BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25868

Title: Solution NMR Structure of Designed Protein DA05R1, Northeast Structural Genomics Consortium (NESG) Target OR690

Authors: Eletsky, Alexander; Federizon, Jasmin; Xu, Xianzhong; Pulavarti, S.V.S.R. Krishna; Jacobs, Tim; Kuhlman, Brian; Szyperski, Thomas

Citation: Jacobs, Tim; Xu, Xianzhong; Eletsky, Alexander; Federizon, Jasmin; Szyperski, Thomas; Kuhlman, Brian. "Design of Structurally Unique Proteins Using Strategies Inspired by Evolution"  Not known ., .-..

Assembly members:
DA05R1, polymer, 208 residues, 23847.180 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
DA05R1: ADENIAKFEKAYKKAEELNQ GELMGRALYNIGLEKNKMGK AREAAEYFFRAAIVFYKEHD TDGLRRAAKSLKEAITAIPE EEGRKEAKEMAKKAEEWLQA EQNNADENIAKFEKAYKKAE ELNQGELMGRALYNIGLEKN KMGKAREAAEYFFRAAIVFY KEHDTDGLRRAAKSLKEAIT AIPEEEGRKEAKEMAKKAEE WLQAEQNN

Data sets:
Data typeCount
13C chemical shifts425
15N chemical shifts94
1H chemical shifts689

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DA05R11

Entities:

Entity 1, DA05R1 208 residues - 23847.180 Da.

1   ALAASPGLUASNILEALALYSPHEGLULYS
2   ALATYRLYSLYSALAGLUGLULEUASNGLN
3   GLYGLULEUMETGLYARGALALEUTYRASN
4   ILEGLYLEUGLULYSASNLYSMETGLYLYS
5   ALAARGGLUALAALAGLUTYRPHEPHEARG
6   ALAALAILEVALPHETYRLYSGLUHISASP
7   THRASPGLYLEUARGARGALAALALYSSER
8   LEULYSGLUALAILETHRALAILEPROGLU
9   GLUGLUGLYARGLYSGLUALALYSGLUMET
10   ALALYSLYSALAGLUGLUTRPLEUGLNALA
11   GLUGLNASNASNALAASPGLUASNILEALA
12   LYSPHEGLULYSALATYRLYSLYSALAGLU
13   GLULEUASNGLNGLYGLULEUMETGLYARG
14   ALALEUTYRASNILEGLYLEUGLULYSASN
15   LYSMETGLYLYSALAARGGLUALAALAGLU
16   TYRPHEPHEARGALAALAILEVALPHETYR
17   LYSGLUHISASPTHRASPGLYLEUARGARG
18   ALAALALYSSERLEULYSGLUALAILETHR
19   ALAILEPROGLUGLUGLUGLYARGLYSGLU
20   ALALYSGLUMETALALYSLYSALAGLUGLU
21   TRPLEUGLNALAGLUGLNASNASN

Samples:

NC5: DA05R1, [U-5% 13C; U-15N], 660 uM; sodium phosphate 25 mM; sodium chloride 50 mM; sodium azide 0.02%; protein inhibitor cocktail 1 mM; DSS 50 uM

NC: DA05R1, [U-13C; U-15N], 1 mM; sodium phosphate 25 mM; sodium chloride 50 mM; sodium azide 0.02%; protein inhibitor cocktail 1 mM; DSS 50 uM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D CT 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
2D CT 1H-13C HSQC aromaticNCisotropicsample_conditions_1
3D 15N/13C-edited 1H-1H NOESYNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aliphaticNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aromaticNCisotropicsample_conditions_1
3D (H)CCH-TOCSYNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
2D CT 1H-13C HSQC aliphatic 28 msNC5isotropicsample_conditions_1
3D 1H-15N TOCSYNC5isotropicsample_conditions_1
3D 1H-15N NOESYNC5isotropicsample_conditions_1

Software:

PROSA v6.4, Guntert - processing

AS-DP v1.0, Huang, Tejero, Powers and Montelione - structure solution

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

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

XEASY v1.3.13, Bartels et al. - data analysis

VNMRJ v4.0, Varian - collection

TALOS-N, Cornilescu, Delaglio and Bax - geometry optimization

PSVS v1.5, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

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