BMRB Entry 25554

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25554
MolProbity Validation Chart

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Title:
NMR solution structure of nucleotide-free Ran GTPase
Deposition date:
2015-03-26
Original release date:
2016-04-18
Authors:
Bacot-Davis, Valjean; Palmenberg, Ann
Citation:

Citation: Bacot-Davis, Valjean; Palmenberg, Ann. "Nuclear Magnetic Resonance Structure of Ran GTPase Determines C-terminal Tail Conformational Dynamics."  J. Biomol. NMR ., .-..

Assembly members:

Assembly members:
entity, polymer, 216 residues, 24456.295 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: pRSET-a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MAAQGEPQVQFKLVLVGDGG TGKTTFVKRHLTGEFEKKYV ATLGVEVHPLVFHTNRGPIK FNVWDTAGQEKFGGLRDGYY IQAQCAIIMFDVTSRVTYKN VPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHR KKNLQYYDISAKSNYNFEKP FLWLARKLIGDPNLEFVAMP ALAPPEVVMDPALAAQYEHD LEVAQTTALPDEDDDL

Data sets:
Data typeCount
13C chemical shifts874
15N chemical shifts294
1H chemical shifts1421

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 216 residues - 24456.295 Da.

1   METALAALAGLNGLYGLUPROGLNVALGLN
2   PHELYSLEUVALLEUVALGLYASPGLYGLY
3   THRGLYLYSTHRTHRPHEVALLYSARGHIS
4   LEUTHRGLYGLUPHEGLULYSLYSTYRVAL
5   ALATHRLEUGLYVALGLUVALHISPROLEU
6   VALPHEHISTHRASNARGGLYPROILELYS
7   PHEASNVALTRPASPTHRALAGLYGLNGLU
8   LYSPHEGLYGLYLEUARGASPGLYTYRTYR
9   ILEGLNALAGLNCYSALAILEILEMETPHE
10   ASPVALTHRSERARGVALTHRTYRLYSASN
11   VALPROASNTRPHISARGASPLEUVALARG
12   VALCYSGLUASNILEPROILEVALLEUCYS
13   GLYASNLYSVALASPILELYSASPARGLYS
14   VALLYSALALYSSERILEVALPHEHISARG
15   LYSLYSASNLEUGLNTYRTYRASPILESER
16   ALALYSSERASNTYRASNPHEGLULYSPRO
17   PHELEUTRPLEUALAARGLYSLEUILEGLY
18   ASPPROASNLEUGLUPHEVALALAMETPRO
19   ALALEUALAPROPROGLUVALVALMETASP
20   PROALALEUALAALAGLNTYRGLUHISASP
21   LEUGLUVALALAGLNTHRTHRALALEUPRO
22   ASPGLUASPASPASPLEU

Samples:

RAN_GTPASE: RAN GTPASE, [U-100% 13C; U-100% 15N], 0.5 mM; D2O, [U-100% 2H], 10%; HEPES 20 mM; DTT 2 mM; sodium azide 0.04%; potassium chloride 100 mM; magnesium chloride 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 102 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCRAN_GTPASEisotropicsample_conditions_1
2D 1H-13C HSQCRAN_GTPASEisotropicsample_conditions_1
3D CBCA(CO)NHRAN_GTPASEisotropicsample_conditions_1
3D HBHA(CO)NHRAN_GTPASEisotropicsample_conditions_1
3D C(CO)NHRAN_GTPASEisotropicsample_conditions_1
3D H(CCO)NHRAN_GTPASEisotropicsample_conditions_1
2D 1H-1H TOCSYRAN_GTPASEisotropicsample_conditions_1
3D 1H-13C NOESYRAN_GTPASEisotropicsample_conditions_1
3D 1H-15N NOESYRAN_GTPASEisotropicsample_conditions_1
3D HNCACBRAN_GTPASEisotropicsample_conditions_1
31P NMRRAN_GTPASEisotropicsample_conditions_1

Software:

CYANA, G??ntert P. - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

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