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

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Found 1 Document (2.505 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

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NMR combined restraints 4 contents Detail