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Found 1 Document (1.466 seconds)

BMRB: 4982

2JPT

1H, 13C and 15N NMR sequence-specific resonance assignments for bovine apo-S100A1(aa) in oxidized form

Authors

Zhukov, I., Ejchart, A., Bierzynski, A.

Assembly

Apo-S100A1(aa) dimer

Entity

1. bovine S100A1(aa) (polymer, Thiol state: all disulfide bound), 94 monomers, 10518.62 × 2 Da Detail

MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK DADAVDKVMK ELDEDGDGEV DFQEYVVLVA ALTVACNNFF WENS

2. BME (non-polymer), 78.133 Da

Total weight

21115.373 Da

Max. entity weight

10518.62 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS86:SG	1:CYS86:SG

Source organism

Bos taurus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 100.0 %, Completeness: 83.7 %, Completeness (bb): 95.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	83.7 % (904 of 1080)	82.6 % (459 of 556)	84.4 % (356 of 422)	87.3 % (89 of 102)
Backbone	95.7 % (540 of 564)	95.4 % (185 of 194)	96.4 % (266 of 276)	94.7 % (89 of 94)
Sidechain	74.0 % (447 of 604)	75.7 % (274 of 362)	73.9 % (173 of 234)	0.0 % (0 of 8)
Aromatic	0.0 % (0 of 86)	0.0 % (0 of 43)	0.0 % (0 of 42)	0.0 % (0 of 1)
Methyl	92.3 % (96 of 104)	98.1 % (51 of 52)	86.5 % (45 of 52)

1. bovine S100A1(aa)

MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK DADAVDKVMK ELDEDGDGEV DFQEYVVLVA ALTVACNNFF WENS

Show sample condition

Sample

Temperature 308 (±1.0) K, pH 6.3 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	bovine S100A1(aa)	[U-98% 13C; U-98% 15N]		1.2 mM

Chem. Shift Complete2

Sequence coverage: 18.1 %, Completeness: 48.4 %, Completeness (bb): 55.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	48.4 % (1045 of 2160)	48.1 % (535 of 1112)	48.2 % (407 of 844)	50.5 % (103 of 204)
Backbone	55.6 % (627 of 1128)	56.4 % (219 of 388)	55.3 % (305 of 552)	54.8 % (103 of 188)
Sidechain	42.5 % (514 of 1208)	43.8 % (317 of 724)	42.1 % (197 of 468)	0.0 % (0 of 16)
Aromatic	2.3 % (4 of 172)	2.3 % (2 of 86)	2.4 % (2 of 84)	0.0 % (0 of 2)
Methyl	52.9 % (110 of 208)	57.7 % (60 of 104)	48.1 % (50 of 104)

1. bovine S100A1(aa)

MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK DADAVDKVMK ELDEDGDGEV DFQEYVVLVA ALTVACNNFF WENS

Show sample condition

Sample

Temperature 308 (±1.0) K, pH 6.3 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	bovine S100A1(aa)	[U-98% 13C; U-98% 15N]		1.2 mM

Chem. Shift Complete3

Sequence coverage: 17.0 %, Completeness: 36.5 %, Completeness (bb): 42.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	36.5 % (1183 of 3240)	35.7 % (596 of 1668)	37.0 % (468 of 1266)	38.9 % (119 of 306)
Backbone	42.3 % (715 of 1692)	42.1 % (245 of 582)	42.4 % (351 of 828)	42.2 % (119 of 282)
Sidechain	31.9 % (578 of 1812)	32.4 % (352 of 1086)	32.2 % (226 of 702)	0.0 % (0 of 24)
Aromatic	1.6 % (4 of 258)	1.6 % (2 of 129)	1.6 % (2 of 126)	0.0 % (0 of 3)
Methyl	42.3 % (132 of 312)	45.5 % (71 of 156)	39.1 % (61 of 156)

1. bovine S100A1(aa)

MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK DADAVDKVMK ELDEDGDGEV DFQEYVVLVA ALTVACNNFF WENS

Show sample condition

Sample

Temperature 308 (±1.0) K, pH 6.3 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	bovine S100A1(aa)	[U-98% 13C; U-98% 15N]		1.2 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 2JPT, Strand ID: A, B Detail

Release date

2003-05-22

Citation 1

Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol
Zhukov, I., Ejchart, A., Bierzynski, A.
Biochemistry (2008), 47, 640-650, PubMed 18088104 , DOI 10.1021/bi701762v , Abstract

Show more 4 citaions

Citation 2

NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , Abstract

Citation 3

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
J. Biomol. NMR (1995), 6, 1-10, PubMed 22911575 , DOI 10.1007/BF00417486 , Abstract

Citation 4

Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., Bax, A.
J. Biomol. NMR (1999), 13, 289-302, PubMed 10212987 , Abstract

Citation 5

1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140, PubMed 8589602 , DOI: , Abstract

Hide non-primary 4 citaions

Related entities 1. bovine S100A1(aa), : 1 : 1 : 268 entities Detail

Interaction partners 1. bovine S100A1(aa), : 6 interactors Detail

More details for 6 interactors identified by 3 citations

Experiments performed 10 experiments Detail

Chemical shift validation 6 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4982_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)
1:86:CYS:SG	2:86:CYS:SG	oxidized, CA 58.9, CB 40.9 ppm	unknown	n/a

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

None

Non-standard residues

None

Content subtype: bmr4982_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1032	100.0 (chain: 1, length: 94)
2	Assigned chemical shifts	shift_set_2	Warning	91	8.5 (chain: 1, length: 94)
3	Assigned chemical shifts	shift_set_3	OK	22	No information
1	Chemical shift references	chemical_shift_reference	OK	3	No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 94, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 364
  - ¹H chemical shifts: 575
  - ¹⁵N chemical shifts: 93
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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
Saveframe: shift_set_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 94, Sequence coverage: 8.5%
- Total number of assignments
  - ¹⁵N chemical shifts: 8
  - ¹H chemical shifts: 51
  - ¹³C chemical shifts: 32
- Completeness of assignments
- 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
Saveframe: shift_set_3
- Status: OK
- Total number of assignments
  - ¹⁵N chemical shifts: 2
  - ¹H chemical shifts: 12
  - ¹³C chemical shifts: 8
- Histogram of normalized assigned chemical shifts

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	422	364	86.3
¹H chemical shifts	556	471	84.7
¹⁵N chemical shifts	102	93	91.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	188	186	98.9
¹H chemical shifts	194	192	99.0
¹⁵N chemical shifts	94	93	98.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	234	178	76.1
¹H chemical shifts	362	279	77.1
¹⁵N chemical shifts	8	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	55	48	87.3
¹H chemical shifts	55	52	94.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	42	0	0.0
¹H chemical shifts	43	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords heteronuclear NMR, S100 proteins, S100A1, sequence-specific assignments

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Found 1 Document (1.466 seconds)

BMRB: 4982

Sample

Sample

Sample

Related entities 1. bovine S100A1(aa), : 1 : 1 : 268 entities Detail

Interaction partners 1. bovine S100A1(aa), : 6 interactors Detail

Experiments performed 10 experiments Detail

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Chemical shift validation 6 contents Detail