BMRBj - BMREntryMaster

	Total	¹H
All	99.4 % (163 of 164)	99.4 % (163 of 164)
Backbone	98.5 % (66 of 67)	98.5 % (66 of 67)
Sidechain	100.0 % (97 of 97)	100.0 % (97 of 97)
Methyl	100.0 % (19 of 19)	100.0 % (19 of 19)

1. C-peptide

EAEDLQVGQV ELGGGPGAGS LQPLALEGSL Q

Show sample condition

Sample

Temperature 283 (±1) K, pH 7.0 (±0.1)

#	Name	Concentration
7	C-peptide	1.2 mM
8	TFE-d2	80 %
9	H2O	20 %

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 98.8 %, Completeness (bb): 97.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	98.8 % (324 of 328)	98.8 % (324 of 328)
Backbone	97.0 % (130 of 134)	97.0 % (130 of 134)
Sidechain	100.0 % (194 of 194)	100.0 % (194 of 194)
Methyl	100.0 % (38 of 38)	100.0 % (38 of 38)

1. C-peptide

EAEDLQVGQV ELGGGPGAGS LQPLALEGSL Q

Show sample condition

Sample

Temperature 283 (±1) K, pH 7.0 (±0.1)

#	Name	Concentration
7	C-peptide	1.2 mM
8	TFE-d2	80 %
9	H2O	20 %

Chem. Shift Complete3

Sequence coverage: 100.0 %, Completeness: 99.0 %, Completeness (bb): 97.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	99.0 % (487 of 492)	99.0 % (487 of 492)
Backbone	97.5 % (196 of 201)	97.5 % (196 of 201)
Sidechain	100.0 % (291 of 291)	100.0 % (291 of 291)
Methyl	100.0 % (57 of 57)	100.0 % (57 of 57)

1. C-peptide

EAEDLQVGQV ELGGGPGAGS LQPLALEGSL Q

Show sample condition

Sample

Temperature 283 (±1) K, pH 7.0 (±0.1)

#	Name	Concentration
7	C-peptide	1.2 mM
8	TFE-d2	80 %
9	H2O	20 %

Protein Blocks Logo

Calculated from 30 models in PDB: 1T0C, Strand ID: A Detail

Release date

2005-10-31

Citation

Solution structure of human proinsulin C-peptide
Munte, C.E., Vilela, L., Kalbitzer, H.R., Garratt, R.C.
FEBS J. (2005), 272, 4284-4293, PubMed 16098208 , DOI 10.1111/j.1742-4658.2005.04843.x , Abstract

Related entities 1. C-peptide, : 1 : 8 : 2 : 19 entities Detail

Interaction partners 1. C-peptide, : 5 interactors Detail

More details for 5 interactors identified by 5 citations

Experiments performed 3 experiments Detail

#	Name	Concentration
1	C-peptide	6 mM
2	D2O	5 %
3	H2O	95 %

#	Name	Concentration
4	C-peptide	3 mM
5	TFE-d2	50 %
6	H2O	50 %

#	Name	Concentration
1	C-peptide	6 mM
2	D2O	5 %
3	H2O	95 %

#	Name	Concentration
4	C-peptide	3 mM
5	TFE-d2	50 %
6	H2O	50 %

#	Name	Concentration
1	C-peptide	6 mM
2	D2O	5 %
3	H2O	95 %

#	Name	Concentration
4	C-peptide	3 mM
5	TFE-d2	50 %
6	H2O	50 %

Chemical shift validation 5 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6623_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	OK

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr6623_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	OK	200	100.0 (chain: 1, length: 31)
2	Assigned chemical shifts	chem_shift_list_2	OK	201	100.0 (chain: 1, length: 31)
3	Assigned chemical shifts	chem_shift_list_3	OK	201	100.0 (chain: 1, length: 31)
1	Chemical shift references	chemical_shift_referencing	OK	1	No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 31, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 200
- 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: chem_shift_list_2
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 31, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 201
- 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: chem_shift_list_3
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 31, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 201
- 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

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Found 1 Document (1.713 seconds)

BMRB: 6623

Sample

Sample

Sample

Related entities 1. C-peptide, : 1 : 8 : 2 : 19 entities Detail

Interaction partners 1. C-peptide, : 5 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample #1

Sample #2

Sample #3

Instrument

Sample #1

Sample #2

Sample #3

Instrument

Sample #1

Sample #2

Sample #3

Chemical shift validation 5 contents Detail