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Found 1 Document (1.481 seconds)

BMRB: 4011

6FRV

1H and 15N Assignments and Secondary Structure of the Starch-binding Domain of Glucoamylase from Aspergillus niger

Authors

Jacks, A.J., Sorimachi, K., Le Gal-Coeffet, M., Williamson, G., Archer, D.B., Williamson, M.P.

Assembly

Starch binding domain

Entity

1. Starch binding domain (polymer), 108 monomers, 11879.77 Da Detail

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Formula weight

11879.77 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	0:CYS1:SG	1:CYS96:SG

Source organism

Aspergillus niger

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 93.5 %, Completeness: 88.2 %, Completeness (bb): 89.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	88.2 % (620 of 703)	87.7 % (519 of 592)	91.0 % (101 of 111)
Backbone	89.4 % (286 of 320)	88.5 % (192 of 217)	91.3 % (94 of 103)
Sidechain	87.2 % (334 of 383)	87.2 % (327 of 375)	87.5 % (7 of 8)
Aromatic	89.6 % (60 of 67)	88.9 % (56 of 63)	100.0 % (4 of 4)
Methyl	93.8 % (60 of 64)	93.8 % (60 of 64)

1. Starch binding domain

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Show sample condition

Sample

Temperature 313 K, pH 5.2

#	Name	Isotope labeling	Concentration
1	Starch binding domain	[U-100% 15N]	1.0 mM
2	H2O		90 %
3	D2O		10 %

Chem. Shift Complete2

Sequence coverage: 23.1 %, Completeness: 48.3 %, Completeness (bb): 51.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	48.3 % (679 of 1406)	47.6 % (563 of 1184)	52.3 % (116 of 222)
Backbone	51.1 % (327 of 640)	50.2 % (218 of 434)	52.9 % (109 of 206)
Sidechain	46.0 % (352 of 766)	46.0 % (345 of 750)	43.8 % (7 of 16)
Aromatic	47.8 % (64 of 134)	47.6 % (60 of 126)	50.0 % (4 of 8)
Methyl	49.2 % (63 of 128)	49.2 % (63 of 128)

1. Starch binding domain

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Show sample condition

Sample

Temperature 313 K, pH 5.2

#	Name	Isotope labeling	Concentration
1	Starch binding domain	[U-100% 15N]	1.0 mM
2	H2O		90 %
3	D2O		10 %

Chem. Shift Complete3

Sequence coverage: 17.6 %, Completeness: 34.5 %, Completeness (bb): 37.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	34.5 % (728 of 2109)	34.0 % (604 of 1776)	37.2 % (124 of 333)
Backbone	37.2 % (357 of 960)	36.9 % (240 of 651)	37.9 % (117 of 309)
Sidechain	32.3 % (371 of 1149)	32.4 % (364 of 1125)	29.2 % (7 of 24)
Aromatic	31.8 % (64 of 201)	31.7 % (60 of 189)	33.3 % (4 of 12)
Methyl	34.4 % (66 of 192)	34.4 % (66 of 192)

1. Starch binding domain

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Show sample condition

Sample

Temperature 313 K, pH 5.2

#	Name	Isotope labeling	Concentration
1	Starch binding domain	[U-100% 15N]	1.0 mM
2	H2O		90 %
3	D2O		10 %

Chem. Shift Complete4

Sequence coverage: 23.1 %, Completeness: 28.6 %, Completeness (bb): 31.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	28.6 % (803 of 2812)	28.1 % (665 of 2368)	31.1 % (138 of 444)
Backbone	31.6 % (404 of 1280)	31.6 % (274 of 868)	31.6 % (130 of 412)
Sidechain	26.1 % (400 of 1532)	26.1 % (392 of 1500)	25.0 % (8 of 32)
Aromatic	24.6 % (66 of 268)	24.2 % (61 of 252)	31.3 % (5 of 16)
Methyl	28.9 % (74 of 256)	28.9 % (74 of 256)

1. Starch binding domain

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Show sample condition

Sample

Temperature 313 K, pH 5.2

#	Name	Isotope labeling	Concentration
1	Starch binding domain	[U-100% 15N]	1.0 mM
2	H2O		90 %
3	D2O		10 %

Chem. Shift Complete5

Sequence coverage: 9.3 %, Completeness: 23.9 %, Completeness (bb): 26.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	23.9 % (841 of 3515)	23.4 % (693 of 2960)	26.7 % (148 of 555)
Backbone	26.8 % (428 of 1600)	26.5 % (288 of 1085)	27.2 % (140 of 515)
Sidechain	21.6 % (414 of 1915)	21.7 % (406 of 1875)	20.0 % (8 of 40)
Aromatic	19.7 % (66 of 335)	19.4 % (61 of 315)	25.0 % (5 of 20)
Methyl	23.7 % (76 of 320)	23.7 % (76 of 320)

1. Starch binding domain

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Show sample condition

Sample

Temperature 313 K, pH 5.2

#	Name	Isotope labeling	Concentration
1	Starch binding domain	[U-100% 15N]	1.0 mM
2	H2O		90 %
3	D2O		10 %

Chem. Shift Complete6

Sequence coverage: 13.0 %, Completeness: 21.4 %, Completeness (bb): 24.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	21.4 % (902 of 4218)	20.9 % (743 of 3552)	23.9 % (159 of 666)
Backbone	24.1 % (462 of 1920)	23.9 % (311 of 1302)	24.4 % (151 of 618)
Sidechain	19.2 % (441 of 2298)	19.2 % (433 of 2250)	16.7 % (8 of 48)
Aromatic	16.4 % (66 of 402)	16.1 % (61 of 378)	20.8 % (5 of 24)
Methyl	20.6 % (79 of 384)	20.6 % (79 of 384)

1. Starch binding domain

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Show sample condition

Sample

Temperature 313 K, pH 5.2

#	Name	Isotope labeling	Concentration
1	Starch binding domain	[U-100% 15N]	1.0 mM
2	H2O		90 %
3	D2O		10 %

Chem. Shift Complete7

Sequence coverage: 12.0 %, Completeness: 19.4 %, Completeness (bb): 22.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	19.4 % (955 of 4921)	18.9 % (784 of 4144)	22.0 % (171 of 777)
Backbone	22.1 % (496 of 2240)	21.9 % (333 of 1519)	22.6 % (163 of 721)
Sidechain	17.2 % (460 of 2681)	17.2 % (452 of 2625)	14.3 % (8 of 56)
Aromatic	14.1 % (66 of 469)	13.8 % (61 of 441)	17.9 % (5 of 28)
Methyl	19.0 % (85 of 448)	19.0 % (85 of 448)

1. Starch binding domain

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Show sample condition

Sample

Temperature 313 K, pH 5.2

#	Name	Isotope labeling	Concentration
1	Starch binding domain	[U-100% 15N]	1.0 mM
2	H2O		90 %
3	D2O		10 %

Chem. Shift Complete8

Sequence coverage: 7.4 %, Completeness: 17.6 %, Completeness (bb): 20.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	17.6 % (992 of 5624)	17.2 % (814 of 4736)	20.0 % (178 of 888)
Backbone	20.1 % (514 of 2560)	19.9 % (345 of 1736)	20.5 % (169 of 824)
Sidechain	15.6 % (479 of 3064)	15.7 % (470 of 3000)	14.1 % (9 of 64)
Aromatic	13.6 % (73 of 536)	13.3 % (67 of 504)	18.8 % (6 of 32)
Methyl	17.6 % (90 of 512)	17.6 % (90 of 512)

1. Starch binding domain

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Show sample condition

Sample

Temperature 313 K, pH 5.2

#	Name	Isotope labeling	Concentration
1	Starch binding domain	[U-100% 15N]	1.0 mM
2	H2O		90 %
3	D2O		10 %

Chem. Shift Complete9

Sequence coverage: 17.6 %, Completeness: 16.8 %, Completeness (bb): 19.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	16.8 % (1065 of 6327)	16.4 % (873 of 5328)	19.2 % (192 of 999)
Backbone	19.3 % (556 of 2880)	19.2 % (374 of 1953)	19.6 % (182 of 927)
Sidechain	14.8 % (509 of 3447)	14.8 % (500 of 3375)	12.5 % (9 of 72)
Aromatic	12.1 % (73 of 603)	11.8 % (67 of 567)	16.7 % (6 of 36)
Methyl	16.8 % (97 of 576)	16.8 % (97 of 576)

