BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	87.5 % (600 of 686)	83.2 % (306 of 368)	93.7 % (239 of 255)	87.3 % (55 of 63)
Backbone	97.4 % (333 of 342)	96.6 % (112 of 116)	98.2 % (166 of 169)	96.5 % (55 of 57)
Sidechain	80.7 % (322 of 399)	77.0 % (194 of 252)	90.8 % (128 of 141)	0.0 % (0 of 6)
Aromatic	20.0 % (4 of 20)	40.0 % (4 of 10)	0.0 % (0 of 10)
Methyl	96.0 % (48 of 50)	96.0 % (24 of 25)	96.0 % (24 of 25)

1. entity 1

GSKTIQEKEQ ELKNLKDNVE LERLKNERHD HDEEAERKAL EDKLADKQEH LDGALRY

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: -0.15 ppm, Outliers: 2 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: -0.15 ppm, Outliers: 2 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: 0.06 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: 0.04 ppm, Outliers: 2 Detail

Protein Blocks Logo

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

Release date

2018-02-04

Citation

Contributions of different modules of the plasminogen-binding Streptococcus pyogenes M-protein that mediate its functional dimerization
Qiu, C., Yuan, Y., Zajicek, J., Liang, Z., Balsara, R.D., Brito-Robionson, T., Lee, S.W., Ploplis, V.A., Castellino, F.J.
J. Struct. Biol. (2018), 204, 151-164, PubMed 30071314 , DOI 10.1016/j.jsb.2018.07.017 , Abstract

Related entities 1. M protein, : 1 : 1 : 7 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_30390_6bzk.nef
Input source #2: Coordindates	6bzk.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-------
GSKTIQEKEQELKNLKDNVELERLKNERHDHDEEAERKALEDKLADKQEHLDGALRY
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSKTIQEKEQELKNLKDNVELERLKNERHDHDEEAERKALEDKLADKQEHLDGALRY

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	57	0	0	100.0

Content subtype: combined_30390_6bzk.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	600		98.2 (chain: A, length: 57)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	414 (1)	noe	96.5 (chain: A, length: 57)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	72 (72)	.	75.4 (chain: A, length: 57)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 57, Sequence coverage: 98.2%
- Total number of assignments
  - ¹H chemical shifts: 306
  - ¹³C chemical shifts: 239
  - ¹⁵N chemical shifts: 55
- 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	368	306	83.2
¹³C chemical shifts	255	239	93.7
¹⁵N chemical shifts	67	55	82.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	116	112	96.6
¹³C chemical shifts	114	111	97.4
¹⁵N chemical shifts	57	55	96.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	252	194	77.0
¹³C chemical shifts	141	128	90.8
¹⁵N chemical shifts	10	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	25	24	96.0
¹³C chemical shifts	25	24	96.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	4	40.0
¹³C chemical shifts	10	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 57, Sequence coverage: 96.5%
- Total number of restraints: 414
- Weight of restraints: 1.0 (414)
- Potential type of restraints: square-well-parabolic (414)
- Range of distance target values: 2.5, 3.75 (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

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 57, Sequence coverage: 75.4%
- Total number of restraints: 72
- Total number of restraints per polymer type: 72
- Weight of restraints: 1.0 (72)
- Potential type of restraints: square-well-parabolic (72)
- 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 (0.639 seconds)

BMRB: 30390

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

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

Experiments performed 9 experiments Detail

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NMR combined restraints 4 contents Detail