BMRBj - BMREntryMaster

Found 1 Document (0.705 seconds)

BMRB: 6807

7MN6

1H, 13C, and 15N chemical shift assignments for stereo-array isotope labelled (SAIL) maltodextrin-binding protein (MBP)

Authors

Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A.MEI., Guntert, P.

Assembly

Maltodextrin-binding protein (MBP)

Entity

1. Maltodextrin-binding protein (polymer, Thiol state: not present), 370 monomers, 40706.77 Da Detail

KIEEGKLVIW 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. BCD (non-polymer), 1134.984 Da

Total weight

41841.754 Da

Max. entity weight

40706.77 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.5 %, Completeness: 73.1 %, Completeness (bb): 83.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	73.1 % (3160 of 4321)	72.0 % (1612 of 2240)	69.7 % (1181 of 1694)	94.8 % (367 of 387)
Backbone	83.1 % (1811 of 2178)	94.5 % (707 of 748)	70.3 % (760 of 1081)	98.6 % (344 of 349)
Sidechain	67.4 % (1673 of 2484)	60.7 % (905 of 1492)	78.1 % (745 of 954)	60.5 % (23 of 38)
Aromatic	45.8 % (173 of 378)	51.9 % (98 of 189)	38.1 % (69 of 181)	75.0 % (6 of 8)
Methyl	81.9 % (344 of 420)	82.9 % (174 of 210)	81.0 % (170 of 210)

1. Maltodextrin-binding protein

Show sample condition

Sample

Temperature 310 (±1) K, pH 7.2 (±0.1)

#	Name	Concentration
1	Maltodextrin-binding protein	0.9 mM
2	beta-cyclodextrin	3.3 mM
3	sodium phosphate	20 mM
4	NaN3	3 mM
5	CompleteMini protease inhibitor mix

LACS Plot; CA

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

Referencing offset: 0.0 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.0 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: -0.11 ppm, Outliers: 1 Detail

Release date

2006-04-24

Citation

Optimal isotope labelling for NMR protein structure determinations
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Mei Ono, A., Guntert, P.
Nature (2006), 440, 52-57, PubMed 16511487 , DOI 10.1038/nature04525 , Abstract

Related entities 1. Maltodextrin-binding protein, : 1 : 35 : 1 : 66 : 11 entities Detail

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

More details for 1 interactors identified by 1 citations

Experiments performed 1 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6807_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: bmr6807_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	3148		98.1 (chain: 1, length: 370)
1	Chemical shift references	chemical_shift_referencing	OK	3		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 370, Sequence coverage: 98.1%
- Total number of assignments
  - ¹H chemical shifts: 1753
  - ¹³C chemical shifts: 1035
  - ¹⁵N chemical shifts: 360
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Tautomeric state of HIS
- 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 (%)
¹H chemical shifts	748	691	92.4
¹³C chemical shifts	740	352	47.6
¹⁵N chemical shifts	349	339	97.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	216	160	74.1
¹³C chemical shifts	216	160	74.1

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Found 1 Document (0.705 seconds)

BMRB: 6807

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Maltodextrin-binding protein, : 1 : 35 : 1 : 66 : 11 entities Detail

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

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 4 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	2240	1433	64.0
¹³C chemical shifts	1694	1035	61.1
¹⁵N chemical shifts	393	360	91.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1492	742	49.7
¹³C chemical shifts	954	683	71.6
¹⁵N chemical shifts	44	21	47.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	189	66	34.9
¹³C chemical shifts	181	40	22.1
¹⁵N chemical shifts	8	5	62.5