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 17705

Title: na1   PubMed: 22002536

Deposition date: 2011-06-15 Original release date: 2011-10-26

Authors: Daubner, Gerrit

Citation: Daubner, Gerrit; Clery, Antoine; Jayne, Sandrine; Stevenin, James; Allain, Frederic H-T. "A syn-anti conformational difference allows SRSF2 to recognize guanines and cytosines equally well."  EMBO J. 31, 162-174 (2012).

Assembly members:
SRSF2_RRM, polymer, 135 residues, 11705.210 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):
SRSF2_RRM: MGSSHHHHHHSSGLVPRGSH MASMTGGQQMGRGSMSYGRP PPDVEGMTSLKVDNLTYRTS PDTLRRVFEKYGRVGDVYIP RDRYTKESRGFAFVRFHDKR DAEDAMDAMDGAVLDGRELR VQMARYGRPPDSHHS

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts96
1H chemical shifts642

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SRSF2_RRM1

Entities:

Entity 1, SRSF2_RRM 135 residues - 11705.210 Da.

Residues 1-34 present the HIS and T7 Tag; Residues 35-131 the RRM domain.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALASERMETTHRGLYGLYGLNGLNMET
4   GLYARGGLYSERMETSERTYRGLYARGPRO
5   PROPROASPVALGLUGLYMETTHRSERLEU
6   LYSVALASPASNLEUTHRTYRARGTHRSER
7   PROASPTHRLEUARGARGVALPHEGLULYS
8   TYRGLYARGVALGLYASPVALTYRILEPRO
9   ARGASPARGTYRTHRLYSGLUSERARGGLY
10   PHEALAPHEVALARGPHEHISASPLYSARG
11   ASPALAGLUASPALAMETASPALAMETASP
12   GLYALAVALLEUASPGLYARGGLULEUARG
13   VALGLNMETALAARGTYRGLYARGPROPRO
14   ASPSERHISHISSER

Samples:

SRSF2_RRM_sample_1: SRSF2 RRM 1, [U-15N], 0.75 ± 0.1 mM; SRSF2 RRM 2, [U-13C; U-15N], 0.75 ± 0.1 mM; L-Arg 50 mM; L-Glu 50 mM; NaH2PO4 20 mM; H2O 90%; D2O 10%

SRSF2_RRM_D2O: SRSF2 RRM 1, [U-15N], 0.75 ± 0.1 mM; L-Arg 50 mM; L-Glu 50 mM; NaH2PO4 20 mM; D2O 100%

SRSF2_RRM_sample_conditions: ionic strength: 120 mM; pH: 5.5; pressure: 1 atm; temperature: 310.8 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
2D 1H-13C HSQCSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
2D 1H-1H TOCSYSRSF2_RRM_D2OisotropicSRSF2_RRM_sample_conditions
3D HCACOSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
3D HNCOSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
3D HNCASRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
3D HN(CO)CASRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
3D CBCA(CO)NHSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
3D HNCACBSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
3D H(CCO)NHSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
3D HCCH-TOCSYSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
3D 1H-13C NOESYSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
3D 1H-15N NOESYSRSF2_RRM_sample_1isotropicSRSF2_RRM_sample_conditions
2D 1H-1H NOESYSRSF2_RRM_D2OisotropicSRSF2_RRM_sample_conditions

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 16444 17706 17707
PDB
DBJ BAC03903 BAC04206 BAC36346 BAC39610 BAC40111
EMBL CAA44306 CAA44307 CAA53383 CAA67134 CAJ82901
GB AAA60306 AAC71000 AAH00339 AAH01303 AAH05493
PIR A42701
PRF 1805195A 1805195B
REF NP_001001305 NP_001009720 NP_001029290 NP_001029490 NP_001070697
SP P30352 Q01130 Q06A98 Q3MHR5 Q5R1W5
TPG DAA18198

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