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 16376

Title: Solution NMR structure of the monomeric W187R mutant of A/Udorn NS1 effector domain. Northeast Structural Genomics target OR8C[W187R].

Authors: Aramini, James; Ma, Li-Chung; Lee, Hsiau-Wei; Zhao, Li; Cunningham, Kellie; Ciccosanti, Colleen; Janjua, Haleema; Fang, Yingyi; Xiao, Rong; Krug, Robert; Montelione, Gaetano

Citation: Aramini, James; Ma, Li-Chung; Lee, Hsiau-Wei; Zhao, Li; Cunningham, Kellie; Ciccosanti, Colleen; Janjua, Haleema; Fang, Yingyi; Xiao, Rong; Krug, Robert; Montelione, Gaetano. "Solution NMR structure of the monomeric W187R mutant of A/Udorn NS1 effector domain. Northeast Structural Genomics target OR8C[W187R]."  Not known ., .-..

Assembly members:
OR8w187r, polymer, 140 residues, 15935.479 Da.

Natural source:   Common Name: Influenzavirus A   Taxonomy ID: 197911   Superkingdom: Viruses   Kingdom: not available   Genus/species: Influenza A not available

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

Entity Sequences (FASTA):
OR8w187r: MPASRYITDMTIEELSRDWF MLMPKQKVEGPLCIRIDQAI MDKNIMLKANFSVIFDRLET LILLRAFTEEGAIVGEISPL PSFPGHTIEDVKNAIGVLIG GLERNDNTVRVSKTLQRFAW GSSNENGRPPLTLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts614
15N chemical shifts139
1H chemical shifts988

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR8w187r1

Entities:

Entity 1, OR8w187r 140 residues - 15935.479 Da.

1   METPROALASERARGTYRILETHRASPMET
2   THRILEGLUGLULEUSERARGASPTRPPHE
3   METLEUMETPROLYSGLNLYSVALGLUGLY
4   PROLEUCYSILEARGILEASPGLNALAILE
5   METASPLYSASNILEMETLEULYSALAASN
6   PHESERVALILEPHEASPARGLEUGLUTHR
7   LEUILELEULEUARGALAPHETHRGLUGLU
8   GLYALAILEVALGLYGLUILESERPROLEU
9   PROSERPHEPROGLYHISTHRILEGLUASP
10   VALLYSASNALAILEGLYVALLEUILEGLY
11   GLYLEUGLUARGASNASPASNTHRVALARG
12   VALSERLYSTHRLEUGLNARGPHEALATRP
13   GLYSERSERASNGLUASNGLYARGPROPRO
14   LEUTHRLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: OR8w187r, [U-100% 13C; U-100% 15N], 0.71 mM; sodium phosphate 20 mM; sodium chloride 100 mM; arginine 50 mM; glutamic acid 50 mM; glycerol 1%; DSS 50 uM

sample_2: OR8w187r, [U-5% 13C; U-100% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 100 mM; arginine 50 mM; glutamic acid 50 mM; glycerol 1%; DSS 50 uM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.9; pressure: 1.0 atm; temperature: 300 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 HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D simultaneous CN NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC high resolution (L/V methyl stereoassignment)sample_2isotropicsample_conditions_1
2D 1H-15N hetNOEsample_2isotropicsample_conditions_1
1D 1H-15N T1 and T2sample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N TROSY (RDCs)sample_2anisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, data analysis

SPARKY v3.112, Goddard - data analysis, peak picking

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, validation

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

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF analysis

PSVS v1.3, Bhattacharya and Montelione - structure quality analysis

MolProbity v3.15, Richardson - structure quality analysis

PDBStat v5.1, Tejero and Montelione - PDB analysis

TALOS vplus, Cornilescu, Delaglio and Bax - dihedral angle constraints

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAJ13312
EMBL CAA24288
GB AAC36138 AAO46755 AAO46757 AAO46759 AAO46765
SP P03495 Q1PUD3 Q288Z0 Q2ICQ4 Q2RFA0