BMRB Entry 18728

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18728
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
SOLUTION STRUCTURE
Deposition date:
2012-09-19
Original release date:
2013-01-03
Authors:
Barraud, Pierre; Allain, Frederic
Citation:

Citation: Barraud, Pierre; Allain, Frederic H-T. "Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology."  J. Biomol. NMR 55, 119-138 (2013).
PubMed: 23247503

Assembly members:

Assembly members:
UP1, polymer, 197 residues, 22229.115 Da.

Natural source:

Natural source:   Common Name: Humans   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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UP1: GGSKSESPKEPEQLRKLFIG GLSFETTDESLRSHFEQWGT LTDCVVMRDPNTKRSRGFGF VTYATVEEVDAAMNARPHKV DGRVVEPKRAVSREDSQRPG AHLTVKKIFVGGIKEDTEEH HLRDYFEQYGKIEVIEIMTD RGSGKKRGFAFVTFDDHDSV DKIVIQKYHTVNGHNCEVRK ALSKQEMASASSSQRGR

Data sets:
Data typeCount
13C chemical shifts801
15N chemical shifts198
1H chemical shifts1267

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UP11

Entities:

Entity 1, UP1 197 residues - 22229.115 Da.

1   GLYGLYSERLYSSERGLUSERPROLYSGLU
2   PROGLUGLNLEUARGLYSLEUPHEILEGLY
3   GLYLEUSERPHEGLUTHRTHRASPGLUSER
4   LEUARGSERHISPHEGLUGLNTRPGLYTHR
5   LEUTHRASPCYSVALVALMETARGASPPRO
6   ASNTHRLYSARGSERARGGLYPHEGLYPHE
7   VALTHRTYRALATHRVALGLUGLUVALASP
8   ALAALAMETASNALAARGPROHISLYSVAL
9   ASPGLYARGVALVALGLUPROLYSARGALA
10   VALSERARGGLUASPSERGLNARGPROGLY
11   ALAHISLEUTHRVALLYSLYSILEPHEVAL
12   GLYGLYILELYSGLUASPTHRGLUGLUHIS
13   HISLEUARGASPTYRPHEGLUGLNTYRGLY
14   LYSILEGLUVALILEGLUILEMETTHRASP
15   ARGGLYSERGLYLYSLYSARGGLYPHEALA
16   PHEVALTHRPHEASPASPHISASPSERVAL
17   ASPLYSILEVALILEGLNLYSTYRHISTHR
18   VALASNGLYHISASNCYSGLUVALARGLYS
19   ALALEUSERLYSGLNGLUMETALASERALA
20   SERSERSERGLNARGGLYARG

Samples:

segmental-labelled: UP1, RRM1[U-13C, U-15N]-RRM2[natural abundance], 1.0 mM; sodium phosphate 10 mM; DTT 1 mM; D2O 100%

15n_h2o: UP1, [U-15N], 0.8 – 1.2 mM; sodium phosphate 10 mM; DTT 1 mM; D2O 10%; H2O 90%

15n_d2o: UP1, [U-15N], 0.8 – 1.2 mM; sodium phosphate 10 mM; DTT 1 mM; D2O 100%

13c15n_h2o: UP1, [U-13C; U-15N], 0.8 – 1.2 mM; sodium phosphate 10 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 10 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 10 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15n_h2oisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic13c15n_h2oisotropicsample_conditions_1
2D 1H-13C HSQC aromatic13c15n_h2oisotropicsample_conditions_1
3D HNCA13c15n_h2oisotropicsample_conditions_1
3D HNCACB13c15n_h2oisotropicsample_conditions_1
3D CBCA(CO)NH13c15n_h2oisotropicsample_conditions_1
3D HNCO13c15n_h2oisotropicsample_conditions_1
3D HN(CA)CO13c15n_h2oisotropicsample_conditions_1
3D H(CCO)NH13c15n_h2oisotropicsample_conditions_1
3D C(CO)NH13c15n_h2oisotropicsample_conditions_1
3D 1H-15N NOESY15n_h2oisotropicsample_conditions_1
3D 1H-13C NOESY aromatic13c15n_h2oisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic13c15n_h2oisotropicsample_conditions_1
2D 1H-1H NOESY15n_d2oisotropicsample_conditions_1
2D 1H-1H TOCSY15n_d2oisotropicsample_conditions_1
2D 1H-15N IPAP HSQC15n_h2oanisotropicsample_conditions_2
2D long-range 1H-15N HSQC15n_h2oisotropicsample_conditions_1
3D 13C F1-edited F3-filtered NOESY-HSQCsegmental-labelledisotropicsample_conditions_1
2D 1H-15N IPAP HSQC15n_h2oisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

CYANA v3.0, Guntert - structure solution

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TALOS vtalos+, Cornilescu, Delaglio and Bax - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

UNP P09651
PDB
DBJ BAA13161 BAA13162 BAB25267 BAC40273 BAE00617
EMBL CAA29922 CAA31191 CAA56072 CAG31480 CAH18571
GB AAA37633 AAA41314 AAB01436 AAH02355 AAH09600
PIR DDRT S04617
REF NP_001011724 NP_001011725 NP_001034218 NP_001036248 NP_001039376
SP A5A6H4 P04256 P09651 P09867 P49312
TPG DAA30020
AlphaFold Q6PJZ7 A5A6H4 P04256 P09651 P09867 P49312

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