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 17628

Title: NMR Structure of Alk1 extracellular domain   PubMed: 22799562

Deposition date: 2011-05-06 Original release date: 2012-08-30

Authors: Ilangovan, Udayar

Citation: Mahlawat, Pardeep; Ilangovan, Udayar; Biswas, Tanuka; Sun, Lu-Zhe; Hinck, Andrew. "Structure of the Alk1 extracellular domain and characterization of its bone morphogenetic protein (BMP) binding properties."  Biochemistry 51, 6328-6341 (2012).

Assembly members:
Alk1, polymer, 97 residues, 11148.615 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: Escherichia coli

Entity Sequences (FASTA):
Alk1: DPVKPSRGPLVTCTCESPHC KGPTCRGAWCTVVLVREEGR HPQEHRGCGNLHRELCRGRP TEFVNHYCCDSHLCNHNVSL VLEATQPPSEQPGTDGQ

Data sets:
Data typeCount
13C chemical shifts361
15N chemical shifts84
1H chemical shifts480

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Alk11

Entities:

Entity 1, Alk1 97 residues - 11148.615 Da.

1   ASPPROVALLYSPROSERARGGLYPROLEU
2   VALTHRCYSTHRCYSGLUSERPROHISCYS
3   LYSGLYPROTHRCYSARGGLYALATRPCYS
4   THRVALVALLEUVALARGGLUGLUGLYARG
5   HISPROGLNGLUHISARGGLYCYSGLYASN
6   LEUHISARGGLULEUCYSARGGLYARGPRO
7   THRGLUPHEVALASNHISTYRCYSCYSASP
8   SERHISLEUCYSASNHISASNVALSERLEU
9   VALLEUGLUALATHRGLNPROPROSERGLU
10   GLNPROGLYTHRASPGLYGLN

Samples:

sample_1: Alk1, [U-100% 15N], 0.5 mM; sodium phosphate 25 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_2: Alk1, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 25 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_3: Alk1, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 25 mM; sodium azide 0.02%; Pf1 phage 5mg/mL mg; H2O 95%; D2O 5%

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 15N-HSQC IPAPsample_3anisotropicsample_conditions_1

Software:

ARIA, Linge, O, . - structure solution

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ModelFree, Palmer - realaxation

Molmol, Koradi, Billeter and Wuthrich - Structure Visualization

PECAN, Eghbalnia, Wang, Bahrami, Assadi, and Markley - chemical shift index calculation

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectral Visualization

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data processing

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - dihedral angle determination

TOPSPIN, Bruker Biospin - data collection

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
EMBL CAA80255 CAH91180
GB AAA16160 AAB61900 AAH42637 AAQ02577 ADJ79922
REF NP_000011 NP_001070869 NP_001125692 XP_001145609 XP_003831124
SP P37023 Q5RAN0

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts