BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	65.3 % (921 of 1411)	71.1 % (503 of 707)	59.8 % (341 of 570)	57.5 % (77 of 134)
Backbone	61.0 % (476 of 780)	66.8 % (181 of 271)	57.7 % (220 of 381)	58.6 % (75 of 128)
Sidechain	70.8 % (531 of 750)	72.7 % (317 of 436)	69.2 % (213 of 308)	16.7 % (1 of 6)
Aromatic	31.6 % (24 of 76)	63.2 % (24 of 38)	0.0 % (0 of 37)	0.0 % (0 of 1)
Methyl	85.0 % (175 of 206)	83.5 % (86 of 103)	86.4 % (89 of 103)

1. protein

DTKISSAAIL GLGIAFAGSK NDEVLGLLLP IAASTDLPIE TAAMASLALA HVFVGTCNGD ITTSIMDNFL ERTAIELKTD WVRFLALALG ILYMGQGEQV DDVLETISAI EHPMTSAIEV LVGSCAYTGT G

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N; U-80% 2H]	0.7 mM
2	HEPES	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	2 mM
5	EDTA	natural abundance	1 mM
6	sodium azide	natural abundance	0.1 %
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
9	protein	[U-100% 15N]	0.7 mM
10	HEPES	natural abundance	50 mM
11	sodium chloride	natural abundance	50 mM
12	DTT	natural abundance	2 mM
13	EDTA	natural abundance	1 mM
14	sodium azide	natural abundance	0.1 %
15	H2O	natural abundance	95 %
16	D2O	natural abundance	5 %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
17	protein	[U-100% 13C]	0.7 mM
18	HEPES	natural abundance	50 mM
19	sodium chloride	natural abundance	50 mM
20	DTT	natural abundance	2 mM
21	EDTA	natural abundance	1 mM
22	sodium azide	natural abundance	0.1 %
23	D2O	natural abundance	100 %

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: 0.07 ppm, Outliers: 2 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: 0.07 ppm, Outliers: 2 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: 0.09 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 2N3T, Strand ID: A Detail

Release date

2016-02-21

Citation

Structures of Rpn1:ubiquitin and Rpn1:K48 diubiquitin define Rpn1 as a novel proteasome ubiquitin receptor
Chen, X., Shi, Y., Shi, Y., Elsasser, S., Vannoy, J., Finley, D., Tarasov, S.G., Walters, K.J.
Not known

Related entities 1. Proteasome protein fragment, : 1 : 33 : 121 entities Detail

Interaction partners 1. Proteasome protein fragment, : 147 interactors Detail

More details for 147 interactors identified by 16 citations

Experiments performed 9 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 850 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N; U-80% 2H]	0.7 mM
2	HEPES	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	2 mM
5	EDTA	natural abundance	1 mM
6	sodium azide	natural abundance	0.1 %
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 850 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
17	protein	[U-100% 13C]	0.7 mM
18	HEPES	natural abundance	50 mM
19	sodium chloride	natural abundance	50 mM
20	DTT	natural abundance	2 mM
21	EDTA	natural abundance	1 mM
22	sodium azide	natural abundance	0.1 %
23	D2O	natural abundance	100 %

3 3D HNCACB

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N; U-80% 2H]	0.7 mM
2	HEPES	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	2 mM
5	EDTA	natural abundance	1 mM
6	sodium azide	natural abundance	0.1 %
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

4 3D HNCA

Instrument

Varian INOVA - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N; U-80% 2H]	0.7 mM
2	HEPES	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	2 mM
5	EDTA	natural abundance	1 mM
6	sodium azide	natural abundance	0.1 %
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

5 3D HN(CO)CA

Instrument

Varian INOVA - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N; U-80% 2H]	0.7 mM
2	HEPES	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	2 mM
5	EDTA	natural abundance	1 mM
6	sodium azide	natural abundance	0.1 %
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

6 3D HNCO

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N; U-80% 2H]	0.7 mM
2	HEPES	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	2 mM
5	EDTA	natural abundance	1 mM
6	sodium azide	natural abundance	0.1 %
7	H2O	natural abundance	95 %
8	D2O	natural abundance	5 %

7 3D HCCH-TOCSY

Instrument

Varian INOVA - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
17	protein	[U-100% 13C]	0.7 mM
18	HEPES	natural abundance	50 mM
19	sodium chloride	natural abundance	50 mM
20	DTT	natural abundance	2 mM
21	EDTA	natural abundance	1 mM
22	sodium azide	natural abundance	0.1 %
23	D2O	natural abundance	100 %

8 3D 1H-15N NOESY

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
9	protein	[U-100% 15N]	0.7 mM
10	HEPES	natural abundance	50 mM
11	sodium chloride	natural abundance	50 mM
12	DTT	natural abundance	2 mM
13	EDTA	natural abundance	1 mM
14	sodium azide	natural abundance	0.1 %
15	H2O	natural abundance	95 %
16	D2O	natural abundance	5 %

9 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Concentration
17	protein	[U-100% 13C]	0.7 mM
18	HEPES	natural abundance	50 mM
19	sodium chloride	natural abundance	50 mM
20	DTT	natural abundance	2 mM
21	EDTA	natural abundance	1 mM
22	sodium azide	natural abundance	0.1 %
23	D2O	natural abundance	100 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25657_2n3t.nef
Input source #2: Coordindates	2n3t.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

------490-------500-------510-------520-------530-------540-------550-------560-------570-------580-
DTKISSAAILGLGIAFAGSKNDEVLGLLLPIAASTDLPIETAAMASLALAHVFVGTCNGDITTSIMDNFLERTAIELKTDWVRFLALALGILYMGQGEQV
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
DTKISSAAILGLGIAFAGSKNDEVLGLLLPIAASTDLPIETAAMASLALAHVFVGTCNGDITTSIMDNFLERTAIELKTDWVRFLALALGILYMGQGEQV
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

------590-------600-------610--
DDVLETISAIEHPMTSAIEVLVGSCAYTGTG
|||||||||||||||||||||||||||||||
DDVLETISAIEHPMTSAIEVLVGSCAYTGTG
-------110-------120-------130-

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	131	0	0	100.0

Content subtype: combined_25657_2n3t.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	844		77.1 (chain: A, length: 131)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1701 (1)	noe	80.2 (chain: A, length: 131)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	118 (1)	hbond	66.4 (chain: A, length: 131)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	182 (182)	.	86.3 (chain: A, length: 131)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 131, Sequence coverage: 77.1%
- Total number of assignments
  - ¹H chemical shifts: 477
  - ¹³C chemical shifts: 304
  - ¹⁵N chemical shifts: 63
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	707	477	67.5
¹³C chemical shifts	570	304	53.3
¹⁵N chemical shifts	136	63	46.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	271	165	60.9
¹³C chemical shifts	262	97	37.0
¹⁵N chemical shifts	128	63	49.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	436	312	71.6
¹³C chemical shifts	308	207	67.2
¹⁵N chemical shifts	8	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	107	90	84.1
¹³C chemical shifts	107	90	84.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	24	63.2
¹³C chemical shifts	37	0	0.0
¹⁵N chemical shifts	1	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 131, Sequence coverage: 80.2%
- Total number of restraints: 1700
- Weight of restraints: 1.0 (1700)
- Potential type of restraints: square-well-parabolic (1700)
- Range of distance target values: 2.65, 4.15 (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: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 131, Sequence coverage: 66.4%
  - Total number of restraints: 118
  - Weight of restraints: 1.0 (118)
  - Potential type of restraints: square-well-parabolic (118)
  - Range of distance target values: 2.15, 2.9 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 131, Sequence coverage: 86.3%
- Total number of restraints: 182
- Total number of restraints per polymer type: 182
- Weight of restraints: 1.0 (182)
- Potential type of restraints: square-well-parabolic (182)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords protein

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Found 1 Document (4.352 seconds)

BMRB: 25657

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Proteasome protein fragment, : 1 : 33 : 121 entities Detail

Interaction partners 1. Proteasome protein fragment, : 147 interactors Detail

Experiments performed 9 experiments Detail

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NMR combined restraints 5 contents Detail