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Found 1 Document (0.947 seconds)

BMRB: 18859

2M1E

Biosynthetic engineered B28K-B29P human insulin monomer structure in in water solutions.

Authors

Bocian, W., Kozerski, L.

Assembly

Biosynthetic engineered B28K-B29P human insulin monomer

Entity

1. Biosynthetic engineered B28K-B29P human insulin monomer, entity 1 (polymer, Thiol state: all disulfide bound), 21 monomers, 2383.696 Da Detail

GIVEQCCTSI CSLYQLENYC N

2. Biosynthetic engineered B28K-B29P human insulin monomer, entity 2 (polymer, Thiol state: all disulfide bound), 30 monomers, 3429.919 Da Detail

FVNQHLCGSH LVEALYLVCG ERGFFYTKPT

Total weight

5813.615 Da

Max. entity weight

3429.919 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

torsion angle dynamics, DGSA-distance geometry simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.1 %, Completeness: 87.7 %, Completeness (bb): 90.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	87.7 % (265 of 302)	87.7 % (265 of 302)
Backbone	90.5 % (95 of 105)	90.5 % (95 of 105)
Sidechain	86.3 % (170 of 197)	86.3 % (170 of 197)
Aromatic	82.9 % (29 of 35)	82.9 % (29 of 35)
Methyl	100.0 % (28 of 28)	100.0 % (28 of 28)

1. entity 1

GIVEQCCTSI CSLYQLENYC N

2. entity 2

FVNQHLCGSH LVEALYLVCG ERGFFYTKPT

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 2.5

#	Name	Isotope labeling	Type	Concentration
1	entity_1	natural abundance		2.5 - 3.0 mM
2	entity_2	natural abundance		2.5 - 3.0 mM

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 2.5

#	Name	Isotope labeling	Type	Concentration
3	entity_1	natural abundance		2.5 - 3.0 mM
4	entity_2	natural abundance		2.5 - 3.0 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 2M1E, Strand ID: A, B Detail

Release date

2013-02-20

Citation

Biosynthetic engineered B28(K)-B29(P) human insulin monomer structure in water and in water/acetonitrile solutions
Borowicz, P., Bocian, W., Sitkowski, J., Bednarek, E., Mikiewicz-Sygua, D., Kurzynoga, D., Stadnik, D., Surmacz-Chwedoruk, W., Komiski, W., Kozerski, L.
J. Biomol. NMR (2013), 55, 303-309, PubMed 23404086 , DOI 10.1007/s10858-013-9713-2 , Abstract

Related entities 1. Biosynthetic engineered B28K-B29P human insulin monomer, entity 1, : 1 : 111 : 13 : 7 : 90 entities Detail

Related entities 2. Biosynthetic engineered B28K-B29P human insulin monomer, entity 2, : 1 : 5 : 126 : 87 entities Detail

Interaction partners 1. Biosynthetic engineered B28K-B29P human insulin monomer, entity 1, : 1 : 1 interactors Detail

More details for 2 interactors identified by 2 citations

Interaction partners 2. Biosynthetic engineered B28K-B29P human insulin monomer, entity 2, : 6 : 1 interactors Detail

More details for 7 interactors identified by 7 citations

Experiments performed 4 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_18859_2m1e.nef
Input source #2: Coordindates	2m1e.cif
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)
A:6:CYS:SG	A:11:CYS:SG	unknown	unknown	2.029
A:7:CYS:SG	B:7:CYS:SG	unknown	unknown	2.039
A:20:CYS:SG	B:19:CYS:SG	unknown	unknown	2.038

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

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20-
GIVEQCCTSICSLYQLENYCN
|||||||||||||||||||||
GIVEQCCTSICSLYQLENYCN

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

--------10--------20--------30
FVNQHLCGSHLVEALYLVCGERGFFYTKPT
||||||||||||||||||||||||||||||
FVNQHLCGSHLVEALYLVCGERGFFYTKPT

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	21	0	0	100.0
B	B	30	0	0	100.0

Content subtype: combined_18859_2m1e.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	3		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	267		95.2 (chain: A, length: 21), 96.7 (chain: B, length: 30)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1047 (1)	noe	95.2 (chain: A, length: 21), 96.7 (chain: B, length: 30)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	456 (456)	.	100.0 (chain: A, length: 21), 100.0 (chain: B, length: 30)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 95.2%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 96.7%
- Total number of assignments
  - ¹H chemical shifts: 267
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A
  - Chain_ID: B

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	120	107	89.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	40	93.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	67	87.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	11	100.0

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	182	160	87.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	62	57	91.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	120	103	85.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	17	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	27	21	77.8

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 95.2%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 96.7%
- Total number of restraints: 1047
- Weight of restraints: 1.0 (1047)
- Potential type of restraints: square-well-parabolic (1047)
- Range of distance target values: 2.52, 5.85 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 100.0%
- Total number of restraints: 456
- Total number of restraints per polymer type: 456
- Weight of restraints: 1.0 (456)
- Potential type of restraints: square-well-parabolic (456)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords Hormone, Human Insulin, mutant, water solution

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Found 1 Document (0.947 seconds)

BMRB: 18859

Sample #1

Sample #2

Related entities 1. Biosynthetic engineered B28K-B29P human insulin monomer, entity 1, : 1 : 111 : 13 : 7 : 90 entities Detail

Related entities 2. Biosynthetic engineered B28K-B29P human insulin monomer, entity 2, : 1 : 5 : 126 : 87 entities Detail

Interaction partners 1. Biosynthetic engineered B28K-B29P human insulin monomer, entity 1, : 1 : 1 interactors Detail

Interaction partners 2. Biosynthetic engineered B28K-B29P human insulin monomer, entity 2, : 6 : 1 interactors Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail