)
- Potential type of restraints: square-well-parabolic (301)
- Range of distance target values: 3.0, 4.4 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 50.6%
- Total number of restraints: 69
- Total number of restraints per polymer type: 69
- Weight of restraints: 1.0 (69)
- Potential type of restraints: square-well-parabolic (69)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords PROTEIN BINDING, Plasminogen binding peptide

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Found 1 Document (0.43 seconds)

BMRB: 30391

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. M protein, : 1 : 2 : 4 entities Detail

Experiments performed 9 experiments Detail

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NMR combined restraints 4 contents Detail