BMRBj - BMREntryMaster

Found 1 Document (2.291 seconds)

BMRB: 51408

1H and 13C chemical shifts for a peptide encompassing residues 2-36 of the human formin INF2 in 30% TFE

Authors

Jimenez, M.

Assembly

INF2(2-36)

Entity

1. INF2(2-36) (polymer, Thiol state: not present), 36 monomers, 3794.074 Da Detail

SVKEGAQRKW AALKEKLGPQ DSDPTEANLE SADPEX

Formula weight

3794.074 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.2 %, Completeness: 89.3 %, Completeness (bb): 79.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	89.3 % (316 of 354)	96.1 % (199 of 207)	79.6 % (117 of 147)
Backbone	79.1 % (136 of 172)	91.3 % (63 of 69)	70.9 % (73 of 103)
Sidechain	99.1 % (213 of 215)	98.6 % (136 of 138)	100.0 % (77 of 77)
Aromatic	100.0 % (11 of 11)	100.0 % (6 of 6)	100.0 % (5 of 5)
Methyl	100.0 % (28 of 28)	100.0 % (14 of 14)	100.0 % (14 of 14)

1. entity 1

SVKEGAQRKW AALKEKLGPQ DSDPTEANLE SADPEX

Show sample condition

Sample

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

#	Name	Isotope labeling	Concentration
1	INF2(2-36)	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

2022-04-21

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: 51388 released on 2022-04-05
    Title 1H and 13C chemical shifts for a peptide encompassing residues 2-19 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(2-36), : 2 : 6 entities Detail

Interaction partners 1. INF2(2-36), : 49 interactors Detail

More details for 49 interactors identified by 8 citations

Experiments performed 6 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr51408_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	36	NH2	AMINO GROUP	Assigned chemical shifts

Content subtype: bmr51408_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	347		100.0 (chain: 1, length: 36)
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: 36, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 235
  - ¹³C chemical shifts: 112
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	209	207	99.0
¹³C chemical shifts	147	112	76.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	67	97.1
¹³C chemical shifts	103	68	66.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	140	140	100.0
¹³C chemical shifts	77	77	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	14	100.0
¹³C chemical shifts	14	14	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, actin, calmodulin-binding, peptide model

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Found 1 Document (2.291 seconds)

BMRB: 51408

Sample

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. INF2(2-36), : 2 : 6 entities Detail

Interaction partners 1. INF2(2-36), : 49 interactors Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 3 contents Detail