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Found 1 Document (1.148 seconds)

BMRB: 17822

2LGT

Backbone 1H, 13C, and 15N Chemical Shift Assignments for QFM(Y)F

Authors

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

Assembly

QFMF

Entity

1. QFMF (polymer), 144 monomers, 16058.45 Da Detail

MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADEFGTAS NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI NQFMYFCDNK FHTEALTALL SDLE

Formula weight

16058.45 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 87.6 %, Completeness (bb): 85.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	87.6 % (1496 of 1708)	92.8 % (828 of 892)	77.7 % (517 of 665)	100.0 % (151 of 151)
Backbone	85.1 % (723 of 850)	97.2 % (280 of 288)	72.0 % (306 of 425)	100.0 % (137 of 137)
Sidechain	91.2 % (907 of 995)	90.7 % (548 of 604)	91.5 % (345 of 377)	100.0 % (14 of 14)
Aromatic	60.0 % (60 of 100)	60.0 % (30 of 50)	59.2 % (29 of 49)	100.0 % (1 of 1)
Methyl	98.3 % (173 of 176)	97.7 % (86 of 88)	98.9 % (87 of 88)

1. entity

MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADEFGTAS NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI NQFMYFCDNK FHTEALTALL SDLE

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6

#	Name	Isotope labeling	Concentration
1	DSS	natural abundance	0.1 mM
2	potassium chloride	natural abundance	100 mM
3	MES	natural abundance	20 mM
4	D2O	[U-2H]	5 %
5	H2O	natural abundance	95 %

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: 0.4 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: 0.4 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: 0.12 ppm, Outliers: 1 Detail

Protein Blocks Logo

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

Release date

2012-08-28

Citation

Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1
Wong, L.E., Li, Y., Pillay, S., Frolova, L., Pervushin, K.
Nucleic Acids Res. (2012), 40, 5751-5765, PubMed 22383581 , DOI 10.1093/nar/gks192 , Abstract

Related entities 1. QFMF, : 1 : 105 entities Detail

Interaction partners 1. QFMF, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 6 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_17822_2lgt.nef
Input source #2: Coordindates	2lgt.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
MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTI
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTI

-------110-------120-------130-------140----
VTEEGKEKKVNIDFEPFKPINQFMYFCDNKFHTEALTALLSDLE
||||||||||||||||||||||||||||||||||||||||||||
VTEEGKEKKVNIDFEPFKPINQFMYFCDNKFHTEALTALLSDLE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	144	0	0	100.0

Content subtype: combined_17822_2lgt.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1484		99.3 (chain: A, length: 144)
1	Distance restraints	DYANA/DIANA_distance_constraints_5	OK	76 (1)	hbond	66.0 (chain: A, length: 144)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_6	OK	256 (256)	.	98.6 (chain: A, length: 144)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 144, Sequence coverage: 99.3%
- Total number of assignments
  - ¹H chemical shifts: 846
  - ¹³C chemical shifts: 488
  - ¹⁵N chemical shifts: 150
- 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)
76	THR	HG1	4.608
102	THR	HG1	4.954

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	892	844	94.6
¹³C chemical shifts	665	488	73.4
¹⁵N chemical shifts	157	150	95.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	288	286	99.3
¹³C chemical shifts	288	143	49.7
¹⁵N chemical shifts	137	136	99.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	604	558	92.4
¹³C chemical shifts	377	345	91.5
¹⁵N chemical shifts	20	14	70.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	92	90	97.8
¹³C chemical shifts	92	90	97.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	30	60.0
¹³C chemical shifts	49	29	59.2
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_5
- Status: OK
- Experiment type: hbond
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 144, Sequence coverage: 66.0%
- Total number of restraints: 76
- Weight of restraints: 1.0 (76)
- Potential type of restraints: upper-bound-parabolic (76)
- Range of distance target values: 2.3, 3.5 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_6
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 144, Sequence coverage: 98.6%
- Total number of restraints: 256
- Total number of restraints per polymer type: 256
- Weight of restraints: 1.0 (256)
- Potential type of restraints: square-well-parabolic (256)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

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Found 1 Document (1.148 seconds)

BMRB: 17822

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. QFMF, : 1 : 105 entities Detail

Interaction partners 1. QFMF, : 1 interactors Detail

Experiments performed 6 experiments Detail

Instrument

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NMR combined restraints 4 contents Detail