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Found 1 Document (0.726 seconds)

BMRB: 17041

3WRP

Backbone dynamics of Tryptophan repressor protein in holo-form

Authors

Goel, A.

Assembly

holoTrpR dimer

Entity

1. TrpR (polymer, Thiol state: not present), 113 monomers, 13046.64 Da Detail

HHHHHHAQQS PYSAAMAEQR HQEWLRFVDL LKNAYQNDLH LPLLNLMLTP DEREALGTRV RIVEELLRGE MSQRELKNEL GAGIATITRG SNSLKAAPVE LRQWLEEVLL KSD

2. TRYPTOPHAN (non-polymer), 1 monomers, 204.225 Da

Total weight

13250.864 Da

Max. entity weight

13046.64 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, heteronucl_NOEs, heteronucl_T1_relaxation, heteronucl_T2_relaxation, order_parameters, spectral_density_values

Chem. Shift Complete

Sequence coverage: 90.3 %, Completeness: 33.4 %, Completeness (bb): 60.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	33.4 % (447 of 1340)	19.7 % (138 of 701)	41.3 % (213 of 516)	78.0 % (96 of 123)
Backbone	60.7 % (407 of 670)	48.0 % (109 of 227)	60.5 % (202 of 334)	88.1 % (96 of 109)
Sidechain	17.4 % (135 of 778)	6.3 % (30 of 474)	36.2 % (105 of 290)	0.0 % (0 of 14)
Aromatic	3.7 % (3 of 82)	7.3 % (3 of 41)	0.0 % (0 of 39)	0.0 % (0 of 2)
Methyl	15.4 % (21 of 136)	7.4 % (5 of 68)	23.5 % (16 of 68)

1. TrpR

HHHHHHAQQS PYSAAMAEQR HQEWLRFVDL LKNAYQNDLH LPLLNLMLTP DEREALGTRV RIVEELLRGE MSQRELKNEL GAGIATITRG SNSLKAAPVE LRQWLEEVLL KSD

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 318 K, pH 5.7

#	Name	Isotope labeling	Concentration
1	TrpR	[U-100% 13C; U-100% 15N]	1 mM
2	L-Tryptophan	natural abundance	5 mM
3	D2O	natural abundance	5 %
4	H2O	natural abundance	95 %
5	PMSF	natural abundance	0.1 mM
6	sodium azide	natural abundance	0.01 %
7	sodium chloride	natural abundance	500 mM
8	sodium phosphate	natural abundance	50 mM
9	EDTA	natural abundance	1 mM

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 318 K, pH 5.7

#	Name	Isotope labeling	Concentration
10	TrpR	[U-100% 13C; U-100% 15N]	1 mM
11	L-Tryptophan	natural abundance	5 mM
12	D2O	natural abundance	5 %
13	H2O	natural abundance	95 %
14	PMSF	natural abundance	0.1 mM
15	sodium azide	natural abundance	0.01 %
16	sodium chloride	natural abundance	500 mM
17	sodium phosphate	natural abundance	50 mM
18	EDTA	natural abundance	1 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: -0.43 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: -0.43 ppm, Outliers: 1 Detail

Heteronucl. T₁

76 T₁ values in 1 lists
Coherence Sz, Field strength (¹H) 600 MHz, Pressure 1 atm, Temperature 318 K, pH 5.7 Detail

Heteronucl. T₂

76 T₂ values in 1 lists
Coherence S(+,-), Field strength (¹H) 600 MHz, Pressure 1 atm, Temperature 318 K, pH 5.7 Detail

Heteronucl. NOE

76 NOE values in 1 lists
Value type peak height, Field strength (¹H) 600 MHz, Pressure 1 atm, Temperature 318 K, pH 5.7 Detail

Heteronucl. T₁/T₂

76 T₁/T₂ values in 1 lists
Field strength (¹H) 600 MHz, Pressure 1 atm, Temperature 318 K, pH 5.7 Detail

Order parameters

72 S² values in 1 lists
Pressure 1 atm, Temperature 318 K, pH 5.7 Detail

Spectral density

83 values in 1 lists
Pressure 1 atm, Temperature 318 K, pH 5.7 Detail

Release date

2010-07-08

Citation 1

Backbone amide dynamics studies of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein (TrpR): comparison with the (15)N NMR relaxation profiles of wild-type and A77V mutant Apo-TrpR repressors
Goel, A., Tripet, B.P., Tyler, R.C., Nebert, L.D., Copie, V.
Biochemistry (2010), 49, 8006-8019, PubMed 20718459 , DOI 10.1021/bi100508u , Abstract

Show more 1 citaion

Citation 2

Backbone amide dynamics studies of apo-L75F-TrpR, a temperature sensitive mutant of the tryptophan repressor protein (TrpR): comparison with the 15N NMR relaxation profiles of wild type and A77V mutant apo-TrpR repressors
Goel, A.P., Tripet, B.P., Copie, V.
Biochemistry

Hide non-primary 1 citaion

Entries sharing articles BMRB: 5 entries Detail

  BMRB: 17046 released on 2010-08-08
    Title Backbone dynamics of Tryptophan repressor L75F mutant protein in holo-form
  BMRB: 17047 released on 2010-08-08
    Title Backbone dynamics of Tryptophan repressor A77V mutant protein in holo-form
  BMRB: 17010 released on 2010-07-08
    Title Backbone Amide relaxation parameters for wild-type Tryptophan Repressor
  BMRB: 17012 released on 2010-07-08
    Title Backbone Amide relaxation parameters for mutant L75F Tryptophan Repressor
  BMRB: 17013 released on 2010-07-08
    Title Backbone Amide relaxation parameters for mutant A77V Tryptophan Repressor

Related entities 1. TrpR, : 1 : 27 : 33 entities Detail

Sample

State anisotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 318 K, pH 5.7

#	Name	Isotope labeling	Concentration
10	TrpR	[U-100% 13C; U-100% 15N]	1 mM
11	L-Tryptophan	natural abundance	5 mM
12	D2O	natural abundance	5 %
13	H2O	natural abundance	95 %
14	PMSF	natural abundance	0.1 mM
15	sodium azide	natural abundance	0.01 %
16	sodium chloride	natural abundance	500 mM
17	sodium phosphate	natural abundance	50 mM
18	EDTA	natural abundance	1 mM

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts, Heteronucl NOE exptl data, Heteronucl T1 relaxation data, Heteronucl T2 relaxation data, Order parameter relaxation analysis	bmr17041_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: bmr17041_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	379		88.5 (chain: 1, length: 113)
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: 113, Sequence coverage: 88.5%
- Total number of assignments
  - ¹³C chemical shifts: 189
  - ¹H chemical shifts: 95
  - ¹⁵N chemical shifts: 95
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- 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	516	189	36.6
¹H chemical shifts	701	95	13.6
¹⁵N chemical shifts	132	95	72.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	226	96	42.5
¹H chemical shifts	227	95	41.9
¹⁵N chemical shifts	109	95	87.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	290	93	32.1
¹H chemical shifts	474	0	0.0
¹⁵N chemical shifts	23	0	0.0

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Found 1 Document (0.726 seconds)

BMRB: 17041

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 5 entries Detail

Related entities 1. TrpR, : 1 : 27 : 33 entities Detail

Interaction partners 1. TrpR, : 2 interactors Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 4 contents Detail