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Found 1 Document (0.495 seconds)

BMRB: 36471

8IF0

solution structure of an anti-CRISPR protein

Authors

Zhao, Y., Yang, F.

Assembly

Anti-CRISPR protein (AcrIIC1)

Entity

1. Anti-CRISPR protein (AcrIIC1) (polymer, Thiol state: all free), 86 monomers, 9627.767 Da Detail

MANKTYKIGK NAGYDGCGLC LAAISENEAI KVKYLRDICP DYDGDDKAED WLRWGTDSRV KAAALEMEQY AYTSVGMASC WEFVEL

Formula weight

9627.767 Da

Source organism

Neisseria meningitidis

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 91.9 %, Completeness (bb): 98.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.9 % (895 of 974)	90.2 % (451 of 500)	92.6 % (351 of 379)	97.9 % (93 of 95)
Backbone	98.2 % (505 of 514)	98.3 % (175 of 178)	98.4 % (247 of 251)	97.6 % (83 of 85)
Sidechain	86.8 % (468 of 539)	85.7 % (276 of 322)	87.9 % (182 of 207)	100.0 % (10 of 10)
Aromatic	67.0 % (63 of 94)	76.6 % (36 of 47)	54.5 % (24 of 44)	100.0 % (3 of 3)
Methyl	100.0 % (84 of 84)	100.0 % (42 of 42)	100.0 % (42 of 42)

1. entity 1

MANKTYKIGK NAGYDGCGLC LAAISENEAI KVKYLRDICP DYDGDDKAED WLRWGTDSRV KAAALEMEQY AYTSVGMASC WEFVEL

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-15N] protein, 20 mM TRIS, 100 mM sodium chloride, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	unit_1	[U-15N]	protein	1 mM
2	TRIS	natural abundance	buffer	20 mM
3	sodium chloride	natural abundance	salt	100 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-13C; U-15N] protein, 20 mM TRIS, 100 mM sodium chloride, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
6	unit_1	[U-13C; U-15N]	protein	1 mM
7	TRIS	natural abundance	buffer	20 mM
8	sodium chloride	natural abundance	salt	100 mM
9	H2O	natural abundance	solvent	90 %
10	D2O	[U-2H]	solvent	10 %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-13C; U-15N] protein, 20 mM TRIS, 100 mM sodium chloride, 100% D2O

#	Name	Isotope labeling	Type	Concentration
11	unit_1	[U-13C; U-15N]	protein	1 mM
12	TRIS	natural abundance	buffer	20 mM
13	sodium chloride	natural abundance	salt	100 mM
14	D2O	[U-2H]	solvent	100 %

Release date

2022-10-12

Citation

The solution structure of an anti-CRISPR protein
Zhao, Y., Yang, F.

Related entities 1. Anti-CRISPR protein (AcrIIC1), : 1 : 3 : 1 entities Detail

Experiments performed 11 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AVANCE - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-15N] protein, 20 mM TRIS, 100 mM sodium chloride, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	unit_1	[U-15N]	protein	1 mM
2	TRIS	natural abundance	buffer	20 mM
3	sodium chloride	natural abundance	salt	100 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

2 2D 1H-13C HSQC

Instrument

Bruker AVANCE - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-13C; U-15N] protein, 20 mM TRIS, 100 mM sodium chloride, 100% D2O

#	Name	Isotope labeling	Type	Concentration
11	unit_1	[U-13C; U-15N]	protein	1 mM
12	TRIS	natural abundance	buffer	20 mM
13	sodium chloride	natural abundance	salt	100 mM
14	D2O	[U-2H]	solvent	100 %

3 3D 1H-15N NOESY-HSQC

Instrument

Bruker AVANCE - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-15N] protein, 20 mM TRIS, 100 mM sodium chloride, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	unit_1	[U-15N]	protein	1 mM
2	TRIS	natural abundance	buffer	20 mM
3	sodium chloride	natural abundance	salt	100 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

4 3D 1H-13C NOESY-HSQC

Instrument

Bruker AVANCE - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-13C; U-15N] protein, 20 mM TRIS, 100 mM sodium chloride, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
6	unit_1	[U-13C; U-15N]	protein	1 mM
7	TRIS	natural abundance	buffer	20 mM
8	sodium chloride	natural abundance	salt	100 mM
9	H2O	natural abundance	solvent	90 %
10	D2O	[U-2H]	solvent	10 %

5 3D CBCA(CO)NH

Instrument

Bruker AVANCE - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
6	unit_1	[U-13C; U-15N]	protein	1 mM
7	TRIS	natural abundance	buffer	20 mM
8	sodium chloride	natural abundance	salt	100 mM
9	H2O	natural abundance	solvent	90 %
10	D2O	[U-2H]	solvent	10 %

6 3D HNCACB

Instrument

Bruker AVANCE - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
6	unit_1	[U-13C; U-15N]	protein	1 mM
7	TRIS	natural abundance	buffer	20 mM
8	sodium chloride	natural abundance	salt	100 mM
9	H2O	natural abundance	solvent	90 %
10	D2O	[U-2H]	solvent	10 %

7 3D HNCO

Instrument

Bruker AVANCE - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
6	unit_1	[U-13C; U-15N]	protein	1 mM
7	TRIS	natural abundance	buffer	20 mM
8	sodium chloride	natural abundance	salt	100 mM
9	H2O	natural abundance	solvent	90 %
10	D2O	[U-2H]	solvent	10 %

8 3D HNCA

Instrument

Bruker AVANCE - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
6	unit_1	[U-13C; U-15N]	protein	1 mM
7	TRIS	natural abundance	buffer	20 mM
8	sodium chloride	natural abundance	salt	100 mM
9	H2O	natural abundance	solvent	90 %
10	D2O	[U-2H]	solvent	10 %

9 3D HBHA(CO)NH

Instrument

Bruker AVANCE - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
6	unit_1	[U-13C; U-15N]	protein	1 mM
7	TRIS	natural abundance	buffer	20 mM
8	sodium chloride	natural abundance	salt	100 mM
9	H2O	natural abundance	solvent	90 %
10	D2O	[U-2H]	solvent	10 %

10 3D HCCH-TOCSY

Instrument

Bruker AVANCE - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-13C; U-15N] protein, 20 mM TRIS, 100 mM sodium chloride, 100% D2O

#	Name	Isotope labeling	Type	Concentration
11	unit_1	[U-13C; U-15N]	protein	1 mM
12	TRIS	natural abundance	buffer	20 mM
13	sodium chloride	natural abundance	salt	100 mM
14	D2O	[U-2H]	solvent	100 %

11 3D HCCH-TOCSY

Instrument

Bruker AVANCE - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-13C; U-15N] protein, 20 mM TRIS, 100 mM sodium chloride, 100% D2O

#	Name	Isotope labeling	Type	Concentration
11	unit_1	[U-13C; U-15N]	protein	1 mM
12	TRIS	natural abundance	buffer	20 mM
13	sodium chloride	natural abundance	salt	100 mM
14	D2O	[U-2H]	solvent	100 %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr36471_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: bmr36471_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	977		100.0 (chain: 1, length: 86)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 86, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 534
  - ¹³C chemical shifts: 350
  - ¹⁵N chemical shifts: 93
- 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	500	450	90.0
¹³C chemical shifts	379	350	92.3
¹⁵N chemical shifts	95	93	97.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	178	174	97.8
¹³C chemical shifts	172	168	97.7
¹⁵N chemical shifts	85	83	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	322	276	85.7
¹³C chemical shifts	207	182	87.9
¹⁵N chemical shifts	10	10	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	45	42	93.3
¹³C chemical shifts	45	42	93.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	36	76.6
¹³C chemical shifts	44	24	54.5
¹⁵N chemical shifts	3	3	100.0

Keywords VIRAL PROTEIN, anti-CRISPR

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Found 1 Document (0.495 seconds)

BMRB: 36471

Sample #1

Sample #2

Sample #3

Related entities 1. Anti-CRISPR protein (AcrIIC1), : 1 : 3 : 1 entities Detail

Experiments performed 11 experiments Detail

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Chemical shift validation 3 contents Detail