BMRBj - BMREntryMaster

Found 1 Document (5.429 seconds)

BMRB: 17432

2L90

Solution structure of murine myristoylated msrA

Authors

Gruschus, J.M., Lim, J., Piszczek, G., Levine, R.L., Tjandra, N.

Assembly

Myristoylated msrA

Entity

1. msrA (polymer), 212 monomers, 23648.28 Da Detail

GDSASKVISA EEALPGRTEP IPVTAKHHVS GNRTVEPFPE GTQMAVFGMG CFWGAERKFW VLKGVYSTQV GFAGGHTRNP TYKEVCSEKT GHAEVVRVVY RPEHISFEEL LKVFWENHDP TQGMRQGNDF GTQYRSAVYP TSAVQMEAAL RSKEEYQKVL SKHNFGPITT DIREGQVFYY AEDYHQQYLS KNPDGYCGLG GTGVSCPMAI KK

2. MYR (non-polymer, Thiol state: not present), 228.371 Da

Total weight

23876.65 Da

Max. entity weight

23648.28 Da

Source organism

Mus musculus

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.1 %, Completeness: 46.6 %, Completeness (bb): 82.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	46.6 % (1138 of 2441)	39.5 % (501 of 1268)	46.2 % (441 of 954)	89.5 % (196 of 219)
Backbone	82.8 % (1033 of 1248)	97.0 % (421 of 434)	67.8 % (416 of 614)	98.0 % (196 of 200)
Sidechain	20.9 % (289 of 1383)	9.6 % (80 of 834)	39.4 % (209 of 530)	0.0 % (0 of 19)
Aromatic	4.3 % (11 of 256)	7.0 % (9 of 128)	1.6 % (2 of 125)	0.0 % (0 of 3)
Methyl	20.2 % (38 of 188)	16.0 % (15 of 94)	24.5 % (23 of 94)

1. msrA

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	msrA	[U-98% 13C; U-98% 15N]	0.3 (±0.05) mM
2	DTT	natural abundance	5 (±0.2) mM
3	TRIS	natural abundance	50 (±1.0) mM
4	EDTA	natural abundance	5 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

LACS Plot; CA

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

Referencing offset: 0.0 ppm, Outliers: 2 Detail

LACS Plot; CB

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

Referencing offset: 0.0 ppm, Outliers: 2 Detail

LACS Plot; HA

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

Referencing offset: 0.06 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 21 models in PDB: 2L90, Strand ID: A Detail

Release date

2012-01-08

Citation

Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A
Lim, J., Gruschus, J.M., Ghesquiere, B., Kim, G., Piszczek, G., Tjandra, N., Levine, R.L.
J. Biol. Chem. (2012), 287, 25589-25595, PubMed 22661718 , DOI 10.1074/jbc.M112.368936 , Abstract

Related entities 1. msrA, : 1 : 3 : 104 entities Detail

Interaction partners 1. msrA, : 13 interactors Detail

More details for 13 interactors identified by 1 citations

Experiments performed 5 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_17432_2l90.nef
Input source #2: Coordindates	2l90.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:1:GLY:N	2:1:MYR:C1	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	1	MYR	MYRISTIC ACID	None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

-------30--------40--------50--------60--------70--------80--------90-------100-------110-------120-
GDSASKVISAEEALPGRTEPIPVTAKHHVSGNRTVEPFPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGHTRNPTYKEVCSEKTGHAEVVRVVY
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GDSASKVISAEEALPGRTEPIPVTAKHHVSGNRTVEPFPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGHTRNPTYKEVCSEKTGHAEVVRVVY
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

------130-------140-------150-------160-------170-------180-------190-------200-------210-------220-
RPEHISFEELLKVFWENHDPTQGMRQGNDFGTQYRSAVYPTSAVQMEAALRSKEEYQKVLSKHNFGPITTDIREGQVFYYAEDYHQQYLSKNPDGYCGLG
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
RPEHISFEELLKVFWENHDPTQGMRQGNDFGTQYRSAVYPTSAVQMEAALRSKEEYQKVLSKHNFGPITTDIREGQVFYYAEDYHQQYLSKNPDGYCGLG
-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200

------230---
GTGVSCPMAIKK
||||||||||||
GTGVSCPMAIKK
-------210--

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	212	0	0	100.0

Content subtype: combined_17432_2l90.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	961		94.3 (chain: A, length: 212)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	2468 (1)	noe	98.6 (chain: A, length: 212)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	Warning	348 (346)	.	98.6 (chain: A, length: 212)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 212, Sequence coverage: 94.3%
- Total number of assignments
  - ¹³C chemical shifts: 376
  - ¹H chemical shifts: 399
  - ¹⁵N chemical shifts: 186
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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	954	376	39.4
¹H chemical shifts	1268	399	31.5
¹⁵N chemical shifts	229	186	81.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	424	199	46.9
¹H chemical shifts	434	399	91.9
¹⁵N chemical shifts	200	186	93.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	530	177	33.4
¹H chemical shifts	834	0	0.0
¹⁵N chemical shifts	29	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	99	13	13.1
¹H chemical shifts	99	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	125	0	0.0
¹H chemical shifts	128	0	0.0
¹⁵N chemical shifts	3	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 212, Sequence coverage: 98.6%
- Total number of restraints: 2468
- Weight of restraints: 1.0 (2468)
- Potential type of restraints: square-well-parabolic (2468)
- Range of distance target values: 1.61, 6.33 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
    None
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 212, Sequence coverage: 98.6%
- Total number of restraints: 346
- Total number of restraints per polymer type: 346
- Weight of restraints: 1.0 (346)
- Potential type of restraints: square-well-parabolic (346)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords methionine (S)-S-oxide reductase

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (5.429 seconds)

BMRB: 17432

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. msrA, : 1 : 3 : 104 entities Detail

Interaction partners 1. msrA, : 13 interactors Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail