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BMRB: 25243

2MYU

AN ARSENATE REDUCTASE IN OXIDIZED STATE

Authors

Jin, C., Hu, C.

Assembly

Arsenate Reductase

Entity

1. Arsenate Reductase (polymer), 131 monomers, 14395.12 Da Detail

MKKVMFVSKR NSSRSQMAEG FAKTLGAGKI AVTSSGLESS RVHPTAIAMM EEVGIDISGQ TSDPIENFNA DDYDVVISLC GCGVNLPPEW VTQEIFEDWQ LEDPDGQSLE VFRTVRGQVK ERVENLIAKI S

Formula weight

14395.12 Da

Source organism

Exptl. method

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.2 %, Completeness: 92.5 %, Completeness (bb): 95.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	92.5 % (1372 of 1484)	90.9 % (700 of 770)	93.2 % (536 of 575)	97.8 % (136 of 139)
Backbone	95.7 % (743 of 776)	95.1 % (254 of 267)	95.6 % (366 of 383)	97.6 % (123 of 126)
Sidechain	90.0 % (746 of 829)	88.7 % (446 of 503)	91.7 % (287 of 313)	100.0 % (13 of 13)
Aromatic	58.1 % (50 of 86)	58.1 % (25 of 43)	56.1 % (23 of 41)	100.0 % (2 of 2)
Methyl	98.6 % (142 of 144)	97.2 % (70 of 72)	100.0 % (72 of 72)

1. entity

MKKVMFVSKR NSSRSQMAEG FAKTLGAGKI AVTSSGLESS RVHPTAIAMM EEVGIDISGQ TSDPIENFNA DDYDVVISLC GCGVNLPPEW VTQEIFEDWQ LEDPDGQSLE VFRTVRGQVK ERVENLIAKI S

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	protein	[U-15N]		0.3 mM
2	sodium phosphate	natural abundance		50 mM
3	sodium chloride	natural abundance		50 mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
4	protein	[U-13C; U-15N]		0.3 mM
5	sodium phosphate	natural abundance		50 mM
6	sodium chloride	natural abundance		50 mM

LACS Plot; CA

Referencing offset: -0.15 ppm, Outliers: 2 Detail

LACS Plot; CB

Referencing offset: -0.15 ppm, Outliers: 2 Detail

LACS Plot; HA

Referencing offset: -0.05 ppm, Outliers: 1 Detail

LACS Plot; CO

Referencing offset: -1.48 ppm, Outliers: 2 Detail

Protein Blocks Logo

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

Release date

2015-08-02

Citation

A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction
Jin, C., Hu, C.
J. Biol. Chem. (2015), 290, 22262-22273, PubMed 26224634 , DOI 10.1074/jbc.M115.659896 , Abstract

Related entities 1. Arsenate Reductase, : 1 : 7 : 59 entities Detail

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	protein	[U-15N]		0.3 mM
2	sodium phosphate	natural abundance		50 mM
3	sodium chloride	natural abundance		50 mM

2 3D HNCO

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
4	protein	[U-13C; U-15N]		0.3 mM
5	sodium phosphate	natural abundance		50 mM
6	sodium chloride	natural abundance		50 mM

3 3D CBCA(CO)NH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
4	protein	[U-13C; U-15N]		0.3 mM
5	sodium phosphate	natural abundance		50 mM
6	sodium chloride	natural abundance		50 mM

4 3D HNCACB

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
4	protein	[U-13C; U-15N]		0.3 mM
5	sodium phosphate	natural abundance		50 mM
6	sodium chloride	natural abundance		50 mM

5 3D HNCA

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
4	protein	[U-13C; U-15N]		0.3 mM
5	sodium phosphate	natural abundance		50 mM
6	sodium chloride	natural abundance		50 mM

6 3D HCCH-COSY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
4	protein	[U-13C; U-15N]		0.3 mM
5	sodium phosphate	natural abundance		50 mM
6	sodium chloride	natural abundance		50 mM

7 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
4	protein	[U-13C; U-15N]		0.3 mM
5	sodium phosphate	natural abundance		50 mM
6	sodium chloride	natural abundance		50 mM

8 3D 1H-15N NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	protein	[U-15N]		0.3 mM
2	sodium phosphate	natural abundance		50 mM
3	sodium chloride	natural abundance		50 mM

9 3D 1H-13C NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
4	protein	[U-13C; U-15N]		0.3 mM
5	sodium phosphate	natural abundance		50 mM
6	sodium chloride	natural abundance		50 mM

10 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
4	protein	[U-13C; U-15N]		0.3 mM
5	sodium phosphate	natural abundance		50 mM
6	sodium chloride	natural abundance		50 mM

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_25243_2myu.nef
Input source #2: Coordindates	2myu.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
A:80:CYS:SG	A:82:CYS:SG	oxidized, CA 54.79, CB 43.288 ppm	unknown, CA 55.903 ppm	2.038

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
MKKVMFVSKRNSSRSQMAEGFAKTLGAGKIAVTSSGLESSRVHPTAIAMMEEVGIDISGQTSDPIENFNADDYDVVISLCGCGVNLPPEWVTQEIFEDWQ
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MKKVMFVSKRNSSRSQMAEGFAKTLGAGKIAVTSSGLESSRVHPTAIAMMEEVGIDISGQTSDPIENFNADDYDVVISLCGCGVNLPPEWVTQEIFEDWQ

-------110-------120-------130-
LEDPDGQSLEVFRTVRGQVKERVENLIAKIS
|||||||||||||||||||||||||||||||
LEDPDGQSLEVFRTVRGQVKERVENLIAKIS

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	131	0	0	100.0

Content subtype: combined_25243_2myu.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	1		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1403		99.2 (chain: A, length: 131)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	3681 (1)	noe	99.2 (chain: A, length: 131)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	3 (1)	undefined	1.5 (chain: A, length: 131)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 131, Sequence coverage: 99.2%
- Total number of assignments
  - ¹H chemical shifts: 723
  - ¹³C chemical shifts: 542
  - ¹⁵N chemical shifts: 138
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 131, Sequence coverage: 99.2%
- Total number of restraints: 3679
- Weight of restraints: 1.0 (3679)
- Potential type of restraints: upper-bound-parabolic (3679)
- Range of distance target values: 2.8, 6.5 (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_3
  - Status: Warning
  - Experiment type: undefined
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 131, Sequence coverage: 1.5%
  - Total number of restraints: 3
  - Weight of restraints: 1.0 (3)
  - Potential type of restraints: upper-bound-parabolic (3)
  - Range of distance target values: 2.1, 3.1 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Keywords alpha/beta/alpha sandwich fold