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Found 1 Document (0.85 seconds)

BMRB: 25195

2MU0

Solution structure of a putative arsenate reductase from Brucella melitensis. Seattle Structural Genomics Center for Infectious Disease target BrabA.00073.a

Authors

Buchko, G.W.

Assembly

putative arsenate reductase from Brucella melitensis

Entity

1. putative arsenate reductase from Brucella melitensis (polymer), 136 monomers, 15144.57 Da Detail

MAHHHHHHMG TLEAQTQGPG SMDVTIYHNP VCGTSRKVLG MIREAGIEPH VIEYMKTPLP RDMLVELLRQ MAISPRALLR AKEARYAELG LDDPALSDEV LIDAMISNPV LMNRPVVVTP KGVRLCRPAE TVQELL

Formula weight

15144.57 Da

Source organism

Brucella melitensis

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.1 %, Completeness: 83.3 %, Completeness (bb): 87.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	83.3 % (1296 of 1556)	80.0 % (648 of 810)	86.5 % (531 of 614)	88.6 % (117 of 132)
Backbone	87.7 % (696 of 794)	86.2 % (232 of 269)	88.0 % (352 of 400)	89.6 % (112 of 125)
Sidechain	80.7 % (718 of 890)	76.9 % (416 of 541)	86.8 % (297 of 342)	71.4 % (5 of 7)
Aromatic	51.8 % (29 of 56)	53.6 % (15 of 28)	50.0 % (14 of 28)
Methyl	88.1 % (155 of 176)	84.1 % (74 of 88)	92.0 % (81 of 88)

1. entity

MAHHHHHHMG TLEAQTQGPG SMDVTIYHNP VCGTSRKVLG MIREAGIEPH VIEYMKTPLP RDMLVELLRQ MAISPRALLR AKEARYAELG LDDPALSDEV LIDAMISNPV LMNRPVVVTP KGVRLCRPAE TVQELL

Show sample condition

Sample #1

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
7	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
8	sodium chloride	natural abundance	100 (±5.0) mM
9	TRIS	natural abundance	20 (±1.0) mM
10	DTT	natural abundance	1 (±0.2) mM
11	D2O	natural abundance	100 %

LACS Plot; CA

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

Referencing offset: -0.03 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -0.03 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.05 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: 0.16 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2MU0, Strand ID: A Detail

Release date

2014-09-14

Citation

Solution structure of an arsenate reductase-related protein, YffB, from Brucella melitensis, the etiological agent responsible for brucellosis
Buchko, G.W., Hewitt, S.N., Van Voorhis, W.C., Myler, P.J.
Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. (2011), 67, 1129-1136, PubMed 21904062 , DOI 10.1107/S1744309111006336 , Abstract

Related entities 1. putative arsenate reductase from Brucella melitensis, : 1 : 46 entities Detail

Experiments performed 11 experiments Detail

1 2D 1H-15N HSQC

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

2 2D 1H-13C HSQC aliphatic

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

3 2D 1H-13C HSQC aromatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

4 3D HNCO

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

5 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

6 3D C(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

7 3D 1H-13C NOESY aliphatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

8 3D 1H-13C NOESY aromatic

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

9 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

10 D2O exchange

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
7	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
8	sodium chloride	natural abundance	100 (±5.0) mM
9	TRIS	natural abundance	20 (±1.0) mM
10	DTT	natural abundance	1 (±0.2) mM
11	D2O	natural abundance	100 %

11 3D 1H-15N NOESY

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 7 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	1 (±0.2) mM
2	sodium chloride	natural abundance	100 (±5.0) mM
3	TRIS	natural abundance	20 (±1.0) mM
4	DTT	natural abundance	1 (±0.2) mM
5	D2O	natural abundance	7 %
6	H2O	natural abundance	93 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25195_2mu0.nef
Input source #2: Coordindates	2mu0.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--------80--------90-------100
MAHHHHHHMGTLEAQTQGPGSMDVTIYHNPVCGTSRKVLGMIREAGIEPHVIEYMKTPLPRDMLVELLRQMAISPRALLRAKEARYAELGLDDPALSDEV
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MAHHHHHHMGTLEAQTQGPGSMDVTIYHNPVCGTSRKVLGMIREAGIEPHVIEYMKTPLPRDMLVELLRQMAISPRALLRAKEARYAELGLDDPALSDEV

-------110-------120-------130------
LIDAMISNPVLMNRPVVVTPKGVRLCRPAETVQELL
||||||||||||||||||||||||||||||||||||
LIDAMISNPVLMNRPVVVTPKGVRLCRPAETVQELL

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	136	0	0	100.0

Content subtype: combined_25195_2mu0.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1278		94.1 (chain: A, length: 136)
1	Distance restraints	DYANA/DIANA_distance_constraints_4	Warning	1826 (1)	noe	89.0 (chain: A, length: 136)
2	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	188 (1)	hbond	50.0 (chain: A, length: 136)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	1188 (1188)	.	98.5 (chain: A, length: 136)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 136, Sequence coverage: 94.1%
- Total number of assignments
  - ¹³C chemical shifts: 524
  - ¹H chemical shifts: 639
  - ¹⁵N chemical shifts: 115
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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 (%)
¹³C chemical shifts	614	524	85.3
¹H chemical shifts	810	639	78.9
¹⁵N chemical shifts	142	115	81.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	272	227	83.5
¹H chemical shifts	269	230	85.5
¹⁵N chemical shifts	125	111	88.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	342	297	86.8
¹H chemical shifts	541	409	75.6
¹⁵N chemical shifts	17	4	23.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	97	88	90.7
¹H chemical shifts	97	81	83.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	28	14	50.0
¹H chemical shifts	28	14	50.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_4
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 136, Sequence coverage: 89.0%
- Total number of restraints: 1826
- Weight of restraints: 1.0 (1826)
- Potential type of restraints: upper-bound-parabolic (1826)
- Range of distance target values: 2.56, 5.5 (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
- Saveframe: DYANA/DIANA_distance_constraints_2
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 136, Sequence coverage: 50.0%
  - Total number of restraints: 188
  - Weight of restraints: 1.0 (188)
  - Potential type of restraints: upper-bound-parabolic (188)
  - Range of distance target values: 1.8, 3.2 (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: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 136, Sequence coverage: 98.5%
- Total number of restraints: 1188
- Total number of restraints per polymer type: 1188
- Weight of restraints: 1.0 (1188)
- Potential type of restraints: square-well-parabolic (1188)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords arsenate reductase, glutaredoxin, infectious disease, brucellosis, Malta fever

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Found 1 Document (0.85 seconds)

BMRB: 25195

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. putative arsenate reductase from Brucella melitensis, : 1 : 46 entities Detail

Experiments performed 11 experiments Detail

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NMR combined restraints 5 contents Detail