BMRB Entry 16646

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16646
MolProbity Validation Chart

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Title:
Solution structure of the RBD1,2 domains from human nucleolin
Deposition date:
2009-12-22
Original release date:
2010-05-13
Authors:
Arumugam, Sengodagounder; Miller, Clarke; Maliekal, James; Bates, Paula; Trent, John; Lane, Andrew
Citation:

Citation: Arumugam, Sengodagounder; Miller, M. Clarke; Maliekal, James; Bates, Paula; Trent, John; Lane, Andrew. "Solution structure of the RBD1,2 domains from human nucleolin."  J. Biomol. NMR 47, 79-83 (2010).
PubMed: 20376532

Assembly members:

Assembly members:
RBD1,2, polymer, 180 residues, 20175.620 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: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RBD1,2: GTEPTTAFNLFVGNLNFNKS APELKTGISDVFAKNDLAVV DVRIGMTRKFGYVDFESAED LEKALELTGLKVFGNEIKLE KPKGKDSKKERDARTLLAKN LPYKVTQDELKEVFEDAAEI RLVSKDGKSKGIAYIEFKTE ADAEKTFEEKQGTEIDGRSI SLYYTGEPKGEGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts725
15N chemical shifts180
1H chemical shifts1091

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 180 residues - 20175.620 Da.

1   GLYTHRGLUPROTHRTHRALAPHEASNLEU
2   PHEVALGLYASNLEUASNPHEASNLYSSER
3   ALAPROGLULEULYSTHRGLYILESERASP
4   VALPHEALALYSASNASPLEUALAVALVAL
5   ASPVALARGILEGLYMETTHRARGLYSPHE
6   GLYTYRVALASPPHEGLUSERALAGLUASP
7   LEUGLULYSALALEUGLULEUTHRGLYLEU
8   LYSVALPHEGLYASNGLUILELYSLEUGLU
9   LYSPROLYSGLYLYSASPSERLYSLYSGLU
10   ARGASPALAARGTHRLEULEUALALYSASN
11   LEUPROTYRLYSVALTHRGLNASPGLULEU
12   LYSGLUVALPHEGLUASPALAALAGLUILE
13   ARGLEUVALSERLYSASPGLYLYSSERLYS
14   GLYILEALATYRILEGLUPHELYSTHRGLU
15   ALAASPALAGLULYSTHRPHEGLUGLULYS
16   GLNGLYTHRGLUILEASPGLYARGSERILE
17   SERLEUTYRTYRTHRGLYGLUPROLYSGLY
18   GLUGLYLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: RBD1,2, [U-13C; U-15N], 1.0 mM; potassium chloride 100 mM; sodium acetate, [U-2H], 20 mM; sodium azide 3 mM; H2O 90%; D2O 10%

sample_2: RBD1,2, [U-15N], 1.0 mM; potassium chloride 100 mM; sodium acetate, [U-2H], 20 mM; sodium azide 3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 123 mM; pH: 5.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement

VNMR v6.1C, Varian - collection

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

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

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