BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	95.5 % (850 of 890)	96.2 % (435 of 452)	93.8 % (333 of 355)	98.8 % (82 of 83)
Backbone	98.3 % (454 of 462)	98.7 % (155 of 157)	97.8 % (223 of 228)	98.7 % (76 of 77)
Sidechain	93.4 % (469 of 502)	94.9 % (280 of 295)	91.0 % (183 of 201)	100.0 % (6 of 6)
Aromatic	83.3 % (65 of 78)	100.0 % (39 of 39)	65.8 % (25 of 38)	100.0 % (1 of 1)
Methyl	99.1 % (107 of 108)	98.1 % (53 of 54)	100.0 % (54 of 54)

1. entity 1

SHMTAVQDFV VDILLNGARD WDVLQTTCTV DRKVYKTICK RGNTYLCFDD TNLYAITGDV VLKFATVSKA RAYLETK

Show sample condition

Sample #1

Solvent system 97% H2O/3% D2O, Pressure 1 atm, Temperature 298 (±0.1) K, pH 6, Details 1.2 mM [U-13C; U-15N] HKU9 NSP3 C domain, 5 mM [U-98% 2H] DTT, 0.02 % sodium azide, 97% H2O/3% D2O.

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

Sample #2

Solvent system 97% H2O/3% D2O, Pressure 1 atm, Temperature 298 (±0.1) K, pH 6, Details 637 uM [U-15N] HKU9 NSP3 C domain, 5 mM [U-98% 2H] DTT, 0.02 % sodium azide, 97% H2O/3% D2O.

#	Name	Isotope labeling	Concentration
4	DTT	[U-98% 2H]	5 (±0.01) mM
5	HKU9 NSP3 C domain	[U-15N]	637 (±0.1) uM
6	sodium azide	natural abundance	0.02 (±0.01) %

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	0.1013291

Referencing offset: 0.06 ppm, Outliers: 2 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	0.1013291

Referencing offset: 0.06 ppm, Outliers: 2 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	0.1013291

Referencing offset: -0.09 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	0.1013291

Referencing offset: -2.1 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5UTV, Strand ID: A Detail

Release date

2017-05-10

Citation

SARS-unique fold in the Rousettus bat coronavirus HKU9
Hammond, R.G., Tan, X., Johnson, M.A.
Protein Sci. (2017), 26, 1726-1737, PubMed 28580734 , DOI 10.1002/pro.3208 , Abstract

Related entities 1. Papain-like proteinase (E.C.3.4.19.12,3.4.22.69), : 2 : 8 entities Detail

Experiments performed 17 experiments Detail

1 3D CBCA(CO)NH

Instrument

Bruker AvanceIII - 600 MHz

Sample

State anisotropic, Solvent system 97% H2O/3% D2O, Pressure 1 atm, Temperature 298 (±0.1) K, pH 6, Details 1.2 mM [U-13C; U-15N] HKU9 NSP3 C domain, 5 mM [U-98% 2H] DTT, 0.02 % sodium azide, 97% H2O/3% D2O.

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

2 3D HNCO

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

3 3D HNCA

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

4 3D 1H-15N NOESY

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

5 3D 1H-13C NOESY aliphatic

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

6 3D HBHA(CO)NH

Instrument

Bruker AvanceIII - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

7 3D 1H-13C NOESY aromatic

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

8 3D C(CO)NH

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

9 3D 1H-15N TOCSY

Instrument

Bruker AvanceIII - 700 MHz

Sample

State anisotropic, Solvent system 97% H2O/3% D2O, Pressure 1 atm, Temperature 298 (±0.1) K, pH 6, Details 637 uM [U-15N] HKU9 NSP3 C domain, 5 mM [U-98% 2H] DTT, 0.02 % sodium azide, 97% H2O/3% D2O.

#	Name	Isotope labeling	Concentration
4	DTT	[U-98% 2H]	5 (±0.01) mM
5	HKU9 NSP3 C domain	[U-15N]	637 (±0.1) uM
6	sodium azide	natural abundance	0.02 (±0.01) %

10 3D HCCH-COSY

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

11 3D HCCH-TOCSY

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

12 2D 1H-15N HSQC

Instrument

Bruker AvanceIII - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

13 2D 1H-13C HSQC aliphatic

Instrument

Bruker AvanceIII - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

14 2D 1H-13C HSQC aromatic

Instrument

Bruker AvanceIII - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

15 3D HNCACB

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

16 2D (HB)CB(CGCD)HD

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

17 2D (HB)CB(CGCDCE)HE

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	DTT	[U-98% 2H]	5 (±0.01) mM
2	HKU9 NSP3 C domain	[U-13C; U-15N]	1.2 (±0.1) mM
3	sodium azide	natural abundance	0.02 (±0.01) %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30247_5utv.nef
Input source #2: Coordindates	5utv.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-------
SHMTAVQDFVVDILLNGARDWDVLQTTCTVDRKVYKTICKRGNTYLCFDDTNLYAITGDVVLKFATVSKARAYLETK
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SHMTAVQDFVVDILLNGARDWDVLQTTCTVDRKVYKTICKRGNTYLCFDDTNLYAITGDVVLKFATVSKARAYLETK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	77	0	0	100.0

Content subtype: combined_30247_5utv.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	846		100.0 (chain: A, length: 77)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	1920 (1)	noe	98.7 (chain: A, length: 77)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	348 (348)	.	100.0 (chain: A, length: 77)
2	Dihedral angle restraints	DYANA/DIANA_dihedral_4	OK	132 (132)	.	97.4 (chain: A, length: 77)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 332
  - ¹H chemical shifts: 431
  - ¹⁵N chemical shifts: 83
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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 (%)
¹³C chemical shifts	355	332	93.5
¹H chemical shifts	452	431	95.4
¹⁵N chemical shifts	87	83	95.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	154	150	97.4
¹H chemical shifts	157	155	98.7
¹⁵N chemical shifts	77	76	98.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	201	182	90.5
¹H chemical shifts	295	276	93.6
¹⁵N chemical shifts	10	7	70.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	55	54	98.2
¹H chemical shifts	55	53	96.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	38	24	63.2
¹H chemical shifts	39	39	100.0
¹⁵N chemical shifts	1	1	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: 77, Sequence coverage: 98.7%
- Total number of restraints: 1920
- Weight of restraints: 1.0 (1920)
- Potential type of restraints: upper-bound-parabolic (1920)
- Range of distance target values: 2.45, 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: 77, Sequence coverage: 100.0%
- Total number of restraints: 348
- Total number of restraints per polymer type: 348
- Weight of restraints: 1.0 (348)
- Potential type of restraints: square-well-parabolic (348)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
- Saveframe: DYANA/DIANA_dihedral_4
  - Status: OK
  - Experiment type: .
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 97.4%
  - Total number of restraints: 132
  - Total number of restraints per polymer type: 132
  - Weight of restraints: 1.0 (132)
  - Potential type of restraints: square-well-parabolic (132)
  - Plot of Phi-Psi angle restraints
  - Dihedral angle restraints per residue
    - Chain_ID: A

Keywords HKU9, SARS-unique domain, VIRAL PROTEIN, coronavirus, nonstructural protein 3

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Found 1 Document (0.542 seconds)

BMRB: 30247

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Papain-like proteinase (E.C.3.4.19.12,3.4.22.69), : 2 : 8 entities Detail

Experiments performed 17 experiments Detail

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NMR combined restraints 5 contents Detail