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Biological Magnetic Resonance Data Bank


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BMRB Entry 19709

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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/BMR19709
MolProbity Validation Chart

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Title: Solution NMR structure of beta-adaptin appendage domain of human adaptor protein complex 4 subunit beta, Northeast Structural Genomics Consortium (NESG) Target HR8998C

Deposition date: 2013-12-26 Original release date: 2014-01-23

Authors: Eletsky, Alexander; Rotshteyn, Daniel; Pederson, Kari; Shastry, Ritu; Maglaqui, Melissa; Janjua, Haleema; Xiao, Rong; Everett, John; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas

Citation: Eletsky, Alexander; Rotshteyn, Daniel; Pederson, Kari; Shastry, Ritu; Maglaqui, Melissa; Janjua, Haleema; Xiao, Rong; Everett, John; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas. "Solution NMR structure of beta-adaptin appendage domain of human adaptor protein complex 4 subunit beta, Northeast Structural Genomics Consortium (NESG) Target HR8998C"  To be published ., .-..

Assembly members:
HR8998C, polymer, 141 residues, 16004.294 Da.

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

Entity Sequences (FASTA):
HR8998C: MGHHHHHHSHMQELPDSGAL MLVPNRQLTADYFEKTWLSL KVAHQQVLPWRGEFHPDTLQ MALQVVNIQTIAMSRAGSRP WKAYLSAQDDTGCLFLTELL LEPGNSEMQISVKQNEARTE TLNSFISVLETVIGTIEEIK S

Data sets:
Data typeCount
13C chemical shifts584
15N chemical shifts147
1H chemical shifts970

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HR8998C1

Entities:

Entity 1, HR8998C 141 residues - 16004.294 Da.

Residues 12-141 correspond to fragment 610-739 of the native sequence. Residues 1-11 represent a non-native purification tag.

1   METGLYHISHISHISHISHISHISSERHIS
2   METGLNGLULEUPROASPSERGLYALALEU
3   METLEUVALPROASNARGGLNLEUTHRALA
4   ASPTYRPHEGLULYSTHRTRPLEUSERLEU
5   LYSVALALAHISGLNGLNVALLEUPROTRP
6   ARGGLYGLUPHEHISPROASPTHRLEUGLN
7   METALALEUGLNVALVALASNILEGLNTHR
8   ILEALAMETSERARGALAGLYSERARGPRO
9   TRPLYSALATYRLEUSERALAGLNASPASP
10   THRGLYCYSLEUPHELEUTHRGLULEULEU
11   LEUGLUPROGLYASNSERGLUMETGLNILE
12   SERVALLYSGLNASNGLUALAARGTHRGLU
13   THRLEUASNSERPHEILESERVALLEUGLU
14   THRVALILEGLYTHRILEGLUGLUILELYS
15   SER

Samples:

NC5: HR8998C, [5%-13C; U-15N], 0.4 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%

NC5_PEG: HR8998C, [5%-13C; U-15N], 0.2 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; C12E5 PEG 4%; 1-hexanol 4%

NC5_PHAGE: HR8998C, [5%-13C; U-15N], 0.2 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; Pf1 phage 12.5 mg/mL

NC_4: HR8998C, [U-13C; U-15N], 0.2 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%

25C: pH: 6.5; pressure: 1 atm; temperature: 298 K

10C: pH: 6.5; pressure: 1 atm; temperature: 283 K

13C: pH: 6.5; pressure: 1 atm; temperature: 286 K

16C: pH: 6.5; pressure: 1 atm; temperature: 289 K

19C: pH: 6.5; pressure: 1 atm; temperature: 292 K

22C: pH: 6.5; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_4isotropic25C
2D 1H-13C HSQC aliphaticNC_4isotropic25C
3D HNCONC_4isotropic25C
3D CBCA(CO)NHNC_4isotropic25C
3D HNCACBNC_4isotropic25C
3D HN(CA)CONC_4isotropic25C
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNC_4isotropic25C
2D 1H-13C HSQC aromaticNC_4isotropic25C
3D HBHA(CO)NHNC_4isotropic25C
3D HA(CO)NHNC_4isotropic25C
3D HNCANC_4isotropic25C
3D (H)CCH-TOCSY aliphaticNC_4isotropic25C
3D (H)CCH-COSY aliphaticNC_4isotropic25C
3D (H)CCH-COSY aromaticNC_4isotropic25C
2D 1H-15N long-range HSQCNC5isotropic25C
2D 1H-15N HSQCNC5isotropic10C
2D 1H-15N HSQCNC5isotropic13C
2D 1H-15N HSQCNC5isotropic16C
2D 1H-15N HSQCNC5isotropic19C
2D 1H-15N HSQCNC5isotropic22C
2D 1H-15N HSQCNC5isotropic25C
2D 1H-15N J-modulated HSQCNC5isotropic10C
2D 1H-15N J-modulated HSQCNC5_PEGanisotropic10C
2D 1H-15N J-modulated HSQCNC5_PHAGEanisotropic10C
2D 1H-13C CT-HSQC methylNC5isotropic25C

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

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

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

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

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

XEASY, Bartels et al. - data analysis

PROSA v6.4, Guntert - processing

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

TALOSN, Shen, Cornilescu, Delaglio and Bax - geometry optimization

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

PSVS v1.5, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Agilent DD2 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

UNP Q9Y6B7
PDB
GB EHH15072 EHH50179
REF XP_001110491 XP_001110876 XP_003892466 XP_005542316 XP_005542317

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