BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	74.4 % (282 of 379)	97.4 % (186 of 191)	38.6 % (56 of 145)	93.0 % (40 of 43)
Backbone	71.3 % (154 of 216)	98.6 % (73 of 74)	43.4 % (46 of 106)	97.2 % (35 of 36)
Sidechain	76.1 % (150 of 197)	96.6 % (113 of 117)	43.8 % (32 of 73)	71.4 % (5 of 7)
Aromatic	41.7 % (10 of 24)	83.3 % (10 of 12)	0.0 % (0 of 12)
Methyl	66.7 % (28 of 42)	100.0 % (21 of 21)	33.3 % (7 of 21)

1. entity 1

KCNTATCATQ RLANFLVHSS NNFGAILSST NVGSNTX

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 278 K, pH 5.3, Details 150 uM [U-99% 13C; U-99% 15N] Islet Amyloid Polypeptide (IAPP or Amylin), 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Islet Amyloid Polypeptide (IAPP or Amylin)	[U-99% 13C; U-99% 15N]		150 uM

Protein Blocks Logo

Calculated from 20 models in PDB: 5MGQ, Strand ID: A Detail

Release date

2017-03-19

Citation

The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes
Rodriguez Camargo, D.C., Tripsianes, K., Buday, K., Franko, A., Gobl, C., Hartlmuller, C., Sarkar, R., Aichler, M., Mettenleiter, G., Schulz, M., Boddrich, A., Erck, C., Martens, H., Walch, A.K., Madl, T., Wanker, E.E., Conrad, M., de Angelis, M.H., Reif, B.
Sci. Rep. (2017), 7, 44041-44041, PubMed 28287098 , DOI 10.1038/srep44041 , Abstract

Related entities 1. Islet amyloid polypeptide, : 9 : 7 entities Detail

Experiments performed 6 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 278 K, pH 5.3, Details 150 uM [U-99% 13C; U-99% 15N] Islet Amyloid Polypeptide (IAPP or Amylin), 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Islet Amyloid Polypeptide (IAPP or Amylin)	[U-99% 13C; U-99% 15N]		150 uM

2 2D 1H-13C HSQC

Instrument

Bruker Bruker Avance - 500 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Islet Amyloid Polypeptide (IAPP or Amylin)	[U-99% 13C; U-99% 15N]		150 uM

3 3D HNCACB

Instrument

Bruker Bruker Avance - 500 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Islet Amyloid Polypeptide (IAPP or Amylin)	[U-99% 13C; U-99% 15N]		150 uM

4 3D CBCA(CO)NH

Instrument

Bruker Bruker Avance - 500 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Islet Amyloid Polypeptide (IAPP or Amylin)	[U-99% 13C; U-99% 15N]		150 uM

5 3D HCCH-TOCSY

Instrument

Bruker Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Islet Amyloid Polypeptide (IAPP or Amylin)	[U-99% 13C; U-99% 15N]		150 uM

6 3D 1H-15N NOESY

Instrument

Bruker Bruker Avance - 750 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Islet Amyloid Polypeptide (IAPP or Amylin)	[U-99% 13C; U-99% 15N]		150 uM

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_34069_5mgq.nef
Input source #2: Coordindates	5mgq.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	True (see coodinates for details)
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:2:CYS:SG	A:7:CYS:SG	oxidized, CA 55.784, CB 41.505 ppm	oxidized, CA 56.73, CB 41.122 ppm	2.016

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

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:36:THR:C	1:37:TYC:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	37	TYC	L-TYROSINAMIDE	Assigned chemical shifts, Distance restraints, Coordinates

Sequence alignments

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

--------10--------20--------30-------
KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTX
|||||||||||||||||||||||||||||||||||||
KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTX

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	37	0	0	100.0

Content subtype: combined_34069_5mgq.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	294		100.0 (chain: A, length: 37)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	580 (1)	noe	100.0 (chain: A, length: 37)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	20 (20)	.	40.5 (chain: A, length: 37)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 196
  - ¹³C chemical shifts: 56
  - ¹⁵N chemical shifts: 42
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Comp_index_ID	Comp_ID
37	TYC

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	191	186	97.4
¹³C chemical shifts	145	54	37.2
¹⁵N chemical shifts	44	41	93.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	74	73	98.6
¹³C chemical shifts	72	22	30.6
¹⁵N chemical shifts	36	35	97.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	117	113	96.6
¹³C chemical shifts	73	32	43.8
¹⁵N chemical shifts	8	6	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	21	21	100.0
¹³C chemical shifts	21	7	33.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	12	10	83.3
¹³C chemical shifts	12	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 100.0%
- Total number of restraints: 575
- Weight of restraints: 1.0 (575)
- Potential type of restraints: square-well-parabolic (575)
- Range of distance target values: 2.4, 3.9 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 40.5%
- Total number of restraints: 20
- Total number of restraints per polymer type: 20
- Weight of restraints: 1.0 (20)
- Potential type of restraints: square-well-parabolic (20)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue

Keywords Recombinant human IAPP, Type II Diabetes, protein fibril

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 (0.617 seconds)

BMRB: 34069

Sample

Related entities 1. Islet amyloid polypeptide, : 9 : 7 entities Detail

Experiments performed 6 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail