BMRBj - BMREntryMaster

Found 1 Document (1.034 seconds)

BMRB: 25260

2MVC

Solution structure of human insulin at pH 1.9

Authors

Hexnerova, R., Krizkova, K., Maletinska, L., Jiracek, J., Brzozowski, A.M., Zakova, L., Veverka, V.

Assembly

human insulin

Entity

1. human insulin, entity 1 (polymer, Thiol state: all disulfide bound), 21 monomers, 2383.696 Da Detail

GIVEQCCTSI CSLYQLENYC N

2. human insulin, entity 2 (polymer, Thiol state: all disulfide bound), 30 monomers, 3429.919 Da Detail

FVNQHLCGSH LVEALYLVCG ERGFFYTPKT

Total weight

5813.615 Da

Max. entity weight

3429.919 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS6:SG	1:CYS11:SG
2	disulfide	sing	1:CYS7:SG	2:CYS7:SG
3	disulfide	sing	1:CYS20:SG	2:CYS19:SG

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

torsion angle dynamics, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 79.7 %, Completeness (bb): 75.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	79.7 % (471 of 591)	98.0 % (296 of 302)	57.1 % (133 of 233)	75.0 % (42 of 56)
Backbone	75.7 % (230 of 304)	97.1 % (102 of 105)	61.7 % (92 of 149)	72.0 % (36 of 50)
Sidechain	85.3 % (285 of 334)	98.5 % (194 of 197)	64.9 % (85 of 131)	100.0 % (6 of 6)
Aromatic	48.6 % (34 of 70)	97.1 % (34 of 35)	0.0 % (0 of 35)
Methyl	87.5 % (49 of 56)	100.0 % (28 of 28)	75.0 % (21 of 28)

1. entity 1

GIVEQCCTSI CSLYQLENYC N

2. entity 2

FVNQHLCGSH LVEALYLVCG ERGFFYTPKT

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 1.9

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	4 mM
2	entity_2	natural abundance	4 mM
3	acetic acid	[U-99% 2H]	20 %
4	H2O	natural abundance	95 %
5	D2O	[U-99% 2H]	5 %

Protein Blocks Logo

Calculated from 50 models in PDB: 2MVC, Strand ID: A, B Detail

Release date

2016-09-12

Citation

Structural and functional study of the GlnB22-insulin mutant responsible for maturity-onset diabetes of the young
Krizkova, K., Veverka, V., Maletinska, L., Hexnerova, R., Brzozowski, A., Jiracek, J.M., Zakova, L.
PLoS One (2014), 9, e112883-e112883, PubMed 25423173 , DOI 10.1371/journal.pone.0112883 , Abstract

Related entities 1. human insulin, entity 1, : 1 : 111 : 13 : 7 : 90 entities Detail

Related entities 2. human insulin, entity 2, : 1 : 109 : 4 : 18 : 86 entities Detail

Interaction partners 1. human insulin, entity 1, : 1 : 1 interactors Detail

More details for 2 interactors identified by 2 citations

Interaction partners 2. human insulin, 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_25260_2mvc.nef
Input source #2: Coordindates	2mvc.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	2.034
A:7:CYS:SG	B:7:CYS:SG	oxidized, CA 57.236, CB 38.994 ppm	oxidized, CB 47.553 ppm	2.032
A:20:CYS:SG	B:19:CYS:SG	oxidized, CA 53.902, CB 36.186 ppm	oxidized, CA 54.608, CB 36.568 ppm	2.031

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
FVNQHLCGSHLVEALYLVCGERGFFYTPKT
||||||||||||||||||||||||||||||
FVNQHLCGSHLVEALYLVCGERGFFYTPKT

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_25260_2mvc.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	Warning	470		100.0 (chain: A, length: 21), 100.0 (chain: B, length: 30)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1231 (1)	noe	100.0 (chain: A, length: 21), 100.0 (chain: B, length: 30)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	64 (64)	.	85.7 (chain: A, length: 21), 96.7 (chain: B, length: 30)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- 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 assignments
  - ¹H chemical shifts: 299
  - ¹³C chemical shifts: 131
  - ¹⁵N chemical shifts: 40
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Redox state of CYS
- Peptide bond of PRO
- 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: A
  - Chain_ID: B

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	120	116	96.7
¹³C chemical shifts	89	53	59.6
¹⁵N chemical shifts	25	17	68.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	41	95.3
¹³C chemical shifts	42	18	42.9
¹⁵N chemical shifts	21	13	61.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	75	97.4
¹³C chemical shifts	47	35	74.5
¹⁵N chemical shifts	4	4	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	11	100.0
¹³C chemical shifts	11	9	81.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	8	100.0
¹³C chemical shifts	8	0	0.0

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
29	LYS	HZ1	7.508
29	LYS	HZ2	7.508
29	LYS	HZ3	7.508

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	182	180	98.9
¹³C chemical shifts	144	78	54.2
¹⁵N chemical shifts	32	23	71.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	62	61	98.4
¹³C chemical shifts	60	28	46.7
¹⁵N chemical shifts	29	21	72.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	120	119	99.2
¹³C chemical shifts	84	50	59.5
¹⁵N chemical shifts	3	2	66.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	17	100.0
¹³C chemical shifts	17	12	70.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	27	26	96.3
¹³C chemical shifts	27	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- 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: 1231
- Weight of restraints: 1.0 (1231)
- Potential type of restraints: square-well-parabolic (1231)
- Range of distance target values: 1.05, 3.25 (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: 85.7%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 96.7%
- Total number of restraints: 64
- Total number of restraints per polymer type: 64
- Weight of restraints: 1.0 (64)
- Potential type of restraints: square-well-parabolic (64)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords insulin

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (1.034 seconds)

BMRB: 25260

Sample

Related entities 1. human insulin, entity 1, : 1 : 111 : 13 : 7 : 90 entities Detail

Related entities 2. human insulin, entity 2, : 1 : 109 : 4 : 18 : 86 entities Detail

Interaction partners 1. human insulin, entity 1, : 1 : 1 interactors Detail

Interaction partners 2. human insulin, 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