BMRBj - BMREntryMaster

Found 1 Document (0.546 seconds)

BMRB: 26632

5UB0

Protein G Domain Beta-1 Sequence H

Authors

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

Assembly

Protein G Domain Beta-1 Sequence H

Entity

1. Protein G Domain Beta-1 Sequence H (polymer, Thiol state: not present), 64 monomers, 7170.823 Da Detail

MHHHHHHGMT FKLIINGKTL KGETTTEAVD AATAEKVLKQ YANDNGIDGE WTYDDATKTF TVTE

Formula weight

7170.823 Da

Source organism

Streptococcus sp. GX7805

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 90.6 %, Completeness: 40.8 %, Completeness (bb): 73.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	40.8 % (293 of 718)	18.4 % (67 of 364)	58.9 % (168 of 285)	84.1 % (58 of 69)
Backbone	73.7 % (283 of 384)	44.4 % (59 of 133)	89.3 % (167 of 187)	89.1 % (57 of 64)
Sidechain	15.8 % (62 of 393)	3.5 % (8 of 231)	33.8 % (53 of 157)	20.0 % (1 of 5)
Aromatic	0.0 % (0 of 72)	0.0 % (0 of 36)	0.0 % (0 of 35)	0.0 % (0 of 1)
Methyl	8.6 % (6 of 70)	0.0 % (0 of 35)	17.1 % (6 of 35)

1. Protein G Domain Beta-1 Sequence H

MHHHHHHGMT FKLIINGKTL KGETTTEAVD AATAEKVLKQ YANDNGIDGE 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 Sequence H	[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: -0.11 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: -0.11 ppm, Outliers: 2 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: 0.16 ppm, Outliers: 4 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

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 30222 released on 2017-02-01
    Title Solution NMR structure of the major species of DANCER-2, a dynamic and natively folded pentamutant of the B1 domain of streptococcal protein G (GB1)
  BMRB: 26630 released on 2015-09-28
    Title Protein G Domain Beta-1 Wild Type

Related entities 1. Protein G Domain Beta-1 Sequence H, : 1 : 1 : 104 entities Detail

Experiments performed 3 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr26632_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: bmr26632_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	281		90.6 (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: 90.6%
- Total number of assignments
  - ¹³C chemical shifts: 167
  - ¹H chemical shifts: 57
  - ¹⁵N chemical shifts: 57
- 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	37	6	16.2
¹H chemical shifts	37	0	0.0

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Found 1 Document (0.546 seconds)

BMRB: 26632

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 2 entries Detail

Related entities 1. Protein G Domain Beta-1 Sequence H, : 1 : 1 : 104 entities 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	167	58.6
¹H chemical shifts	364	57	15.7
¹⁵N chemical shifts	69	57	82.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	128	115	89.8
¹H chemical shifts	133	57	42.9
¹⁵N chemical shifts	64	57	89.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	157	52	33.1
¹H chemical shifts	231	0	0.0
¹⁵N chemical shifts	5	0	0.0