BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25139

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

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

Data typeCount
13C chemical shifts713
15N chemical shifts205
1H chemical shifts1215

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 114 residues - 12837.496 Da.

1   GLYALAASPCYSLEUASNSERPHETHRALA
2   GLYVALPROGLYPHEVALLEUASPTHRGLN
3   ALASERVALSERASNGLYALATHRPHELEU
4   GLUSERPROTHRVALARGARGGLYTRPASP
5   CYSVALARGALACYSCYSTHRTHRGLNASN
6   CYSASNLEUALALEUVALGLULEUGLNPRO
7   ASPARGGLYGLUASPALAILEALAALACYS
8   PHELEUILEASNCYSLEUTYRGLUGLNASN
9   PHEVALCYSLYSPHEALAPROARGGLUGLY
10   PHEILEASNTYRLEUTHRARGGLUVALTYR
11   ARGSERTYRARGGLNLEUVALASPHISHIS
12   HISHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
4D HabCab(CO)NHsample_1isotropicsample_conditions_2
4D HCCH-TOCSYsample_1isotropicsample_conditions_2
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_2
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_2
3D HBCB(CGCD)HDsample_1isotropicsample_conditions_2
3D HBCB(CGCDCE)HEsample_1isotropicsample_conditions_2
3D 13C-edited NOESY HSQCsample_1isotropicsample_conditions_2
4D 13Cali,13Caro-edited HMQC-NOESY-HSQCsample_1isotropicsample_conditions_2
4D 13Cali,13Cali-edited HMQC-NOESY-HMQCsample_1isotropicsample_conditions_2
4D 15N,13C edited HMQC-NOESY-HSQCsample_1isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
2D 1H-13C HSQCsample_1isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_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