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Found 1 Document (1.148 seconds)

BMRB: 25020

2MQ9

Solution structure of E55Q mutant of eRF1 N-domain

Authors

Pillay, S., Li, Y., Wong, L., Pervushin, K.

Assembly

E55Q mutant of eRF1 N-domain

Entity

1. E55Q mutant of eRF1 N-domain (polymer), 142 monomers, 15676.02 Da Detail

MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADQFGTAS NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI NTSLYLCDNK FHTEALTALL SD

Formula weight

15676.02 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

torsion angle dynamics, simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.3 %, Completeness: 85.3 %, Completeness (bb): 83.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	85.3 % (1422 of 1668)	91.4 % (795 of 870)	74.0 % (480 of 649)	98.7 % (147 of 149)
Backbone	83.8 % (702 of 838)	97.5 % (277 of 284)	69.5 % (291 of 419)	99.3 % (134 of 135)
Sidechain	87.6 % (845 of 965)	88.4 % (518 of 586)	86.0 % (314 of 365)	92.9 % (13 of 14)
Aromatic	65.0 % (52 of 80)	65.0 % (26 of 40)	64.1 % (25 of 39)	100.0 % (1 of 1)
Methyl	97.3 % (177 of 182)	94.5 % (86 of 91)	100.0 % (91 of 91)

1. entity

MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADQFGTAS NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI NTSLYLCDNK FHTEALTALL SD

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	MES	natural abundance	20 mM
2	potassium chloride	natural abundance	100 mM
3	DTT	natural abundance	2 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

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: 0.34 ppm, Outliers: 4 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: 0.34 ppm, Outliers: 4 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: 0.22 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2MQ9, Strand ID: A Detail

Release date

2015-06-28

Citation

Structural insights of eRF1 mutants and their correlation with stop codon recognition
Pillay, S., Li, Y., Wong, L., Pervushin, K.
ACS Chemical Biology

Related entities 1. E55Q mutant of eRF1 N-domain, : 1 : 16 : 93 entities Detail

Interaction partners 1. E55Q mutant of eRF1 N-domain, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 4 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, RDC restraints	combined_25020_2mq9.nef
Input source #2: Coordindates	2mq9.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
MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADQFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTI
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADQFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTI

-------110-------120-------130-------140--
VTEEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSD
||||||||||||||||||||||||||||||||||||||||||
VTEEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSD

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	142	0	0	100.0

Content subtype: combined_25020_2mq9.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1378		98.6 (chain: A, length: 142)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	1391 (1)	noe	97.2 (chain: A, length: 142)
1	RDC restraints	DYANA/DIANA_dipolar_coupling_2	Warning	29 (29)	.	20.4 (chain: A, length: 142)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 142, Sequence coverage: 98.6%
- Total number of assignments
  - ¹H chemical shifts: 788
  - ¹³C chemical shifts: 444
  - ¹⁵N chemical shifts: 146
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
32	THR	HG1	4.683
76	THR	HG1	4.594
77	SER	HG	4.536
127	CYS	HG	1.314

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	870	784	90.1
¹³C chemical shifts	649	444	68.4
¹⁵N chemical shifts	155	146	94.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	284	279	98.2
¹³C chemical shifts	284	137	48.2
¹⁵N chemical shifts	135	133	98.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	586	505	86.2
¹³C chemical shifts	365	307	84.1
¹⁵N chemical shifts	20	13	65.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	94	89	94.7
¹³C chemical shifts	94	92	97.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	20	50.0
¹³C chemical shifts	39	24	61.5
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_3
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 142, Sequence coverage: 97.2%
- Total number of restraints: 1391
- Weight of restraints: 1.0 (1391)
- Potential type of restraints: upper-bound-parabolic (1391)
- Range of distance target values: 2.3, 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

RDC restraints

Saveframe: DYANA/DIANA_dipolar_coupling_2
- Status: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 142, Sequence coverage: 20.4%
- Total number of restraints: 29
- Potential type of restraints: undefined (29)
- Range of observed RDC values: 100.0, -100.0 (Hz)
- RDC restraints per residue

Keywords eRF1, protein

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Found 1 Document (1.148 seconds)

BMRB: 25020

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. E55Q mutant of eRF1 N-domain, : 1 : 16 : 93 entities Detail

Interaction partners 1. E55Q mutant of eRF1 N-domain, : 1 interactors Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail