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Found 1 Document (0.459 seconds)

BMRB: 10010

1CJ5

bovine beta-lactoglobulin A34C mutant

Authors

Sakurai, K., Goto, Y.

Assembly

bovine beta-lactoglobulin A34C; disulfide linked dimer

Entity

1. bovine beta-lactoglobulin A34C; disulfide linked dimer (polymer, Thiol state: free and disulfide bound), 165 monomers, 18736.38 × 2 Da Detail

EAEAYVTQTM KGLDIQKVAG TWYSLAMAAS DISLLDCQSA PLRVYVEELK PTPEGDLEIL LQKWENDECA QKKIIAEKTK IPAVFKIDAL NENKVLVLDT DYKKYLLFCM ENSAEPEQSL VCQCLVRTPE VDDEALEKFD KALKALPMHI RLSFNPTQLE EQCHI

Total weight

37472.76 Da

Max. entity weight

18736.38 Da

Entity Connection

disulfide 5 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS69:SG	1:CYS163:SG
2	disulfide	sing	1:CYS109:SG	1:CYS122:SG
3	disulfide	sing	1:CYS37:SG	1:CYS37:SG
4	disulfide	sing	1:CYS69:SG	1:CYS163:SG
5	disulfide	sing	1:CYS109:SG	1:CYS122:SG

Source organism

Bos taurus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.8 %, Completeness: 44.0 %, Completeness (bb): 79.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	44.0 % (863 of 1960)	21.9 % (224 of 1021)	64.2 % (492 of 766)	85.0 % (147 of 173)
Backbone	79.9 % (778 of 974)	50.8 % (165 of 325)	94.7 % (466 of 492)	93.6 % (147 of 157)
Sidechain	20.8 % (239 of 1148)	8.5 % (59 of 696)	41.3 % (180 of 436)	0.0 % (0 of 16)
Aromatic	0.0 % (0 of 112)	0.0 % (0 of 56)	0.0 % (0 of 54)	0.0 % (0 of 2)
Methyl	21.8 % (45 of 206)	15.5 % (16 of 103)	28.2 % (29 of 103)

1. BLG A34C

EAEAYVTQTM KGLDIQKVAG TWYSLAMAAS DISLLDCQSA PLRVYVEELK PTPEGDLEIL LQKWENDECA QKKIIAEKTK IPAVFKIDAL NENKVLVLDT DYKKYLLFCM ENSAEPEQSL VCQCLVRTPE VDDEALEKFD KALKALPMHI RLSFNPTQLE EQCHI

Show sample condition

Sample

Temperature 313 (±0.1) K, pH 6.5 (±0.1), Details Protein dissolved into water. (No buffer is added.) pH is adjusted by adding HCl.

#	Name	Isotope labeling	Type	Concentration
1	beta-lactoglobulin A34C polypeptide	[U-99% 13C; U-99.3% 15N]	protein	2 (±0.2) mM
2	Hydrochloric acid		acid	7.0 ~ 9.0 mM

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: -0.12 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: -0.12 ppm, Outliers: 1 Detail

LACS Plot; CO

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: 0.51 ppm, Outliers: 2 Detail

Release date

2007-06-12

Citation 1

Dynamics and mechanism of the Tanford transition of bovine beta-lactoglobulin studied using heteronuclear NMR spectroscopy
Sakurai, K., Goto, Y.
J. Mol. Biol. (2006), 356, 483-496, PubMed 16368109 , DOI 10.1016/j.jmb.2005.11.038 , Abstract

Show more 3 citaions

Citation 2

High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties
Kim, T., Goto, Y., Hirota, N., Kuwata, K., Denton, H., Wu, S., Sawyer, L., Batt, C.A.
Protein Eng. (1997), 10, 1339-1345, PubMed 9514124 , DOI 10.1093/protein/10.11.1339 , Abstract

Citation 3

alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR
Kuwata, K., Hoshino, M., Era, S., Batt, C.A., Goto, Y.
J. Mol. Biol. (1998), 283, 731-739, PubMed 9790836 , DOI 10.1006/jmbi.1998.2117 , Abstract

Citation 4

Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form
Uhrinova, S., Uhrin, D., Denton, H., Smith, M., Sawyer, L., Barlow, P.N.
J. Biomol. NMR (1998), 12, 89-107, PubMed 9729790 , Abstract

Hide non-primary 3 citaions

Related entities 1. bovine beta-lactoglobulin A34C; disulfide linked dimer, : 1 : 94 : 92 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr10010_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)
1:69:CYS:SG	1:163:CYS:SG	oxidized, CA 55.23, CB 39.75 ppm	unknown	n/a
1:109:CYS:SG	1:122:CYS:SG	oxidized, CA 55.74, CB 49.56 ppm	oxidized, CA 55.35, CB 50.23 ppm	n/a
1:37:CYS:SG	2:37:CYS:SG	oxidized, CA 58.16, CB 45.24 ppm	unknown	n/a
2:69:CYS:SG	2:163:CYS:SG	unknown	unknown	n/a
2:109:CYS:SG	2:122: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: bmr10010_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assignment_for_bLG_A34C_at_pH_6.5	Warning	757		95.2 (chain: 1, length: 165)
1	Chemical shift references	default_reference	OK	3		No information

Assigned chemical shifts

Saveframe: assignment_for_bLG_A34C_at_pH_6.5
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 165, Sequence coverage: 95.2%
- Total number of assignments
  - ¹³C chemical shifts: 463
  - ¹H chemical shifts: 147
  - ¹⁵N chemical shifts: 147
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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	766	463	60.4
¹H chemical shifts	1021	147	14.4
¹⁵N chemical shifts	176	147	83.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	330	310	93.9
¹H chemical shifts	325	147	45.2
¹⁵N chemical shifts	157	147	93.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	436	153	35.1
¹H chemical shifts	696	0	0.0
¹⁵N chemical shifts	19	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	107	15	14.0
¹H chemical shifts	107	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	54	0	0.0
¹H chemical shifts	56	0	0.0
¹⁵N chemical shifts	2	0	0.0

Keywords beta-barrel, lipocalin, beta-lactoglobulin

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Found 1 Document (0.459 seconds)

BMRB: 10010

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. bovine beta-lactoglobulin A34C; disulfide linked dimer, : 1 : 94 : 92 entities Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail