BMRBj - BMREntryMaster

Found 1 Document (1.311 seconds)

BMRB: 4987

7MN6

Backbone 1H,13C and 15N chemical shift assignment for the maltotriose-bound state of 2H,13C,15N-labeled maltodextrin-binding protein

Authors

Evenas, J., Tugarinov, V., Skrynnikov, N.R., Goto, N.K., Muhandiram, R., Kay, L.E.

Assembly

maltodextrin-binding protein

Entity

1. maltodextrin-binding protein (polymer, Thiol state: not present), 370 monomers, 40694.71 Da Detail

KTEEGKLVIW INGDKGYNGL AEVGKKFEKD TGIKVTVEHP DKLEEKFPQV AATGDGPDII FWAHDRFGGY AQSGLLAEIT PDKAFQDKLY PFTWDAVRYN GKLIAYPIAV EALSLIYNKD LLPNPPKTWE EIPALDKELK AKGKSALMFN LQEPYFTWPL IAADGGYAFK YENGKYDIKD VGVDNAGAKA GLTFLVDLIK NKHMNADTDY SIAEAAFNKG ETAMTINGPW AWSNIDTSKV NYGVTVLPTF KGQPSKPFVG VLSAGINAAS PNKELAKEFL ENYLLTDEGL EAVNKDKPLG AVALKSYEEE LAKDPRIAAT MENAQKGEIM PNIPQMSAFW YAVRTAVINA ASGRQTVDEA LKDAQTRITK

2. MLR (non-polymer), 504.437 Da

Total weight

41199.15 Da

Max. entity weight

40694.71 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.2 %, Completeness: 47.3 %, Completeness (bb): 82.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	47.3 % (2042 of 4316)	26.6 % (596 of 2237)	65.2 % (1104 of 1692)	88.4 % (342 of 387)
Backbone	82.2 % (1791 of 2178)	54.4 % (407 of 748)	96.6 % (1044 of 1081)	97.4 % (340 of 349)
Sidechain	23.8 % (589 of 2479)	12.8 % (190 of 1489)	41.7 % (397 of 952)	5.3 % (2 of 38)
Aromatic	2.4 % (9 of 378)	3.7 % (7 of 189)	1.1 % (2 of 181)	0.0 % (0 of 8)
Methyl	28.2 % (118 of 418)	21.1 % (44 of 209)	35.4 % (74 of 209)

1. maltodextrin-binding protein

Show sample condition

Sample

Temperature 310 (±0.5) K, pH 7.2 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	maltodextrin-binding protein	[U-2H; U-15N; U-13C]		1.3 mM
2	maltotriose			1.3 mM

Release date

2001-09-11

Citation

Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy
Evenas, J., Tugarinov, V., Skrynnikov, N.R., Goto, N.K., Muhandiram, R., Kay, L.E.
J. Mol. Biol. (2001), 309, 961-974, PubMed 11399072 , DOI 10.1006/jmbi.2001.4695 , Abstract

Related entities 1. maltodextrin-binding protein, : 1 : 4 : 95 : 13 entities Detail

Interaction partners 1. maltodextrin-binding protein, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 3 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4987_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: bmr4987_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1725		98.9 (chain: 1, length: 370)
1	Chemical shift references	chemical_shift_reference	Warning	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 370, Sequence coverage: 98.9%
- Total number of assignments
  - ¹³C chemical shifts: 1043
  - ¹⁵N chemical shifts: 341
  - ¹H chemical shifts: 341
- 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	1692	1043	61.6
¹⁵N chemical shifts	393	341	86.8
¹H chemical shifts	2237	341	15.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	740	706	95.4
¹⁵N chemical shifts	349	341	97.7
¹H chemical shifts	748	341	45.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	952	337	35.4
¹⁵N chemical shifts	44	0	0.0
¹H chemical shifts	1489	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	215	44	20.5
¹H chemical shifts	215	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	181	0	0.0
¹⁵N chemical shifts	8	0	0.0
¹H chemical shifts	189	0	0.0

Keywords chemical shift assignment, dipolar couplings, maltodextrin binding protein, protein domains, solution conformation

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (1.311 seconds)

BMRB: 4987

Sample

Related entities 1. maltodextrin-binding protein, : 1 : 4 : 95 : 13 entities Detail

Interaction partners 1. maltodextrin-binding protein, : 1 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 4 contents Detail