BMRB Entry 11061

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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/BMR11061
MolProbity Validation Chart

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Title:
Solution structure of the monomeric form of mouse APOBEC2
Deposition date:
2008-12-16
Original release date:
2010-03-11
Authors:
Hayashi, Fumiaki; Nagata, Takashi; Nagashima, Toshio; Muto, Yutaka; Inoue, Makoto; Kigawa, Takanori; Yokoyama, Shigeyuki
Citation:

Citation: Hayashi, Fumiaki; Umehara, Takashi; Kigawa, Takanori; Yokoyama, Shigeyuki. "."  .

Assembly members:

Assembly members:
APOBEC2, polymer, 192 residues, 21856.842 Da.
ZN, non-polymer, 65.380 Da.

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: Escherichia coli   Vector: P021021-43

Entity Sequences (FASTA):

Entity Sequences (FASTA):
APOBEC2: GSSGSSGRLPVNFFKFQFRN VEYSSGRNKTFLCYVVEVQS KGGQAQATQGYLEDEHAGAH AEEAFFNTILPAFDPALKYN VTWYVSSSPCAACADRILKT LSKTKNLRLLILVSRLFMWE EPEVQAALKKLKEAGCKLRI MKPQDFEYIWQNFVEQEEGE SKAFEPWEDIQENFLYYEEK LADILKSGPSSG

Data sets:
Data typeCount
13C chemical shifts837
15N chemical shifts183
1H chemical shifts1357

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TRIS1
2ZINC ION2

Entities:

Entity 1, TRIS 192 residues - 21856.842 Da.

1   GLYSERSERGLYSERSERGLYARGLEUPRO
2   VALASNPHEPHELYSPHEGLNPHEARGASN
3   VALGLUTYRSERSERGLYARGASNLYSTHR
4   PHELEUCYSTYRVALVALGLUVALGLNSER
5   LYSGLYGLYGLNALAGLNALATHRGLNGLY
6   TYRLEUGLUASPGLUHISALAGLYALAHIS
7   ALAGLUGLUALAPHEPHEASNTHRILELEU
8   PROALAPHEASPPROALALEULYSTYRASN
9   VALTHRTRPTYRVALSERSERSERPROCYS
10   ALAALACYSALAASPARGILELEULYSTHR
11   LEUSERLYSTHRLYSASNLEUARGLEULEU
12   ILELEUVALSERARGLEUPHEMETTRPGLU
13   GLUPROGLUVALGLNALAALALEULYSLYS
14   LEULYSGLUALAGLYCYSLYSLEUARGILE
15   METLYSPROGLNASPPHEGLUTYRILETRP
16   GLNASNPHEVALGLUGLNGLUGLUGLYGLU
17   SERLYSALAPHEGLUPROTRPGLUASPILE
18   GLNGLUASNPHELEUTYRTYRGLUGLULYS
19   LEUALAASPILELEULYSSERGLYPROSER
20   SERGLY

Entity 2, ZINC ION - Zn - 65.380 Da.

1   ZN

Samples:

sample_1: APOBEC2, [U-13C; U-15N], 1.25 mM; TRIS, [U-2H], 20 mM; DTT, [U-2H], 1 mM; sodium chloride 100 mM; sodium azide 0.02%; ZnCl2 100 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHAHNsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

VNMR v6.1c, Varian - collection

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

NMRView, Johnson, One Moon Scientific - data analysis

Kujira, Kobayashi, Iwahara, Koshiba, Tomizawa, Tochio, Kigawa, and Yokoyama - data analysis

CYANA v2.1, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
GB AAD45361 AAH27530 AAI68177 EDL23623 EDM18937
REF NP_001100353 NP_033824 XP_003511809 XP_007637965
SP Q9WV35
AlphaFold Q9WV35

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