BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	96.2 % (925 of 962)	95.7 % (486 of 508)	96.5 % (357 of 370)	97.6 % (82 of 84)
Backbone	97.2 % (449 of 462)	97.4 % (149 of 153)	97.0 % (227 of 234)	97.3 % (73 of 75)
Sidechain	95.5 % (552 of 578)	94.9 % (337 of 355)	96.3 % (206 of 214)	100.0 % (9 of 9)
Aromatic	82.3 % (51 of 62)	83.9 % (26 of 31)	80.6 % (25 of 31)
Methyl	100.0 % (82 of 82)	100.0 % (41 of 41)	100.0 % (41 of 41)

1. entity

SDDYVDEETY NLQKLLAPYH KAKTLERQVY ELEKLQEKLP EKYKAEYKKK LDQTRVELAD QVKSAVTEFE NVTPTNDQ

Show sample condition

Sample #1

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
1	IsdH linker	[U-100% 15N]	1.1 mM
2	potassium phosphate	natural abundance	20 mM
3	potassium chloride	natural abundance	50 mM
4	AEBSF protease inhibitor	natural abundance	100 uM
5	sodium azide	natural abundance	0.01 %
6	D2O	natural abundance	7 %
7	H2O	natural abundance	93 %

Sample #2

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
15	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
16	potassium phosphate	natural abundance	20 mM
17	potassium chloride	natural abundance	50 mM
18	AEBSF protease inhibitor	natural abundance	100 uM
19	sodium azide	natural abundance	0.01 %
20	D2O	natural abundance	100 %

LACS Plot; CA

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

Referencing offset: 0.21 ppm, Outliers: 2 Detail

LACS Plot; CB

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

Referencing offset: 0.21 ppm, Outliers: 2 Detail

LACS Plot; HA

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

Referencing offset: 0.09 ppm, Outliers: 2 Detail

LACS Plot; CO

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

Referencing offset: 0.11 ppm, Outliers: 4 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2LHR, Strand ID: A Detail

Release date

2012-06-18

Citation

Structural basis for hemoglobin capture by Staphylococcus aureus cell-surface protein, IsdH
Krishna Kumar, K., Jacques, D.A., Pishchany, G., Caradoc-Davies, T., Spirig, T., Malmirchegini, G., Langley, D.B., Dickson, C.F., Mackay, J.P., Clubb, R.T., Skaar, E.P., Guss, J., Gell, D.A.
J. Biol. Chem. (2011), 286, 38439-38447, PubMed 21917915 , DOI 10.1074/jbc.M111.287300 , Abstract

Related entities 1. Staphylococcus aureus IsdH linker domain, : 1 : 9 : 8 entities Detail

Experiments performed 21 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 6.0

#	Name	Isotope labeling	Concentration
1	IsdH linker	[U-100% 15N]	1.1 mM
2	potassium phosphate	natural abundance	20 mM
3	potassium chloride	natural abundance	50 mM
4	AEBSF protease inhibitor	natural abundance	100 uM
5	sodium azide	natural abundance	0.01 %
6	D2O	natural abundance	7 %
7	H2O	natural abundance	93 %

2 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

3 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

4 3D HN(CA)CO

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

5 3D HNCO

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

6 3D CC(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

7 3D HBHA(CO)NH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

8 3D HNHA

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
1	IsdH linker	[U-100% 15N]	1.1 mM
2	potassium phosphate	natural abundance	20 mM
3	potassium chloride	natural abundance	50 mM
4	AEBSF protease inhibitor	natural abundance	100 uM
5	sodium azide	natural abundance	0.01 %
6	D2O	natural abundance	7 %
7	H2O	natural abundance	93 %

9 3D HNHB

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
1	IsdH linker	[U-100% 15N]	1.1 mM
2	potassium phosphate	natural abundance	20 mM
3	potassium chloride	natural abundance	50 mM
4	AEBSF protease inhibitor	natural abundance	100 uM
5	sodium azide	natural abundance	0.01 %
6	D2O	natural abundance	7 %
7	H2O	natural abundance	93 %

10 3D HCCH-TOCSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

11 3D 1H-15N TOCSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
1	IsdH linker	[U-100% 15N]	1.1 mM
2	potassium phosphate	natural abundance	20 mM
3	potassium chloride	natural abundance	50 mM
4	AEBSF protease inhibitor	natural abundance	100 uM
5	sodium azide	natural abundance	0.01 %
6	D2O	natural abundance	7 %
7	H2O	natural abundance	93 %

12 3D HCCH-COSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

13 3D HCCH-TOCSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
15	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
16	potassium phosphate	natural abundance	20 mM
17	potassium chloride	natural abundance	50 mM
18	AEBSF protease inhibitor	natural abundance	100 uM
19	sodium azide	natural abundance	0.01 %
20	D2O	natural abundance	100 %

14 3D 1H-15N NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
1	IsdH linker	[U-100% 15N]	1.1 mM
2	potassium phosphate	natural abundance	20 mM
3	potassium chloride	natural abundance	50 mM
4	AEBSF protease inhibitor	natural abundance	100 uM
5	sodium azide	natural abundance	0.01 %
6	D2O	natural abundance	7 %
7	H2O	natural abundance	93 %

15 3D 1H-13C NOESY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

16 3D 1H-13C NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
15	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
16	potassium phosphate	natural abundance	20 mM
17	potassium chloride	natural abundance	50 mM
18	AEBSF protease inhibitor	natural abundance	100 uM
19	sodium azide	natural abundance	0.01 %
20	D2O	natural abundance	100 %

17 2D 1H-13C HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
8	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
9	potassium phosphate	natural abundance	20 mM
10	potassium chloride	natural abundance	50 mM
11	AEBSF protease inhibitor	natural abundance	100 uM
12	sodium azide	natural abundance	0.01 %
13	D2O	natural abundance	7 %
14	H2O	natural abundance	93 %

18 2D 1H-13C HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
15	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
16	potassium phosphate	natural abundance	20 mM
17	potassium chloride	natural abundance	50 mM
18	AEBSF protease inhibitor	natural abundance	100 uM
19	sodium azide	natural abundance	0.01 %
20	D2O	natural abundance	100 %

19 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
15	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
16	potassium phosphate	natural abundance	20 mM
17	potassium chloride	natural abundance	50 mM
18	AEBSF protease inhibitor	natural abundance	100 uM
19	sodium azide	natural abundance	0.01 %
20	D2O	natural abundance	100 %

20 2D CB(CGCD)HD

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
15	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
16	potassium phosphate	natural abundance	20 mM
17	potassium chloride	natural abundance	50 mM
18	AEBSF protease inhibitor	natural abundance	100 uM
19	sodium azide	natural abundance	0.01 %
20	D2O	natural abundance	100 %

21 2D CB(CGCD)HE

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
15	IsdH linker	[U-100% 13C; U-100% 15N]	1.3 mM
16	potassium phosphate	natural abundance	20 mM
17	potassium chloride	natural abundance	50 mM
18	AEBSF protease inhibitor	natural abundance	100 uM
19	sodium azide	natural abundance	0.01 %
20	D2O	natural abundance	100 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_17862_2lhr.nef
Input source #2: Coordindates	2lhr.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

--470-------480-------490-------500-------510-------520-------530-------540---
SDDYVDEETYNLQKLLAPYHKAKTLERQVYELEKLQEKLPEKYKAEYKKKLDQTRVELADQVKSAVTEFENVTPTNDQ
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SDDYVDEETYNLQKLLAPYHKAKTLERQVYELEKLQEKLPEKYKAEYKKKLDQTRVELADQVKSAVTEFENVTPTNDQ
--------10--------20--------30--------40--------50--------60--------70--------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	78	0	0	100.0

Content subtype: combined_17862_2lhr.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	925		97.4 (chain: A, length: 78)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	3132 (1)	noe	97.4 (chain: A, length: 78)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	112 (112)	.	71.8 (chain: A, length: 78)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 78, Sequence coverage: 97.4%
- Total number of assignments
  - ¹H chemical shifts: 486
  - ¹³C chemical shifts: 357
  - ¹⁵N chemical shifts: 82
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- Tautomeric state of HIS
- 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	508	486	95.7
¹³C chemical shifts	370	357	96.5
¹⁵N chemical shifts	86	82	95.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	153	149	97.4
¹³C chemical shifts	156	151	96.8
¹⁵N chemical shifts	75	73	97.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	355	337	94.9
¹³C chemical shifts	214	206	96.3
¹⁵N chemical shifts	11	9	81.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	41	41	100.0
¹³C chemical shifts	41	41	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	31	26	83.9
¹³C chemical shifts	31	25	80.6

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 78, Sequence coverage: 97.4%
- Total number of restraints: 3132
- Weight of restraints: 1.0 (3132)
- Potential type of restraints: square-well-parabolic (3132)
- Range of distance target values: 2.13, 4.8 (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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 78, Sequence coverage: 71.8%
- Total number of restraints: 112
- Total number of restraints per polymer type: 112
- Weight of restraints: 1.0 (112)
- Potential type of restraints: square-well-parabolic (112)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Heme acquisition, Hemoglobin receptor, Iron uptake, NEAT domain, Staphylococcus aureus

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Found 1 Document (0.678 seconds)

BMRB: 17862

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Staphylococcus aureus IsdH linker domain, : 1 : 9 : 8 entities Detail

Experiments performed 21 experiments Detail

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NMR combined restraints 4 contents Detail