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Found 1 Document (1.282 seconds)

BMRB: 5222

1OKD

1H, 15N and 13C resonance assignments and secondary structure of Tryparedoxin-I from Crithidia fasciculata

Authors

Krumme, D., Hecht, H., Menge, U., Ross, A., Wray, V., Flohe, L.

Assembly

tryparedoxin I

Entity

1. tryparedoxin I (polymer, Thiol state: free and disulfide bound), 153 monomers, 17414.38 Da Detail

SGLDKYLPGI EKLRRGDGEV EVKSLAGKLV FFYFSASWCP PCRGFTPQLI EFYDKFHESK NFEVVFCTWD EEEDGFAGYF AKMPWLAVPF AQSEAVQKLS KHFNVESIPT LIGVDADSGD VVTTRARATL VKDPEGEQFP WKDAPLEHHH HHH

Formula weight

17414.38 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS39:SG	1:CYS42:SG

Source organism

Crithidia fasciculata

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.1 %, Completeness: 71.1 %, Completeness (bb): 92.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	71.1 % (1291 of 1816)	77.0 % (724 of 940)	59.8 % (432 of 723)	88.2 % (135 of 153)
Backbone	92.3 % (829 of 898)	93.8 % (288 of 307)	90.8 % (407 of 448)	93.7 % (134 of 143)
Sidechain	56.1 % (595 of 1060)	68.9 % (436 of 633)	37.9 % (158 of 417)	10.0 % (1 of 10)
Aromatic	3.7 % (9 of 242)	5.8 % (7 of 121)	1.7 % (2 of 117)	0.0 % (0 of 4)
Methyl	57.0 % (81 of 142)	90.1 % (64 of 71)	23.9 % (17 of 71)

1. tryparedoxin I

SGLDKYLPGI EKLRRGDGEV EVKSLAGKLV FFYFSASWCP PCRGFTPQLI EFYDKFHESK NFEVVFCTWD EEEDGFAGYF AKMPWLAVPF AQSEAVQKLS KHFNVESIPT LIGVDADSGD VVTTRARATL VKDPEGEQFP WKDAPLEHHH HHH

Show sample condition

Sample

Temperature 303 (±0.2) K, pH 6.5 (±0.5)

#	Name	Isotope labeling	Type	Concentration
1	tryparedoxin I	[U-13C; U-15N]		1 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.8 ppm	internal	direct	1.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: 2.49 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.8 ppm	internal	direct	1.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: 2.49 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.8 ppm	internal	direct	1.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: -0.15 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.8 ppm	internal	direct	1.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: 2.42 ppm, Outliers: 2 Detail

Release date

2001-12-03

Citation

1H, 15N and 13C resonance assignments and secondary structure of tryparedoxin-I from Crithidia fasciculata
Krumme, D., Hecht, H., Menge, U., Ross, A., Wray, V., Flohe, L.
J. Biomol. NMR (2002), 22, 375-376, PubMed 12018487 , DOI: , Abstract

Related entities 1. tryparedoxin I, : 1 : 1 : 6 : 62 entities Detail

Experiments performed 10 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5222_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:39:CYS:SG	1:42:CYS:SG	oxidized, CA 50.2, CB 42.8 ppm	reduced, CA 61.6, CB 30.7 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr5222_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1361		92.8 (chain: 1, length: 153)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 153, Sequence coverage: 92.8%
- Total number of assignments
  - ¹H chemical shifts: 824
  - ¹³C chemical shifts: 404
  - ¹⁵N chemical shifts: 133
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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 (%)
¹H chemical shifts	940	698	74.3
¹³C chemical shifts	723	404	55.9
¹⁵N chemical shifts	158	133	84.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	307	283	92.2
¹³C chemical shifts	306	272	88.9
¹⁵N chemical shifts	143	133	93.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	633	415	65.6
¹³C chemical shifts	417	132	31.7
¹⁵N chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	72	63	87.5
¹³C chemical shifts	72	11	15.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	121	0	0.0
¹³C chemical shifts	117	0	0.0
¹⁵N chemical shifts	4	0	0.0

Keywords hydroperoxide detoxification, oxidoreductase, secondary structure, trypanosoma, tryparedoxin

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Found 1 Document (1.282 seconds)

BMRB: 5222

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. tryparedoxin I, : 1 : 1 : 6 : 62 entities Detail

Experiments performed 10 experiments Detail

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Chemical shift validation 3 contents Detail