BMRB Entry 15956

Title:
NMR structure analysis of a BMP receptor
Deposition date:
2008-09-17
Original release date:
2009-02-10
Authors:
Klages, Jochen; Kotzsch, Alexander; Mueller, Thomas; Kessler, Horst
Citation:

Citation: Klages, Jochen; Kotzsch, Alexander; Coles, Murray; Nickel, Joachim; Mueller, Thomas; Kessler, Horst. "The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding"  Biochemistry 47, 11930-11939 (2008).
PubMed: 18937504

Assembly members:

Assembly members:
Bone_Morphogenetic_Protein_Receptor_Type_IA, polymer, 102 residues, 11278.752 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts379
15N chemical shifts101
1H chemical shifts626

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Bone Morphogenetic Protein Receptor Type IA1

Entities:

Entity 1, Bone Morphogenetic Protein Receptor Type IA 102 residues - 11278.752 Da.

27 N-terminal amino acids were truncated to facilitate structure analysis.

1   GLYPROGLUASPTHRLEUPROPHELEULYS
2   CYSTYRCYSSERGLYHISCYSPROASPASP
3   ALAILEASNASNTHRCYSILETHRASNGLY
4   HISCYSPHEALAILEILEGLUGLUASPASP
5   GLNGLYGLUTHRTHRLEUALASERGLYCYS
6   METLYSTYRGLUGLYSERASPPHEGLNCYS
7   LYSASPSERPROLYSALAGLNLEUARGARG
8   THRILEGLUCYSCYSARGTHRASNLEUCYS
9   ASNGLNTYRLEUGLNPROTHRLEUPROPRO
10   VALVALILEGLYPROPHEPHEASPGLYSER
11   ILEARG

Samples:

sample_1: Bone Morphogenetic Protein Receptor Type IA, [U-99% 15N], 1.1 mM; H2O 95%; D2O 5%; potassium phosphate 10 mM; sodium azide 0.2 w/v

sample_2: Bone Morphogenetic Protein Receptor Type IA, [U-94% 13C; U-98% 15N], 0.5 mM; H2O 95%; D2O 5%; potassium phosphate 10 mM; sodium azide 0.2 w/v

sample_conditions_1: pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N-13C NIOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)HAsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.4a, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TOPSPIN v1.3, Bruker Biospin - collection, processing

SPARKY, Goddard - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

ProcheckNMR, Laskowski and MacArthur - geometry optimization

AQUA, Rullmann, Doreleijers and Kaptein - geometry optimization

WhatIF, Vriend - geometry optimization

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker DMX 750 MHz
  • Bruker DMX 600 MHz
  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAA03769 BAA04549 BAA07275 BAE20961 BAF84453
EMBL CAA70474 CAA80257 CAA80678
GB AAA21514 AAA21515 AAB33865 AAH28383 AAH42611
REF NP_001070268 NP_001138622 NP_001191696 NP_001247522 NP_001267643
SP P36894 P36895 Q78EA7
TPG DAA14159
AlphaFold P36894 P36895 Q78EA7

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks