BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18097

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for primate innate immunity protein   PubMed: 22847415

Deposition date: 2011-11-21 Original release date: 2012-08-06

Authors: Biris, Nikolaos; Yang, Yang; Taylor, Alexander; Tomashevski, Andrei; Guo, Miao; Hart, P.; Diaz-Griffero, Felipe; Ivanov, Dmitri

Citation: Biris, Nikolaos; Yang, Yang; Taylor, Alexander; Tomashevski, Andrei; Guo, Miao; Hart, P. John; Diaz-Griffero, Felipe; Ivanov, Dmitri. "Structure of the rhesus monkey TRIM5 PRYSPRY domain, the HIV capsid recognition module."  Proc. Natl. Acad. Sci. U.S.A. 109, 13278-13283 (2012).

Assembly members:
SPRY, polymer, 208 residues, Formula weight is not available

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   Vector: pET 30a

Entity Sequences (FASTA):
SPRY: GTELTDARRYWVDVTLATNN ISHAVIAEDKRQVSSRNPQI MYQAPGTLFTFPSLTNFNYC TGVLGSQSITSGKHYWEVDV SKKSAWILGVCAGFQSDAMY NIEQNENYQPKYGYWVIGLQ EGVKYSVFQDGSSHTPFAPF IVPLSVIICPDRVGVFVDYE ACTVSFFNITNHGFLIYKFS QCSFSKPVFPYLNPRKCTVP MTLCSPSS

Data sets:
Data typeCount
13C chemical shifts326
15N chemical shifts143
1H chemical shifts341

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1rhesus SPRY1

Entities:

Entity 1, rhesus SPRY 208 residues - Formula weight is not available

1   GLYTHRGLULEUTHRASPALAARGARGTYR
2   TRPVALASPVALTHRLEUALATHRASNASN
3   ILESERHISALAVALILEALAGLUASPLYS
4   ARGGLNVALSERSERARGASNPROGLNILE
5   METTYRGLNALAPROGLYTHRLEUPHETHR
6   PHEPROSERLEUTHRASNPHEASNTYRCYS
7   THRGLYVALLEUGLYSERGLNSERILETHR
8   SERGLYLYSHISTYRTRPGLUVALASPVAL
9   SERLYSLYSSERALATRPILELEUGLYVAL
10   CYSALAGLYPHEGLNSERASPALAMETTYR
11   ASNILEGLUGLNASNGLUASNTYRGLNPRO
12   LYSTYRGLYTYRTRPVALILEGLYLEUGLN
13   GLUGLYVALLYSTYRSERVALPHEGLNASP
14   GLYSERSERHISTHRPROPHEALAPROPHE
15   ILEVALPROLEUSERVALILEILECYSPRO
16   ASPARGVALGLYVALPHEVALASPTYRGLU
17   ALACYSTHRVALSERPHEPHEASNILETHR
18   ASNHISGLYPHELEUILETYRLYSPHESER
19   GLNCYSSERPHESERLYSPROVALPHEPRO
20   TYRLEUASNPROARGLYSCYSTHRVALPRO
21   METTHRLEUCYSSERPROSERSER

Samples:

sample_1: SPRY, [U-98% 15N], 250 mM; H2O 93%; D2O 7%

sample_2: SPRY, [U-99% 13C; U-99% 15N], 250 mM; H2O 93%; D2O 7%

sample_3: SPRY, [U-13C; U-15N; U-2H], 250 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(COCA)CBsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAS48505 AAT48102 AAV91976 AAW55814 AAW55816
REF NP_001028082 NP_001106102 NP_001292893 XP_011827364 XP_011900561
SP Q0PF16 Q2YEN2 Q5D7J2

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