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Found 1 Document (1.289 seconds)

BMRB: 4573

1RSI

1HN,15N,13CO,13Ca,13Cb chemical shifts of 7,8-dihydroneopterin aldolase (DHNA) from Staphylococcus aureus

Authors

Salzmann, M., Pervushin, K., Wider, G., Senn, H., Wuthrich, K.

Assembly

7,8-dihydroneopterin aldolase

Entity

1. 7,8-dihydroneopterin aldolase (polymer, Thiol state: not present), 121 monomers, 13750.47 × 8 Da Detail

MQDTIFLKGM RFYGYHGALS AENEIGQIFK VDVTLKVDLS EAGRTDNVID TVHYGEVFEE VKSIMEGKAV NLLEHLAERI ANRINSQYNR VMETKVRITK ENPPIPGHYD GVGIEIVREN K

Total weight

110003.76 Da

Max. entity weight

13750.47 Da

Source organism

Staphylococcus aureus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.9 %, Completeness: 39.0 %, Completeness (bb): 73.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	39.0 % (554 of 1422)	18.4 % (136 of 740)	55.5 % (307 of 553)	86.0 % (111 of 129)
Backbone	73.9 % (532 of 720)	47.8 % (119 of 249)	85.6 % (302 of 353)	94.1 % (111 of 118)
Sidechain	12.3 % (100 of 813)	3.5 % (17 of 491)	26.7 % (83 of 311)	0.0 % (0 of 11)
Aromatic	0.0 % (0 of 96)	0.0 % (0 of 48)	0.0 % (0 of 48)
Methyl	5.6 % (8 of 144)	2.8 % (2 of 72)	8.3 % (6 of 72)

1. Aldolase

MQDTIFLKGM RFYGYHGALS AENEIGQIFK VDVTLKVDLS EAGRTDNVID TVHYGEVFEE VKSIMEGKAV NLLEHLAERI ANRINSQYNR VMETKVRITK ENPPIPGHYD GVGIEIVREN K

Show sample condition

Sample

Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Aldolase	[U-95% 2H; U-98% 13C; U-99% 15N]		0.5 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹H	TSP	methyl protons	null	null
¹³C	TSP	methyl protons	null	indirect
¹⁵N	TSP	methyl protons	null	indirect

Referencing offset: 0.63 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹H	TSP	methyl protons	null	null
¹³C	TSP	methyl protons	null	indirect
¹⁵N	TSP	methyl protons	null	indirect

Referencing offset: 0.63 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹H	TSP	methyl protons	null	null
¹³C	TSP	methyl protons	null	indirect
¹⁵N	TSP	methyl protons	null	indirect

Referencing offset: 0.62 ppm, Outliers: 1 Detail

Release date

2004-05-14

Citation 1

NMR Assignment and Secondary Structure Determination of an Octameric 110 kDa Protein Using TROSY in Triple Resonance Experiments
Salzmann, M., Pervushin, K., Wider, G., Senn, H., Wuthrich, K.
J. Am. Chem. Soc. (2000), 122, 7543-7548, DOI 10.1021/ja0003268

Show more 1 citaion

Citation 2

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data
Wishart, D.S., Sykes, B.D.
J. Biomol. NMR (1994), 4, 171-180, PubMed 8019132 , DOI 10.1007/bf00175245 , Abstract

Hide non-primary 1 citaion

Entries sharing articles BMRB: 4 entries Detail

  BMRB: 4467 released on 2000-12-14
    Title Sequence-specific 1H, 13C, and 15N Assignments of the MAR-binding Domain of Chicken MeCP2/ARBP
  BMRB: 4376 released on 1999-10-12
    Title Chemical shift assignments, 3JHNHA coupling constants, secondary structure and 15N{1H} Heteronuclear NOE values of the N-domain of VAT (VCP like ATPase of Thermoplasma). A group II AAA ATPase.
  BMRB: 4130 released on 1998-08-11
    Title 1H, 15N, 13C Chemical Shifts of Recombinant Rat Ferrocytochrome b5, A conformation
  BMRB: 4131 released on 1998-08-11
    Title 1H, 15N, 13C chemical shifts of recombinant rat ferrocytochrome b5, B conformation

Related entities 1. 7,8-dihydroneopterin aldolase, : 1 : 12 : 2 : 47 entities Detail

Chemical shift validation 3 contents Detail

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_label	Warning	520		95.9 (chain: 1, length: 121)
1	Chemical shift references	chemical_shift_reference_label	OK	3		No information

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	740	109	14.7
¹³C chemical shifts	553	302	54.6
¹⁵N chemical shifts	136	109	80.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	249	109	43.8
¹³C chemical shifts	242	225	93.0
¹⁵N chemical shifts	118	109	92.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	491	0	0.0
¹³C chemical shifts	311	77	24.8
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	76	0	0.0
¹³C chemical shifts	76	4	5.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	0	0.0
¹³C chemical shifts	48	0	0.0

Keywords NMR, TROSY, DHNA, Aldolase, Large Protein

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4573_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

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Found 1 Document (1.289 seconds)

BMRB: 4573

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. 7,8-dihydroneopterin aldolase, : 1 : 12 : 2 : 47 entities Detail

Chemical shift validation 3 contents Detail