BMRBj - BMREntryMaster

Found 1 Document (0.411 seconds)

BMRB: 26630

6V9I

Protein G Domain Beta-1 Wild Type

Authors

Davey, J.A., Damry, A.M., Euler, C.K., Goto, N.K., Chica, R.A.

Assembly

Protein G Domain Beta-1 Wild-Type

Entity

1. Protein G Domain Beta-1 Wild-Type (polymer, Thiol state: not present), 64 monomers, 7206.812 Da Detail

MHHHHHHGMT YKLILNGKTL KGETTTEAVD AATAEKVFKQ YANDNGVDGE WTYDDATKTF TVTE

Formula weight

7206.812 Da

Source organism

Streptococcus sp. GX7805

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 89.1 %, Completeness: 43.0 %, Completeness (bb): 73.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	43.0 % (308 of 717)	21.5 % (78 of 363)	60.7 % (173 of 285)	82.6 % (57 of 69)
Backbone	73.4 % (282 of 384)	45.9 % (61 of 133)	88.2 % (165 of 187)	87.5 % (56 of 64)
Sidechain	19.9 % (78 of 392)	7.4 % (17 of 230)	38.2 % (60 of 157)	20.0 % (1 of 5)
Aromatic	15.0 % (12 of 80)	15.0 % (6 of 40)	12.8 % (5 of 39)	100.0 % (1 of 1)
Methyl	18.2 % (12 of 66)	12.1 % (4 of 33)	24.2 % (8 of 33)

1. Protein G Domain Beta-1 Wild Type

MHHHHHHGMT YKLILNGKTL KGETTTEAVD AATAEKVFKQ YANDNGVDGE WTYDDATKTF TVTE

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298.15 K, pH 7.4

#	Name	Isotope labeling	Concentration
1	Protein G Domain Beta-1 Wild Type	[U-99% 13C; U-98% 15N]	0.5 ~ 2.0 mM
2	D2O	[U-99.9% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium phosphate	natural abundance	10 mM

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: -0.01 ppm, Outliers: 1 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: -0.01 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.25 ppm, Outliers: 6 Detail

Release date

2015-09-28

Citation

Prediction of Stable Globular Proteins Using Negative Design with Non-native Backbone Ensembles
Davey, J.A., Damry, A.M., Euler, C.K., Goto, N.K., Chica, R.A.
Structure (2015), 23, 2011-2021, PubMed 26412333 , DOI 10.1016/j.str.2015.07.021 , Abstract

Related entities 1. Protein G Domain Beta-1 Wild-Type, : 1 : 1 : 57 : 47 entities Detail

Interaction partners 1. Protein G Domain Beta-1 Wild-Type, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 3 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr26630_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: bmr26630_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	277		89.1 (chain: 1, length: 64)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 64, Sequence coverage: 89.1%
- Total number of assignments
  - ¹³C chemical shifts: 165
  - ¹H chemical shifts: 56
  - ¹⁵N chemical shifts: 56
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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 (%)
¹³C chemical shifts	35	6	17.1
¹H chemical shifts	35	0	0.0

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Found 1 Document (0.411 seconds)

BMRB: 26630

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Protein G Domain Beta-1 Wild-Type, : 1 : 1 : 57 : 47 entities Detail

Interaction partners 1. Protein G Domain Beta-1 Wild-Type, : 1 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	285	165	57.9
¹H chemical shifts	363	56	15.4
¹⁵N chemical shifts	69	56	81.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	128	113	88.3
¹H chemical shifts	133	56	42.1
¹⁵N chemical shifts	64	56	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	157	52	33.1
¹H chemical shifts	230	0	0.0
¹⁵N chemical shifts	5	0	0.0