BMRB Entry 34155

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34155
MolProbity Validation Chart

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Title:
NMR solution structure of U11/U12 65K protein's C-terminal RRM domain (381-516)
Deposition date:
2017-06-28
Original release date:
2018-01-23
Authors:
Norppa, A.; Kauppala, T.; Heikkinen, H.; Verma, B.; Iwai, H.; Frilander, M.
Citation:

Citation: Norppa, A.; Kauppala, T.; Heikkinen, H.; Verma, B.; Iwai, H.; Frilander, M.. "Mutations in the U11/U12-65K protein associated with isolated growth hormone deficiency lead to structural destabilization and impaired binding of U12 snRNA."  RNA 24, 396-409 (2018).
PubMed: 29255062

Assembly members:

Assembly members:
entity_1, polymer, 136 residues, 15796.292 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SDEMPSECISRRELEKGRIS REEMETLSVFRSYEPGEPNC RIYVKNLAKHVQEKDLKYIF GRYVDFSSETQRIMFDIRLM KEGRMKGQAFIGLPNEKAAA KALKEANGYVLFGKPMVVQF ARSARPKQDPKEGKRK

Data sets:
Data typeCount
13C chemical shifts607
15N chemical shifts139
1H chemical shifts968

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 136 residues - 15796.292 Da.

1   SERASPGLUMETPROSERGLUCYSILESER
2   ARGARGGLULEUGLULYSGLYARGILESER
3   ARGGLUGLUMETGLUTHRLEUSERVALPHE
4   ARGSERTYRGLUPROGLYGLUPROASNCYS
5   ARGILETYRVALLYSASNLEUALALYSHIS
6   VALGLNGLULYSASPLEULYSTYRILEPHE
7   GLYARGTYRVALASPPHESERSERGLUTHR
8   GLNARGILEMETPHEASPILEARGLEUMET
9   LYSGLUGLYARGMETLYSGLYGLNALAPHE
10   ILEGLYLEUPROASNGLULYSALAALAALA
11   LYSALALEULYSGLUALAASNGLYTYRVAL
12   LEUPHEGLYLYSPROMETVALVALGLNPHE
13   ALAARGSERALAARGPROLYSGLNASPPRO
14   LYSGLUGLYLYSARGLYS

Samples:

sample_1: U11/U12 65K C-terminal RRM, [U-100% 13C; U-100% 15N], 0.2 mM

sample_conditions_1: ionic strength: 20.0 mM; pH: 6.0; pressure: 1 atm; temperature: 303.3 K

sample_conditions_2: ionic strength: 20.0 mM; pH: 6.0; pressure: 1 atm; temperature: 298.3 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_2
3D HN(COCA)CBsample_1isotropicsample_conditions_2
HNCOsample_1isotropicsample_conditions_1
HN(CA)COsample_1isotropicsample_conditions_2
CONsample_1isotropicsample_conditions_2
CACOsample_1isotropicsample_conditions_2
(H)CCCONHsample_1isotropicsample_conditions_1
H(CCO)NHsample_1isotropicsample_conditions_1
HBHACONHsample_1isotropicsample_conditions_1
HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
CBCGCDHDsample_1isotropicsample_conditions_1
CBCGCDCEHEsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

AMBER v14.0, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CcpNMR v2.4.1, CCPN - chemical shift assignment

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

TALOS vN, Cornilescu, Delaglio and Bax - structure calculation

PSVS v1.5, Bhattacharya and Montelione - data analysis

TOPSPIN v3.2, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 850 MHz

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