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Biological Magnetic Resonance Data Bank


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BMRB Entry 17711

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17711
MolProbity Validation Chart

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Title: Solution structure of the core SMN-Gemin2 complex   PubMed: 22607171

Deposition date: 2011-06-15 Original release date: 2012-06-05

Authors: Sarachan, Kathryn; Valentine, Kathleen; Gupta, Kushol; Moorman, Veronica; Gledhill, John; Bernens, Matthew; Tommos, Cecilia; Wand, A.; Van Duyne, Gregory

Citation: Sarachan, Kathryn; Valentine, Kathleen; Gupta, Kushol; Moorman, Veronica; Gledhill Jr, John; Bernens, Matthew; Tommos, Cecilia; Wand, A. Joshua; Van Duyne, Gregory. "Solution structure of the core SMN-Gemin2 complex."  Biochem J. 445, 361-370 (2012).

Assembly members:
gemin2, polymer, 189 residues, 21609.596 Da.
smn, polymer, 26 residues, 2863.100 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):
gemin2: GYSPTLQWQQQQVAQFSTVR QNVNKHRSHWKSQQLDSNVT MPKSEDEEGWKKFCLGEKLC ADGAVGPATNESPGIDYVQI GFPPLLSIVSRMNQATVTSV LEYLSNWFGERDFTPELGRW LYALLACLEKPLLPEAHSLI RQLARRCSEVRLLVDSKDDE RVPALNLLICLVSRYFDQRD LADEPSLEY
smn: GQSDDSDIWDDTALIKAYDK AVASFK

Data sets:
Data typeCount
13C chemical shifts914
15N chemical shifts206
1H chemical shifts1425

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1gemin21
2smn2

Entities:

Entity 1, gemin2 189 residues - 21609.596 Da.

The C-terminal residues Leu-Glu-Tyr are a non-native cloning artifact.

1   GLYTYRSERPROTHRLEUGLNTRPGLNGLN
2   GLNGLNVALALAGLNPHESERTHRVALARG
3   GLNASNVALASNLYSHISARGSERHISTRP
4   LYSSERGLNGLNLEUASPSERASNVALTHR
5   METPROLYSSERGLUASPGLUGLUGLYTRP
6   LYSLYSPHECYSLEUGLYGLULYSLEUCYS
7   ALAASPGLYALAVALGLYPROALATHRASN
8   GLUSERPROGLYILEASPTYRVALGLNILE
9   GLYPHEPROPROLEULEUSERILEVALSER
10   ARGMETASNGLNALATHRVALTHRSERVAL
11   LEUGLUTYRLEUSERASNTRPPHEGLYGLU
12   ARGASPPHETHRPROGLULEUGLYARGTRP
13   LEUTYRALALEULEUALACYSLEUGLULYS
14   PROLEULEUPROGLUALAHISSERLEUILE
15   ARGGLNLEUALAARGARGCYSSERGLUVAL
16   ARGLEULEUVALASPSERLYSASPASPGLU
17   ARGVALPROALALEUASNLEULEUILECYS
18   LEUVALSERARGTYRPHEASPGLNARGASP
19   LEUALAASPGLUPROSERLEUGLUTYR

Entity 2, smn 26 residues - 2863.100 Da.

1   GLYGLNSERASPASPSERASPILETRPASP
2   ASPTHRALALEUILELYSALATYRASPLYS
3   ALAVALALASERPHELYS

Samples:

sample_1: gemin2, [U-99% 13C; U-99% 15N], 1.0 mM; smn, [U-99% 13C; U-99% 15N], 1.0 mM; sodium chloride 50 mM; DTT 50 mM; EDTA 50 uM; sodium azide 200 nM; sodium phosphate 34.25 mM; potassium phosphate 15.75 mM; H2O 95%; D2O 5%

sample_2: gemin2, [U-99% 13C; U-99% 15N], 1.0 mM; smn, [U-99% 13C; U-99% 15N], 1.0 mM; sodium chloride 50 mM; DTT, [U-98% 2H], 50 mM; EDTA 50 uM; sodium azide 200 nM; sodium phosphate 34.25 mM; potassium phosphate 15.75 mM; D2O 100%

sample_3: gemin2, [U-10% 13C; U-99% 15N], 1.0 mM; smn, [U-10% 13C; U-99% 15N], 1.0 mM; sodium chloride 50 mM; DTT 50 mM; EDTA 50 uM; sodium azide 200 nM; sodium phosphate 34.25 mM; potassium phosphate 15.75 mM; H2O 95%; D2O 5%

sample_4: gemin2, [U-98% 15N]-Leu, 1.0 mM; smn 1.0 mM; sodium chloride 50 mM; DTT 50 mM; EDTA 50 uM; sodium azide 200 nM; sodium phosphate 34.25 mM; potassium phosphate 15.75 mM; H2O 95%; D2O 5%

sample_5: gemin2 1.0 mM; smn, [U-99% 15N], 1.0 mM; sodium chloride 50 mM; DTT 50 mM; EDTA 50 uM; sodium azide 200 nM; sodium phosphate 34.25 mM; potassium phosphate 15.75 mM; H2O 95%; D2O 5%

sample_6: gemin2, [U-99% 15N], 1.0 mM; smn, [U-99% 15N], 1.0 mM; sodium chloride 50 mM; DTT 50 mM; EDTA 50 uM; sodium azide 200 nM; sodium phosphate 34.25 mM; potassium phosphate 15.75 mM; bacteriophage Pf1 strain LP11-92 12 mg/ml; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
4D HNCH-NOESY-HSQCsample_1isotropicsample_conditions_1
4D HCCH-NOESY-HMQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_6isotropicsample_conditions_1

Software:

X-PLOR NIH vv2.26, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

FELIX, Accelrys Software Inc. - processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAB03509 BAG36665 BAD51989 BAE02007 BAE26061 BAE39854 BAF82358
EMBL CAC16117 CAA73356 CAB41938 CAH89989 CDQ72355
GB AAB82297 AAI04969 AIC50129 EAW65825 EAW65829 AAA64505 AAA66242 AAB58318 AAB96377 AAC01747
REF NP_001009183 NP_003607 XP_001092707 XP_001145975 XP_002807275 NP_000335 NP_001003226 NP_001009328 NP_001124207 NP_001124942
SP O14893 O02771 O35876 P97801 Q16637 Q4R4F8
PRF 2208336A

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