BMRBj - BMREntryMaster

Found 1 Document (0.487 seconds)

BMRB: 30874

7LXC

Structure and Interactions of DED1 of human cFLIP

Authors

Panaitiu, A.E., Basiashvili, T., Mierke, D.F., Pellegrini, M.

Assembly

DED1ch

Entity

1. DED1ch (polymer), 105 monomers, 12396.30 Da Detail

MHHHHHHMSA EVIHQVEEAL SSSELTELKY LCLGRVGKRK LERVQSGVRD LLDILRERGK LSVGDLAELL YRVRRFDLLK RILKMDRKAV ETHLLRNPHL VSDYR

Formula weight

12396.3 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 95.2 %, Completeness: 80.9 %, Completeness (bb): 81.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	80.9 % (1040 of 1285)	86.4 % (577 of 668)	72.8 % (362 of 497)	84.2 % (101 of 120)
Backbone	81.4 % (511 of 628)	92.5 % (198 of 214)	69.7 % (216 of 310)	93.3 % (97 of 104)
Sidechain	81.9 % (620 of 757)	83.5 % (379 of 454)	82.6 % (237 of 287)	25.0 % (4 of 16)
Aromatic	58.6 % (41 of 70)	60.0 % (21 of 35)	57.1 % (20 of 35)
Methyl	89.0 % (121 of 136)	91.2 % (62 of 68)	86.8 % (59 of 68)

1. entity 1

MHHHHHHMSA EVIHQVEEAL SSSELTELKY LCLGRVGKRK LERVQSGVRD LLDILRERGK LSVGDLAELL YRVRRFDLLK RILKMDRKAV ETHLLRNPHL VSDYR

Show sample condition

Sample

Solvent system 99% H2O/1% D2O, Pressure 1 atm, Temperature 291 K, pH 5.8, Details 20 mM sodium succinate, 250 mM sodium chloride, 3 mM DTT, 0.2 mM pefabloc, 99% H2O/1% D2O

#	Name	Isotope labeling	Concentration
1	entity_1	[U-13C; U-15N]	300 uM
2	sodium succinate	natural abundance	20 mM
3	sodium chloride	natural abundance	250 mM
4	DTT	natural abundance	3 mM
5	pefabloc	natural abundance	0.2 mM

Chem. Shift Complete2

Sequence coverage: 97.1 %, Completeness: 81.0 %, Completeness (bb): 81.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	81.0 % (2081 of 2570)	86.4 % (1154 of 1336)	72.7 % (723 of 994)	85.0 % (204 of 240)
Backbone	81.1 % (1018 of 1256)	92.5 % (396 of 428)	68.7 % (426 of 620)	94.2 % (196 of 208)
Sidechain	82.4 % (1248 of 1514)	83.5 % (758 of 908)	84.0 % (482 of 574)	25.0 % (8 of 32)
Aromatic	58.6 % (82 of 140)	60.0 % (42 of 70)	57.1 % (40 of 70)
Methyl	90.1 % (245 of 272)	91.9 % (125 of 136)	88.2 % (120 of 136)

1. entity 1

MHHHHHHMSA EVIHQVEEAL SSSELTELKY LCLGRVGKRK LERVQSGVRD LLDILRERGK LSVGDLAELL YRVRRFDLLK RILKMDRKAV ETHLLRNPHL VSDYR

Show sample condition

Sample

Solvent system 99% H2O/1% D2O, Pressure 1 atm, Temperature 291 K, pH 5.8, Details 20 mM sodium succinate, 250 mM sodium chloride, 3 mM DTT, 0.2 mM pefabloc, 99% H2O/1% D2O

#	Name	Isotope labeling	Concentration
1	entity_1	[U-13C; U-15N]	300 uM
2	sodium succinate	natural abundance	20 mM
3	sodium chloride	natural abundance	250 mM
4	DTT	natural abundance	3 mM
5	pefabloc	natural abundance	0.2 mM

Release date

2021-03-04

Citation

An engineered construct of cFLIP provides insight into DED1 structure and interactions
Panaitiu, A.E., Basiashvili, T., Mierke, D.F., Pellegrini, M.
Structure (2022), 30, 229-239, PubMed 34800372 , DOI 10.1016/j.str.2021.10.011 , Abstract

Related entities 1. DED1ch, : 1 : 20 entities Detail

Experiments performed 4 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30874_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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr30874_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1120	91.4 (chain: 1, length: 105)
2	Assigned chemical shifts	assigned_chemical_shifts_2	Warning	1119	91.4 (chain: 1, length: 105)
1	Chemical shift references	chem_shift_reference_1	OK	3	No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 105, Sequence coverage: 91.4%
- Total number of assignments
  - ¹H chemical shifts: 694
  - ¹³C chemical shifts: 331
  - ¹⁵N chemical shifts: 95
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1
Saveframe: assigned_chemical_shifts_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 105, Sequence coverage: 91.4%
- Total number of assignments
  - ¹H chemical shifts: 694
  - ¹³C chemical shifts: 331
  - ¹⁵N chemical shifts: 94
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	668	568	85.0
¹³C chemical shifts	497	331	66.6
¹⁵N chemical shifts	120	95	79.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	214	190	88.8
¹³C chemical shifts	210	95	45.2
¹⁵N chemical shifts	104	91	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	454	378	83.3
¹³C chemical shifts	287	236	82.2
¹⁵N chemical shifts	16	4	25.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	71	63	88.7
¹³C chemical shifts	71	60	84.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	35	21	60.0
¹³C chemical shifts	35	20	57.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	668	568	85.0
¹³C chemical shifts	497	331	66.6
¹⁵N chemical shifts	120	94	78.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	214	190	88.8
¹³C chemical shifts	210	95	45.2
¹⁵N chemical shifts	104	91	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	454	378	83.3
¹³C chemical shifts	287	236	82.2
¹⁵N chemical shifts	16	3	18.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	71	63	88.7
¹³C chemical shifts	71	60	84.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	35	21	60.0
¹³C chemical shifts	35	20	57.1

Keywords DED1, Death Effector Domain, PROTEIN BINDING, apoptosis, cFLIP, chimera

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Found 1 Document (0.487 seconds)

BMRB: 30874

Sample

Sample

Related entities 1. DED1ch, : 1 : 20 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 4 contents Detail