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BMRB: 25909

2N9K

1H, 13C, and 15N Chemical Shift Assignments for in vitro GB1

Authors

Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Guentert, P., Ito, Y.

Assembly

in vitro GB1

Entity

1. in vitro GB1 (polymer, Thiol state: not present), 57 monomers, 6252.784 Da Detail

MGTYKLILNG KTLKGETTTE AVDAATAEKV FKQYANDNGV DGEWTYDDAT KTFTVTE

Formula weight

6252.784 Da

Source organism

Staphylococcus aureus

Exptl. method

Refine. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 99.4 %, Completeness (bb): 99.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	99.4 % (628 of 632)	98.8 % (316 of 320)	100.0 % (250 of 250)	100.0 % (62 of 62)
Backbone	99.4 % (340 of 342)	98.3 % (117 of 119)	100.0 % (166 of 166)	100.0 % (57 of 57)
Sidechain	99.4 % (340 of 342)	99.0 % (199 of 201)	100.0 % (136 of 136)	100.0 % (5 of 5)
Aromatic	96.4 % (54 of 56)	92.9 % (26 of 28)	100.0 % (27 of 27)	100.0 % (1 of 1)
Methyl	100.0 % (66 of 66)	100.0 % (33 of 33)	100.0 % (33 of 33)

1. entity

MGTYKLILNG KTLKGETTTE AVDAATAEKV FKQYANDNGV DGEWTYDDAT KTFTVTE

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

LACS Plot; CA

Referencing offset: -0.01 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: -0.01 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: -0.08 ppm, Outliers: 1 Detail

LACS Plot; CO

Referencing offset: 0.03 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2N9K, Strand ID: A Detail

Release date

2015-12-01

Citation

Improved in-cell structure determination of proteins at near-physiological concentration
Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Guentert, P., Ito, Y.
Sci. Rep. (2016), 6, 38312-38312, PubMed 27910948 , DOI 10.1038/srep38312 , Abstract

Related entities 1. in vitro GB1, : 1 : 2 : 67 : 36 entities Detail

Interaction partners 1. in vitro GB1, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 12 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 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

3 3D CBCANH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

4 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

5 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

6 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

7 3D HN(CA)CO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

8 3D HBHA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

9 3D H(CCO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

10 3D HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

11 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

12 3D 1H-13C NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Protein G B1	[U-100% 13C; U-100% 15N]		1 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25909_2n9k.nef
Input source #2: Coordindates	2n9k.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-------
MGTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MGTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	57	0	0	100.0

Content subtype: combined_25909_2n9k.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	629		100.0 (chain: A, length: 57)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	2077 (1)	noe	100.0 (chain: A, length: 57)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	513 (513)	.	98.2 (chain: A, length: 57)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 57, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 316
  - ¹³C chemical shifts: 251
  - ¹⁵N chemical shifts: 62
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 57, Sequence coverage: 100.0%
- Total number of restraints: 2077
- Weight of restraints: 1.0 (2077)
- Potential type of restraints: upper-bound-parabolic (2077)
- Range of distance target values: 2.35, 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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 57, Sequence coverage: 98.2%
- Total number of restraints: 513
- Total number of restraints per polymer type: 513
- Weight of restraints: 1.0 (513)
- Potential type of restraints: square-well-parabolic (513)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Protein G B1, in-cell NMR