BMRB Entry 18017

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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/BMR18017
MolProbity Validation Chart

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Title:
The solution structure of RRM
Deposition date:
2011-10-23
Original release date:
2012-08-06
Authors:
Song, Zhenwei; Wu, Peiwen; Zhang, Jiahai; Wu, Jihui; Shi, Yunyu
Citation:

Citation: Song, Zhenwei; Wu, Peiwen; Ji, Peng; Zhang, Jiahai; Gong, Qingguo; Wu, Jihui; Shi, Yunyu. "Solution structure of the second RRM domain of RBM5 and its unusual binding characters for different RNA targets."  Biochemistry 51, 6667-6678 (2012).
PubMed: 22839758

Assembly members:

Assembly members:
entity, polymer, 95 residues, 10518.233 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: pET28a modified

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MGHHHHHHMDTIILRNIAPH TVVDSIMTALSPYASLAVNN IRLIKDKQTQQNRGFAFVQL SSAMDASQLLQILQSLHPPL KIDGKTIGVDFAKSA

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts94
1H chemical shifts642

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM1

Entities:

Entity 1, RRM 95 residues - 10518.233 Da.

1   METGLYHISHISHISHISHISHISMETASP
2   THRILEILELEUARGASNILEALAPROHIS
3   THRVALVALASPSERILEMETTHRALALEU
4   SERPROTYRALASERLEUALAVALASNASN
5   ILEARGLEUILELYSASPLYSGLNTHRGLN
6   GLNASNARGGLYPHEALAPHEVALGLNLEU
7   SERSERALAMETASPALASERGLNLEULEU
8   GLNILELEUGLNSERLEUHISPROPROLEU
9   LYSILEASPGLYLYSTHRILEGLYVALASP
10   PHEALALYSSERALA

Samples:

sample_1: RRM1.2 – 1.4 mM; sodium phosphate 40 mM; sodium chloride 50 mM; EDTA 2 mM; sodium azide 1 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 40 mM; sodium chloride 50 mM; EDTA 2 mM; sodium azide 1 mM; D2O 100%

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

ProcheckNMR, Laskowski and MacArthur - refinement

SPARKY, Goddard - chemical shift assignment, chemical shift calculation, peak picking

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
REF XP_006511938 XP_006511939 XP_006712982 XP_012373044

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