BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	88.1 % (563 of 639)	97.9 % (330 of 337)	73.1 % (171 of 234)	91.2 % (62 of 68)
Backbone	81.2 % (323 of 398)	95.8 % (137 of 143)	66.8 % (127 of 190)	90.8 % (59 of 65)
Sidechain	99.7 % (296 of 297)	99.5 % (193 of 194)	100.0 % (100 of 100)	100.0 % (3 of 3)
Methyl	100.0 % (16 of 16)	100.0 % (8 of 8)	100.0 % (8 of 8)

1. entity 1

GSGKGKGEKC TSACRSEPCQ CGSKCQCGEG CTCAACKTCN CTSDGCKCGK ECTGPDSCKC GSSCSCK

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1.0 atm, Temperature 298 (±0.2) K, pH 7.0 (±0.1), Details 0.5mM protein, [U-13C,15N], 10 mM [U-2H] TRIS, 1 mM TSP, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1	[U-13C; U-15N]	0.5 mM
2	TRIS	[U-2H]	10 (±1.0) mM
3	TSP	none	1 (±0.1) mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1.0 atm, Temperature 298 (±0.2) K, pH 7.0 (±0.1), Details 0.5mM protein, [U-13C,15N], 10 mM [U-2H] TRIS, 1 mM TSP, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl protons	internal	indirect	0.2514495
¹H	TSP	methyl protons	internal	direct	1.0
¹⁵N	TSP	methyl protons	internal	indirect	0.101329

Referencing offset: 0.34 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl protons	internal	indirect	0.2514495
¹H	TSP	methyl protons	internal	direct	1.0
¹⁵N	TSP	methyl protons	internal	indirect	0.101329

Referencing offset: 0.34 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl protons	internal	indirect	0.2514495
¹H	TSP	methyl protons	internal	direct	1.0
¹⁵N	TSP	methyl protons	internal	indirect	0.101329

Referencing offset: 0.04 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 6QK6, Strand ID: A Detail

Release date

2019-12-08

Citation

The Solution Structure and Dynamics of Cd-Metallothionein from Helix pomatia Reveal Optimization for Binding Cd over Zn
Beil, A., Jurt, S., Walser, R., Schonhut, T., Guntert, P., Palacios, O., Atrian, S., Capdevila, M., Dallinger, R., Zerbe, O.
Biochemistry (2019), 58, 4570-4581, PubMed 31633358 , DOI 10.1021/acs.biochem.9b00830 , Abstract

Related entities 1. Cadmium-metallothionein, entity 1, : 1 : 1 : 1 : 15 entities Detail

Experiments performed 12 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Neo - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1.0 atm, Temperature 298 (±0.2) K, pH 7.0 (±0.1), Details 0.5mM protein, [U-13C,15N], 10 mM [U-2H] TRIS, 1 mM TSP, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1	[U-13C; U-15N]	0.5 mM
2	TRIS	[U-2H]	10 (±1.0) mM
3	TSP	none	1 (±0.1) mM

2 2D 1H-15N HSQC

Instrument

Bruker Neo - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	entity_1	[U-13C; U-15N]	0.5 mM
2	TRIS	[U-2H]	10 (±1.0) mM
3	TSP	none	1 (±0.1) mM

3 2D 1H-15N HSQC

Instrument

Bruker Neo - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

4 2D 1H-13C HSQC aliphatic

Instrument

Bruker Neo - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

5 3D CBCA(CO)NH

Instrument

Bruker Neo - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

6 3D HNCO

Instrument

Bruker Neo - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

7 3D HNCACB

Instrument

Bruker Neo - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

8 3D HCCH-TOCSY

Instrument

Bruker Neo - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

9 3D 1H-13C NOESY aliphatic

Instrument

Bruker Neo - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

10 3D 1H-15N NOESY

Instrument

Bruker Neo - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

11 3D HBHA(CO)NH

Instrument

Bruker Neo - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

12 3D HNCACO

Instrument

Bruker Neo - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
4	entity_1	[U-13C; U-15N]	0.5 mM
5	TRIS	[U-2H]	10 (±1.0) mM
6	TSP	none	1 (±0.1) mM

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34356_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: bmr34356_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	575		100.0 (chain: 1, length: 67)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 67, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 346
  - ¹³C chemical shifts: 167
  - ¹⁵N chemical shifts: 62
- 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 (%)
¹H chemical shifts	337	330	97.9
¹³C chemical shifts	234	167	71.4
¹⁵N chemical shifts	69	62	89.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	143	137	95.8
¹³C chemical shifts	134	67	50.0
¹⁵N chemical shifts	65	59	90.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	194	193	99.5
¹³C chemical shifts	100	100	100.0
¹⁵N chemical shifts	4	3	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	8	100.0
¹³C chemical shifts	8	8	100.0

Keywords Cadmium protein, Helix pomatia, METAL BINDING PROTEIN, metallothionein, snail protein

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Found 1 Document (0.575 seconds)

BMRB: 34356

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Cadmium-metallothionein, entity 1, : 1 : 1 : 1 : 15 entities Detail

Experiments performed 12 experiments Detail

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Chemical shift validation 4 contents Detail