BMRBj - BMREntryMaster

Found 1 Document (1.311 seconds)

BMRB: 5656

7BG9

Resonance Assignments for the Z Domain of Staphylococcal Protein A using a 2H, 13C, 15N enriched, selective methyl protonated sample

Authors

Zheng, D., Swapna, G., Hunter, M.N.B., Montelione, G.T.

Assembly

staphylococcal protein A Z domain

Entity

1. staphylococcal protein A Z domain (polymer, Thiol state: not present), 71 monomers, 8077.847 Da Detail

KAIFVLNAQH DEAVDNKFNK EQQNAFYEIL HLPNLNEEQR NAFIQSLKDD PSQSANLLAE AKKLNDAQAP K

Formula weight

8077.847 Da

Source organism

Staphylococcus aureus

Exptl. method

NMR

Refine. method

SIMULATED ANNEALING WITH RESTRAINED MOLECULAR DYNAMICS, PROTOCAL USED: ANNEAL.INP

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 56.7 %, Completeness (bb): 83.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	56.7 % (485 of 855)	37.3 % (168 of 451)	72.8 % (233 of 320)	100.0 % (84 of 84)
Backbone	83.3 % (350 of 420)	56.1 % (78 of 139)	95.8 % (204 of 213)	100.0 % (68 of 68)
Sidechain	40.7 % (206 of 506)	29.5 % (92 of 312)	55.1 % (98 of 178)	100.0 % (16 of 16)
Aromatic	14.3 % (8 of 56)	14.3 % (4 of 28)	14.3 % (4 of 28)
Methyl	76.4 % (55 of 72)	69.4 % (25 of 36)	83.3 % (30 of 36)

1. staphylococcal protein A Z domain

KAIFVLNAQH DEAVDNKFNK EQQNAFYEIL HLPNLNEEQR NAFIQSLKDD PSQSANLLAE AKKLNDAQAP K

Show sample condition

Sample

Temperature 303 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	staphylococcal protein A Z domain	[U-13C; U-15N; U-2H] with Val, Leu, Ile(delta) methyl protonated		1.1 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	null	null	1.0
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.51 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	null	null	1.0
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.51 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	null	null	1.0
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.33 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 1Q2N, Strand ID: A Detail

Release date

2005-05-02

Citation

Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data
Zheng, D., Aramini, J.M., Montelione, G.T.
Protein Sci. (2004), 13, 549-554, PubMed 14718654 , DOI 10.1110/ps.03351704 , Abstract

Related entities 1. staphylococcal protein A Z domain, : 2 : 75 : 73 entities Detail

Interaction partners 1. staphylococcal protein A Z domain, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 8 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5656_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: bmr5656_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_one	OK	486		100.0 (chain: 1, length: 71)
1	Chemical shift references	chemical_shift_reference_one	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_one
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 71, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 235
  - ¹H chemical shifts: 168
  - ¹⁵N chemical shifts: 83
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	142	141	99.3
¹H chemical shifts	139	67	48.2
¹⁵N chemical shifts	68	67	98.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	320	235	73.4
¹H chemical shifts	451	122	27.1
¹⁵N chemical shifts	85	83	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	178	94	52.8
¹H chemical shifts	312	55	17.6
¹⁵N chemical shifts	17	16	94.1

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Found 1 Document (1.311 seconds)

BMRB: 5656

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. staphylococcal protein A Z domain, : 2 : 75 : 73 entities Detail

Interaction partners 1. staphylococcal protein A Z domain, : 1 interactors Detail

Experiments performed 8 experiments Detail

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Chemical shift validation 3 contents Detail