BMRBj - BMREntryMaster

Found 1 Document (1.205 seconds)

BMRB: 51388

1H and 13C chemical shifts for a peptide encompassing residues 2-19 of the human formin INF2 in 30% TFE

Authors

Jimenez, M., Comas, L.

Assembly

INF2(2-19)

Entity

1. INF2(2-19) (polymer, Thiol state: not present), 19 monomers, 1997.322 Da Detail

SVKEGAQRKW AALKEKLGX

Formula weight

1997.322 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.7 %, Completeness: 85.9 %, Completeness (bb): 74.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	85.9 % (171 of 199)	90.6 % (106 of 117)	79.3 % (65 of 82)
Backbone	74.4 % (67 of 90)	84.2 % (32 of 38)	67.3 % (35 of 52)
Sidechain	96.0 % (120 of 125)	93.7 % (74 of 79)	100.0 % (46 of 46)
Aromatic	100.0 % (11 of 11)	100.0 % (6 of 6)	100.0 % (5 of 5)
Methyl	94.4 % (17 of 18)	88.9 % (8 of 9)	100.0 % (9 of 9)

1. entity 1

SVKEGAQRKW AALKEKLGX

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Concentration
1	INF2(2-19)	natural abundance	1 mM
2	D2O	[U-2H]	7 % v/v
3	H2O	natural abundance	63 % v/v
4	DSS	natural abundance	0.1 mM
5	TFE	[U-98% 2H]	30 % v/v

Release date

2022-04-05

Citation

Structure and function of the N-terminal extension of the formin INF2
Labat-de-Hoz, L., Comas, L., Rubio-Ramos, A., Casares-Arias, J., Fernandez-Martin, L., Pantoja-Uceda, D., Martin, M., Kremer, L., Jimenez, M., Correas, I., Alonso, M.A.
Cell. Mol. Life Sci. (2022), 79, 571-571, PubMed 36306014 , DOI 10.1007/s00018-022-04581-y , Abstract

Entries sharing articles BMRB: 4 entries Detail

  BMRB: 51422 released on 2022-04-27
    Title 1H, 13C and 15N backbone chemical shifts for human calmodulin in aqueous solution
  BMRB: 51407 released on 2022-04-21
    Title 1H and 13C chemical shifts for a peptide encompassing residues 2-36 of the human formin INF2 in aqueous solution
  BMRB: 51408 released on 2022-04-21
    Title 1H and 13C chemical shifts for a peptide encompassing residues 2-36 of the human formin INF2 in 30% TFE
  BMRB: 51389 released on 2022-04-05
    Title 1H and 13C chemical shifts for a peptide encompassing residues 2-19 of the human formin INF2 in aqueous solution

Related entities 1. INF2(2-19), : 5 : 2 entities Detail

Interaction partners 1. INF2(2-19), : 3 interactors Detail

More details for 3 interactors identified by 3 citations

Experiments performed 6 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr51388_3.str
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	OK

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
1	19	NH2	AMINO GROUP	Assigned chemical shifts

Content subtype: bmr51388_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	199		100.0 (chain: 1, length: 19)
1	Chemical shift references	chem_shift_reference_1	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 19, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 135
  - ¹³C chemical shifts: 64
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	119	117	98.3
¹³C chemical shifts	82	64	78.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	36	94.7
¹³C chemical shifts	52	34	65.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	81	81	100.0
¹³C chemical shifts	46	46	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	9	100.0
¹³C chemical shifts	9	9	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	5	5	100.0

Keywords formins, INF2, calmodulin-binding, peptide model

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Found 1 Document (1.205 seconds)

BMRB: 51388

Sample

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. INF2(2-19), : 5 : 2 entities Detail

Interaction partners 1. INF2(2-19), : 3 interactors Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 3 contents Detail