BMRB Entry 16376

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16376
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution NMR structure of the monomeric W187R mutant of A/Udorn NS1 effector domain. Northeast Structural Genomics target OR8C[W187R].
Deposition date:
2009-06-29
Original release date:
2009-07-06
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:

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]."  .

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: OR8C-W187R-21.1

Entity Sequences (FASTA):

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

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

Time Domain Data

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
AlphaFold P03495 Q1PUD3 Q288Z0 Q2ICQ4 Q2RFA0

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