1. Starch binding domain

CTTPTAVAVT FDLTATTTYG ENIYLVGSIS QLGDWETSDG IALSADKYTS SDPLWYVTVT LPAGESFEYK FIRIESDDSV EWESDPNREY TVPQACGTST ATVTDTWR

Show sample condition

Sample

Temperature 313 K, pH 5.2

#	Name	Isotope labeling	Concentration
1	Starch binding domain	[U-100% 15N]	1.0 mM
2	H2O		90 %
3	D2O		10 %

Release date

2000-11-09

Citation

1H and 15N assignments and secondary structure of the starch-binding domain of glucoamylase from Aspergillus niger
Jacks, A.J., Sorimachi, K., Le Gal-Coeffet, M., Williamson, G., Archer, D.B., Williamson, M.P.
Eur. J. Biochem. (1995), 233, 568-578, PubMed 7588803 , DOI: , Abstract

Related entities 1. Starch binding domain, : 1 : 6 : 112 entities Detail

Chemical shift validation 11 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4011_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:1:CYS:SG	1:96:CYS:SG	unknown	unknown	n/a

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

None

Non-standard residues

None

Content subtype: bmr4011_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_one	Warning	762	93.5 (chain: 1, length: 108)
2	Assigned chemical shifts	assigned_chemical_shifts_two	Warning	11	1.9 (chain: 1, length: 108)
3	Assigned chemical shifts	assigned_chemical_shifts_three	Warning	3	0.9 (chain: 1, length: 108)
4	Assigned chemical shifts	assigned_chemical_shifts_four	Warning	11	1.9 (chain: 1, length: 108)
5	Assigned chemical shifts	assigned_chemical_shifts_five	Warning	3	0.9 (chain: 1, length: 108)
6	Assigned chemical shifts	assigned_chemical_shifts_six	Warning	15	2.8 (chain: 1, length: 108)
7	Assigned chemical shifts	assigned_chemical_shifts_seven	Warning	17	2.8 (chain: 1, length: 108)
8	Assigned chemical shifts	assigned_chemical_shifts_eight	Warning	6	0.9 (chain: 1, length: 108)
9	Assigned chemical shifts	assigned_chemical_shifts_nine	Warning	5	0.9 (chain: 1, length: 108)
1	Chemical shift references	chemical_shift_reference_one	OK	2	No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 93.5%
- Total number of assignments
  - ¹H chemical shifts: 661
  - ¹⁵N chemical shifts: 101
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: assigned_chemical_shifts_two
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 1.9%
- Total number of assignments
  - ¹H chemical shifts: 10
  - ¹⁵N chemical shifts: 1
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: assigned_chemical_shifts_three
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 0.9%
- Total number of assignments
  - ¹H chemical shifts: 3
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
Saveframe: assigned_chemical_shifts_four
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 1.9%
- Total number of assignments
  - ¹H chemical shifts: 10
  - ¹⁵N chemical shifts: 1
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: assigned_chemical_shifts_five
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 0.9%
- Total number of assignments
  - ¹H chemical shifts: 3
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
Saveframe: assigned_chemical_shifts_six
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 2.8%
- Total number of assignments
  - ¹H chemical shifts: 13
  - ¹⁵N chemical shifts: 2
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: assigned_chemical_shifts_seven
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 2.8%
- Total number of assignments
  - ¹H chemical shifts: 15
  - ¹⁵N chemical shifts: 2
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: assigned_chemical_shifts_eight
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 0.9%
- Total number of assignments
  - ¹H chemical shifts: 5
  - ¹⁵N chemical shifts: 1
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: assigned_chemical_shifts_nine
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 0.9%
- Total number of assignments
  - ¹H chemical shifts: 5
- Completeness of assignments
- 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	592	539	91.0
¹⁵N chemical shifts	114	101	88.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	217	203	93.5
¹⁵N chemical shifts	103	94	91.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	375	336	89.6
¹⁵N chemical shifts	11	7	63.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	64	61	95.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	56	88.9
¹⁵N chemical shifts	4	4	100.0

Keywords glucoamylase, NMR, nuclear magnetic resonance, protein, resonance assignments, SBD, secondary structure, starch binding domain

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BMRB: 4011

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Related entities 1. Starch binding domain, : 1 : 6 : 112 entities Detail

Chemical shift validation 11 contents Detail