BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	97.2 % (827 of 851)	99.1 % (449 of 453)	93.8 % (300 of 320)	100.0 % (78 of 78)
Backbone	95.4 % (416 of 436)	100.0 % (146 of 146)	90.9 % (200 of 220)	100.0 % (70 of 70)
Sidechain	99.2 % (483 of 487)	98.7 % (303 of 307)	100.0 % (172 of 172)	100.0 % (8 of 8)
Aromatic	100.0 % (18 of 18)	100.0 % (9 of 9)	100.0 % (9 of 9)
Methyl	100.0 % (70 of 70)	100.0 % (35 of 35)	100.0 % (35 of 35)

1. entity

QQQAVLEQER RDRELALRIA QSEAELISDE AQADLALRRS LDSYPVSKND GTRPKMTPEQ MAKEMSEFLS RGPA

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 283 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-13C; U-15N]	0.7 mM
2	sodium phosphate buffer	natural abundance	20 mM
3	NaCl	natural abundance	50 mM
4	DTT	natural abundance	2 mM
5	NaN3	natural abundance	0.1 %
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

LACS Plot; CA

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

Referencing offset: -0.02 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -0.02 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.05 ppm, Outliers: 2 Detail

LACS Plot; CO

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

Referencing offset: 2.87 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2N11, Strand ID: A Detail

Release date

2016-03-06

Citation

Myosin VI Contains a Compact Structural Motif that Binds to Ubiquitin Chains
He, F., Wollscheid, H., Nowicka, U., Biancospino, M., Valentini, E., Ehlinger, A., Acconcia, F., Magistrati, E., Polo, S., Walters, K.J.
Cell Rep. (2016), 14, 2683-2694, PubMed 26971995 , DOI 10.1016/j.celrep.2016.01.079 , Abstract

Entries sharing articles BMRB: 4 entries Detail

  BMRB: 25541 released on 2016-03-06
    Title Solution structure of MyUb (1080-1122) of human Myosin VI
  BMRB: 25542 released on 2016-03-06
    Title Solution structure of MyUb (1080-1131) of human Myosin VI
  BMRB: 25545 released on 2016-03-06
    Title Complex structure of MyUb (1080-1122) of human Myosin VI with K63-diUb
  BMRB: 25544 released on 2016-02-28
    Title Solution structure of human Myosin VI isoform3 (1050-1131)

Related entities 1. human Myosin VI isoform3 (998-1071), : 1 : 2 : 8 entities Detail

Interaction partners 1. human Myosin VI isoform3 (998-1071), : 75 interactors Detail

More details for 75 interactors identified by 23 citations

Experiments performed 2 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25543_2n11.nef
Input source #2: Coordindates	2n11.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---------
QQQAVLEQERRDRELALRIAQSEAELISDEAQADLALRRSLDSYPVSKNDGTRPKMTPEQMAKEMSEFLSRGPA
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
QQQAVLEQERRDRELALRIAQSEAELISDEAQADLALRRSLDSYPVSKNDGTRPKMTPEQMAKEMSEFLSRGPA
--------10--------20--------30--------40--------50--------60--------70----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	74	0	0	100.0

Content subtype: combined_25543_2n11.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	825		100.0 (chain: A, length: 74)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	1707 (1)	noe	100.0 (chain: A, length: 74)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	72 (1)	hbond	64.9 (chain: A, length: 74)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_4	OK	112 (112)	.	93.2 (chain: A, length: 74)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 74, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 449
  - ¹³C chemical shifts: 294
  - ¹⁵N chemical shifts: 82
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	453	448	98.9
¹³C chemical shifts	320	294	91.9
¹⁵N chemical shifts	86	82	95.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	146	145	99.3
¹³C chemical shifts	148	122	82.4
¹⁵N chemical shifts	70	70	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	307	303	98.7
¹³C chemical shifts	172	172	100.0
¹⁵N chemical shifts	16	12	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	38	100.0
¹³C chemical shifts	38	38	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

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 74, Sequence coverage: 100.0%
- Total number of restraints: 1707
- Weight of restraints: 1.0 (1707)
- Potential type of restraints: upper-bound-parabolic (1707)
- Range of distance target values: 2.67, 5.5 (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
- Saveframe: DYANA/DIANA_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 74, Sequence coverage: 64.9%
  - Total number of restraints: 72
  - Weight of restraints: 1.0 (72)
  - Potential type of restraints: upper-bound-parabolic (72)
  - Range of distance target values: 2.0, 3.0 (Å)
  - Histogram of 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: 74, Sequence coverage: 93.2%
- Total number of restraints: 112
- Total number of restraints per polymer type: 112
- Weight of restraints: 1.0 (112)
- Potential type of restraints: square-well-parabolic (112)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords MIU, Myosin VI

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Found 1 Document (4.598 seconds)

BMRB: 25543

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. human Myosin VI isoform3 (998-1071), : 1 : 2 : 8 entities Detail

Interaction partners 1. human Myosin VI isoform3 (998-1071), : 75 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail