BMRBj - BMREntryMaster

Found 1 Document (1.124 seconds)

BMRB: 16627

5LDE

Backbone and stereospecific beta-sidechain assignments of 1H, 13C and 15N for Protein G Unfolded in 7.4M Urea, pH 2.0.

Authors

Vajpai, N., Gentner, M., Grzesiek, S.

Assembly

Protein GB1

Entity

1. Protein GB1 (polymer, Thiol state: not present), 56 monomers, 6222.757 Da Detail

MQYKLILNGK TLKGETTTEA VDAATAEKVF KQYANDNGVD GEWTYDDATK TFTVTE

Formula weight

6222.757 Da

Source organism

Streptococcus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 67.8 %, Completeness (bb): 99.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	67.8 % (428 of 631)	65.1 % (209 of 321)	65.3 % (162 of 248)	91.9 % (57 of 62)
Backbone	99.1 % (333 of 336)	100.0 % (116 of 116)	98.2 % (161 of 164)	100.0 % (56 of 56)
Sidechain	42.4 % (147 of 347)	45.9 % (94 of 205)	38.2 % (52 of 136)	16.7 % (1 of 6)
Aromatic	0.0 % (0 of 56)	0.0 % (0 of 28)	0.0 % (0 of 27)	0.0 % (0 of 1)
Methyl	25.0 % (16 of 64)	28.1 % (9 of 32)	21.9 % (7 of 32)

1. Protein GB1 (2Q6I)

MQYKLILNGK TLKGETTTEA VDAATAEKVF KQYANDNGVD GEWTYDDATK TFTVTE

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 2.0, Details protein GB1-13C,15N

#	Name	Isotope labeling	Concentration
1	Protein GB1 (2Q6I)	[U-100% 13C; U-100% 15N]	0.6 mM
2	urea	natural abundance	7.4 M
3	H2O	natural abundance	95 %
4	D2O	natural abundance	5 %

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: 0.26 ppm, Outliers: 5 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: 0.26 ppm, Outliers: 5 Detail

LACS Plot; HA

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: 0.22 ppm, Outliers: 4 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: 0.67 ppm, Outliers: 1 Detail

Release date

2010-01-24

Citation

Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings
Vajpai, N., Gentner, M., Huang, J., Blackledge, M., Grzesiek, S.
J. Am. Chem. Soc. (2010), 132, 3196-3203, PubMed 20155903 , DOI 10.1021/ja910331t , Abstract

Related entities 1. Protein GB1, : 1 : 20 : 2 : 47 : 38 entities Detail

Interaction partners 1. Protein GB1, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr16627_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	OK

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr16627_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	426		100.0 (chain: 1, length: 56)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 56, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 210
  - ¹³C chemical shifts: 161
  - ¹⁵N chemical shifts: 55
- 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 (%)
¹H chemical shifts	321	198	61.7
¹³C chemical shifts	248	161	64.9
¹⁵N chemical shifts	62	55	88.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	116	115	99.1
¹³C chemical shifts	112	110	98.2
¹⁵N chemical shifts	56	55	98.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	205	83	40.5
¹³C chemical shifts	136	51	37.5
¹⁵N chemical shifts	6	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	33	6	18.2
¹³C chemical shifts	33	6	18.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	28	0	0.0
¹³C chemical shifts	27	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords 3J coupling constants, Coil model, populations, RDCs, Side-chains

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Found 1 Document (1.124 seconds)

BMRB: 16627

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Protein GB1, : 1 : 20 : 2 : 47 : 38 entities Detail

Interaction partners 1. Protein GB1, : 1 interactors Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail