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Found 1 Document (2.157 seconds)

BMRB: 15388

2JT3

Solution Structure of F153W cardiac troponin C

Authors

Wang, X., Mercier, P., Letourneau, P., Sykes, B.D.

Assembly

F153W cTnC

Entity

1. F153W (polymer, Thiol state: not present), 161 monomers, 18409.24 Da Detail

MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGSISTKE LGKVMRMLGQ NPTPEELQEM IDEVDEDGSG TVDFDEFLVM MVRSMKDDSK GKSEEELSDL FRMFDKNADG YIDLDELKIM LQATGETITE DDIEELMKDG DKNNDGRIDY DEWLEFMKGV E

2. CA (non-polymer), 40.078 Da

Total weight

18449.318 Da

Max. entity weight

18409.24 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.1 %, Completeness: 81.1 %, Completeness (bb): 83.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	81.1 % (1506 of 1858)	83.4 % (809 of 970)	75.3 % (541 of 718)	91.8 % (156 of 170)
Backbone	83.8 % (806 of 962)	95.5 % (317 of 332)	71.3 % (336 of 471)	96.2 % (153 of 159)
Sidechain	80.9 % (845 of 1045)	77.1 % (492 of 638)	88.4 % (350 of 396)	27.3 % (3 of 11)
Aromatic	43.1 % (50 of 116)	44.8 % (26 of 58)	40.4 % (23 of 57)	100.0 % (1 of 1)
Methyl	97.3 % (144 of 148)	97.3 % (72 of 74)	97.3 % (72 of 74)

1. F153W

MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGSISTKE LGKVMRMLGQ NPTPEELQEM IDEVDEDGSG TVDFDEFLVM MVRSMKDDSK GKSEEELSDL FRMFDKNADG YIDLDELKIM LQATGETITE DDIEELMKDG DKNNDGRIDY DEWLEFMKGV E

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 (±0.5) K, pH 6.7 (±0.2)

#	Name	Isotope labeling	Concentration
1	F153W	natural abundance	1.0 (±0.2) mM
2	Calcium	natural abundance	10 (±1.0) mM
3	potassium chloride	natural abundance	100 (±10.0) mM

LACS Plot; CA

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

Referencing offset: 0.27 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.27 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.0 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 2JT3, Strand ID: A Detail

Release date

2008-03-12

Citation

Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies
Wang, X., Mercier, P., Letourneau, P., Sykes, B.
Protein Sci. (2005), 14, 2447-2460, PubMed 16131667 , DOI 10.1110/ps.051595805 , Abstract

Entries sharing articles BMRB: 3 entries Detail

  BMRB: 15427 released on 2008-03-13
    Title Chemical shift assignments of the F104-to-5-flurotryptophan mutant of cardiac troponin C
  BMRB: 15385 released on 2007-08-14
    Title Solution structure of F104W cardiac troponin C
  BMRB: 15400 released on 2007-08-12
    Title Backbone and side chain chemical shift assignments of the F153-to-5-flurotryptophan mutant of human cardiac troponin C

Related entities 1. F153W, : 1 : 13 : 1 : 234 entities Detail

Interaction partners 1. F153W, : 8 interactors Detail

More details for 8 interactors identified by 5 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_15388_2jt3.nef
Input source #2: Coordindates	2jt3.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
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGSISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRSMKDDSKGKSEEELSDL
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGSISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRSMKDDSKGKSEEELSDL

-------110-------120-------130-------140-------150-------160-
FRMFDKNADGYIDLDELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEWLEFMKGVE
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
FRMFDKNADGYIDLDELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEWLEFMKGVE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	161	0	0	100.0

Content subtype: combined_15388_2jt3.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1453		98.1 (chain: A, length: 161)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	2553 (1)	noe	95.0 (chain: A, length: 161)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_4	OK	926 (926)	.	94.4 (chain: A, length: 161)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 161, Sequence coverage: 98.1%
- Total number of assignments
  - ¹³C chemical shifts: 509
  - ¹H chemical shifts: 790
  - ¹⁵N chemical shifts: 154
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
62	ASP	CG	30.05

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	718	508	70.8
¹H chemical shifts	970	790	81.4
¹⁵N chemical shifts	174	154	88.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	322	158	49.1
¹H chemical shifts	332	316	95.2
¹⁵N chemical shifts	159	152	95.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	396	350	88.4
¹H chemical shifts	638	474	74.3
¹⁵N chemical shifts	15	2	13.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	85	82	96.5
¹H chemical shifts	85	83	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	57	23	40.4
¹H chemical shifts	58	26	44.8
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 161, Sequence coverage: 95.0%
- Total number of restraints: 2553
- Weight of restraints: 1.0 (2553)
- Potential type of restraints: upper-bound-parabolic (2553)
- Range of distance target values: 2.28, 6.0 (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_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 161, Sequence coverage: 94.4%
- Total number of restraints: 926
- Total number of restraints per polymer type: 926
- Weight of restraints: 1.0 (926)
- Potential type of restraints: square-well-parabolic (926)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords calcium-binding protein, EF-hand protein, muscle regulatory protein, Trp mutation, Calcium-bind protein, Phe-to-Trp mutation

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Found 1 Document (2.157 seconds)

BMRB: 15388

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 3 entries Detail

Related entities 1. F153W, : 1 : 13 : 1 : 234 entities Detail

Interaction partners 1. F153W, : 8 interactors Detail

Experiments performed 6 experiments Detail

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NMR combined restraints 4 contents Detail