BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	96.7 % (967 of 1000)	97.5 % (517 of 530)	94.8 % (366 of 386)	100.0 % (84 of 84)
Backbone	96.3 % (468 of 486)	98.8 % (161 of 163)	93.4 % (228 of 244)	100.0 % (79 of 79)
Sidechain	97.3 % (578 of 594)	97.0 % (356 of 367)	97.7 % (217 of 222)	100.0 % (5 of 5)
Aromatic	97.4 % (74 of 76)	97.4 % (37 of 38)	97.2 % (35 of 36)	100.0 % (2 of 2)
Methyl	100.0 % (74 of 74)	100.0 % (37 of 37)	100.0 % (37 of 37)

1. entity

RPKMTPEQMA KEMSEFLSRG PAVLATKAAA GTKKYDLSKW KYAELRDTIN TSCDIELLAA CREEFHRRLK VYHAWKSKNK KR

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: 0.05 ppm, Outliers: 4 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: 0.05 ppm, Outliers: 4 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: 0.06 ppm, Outliers: 1 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: 2.44 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2N12, Strand ID: A Detail

Release date

2016-02-28

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

Related entities 1. human Myosin VI isoform3 (1050-1131), : 1 : 3 : 9 entities Detail

Interaction partners 1. human Myosin VI isoform3 (1050-1131), : 74 interactors Detail

More details for 74 interactors identified by 22 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_25544_2n12.nef
Input source #2: Coordindates	2n12.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

--60-------70--------80--------90-------100-------110-------120-------130---------
RPKMTPEQMAKEMSEFLSRGPAVLATKAAAGTKKYDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKR
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
RPKMTPEQMAKEMSEFLSRGPAVLATKAAAGTKKYDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKR
--------10--------20--------30--------40--------50--------60--------70--------80--

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	82	0	0	100.0

Content subtype: combined_25544_2n12.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	982		100.0 (chain: A, length: 82)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	2435 (1)	noe	100.0 (chain: A, length: 82)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	84 (1)	hbond	67.1 (chain: A, length: 82)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_4	OK	102 (102)	.	76.8 (chain: A, length: 82)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 82, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 527
  - ¹³C chemical shifts: 366
  - ¹⁵N chemical shifts: 89
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	530	526	99.2
¹³C chemical shifts	386	366	94.8
¹⁵N chemical shifts	91	89	97.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	163	162	99.4
¹³C chemical shifts	164	145	88.4
¹⁵N chemical shifts	79	79	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	367	364	99.2
¹³C chemical shifts	222	221	99.5
¹⁵N chemical shifts	12	10	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	40	100.0
¹³C chemical shifts	40	40	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	37	97.4
¹³C chemical shifts	36	35	97.2
¹⁵N chemical shifts	2	2	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 82, Sequence coverage: 100.0%
- Total number of restraints: 2435
- Weight of restraints: 1.0 (2435)
- Potential type of restraints: upper-bound-parabolic (2435)
- Range of distance target values: 2.31, 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: 82, Sequence coverage: 67.1%
  - Total number of restraints: 84
  - Weight of restraints: 1.0 (84)
  - Potential type of restraints: upper-bound-parabolic (84)
  - 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: 82, Sequence coverage: 76.8%
- Total number of restraints: 102
- Total number of restraints per polymer type: 102
- Weight of restraints: 1.0 (102)
- Potential type of restraints: square-well-parabolic (102)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords MyUb, Myosin VI

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Found 1 Document (4.583 seconds)

BMRB: 25544

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. human Myosin VI isoform3 (1050-1131), : 1 : 3 : 9 entities Detail

Interaction partners 1. human Myosin VI isoform3 (1050-1131), : 74 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail