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Found 1 Document (1.067 seconds)

BMRB: 18518

2LUE

LC3B OPTN-LIR Ptot complex structure

Authors

Rogov, V.V., Rozenknop, A., Loehr, F., Guentert, P., Doetsch, V.

Assembly

LC3B OPTN-LIR Ptot complex structure

Entity

1. LC3B OPTN-LIR Ptot complex structure, entity 1 (polymer, Thiol state: not present), 119 monomers, 13943.93 Da Detail

GAMGKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVYASQETF

2. LC3B OPTN-LIR Ptot complex structure, entity 2 (polymer, Thiol state: not present), 17 monomers, 2244.804 Da Detail

NXXGXXEDXF VEIRMAE

Total weight

16188.733 Da

Max. entity weight

13943.93 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

restrained energy refinement

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.3 %, Completeness: 92.3 %, Completeness (bb): 91.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	92.3 % (1483 of 1606)	97.9 % (826 of 844)	85.4 % (533 of 624)	89.9 % (124 of 138)
Backbone	91.8 % (712 of 776)	98.1 % (258 of 263)	88.1 % (341 of 387)	89.7 % (113 of 126)
Sidechain	92.6 % (884 of 955)	97.8 % (568 of 581)	84.3 % (305 of 362)	91.7 % (11 of 12)
Aromatic	78.2 % (97 of 124)	100.0 % (62 of 62)	56.5 % (35 of 62)
Methyl	91.8 % (134 of 146)	94.5 % (69 of 73)	89.0 % (65 of 73)

1. entity 1

GAMGKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVYASQETF

2. entity 2

NXXGXXEDXF VEIRMAE

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of OPTN-LIR in complex with LC3B Ptot

#	Name	Isotope labeling	Concentration
9	entity_1	[U-98% 13C; U-98% 15N]	2.5 (±0.05) mM
10	entity_2	natural abundance	0.4 (±0.04) mM
11	sodium phosphate	natural abundance	70 mM
12	sodium chloride	natural abundance	30 mM
13	DSS	natural abundance	0.3 mM
14	Protease inhibitors cocktail	natural abundance	5 mM
15	H2O	natural abundance	95 %
16	D2O	natural abundance	5 %

Protein Blocks Logo

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

Release date

2013-07-14

Citation

Structural basis for phosphorylation-triggered autophagic clearance of Salmonella
Rogov, V.V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D.G., Lohr, F., Guntert, P., Dikic, I., Wakatsuki, S., Dotsch, V.
Biochem. J. (2013), 454, 459-466, PubMed 23805866 , DOI 10.1042/BJ20121907 , Abstract

Related entities 1. LC3B OPTN-LIR Ptot complex structure, entity 1, : 2 : 74 entities Detail

Related entities 2. LC3B OPTN-LIR Ptot complex structure, entity 2, : 1 entities Detail

Experiments performed 12 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

3 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

4 3D HNCACB

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

5 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

6 3D HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

7 3D 1H-15N NOESY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

8 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

9 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

10 3D NOESY-[13C,1H]-HSQC 13C/15N filtered in F1

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

11 2D 1H-1H NOESY F1,F2 13C/15N filtered

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of OPTN-LIR in complex with LC3B Ptot

#	Name	Isotope labeling	Concentration
9	entity_1	[U-98% 13C; U-98% 15N]	2.5 (±0.05) mM
10	entity_2	natural abundance	0.4 (±0.04) mM
11	sodium phosphate	natural abundance	70 mM
12	sodium chloride	natural abundance	30 mM
13	DSS	natural abundance	0.3 mM
14	Protease inhibitors cocktail	natural abundance	5 mM
15	H2O	natural abundance	95 %
16	D2O	natural abundance	5 %

12 3D NOESY-[15N,1H]-FHSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 288 K, pH 6.8, Details Assignment and distance restraints of LC3B in complex with OPTN-LIR Ptot

#	Name	Isotope labeling	Concentration
1	entity_1	[U-98% 13C; U-98% 15N]	0.6 (±0.05) mM
2	entity_2	natural abundance	4.9 (±0.5) mM
3	sodium phosphate	natural abundance	70 mM
4	sodium chloride	natural abundance	30 mM
5	DSS	natural abundance	0.3 mM
6	Protease inhibitors cocktail	natural abundance	5 mM
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_18518_2lue.nef
Input source #2: Coordindates	2lue.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
2:1:ASN:C	2:2:SEP:N	unknown	unknown	n/a
2:2:SEP:C	2:3:SEP:N	unknown	unknown	n/a
2:3:SEP:C	2:4:GLY:N	unknown	unknown	n/a
2:4:GLY:C	2:5:SEP:N	unknown	unknown	n/a
2:5:SEP:C	2:6:SEP:N	unknown	unknown	n/a
2:6:SEP:C	2:7:GLU:N	unknown	unknown	n/a
2:8:ASP:C	2:9:SEP:N	unknown	unknown	n/a
2:9:SEP:C	2:10:PHE:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	170	SEP	PHOSPHOSERINE	Assigned chemical shifts, Coordinates
B	171	SEP	PHOSPHOSERINE	Assigned chemical shifts, Coordinates
B	173	SEP	PHOSPHOSERINE	Assigned chemical shifts, Coordinates
B	174	SEP	PHOSPHOSERINE	Assigned chemical shifts, Coordinates
B	177	SEP	PHOSPHOSERINE	Assigned chemical shifts, Coordinates

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
GAMGKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYE
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GAMGKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYE

-------110---------
SEKDEDGFLYMVYASQETF
|||||||||||||||||||
SEKDEDGFLYMVYASQETF

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

-170-----180-----
NXXGXXEDXFVEIRMAE
|||||||||||||||||
NXXGXXEDXFVEIRMAE
--------10-------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	119	0	0	100.0
B	B	17	0	0	100.0

Content subtype: combined_18518_2lue.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	8		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1567		100.0 (chain: A, length: 119), 100.0 (chain: B, length: 17)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	4511 (1)	noe	99.2 (chain: A, length: 119), 52.9 (chain: B, length: 17)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	94 (1)	hbond	51.3 (chain: A, length: 119), 11.8 (chain: B, length: 17)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_4	OK	243 (243)	.	99.2 (chain: A, length: 119), 58.8 (chain: B, length: 17)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 119, Sequence coverage: 100.0%

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
GAMGKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYE
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GAMGKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYE

-------110---------
SEKDEDGFLYMVYASQETF
|||||||||||||||||||
SEKDEDGFLYMVYASQETF

Entity_assembly_ID: B, Chain length: 17, Sequence coverage: 100.0%

-170-----180-----
NXXGXXEDXFVEIRMAE
|||||||||||||||||
NXXGXXEDXFVEIRMAE

Total number of assignments
- ¹H chemical shifts: 878
- ¹³C chemical shifts: 548
- ¹⁵N chemical shifts: 141

Completeness of assignments

Entity_assemble_ID: A

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
9	GLN	CD	180.738
10	ARG	HH12	6.88
10	ARG	HH22	7.56
11	ARG	HH12	7.215
11	ARG	HH22	7.256
11	ARG	NH1	72.531
11	ARG	NH2	72.478
15	GLN	CD	180.549
21	ARG	HH11	7.053
21	ARG	HH12	6.835
21	ARG	HH21	7.118
21	ARG	HH22	6.99
21	ARG	NH1	71.77
21	ARG	NH2	71.77
24	ARG	HH12	6.53
24	ARG	HH22	7.116
24	ARG	NH1	71.595
24	ARG	NH2	71.595
26	GLN	CD	179.885
37	ARG	HH12	6.498
37	ARG	HH22	6.555
37	ARG	NH1	69.721
37	ARG	NH2	70.893
43	GLN	CD	180.164
59	ASN	CG	175.864
68	ARG	HH22	7.488
69	ARG	HH22	7.5
70	ARG	HH12	7.215
70	ARG	HH22	7.256
70	ARG	NH1	72.531
70	ARG	NH2	72.478
72	GLN	CD	181.782
74	ASN	CG	176.469
76	ASN	CG	177.398
77	GLN	CD	180.096
84	ASN	CG	178.541
116	GLN	CD	180.772

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	773	767	99.2
¹³C chemical shifts	572	537	93.9
¹⁵N chemical shifts	134	131	97.8

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	238	236	99.2
¹³C chemical shifts	238	228	95.8
¹⁵N chemical shifts	114	112	98.2

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	535	531	99.3
¹³C chemical shifts	334	309	92.5
¹⁵N chemical shifts	20	19	95.0

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	72	71	98.6
¹³C chemical shifts	72	71	98.6

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	57	57	100.0
¹³C chemical shifts	57	35	61.4

Entity_assemble_ID: B

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
- Chain_ID: B

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	91	89	97.8
¹³C chemical shifts	62	0	0.0
¹⁵N chemical shifts	19	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	35	34	97.1
¹³C chemical shifts	29	0	0.0
¹⁵N chemical shifts	17	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	56	55	98.2
¹³C chemical shifts	33	0	0.0
¹⁵N chemical shifts	2	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	6	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	5	100.0
¹³C chemical shifts	5	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 119, Sequence coverage: 99.2%
  - Entity_assembly_ID: B, Chain length: 17, Sequence coverage: 52.9%
- Total number of restraints: 4480
- Weight of restraints: 1.0 (4480)
- Potential type of restraints: upper-bound-parabolic (4480)
- Range of distance target values: 2.45, 8.77 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: DYANA/DIANA_distance_constraints_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 119, Sequence coverage: 51.3%
    - Entity_assembly_ID: B, Chain length: 17, Sequence coverage: 11.8%
  - Total number of restraints: 94
  - Weight of restraints: 1.0 (94)
  - Potential type of restraints: upper-bound-parabolic (94)
  - Range of distance target values: 2.1, 3.1 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
  - 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: 119, Sequence coverage: 99.2%
  - Entity_assembly_ID: B, Chain length: 17, Sequence coverage: 58.8%
- Total number of restraints: 243
- Total number of restraints per polymer type: 243
- Weight of restraints: 1.0 (243)
- Potential type of restraints: square-well-parabolic (243)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords LC3 proteins, Phosphoserine, Protein-peptide complex, Selective autophagy, Signaling protein

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Found 1 Document (1.067 seconds)

BMRB: 18518

Sample #1

Sample #2

Related entities 1. LC3B OPTN-LIR Ptot complex structure, entity 1, : 2 : 74 entities Detail

Related entities 2. LC3B OPTN-LIR Ptot complex structure, entity 2, : 1 entities Detail

Experiments performed 12 experiments Detail

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NMR combined restraints 5 contents Detail