BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	98.0 % (888 of 906)	98.3 % (468 of 476)	97.7 % (341 of 349)	97.5 % (79 of 81)
Backbone	97.8 % (440 of 450)	98.7 % (153 of 155)	97.3 % (216 of 222)	97.3 % (71 of 73)
Sidechain	98.5 % (518 of 526)	98.1 % (315 of 321)	99.0 % (195 of 197)	100.0 % (8 of 8)
Aromatic	100.0 % (32 of 32)	100.0 % (16 of 16)	100.0 % (16 of 16)
Methyl	100.0 % (98 of 98)	100.0 % (49 of 49)	100.0 % (49 of 49)

1. ubiquitin

MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ NRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG

Show sample condition

Sample

Solvent system 88% H2O/12% D2O, Pressure 2500 bar, Temperature 298 K, pH 7.2

#	Name	Isotope labeling	Type	Concentration
1	ubiquitin	[U-100% 13C; U-100% 15N]	protein	2 mM
2	Tris(hydroxymethyl)aminomethane	[U-100% 2H]	buffer	20 mM
3	DSS	natural abundance		0.2 mM
4	H2O		solvent	88 %
5	D2O		solvent	12 %

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	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.101329

Referencing offset: -0.09 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	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.101329

Referencing offset: -0.09 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	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.101329

Referencing offset: -0.01 ppm, Outliers: 1 Detail

LACS Plot; CO

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	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.101329

Referencing offset: 0.07 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2RU6, Strand ID: A Detail

Release date

2014-02-03

Citation

Close identity between alternatively folded state N2 of ubiquitin and the conformation of the protein bound to the ubiquitin-activating enzyme
Kitazawa, S., Kameda, T., Kumo, A., Utsumi, M., Baxter, N., Kato, K., Williamson, M.P., Kitahara, R.
Biochemistry (2014), 53, 447-449, PubMed 24401037 , DOI 10.1021/bi401617n , Abstract

Related entities 1. the pure alternative state of ubiquitin, : 1 : 2 : 381 : 340 entities Detail

Interaction partners 1. the pure alternative state of ubiquitin, : 27 interactors Detail

More details for 27 interactors identified by 16 citations

Experiments performed 5 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_11547_2ru6.nef
Input source #2: Coordindates	2ru6.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------
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQNRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQNRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	76	0	0	100.0

Content subtype: combined_11547_2ru6.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	882		100.0 (chain: A, length: 76)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	1527 (1)	noe	97.4 (chain: A, length: 76)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	72 (72)	.	64.5 (chain: A, length: 76)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 76, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 466
  - ¹³C chemical shifts: 337
  - ¹⁵N chemical shifts: 79
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	476	466	97.9
¹³C chemical shifts	349	337	96.6
¹⁵N chemical shifts	85	79	92.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	155	152	98.1
¹³C chemical shifts	152	143	94.1
¹⁵N chemical shifts	73	71	97.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	321	314	97.8
¹³C chemical shifts	197	194	98.5
¹⁵N chemical shifts	12	8	66.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	49	98.0
¹³C chemical shifts	50	49	98.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	16	16	100.0
¹³C chemical shifts	16	16	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 76, Sequence coverage: 97.4%
- Total number of restraints: 1525
- Weight of restraints: 1.0 (1525)
- Potential type of restraints: upper-bound-parabolic (1525)
- Range of distance target values: 2.58, 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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 76, Sequence coverage: 64.5%
- Total number of restraints: 72
- Total number of restraints per polymer type: 72
- Weight of restraints: 1.0 (72)
- Potential type of restraints: square-well-parabolic (72)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords alternatively folded state, high-pressure NMR, ubiquitin

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 (2.628 seconds)

BMRB: 11547

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. the pure alternative state of ubiquitin, : 1 : 2 : 381 : 340 entities Detail

Interaction partners 1. the pure alternative state of ubiquitin, : 27 interactors Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail