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Found 1 Document (1.549 seconds)

BMRB: 4376

1CZ5

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.

Authors

Coles, M., Diercks, T., Liermann, J., Groeger, A., Rockel, B., Baumeister, W., Koretke, K.K., Lupas, A., Peters, J., Kessler, H.

Assembly

VATN VCP-like ATPase of Thermoplasma N-domain

Entity

1. VATN VCP-like ATPase of Thermoplasma N-domain (polymer), 185 monomers, 20616.52 Da Detail

MESNNGIILR VAEANSTDPG MSRVRLDESS RRLLDAEIGD VVEIEKVRKT VGRVYRARPE DENKGIVRID SVMRNNCGAS IGDKVKVRKV RTEIAKKVTL APIIRKDQRL KFGEGIEEYV QRALIRRPML EQDNISVPGL TLAGQTGLLF KVVKTLPSKV PVEIGEETKI EIREEPASEV LEEGG

Formula weight

20616.52 Da

Source organism

Thermoplasma

Exptl. method

NMR

Data set

assigned_chemical_shifts, coupling_constants, heteronucl_NOEs

Chem. Shift Complete

Sequence coverage: 99.5 %, Completeness: 96.0 %, Completeness (bb): 98.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	96.0 % (2061 of 2146)	96.6 % (1094 of 1132)	94.7 % (782 of 826)	98.4 % (185 of 188)
Backbone	98.2 % (1074 of 1094)	99.2 % (374 of 377)	97.2 % (525 of 540)	98.9 % (175 of 177)
Sidechain	94.5 % (1155 of 1222)	95.4 % (720 of 755)	93.2 % (425 of 456)	90.9 % (10 of 11)
Aromatic	50.0 % (18 of 36)	100.0 % (18 of 18)	0.0 % (0 of 18)
Methyl	100.0 % (236 of 236)	100.0 % (118 of 118)	100.0 % (118 of 118)

1. VCP-like ATPase of Thermoplasma N-domain

Show sample condition

Sample

Temperature 320 K, pH 5.9

#	Name	Isotope labeling	Concentration
1	VCP-like ATPase of Thermoplasma N-domain	[U-15N]	1.40 mM
2	phosphate buffer		40 mM
3	sodium chloride		80 mM
4	sodium azide		10 mM
5	D2O		10.0 %
6	H2O		90.0 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TMS	methyl protons	null	indirect	0.2514495
¹H	TMS	methyl protons	internal	direct	0.0
¹⁵N	TMS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.26 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TMS	methyl protons	null	indirect	0.2514495
¹H	TMS	methyl protons	internal	direct	0.0
¹⁵N	TMS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.26 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TMS	methyl protons	null	indirect	0.2514495
¹H	TMS	methyl protons	internal	direct	0.0
¹⁵N	TMS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.27 ppm, Outliers: 3 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TMS	methyl protons	null	indirect	0.2514495
¹H	TMS	methyl protons	internal	direct	0.0
¹⁵N	TMS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.06 ppm, Outliers: 1 Detail

Heteronucl. NOE

183 NOE values in 1 lists
Value type relative intensities, Field strength (¹H) 600 MHz, Temperature 320 K, pH 5.9 Detail

Coupling constant

150 J values in 1 lists
Temperature 320 K, pH 5.9 Detail

Release date

1999-10-12

Citation 1

The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple betaalphabetabeta element
Coles, M., Diercks, T., Liermann, J., Groeger, A., Rockel, B., Baumeister, W., Koretke, K.K., Lupas, A., Peters, J., Kessler, H.
Curr. Biol. (1999), 9, 1158-1168, PubMed 10531028 , DOI 10.1016/S0960-9822(00)80017-2 , Abstract

Show more 3 citaions

Citation 2

The Janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding
Golbik, R., Lupas, A.N., Koretke, K.K., Baumeister, W., Peters, J.
Biol. Chem. (1999), 380, 1049-1062, PubMed 10543442 , DOI 10.1515/BC.1999.131 , Abstract

Citation 3

Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum
Pamnani, V., Tamura, T., Lupas, A., Peters, J., Cejka, Z., Ashraf, W., Baumeister, W.
FEBS Lett. (1997), 404, 263-268, PubMed 9119075 , DOI 10.1016/s0014-5793(97)00138-5 , Abstract

Citation 4

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 3 citaions

Entries sharing articles BMRB: 4, Swiss-Prot: 1 entries Detail

  BMRB: 4573 released on 2004-05-14
    Title 1HN,15N,13CO,13Ca,13Cb chemical shifts of 7,8-dihydroneopterin aldolase (DHNA) from Staphylococcus aureus
  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: 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
  Swiss-Prot: O05209 released on 2000-12-01
    Title VAT_THEAC Entity VCP-like ATPase

Related entities 1. VATN VCP-like ATPase of Thermoplasma N-domain, : 1 : 1 : 3 : 11 entities Detail

Experiments performed 1 experiments Detail

#	Name	Isotope labeling	Concentration
7	VCP-like ATPase of Thermoplasma N-domain	[U-15N; U-13C]	1.20 mM
8	phosphate buffer		100 mM
9	sodium chloride		200 mM
10	sodium azide		10 mM
11	D2O		10.0 %
12	H2O		90.0 %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts, Heteronucl NOE exptl data	bmr4376_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	Error

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr4376_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts	Warning	2287		98.9 (chain: 1, length: 185)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 185, Sequence coverage: 98.9%
- Total number of assignments
  - ¹H chemical shifts: 1319
  - ¹³C chemical shifts: 785
  - ¹⁵N chemical shifts: 183
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
4	ASN	CG	177.42
5	ASN	CG	177.69
63	ASN	CG	178.97
75	ASN	CG	176.77
108	GLN	CD	180.26
121	GLN	CD	179.33
132	GLN	CD	180.65
145	GLN	CD	180.26

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1132	1077	95.1
¹³C chemical shifts	826	777	94.1
¹⁵N chemical shifts	207	183	88.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	377	371	98.4
¹³C chemical shifts	370	356	96.2
¹⁵N chemical shifts	177	173	97.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	755	706	93.5
¹³C chemical shifts	456	421	92.3
¹⁵N chemical shifts	30	10	33.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	122	121	99.2
¹³C chemical shifts	122	121	99.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	18	100.0
¹³C chemical shifts	18	0	0.0

Keywords AAA ATPaseN-domain, coupling constants, NMR, protein, resonance assignment, secondary structure, VAT-N

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Found 1 Document (1.549 seconds)

BMRB: 4376

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 4, Swiss-Prot: 1 entries Detail

Related entities 1. VATN VCP-like ATPase of Thermoplasma N-domain, : 1 : 1 : 3 : 11 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample #1

Sample #2

Chemical shift validation 3 contents Detail