BMRB Entry 25139
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25139
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Title: The solution structure of the MANEC-type domain from Hepatocyte Growth Factor Inhibitor 1 reveals an unexpected PAN/apple domain-type fold PubMed: 25510835
Deposition date: 2014-08-09 Original release date: 2015-09-02
Authors: Hong, Zebin; Nowakowski, Michal; Spronk, Chris; Petersen, Steen; Petersen, Jan; Kozminski, Wiktor; Mulder, Frans; Jensen, Jan
Citation: Hong, Zebin; Nowakowski, Michal; Spronk, Chris; Petersen, Steen; Petersen, Jan; Kozminski, Wiktor; Mulder, Frans; Jensen, Jan. "The solution structure of the MANEC-type domain from Hepatocyte Growth Factor Activator Inhibitor 1 reveals an unexpected PAN/apple domain-type fold" Biochem. J. 466, 299-309 (2015).
Assembly members:
entity_1, polymer, 114 residues, 12837.496 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Pichia pastoris
Entity Sequences (FASTA):
entity_1: GADCLNSFTAGVPGFVLDTQ
ASVSNGATFLESPTVRRGWD
CVRACCTTQNCNLALVELQP
DRGEDAIAACFLINCLYEQN
FVCKFAPREGFINYLTREVY
RSYRQLVDHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 713 |
| 15N chemical shifts | 205 |
| 1H chemical shifts | 1215 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 114 residues - 12837.496 Da.
| 1 | GLY | ALA | ASP | CYS | LEU | ASN | SER | PHE | THR | ALA | ||||
| 2 | GLY | VAL | PRO | GLY | PHE | VAL | LEU | ASP | THR | GLN | ||||
| 3 | ALA | SER | VAL | SER | ASN | GLY | ALA | THR | PHE | LEU | ||||
| 4 | GLU | SER | PRO | THR | VAL | ARG | ARG | GLY | TRP | ASP | ||||
| 5 | CYS | VAL | ARG | ALA | CYS | CYS | THR | THR | GLN | ASN | ||||
| 6 | CYS | ASN | LEU | ALA | LEU | VAL | GLU | LEU | GLN | PRO | ||||
| 7 | ASP | ARG | GLY | GLU | ASP | ALA | ILE | ALA | ALA | CYS | ||||
| 8 | PHE | LEU | ILE | ASN | CYS | LEU | TYR | GLU | GLN | ASN | ||||
| 9 | PHE | VAL | CYS | LYS | PHE | ALA | PRO | ARG | GLU | GLY | ||||
| 10 | PHE | ILE | ASN | TYR | LEU | THR | ARG | GLU | VAL | TYR | ||||
| 11 | ARG | SER | TYR | ARG | GLN | LEU | VAL | ASP | HIS | HIS | ||||
| 12 | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity_1, [U-99% 13C; U-99% 15N], 1 mM; H2O 93%; D2O 7%; NaH2PO4 pH 6.5 20 mM; NaCl 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K
sample_conditions_2: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 4D HabCab(CO)NH | sample_1 | isotropic | sample_conditions_2 |
| 4D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_2 |
| 2D (HB)CB(CGCD)HD | sample_1 | isotropic | sample_conditions_2 |
| 2D (HB)CB(CGCDCE)HE | sample_1 | isotropic | sample_conditions_2 |
| 3D HBCB(CGCD)HD | sample_1 | isotropic | sample_conditions_2 |
| 3D HBCB(CGCDCE)HE | sample_1 | isotropic | sample_conditions_2 |
| 3D 13C-edited NOESY HSQC | sample_1 | isotropic | sample_conditions_2 |
| 4D 13Cali,13Caro-edited HMQC-NOESY-HSQC | sample_1 | isotropic | sample_conditions_2 |
| 4D 13Cali,13Cali-edited HMQC-NOESY-HMQC | sample_1 | isotropic | sample_conditions_2 |
| 4D 15N,13C edited HMQC-NOESY-HSQC | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
SPARKY, Goddard - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
YASARA2, YASARA2-Krieger - refinement
SSA_software_package, Stanek, Kosinski, Kozminski - processing
NMR spectrometers:
- Bruker Plus 500 MHz
- Agilent DDR2 600 MHz
- Agilent DDR2 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA25014 BAG37346 BAG61968 |
| GB | AAH04140 AAH18702 AAP36093 AAP44001 AAP88884 |
| REF | NP_001027539 NP_003701 NP_857593 XP_003266791 XP_003314674 |
| SP | O43278 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts