BMRBj - BMREntryMaster

Found 1 Document (2.492 seconds)

BMRB: 15092

7BXG

1H, 13C, 15N chemical shift assignments for the human E2 ubiquitin conjugating enzyme Ubc13

Authors

Mercier, P., Lewis, M.J., Hau, D.DUONG., Saltibus, L.F., Xiao, W., Spyracopoulos, L.

Assembly

single polypeptide

Entity

1. single polypeptide (polymer, Thiol state: all free), 157 monomers, 17549.05 Da Detail

GPLGSMAGLP RRIIKETQRL LAEPVPGIKA EPDESNARYF HVVIAGPQDS PFEGGTFKLE LFLPEEYPMA APKVRFMTKI YHPNVDKLGR ICLDILKDKW SPALQIRTVL LSIQALLSAP NPDDPLANDV AEQWKTNEAQ AIETARAWTR LYAMNNI

Formula weight

17549.05 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.7 %, Completeness: 61.5 %, Completeness (bb): 74.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	61.5 % (1143 of 1859)	58.6 % (570 of 973)	61.4 % (447 of 728)	79.7 % (126 of 158)
Backbone	74.1 % (676 of 912)	82.4 % (253 of 307)	64.1 % (297 of 463)	88.7 % (126 of 142)
Sidechain	55.2 % (605 of 1096)	47.6 % (317 of 666)	69.6 % (288 of 414)	0.0 % (0 of 16)
Aromatic	0.0 % (0 of 126)	0.0 % (0 of 63)	0.0 % (0 of 60)	0.0 % (0 of 3)
Methyl	89.4 % (168 of 188)	89.4 % (84 of 94)	89.4 % (84 of 94)

1. Ubc13

GPLGSMAGLP RRIIKETQRL LAEPVPGIKA EPDESNARYF HVVIAGPQDS PFEGGTFKLE LFLPEEYPMA APKVRFMTKI YHPNVDKLGR ICLDILKDKW SPALQIRTVL LSIQALLSAP NPDDPLANDV AEQWKTNEAQ AIETARAWTR LYAMNNI

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.5, Details Additionally contained 3 uL of 100X stock protease inhibitor cocktail I (Calbiochem catalog #539131)

#	Name	Isotope labeling	Concentration
1	Ubc13	[U-13C; U-15N]	0.5 mM
2	DSS	none	1 mM
3	DTT	none	1 mM

LACS Plot; CA

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

Referencing offset: 0.0 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.0 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: -0.13 ppm, Outliers: 3 Detail

Release date

2007-04-23

Citation

Structure, interactions, and dynamics of the RING domain from human TRAF6
Mercier, P., Lewis, M.J., Hau, D.DUONG., Saltibus, L.F., Xiao, W., Spyracopoulos, L.
Protein Sci. (2007), 16, 602-614, PubMed 17327397 , DOI 10.1110/ps.062358007 , Abstract

Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail

  BMRB: 15014 released on 2007-04-23
    Title Solution structure of the RING domain from human TRAF6.
  Swiss-Prot: Q9Y4K3 released on 2003-05-09
    Title TRAF6_HUMAN Entity TNF receptor-associated factor 6

Related entities 1. single polypeptide, : 1 : 30 : 267 entities Detail

Interaction partners 1. single polypeptide, : 105 interactors Detail

More details for 105 interactors identified by 21 citations

Experiments performed 7 experiments Detail

1 2D 1H-15N HSQC

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.5, Details Additionally contained 3 uL of 100X stock protease inhibitor cocktail I (Calbiochem catalog #539131)

#	Name	Isotope labeling	Concentration
1	Ubc13	[U-13C; U-15N]	0.5 mM
2	DSS	none	1 mM
3	DTT	none	1 mM

2 2D 1H-13C HSQC

Instrument

Varian INOVA - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Ubc13	[U-13C; U-15N]	0.5 mM
2	DSS	none	1 mM
3	DTT	none	1 mM

3 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Ubc13	[U-13C; U-15N]	0.5 mM
2	DSS	none	1 mM
3	DTT	none	1 mM

4 3D CBCA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Ubc13	[U-13C; U-15N]	0.5 mM
2	DSS	none	1 mM
3	DTT	none	1 mM

5 3D HCCH-TOCSY

Instrument

Varian INOVA - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Ubc13	[U-13C; U-15N]	0.5 mM
2	DSS	none	1 mM
3	DTT	none	1 mM

6 3D H(CCO)NH

Instrument

Varian INOVA - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Ubc13	[U-13C; U-15N]	0.5 mM
2	DSS	none	1 mM
3	DTT	none	1 mM

7 3D C(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Ubc13	[U-13C; U-15N]	0.5 mM
2	DSS	none	1 mM
3	DTT	none	1 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr15092_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: bmr15092_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1268		90.4 (chain: 1, length: 157)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 157, Sequence coverage: 90.4%
- Total number of assignments
  - ¹H chemical shifts: 721
  - ¹³C chemical shifts: 423
  - ¹⁵N chemical shifts: 124
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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	973	557	57.2
¹³C chemical shifts	728	423	58.1
¹⁵N chemical shifts	167	124	74.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	307	251	81.8
¹³C chemical shifts	314	141	44.9
¹⁵N chemical shifts	142	124	87.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	666	306	45.9
¹³C chemical shifts	414	282	68.1
¹⁵N chemical shifts	25	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	98	82	83.7
¹³C chemical shifts	98	80	81.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	0	0.0
¹³C chemical shifts	60	0	0.0
¹⁵N chemical shifts	3	0	0.0

Keywords E2, polyubiquitination, Ubc13, ubiquitin, ubiquitin conjugating enzyme

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (2.492 seconds)

BMRB: 15092

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail

Related entities 1. single polypeptide, : 1 : 30 : 267 entities Detail

Interaction partners 1. single polypeptide, : 105 interactors Detail

Experiments performed 7 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail