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 18221

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18221
MolProbity Validation Chart

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Title: Backbone structure of human membrane protein FAM14B (Interferon alpha-inducible protein 27-like protein 1)   PubMed: 22609626

Deposition date: 2012-01-26 Original release date: 2012-05-22

Authors: Klammt, Christian; Chui, Ellis; Maslennikov, Innokentiy; Kwiatkowski, Witek; Choe, Senyon

Citation: Klammt, Christian; Maslennikov, Innokentiy; Bayrhuber, Monika; Eichmann, Cedric; Vajpai, Navratna; Chiu, Ellis Jeremy Chua; Blain, Katherine; Esquivies, Luis; Kwon, June Hyun Jung; Balana, Bartosz; Pieper, Ursula; Sali, Andrej; Slesinger, Paul; Kwiatkowski, Witek; Riek, Roland; Choe, Senyon. "Facile backbone structure determination of human membrane proteins by NMR spectroscopy."  Nat. Methods 9, 834-839 (2012).

Assembly members:
entity, polymer, 113 residues, 9553.060 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free

Entity Sequences (FASTA):
entity: MTSLYKKVGMGKESGWDSGR AAVAAVVGGVVAVGTVLVAL SAMGFTSVGIAASSIAAKMM STAAIANGGGVAAGSLVAIL QSVGAAGLSVTSKVIGGFAG TALGAWLGSPPSS

Data sets:
Data typeCount
13C chemical shifts350
15N chemical shifts107
1H chemical shifts428

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FAM14B1

Entities:

Entity 1, FAM14B 113 residues - 9553.060 Da.

Residues 1-9 represent GW cloning tag.

1   METTHRSERLEUTYRLYSLYSVALGLYMET
2   GLYLYSGLUSERGLYTRPASPSERGLYARG
3   ALAALAVALALAALAVALVALGLYGLYVAL
4   VALALAVALGLYTHRVALLEUVALALALEU
5   SERALAMETGLYPHETHRSERVALGLYILE
6   ALAALASERSERILEALAALALYSMETMET
7   SERTHRALAALAILEALAASNGLYGLYGLY
8   VALALAALAGLYSERLEUVALALAILELEU
9   GLNSERVALGLYALAALAGLYLEUSERVAL
10   THRSERLYSVALILEGLYGLYPHEALAGLY
11   THRALALEUGLYALATRPLEUGLYSERPRO
12   PROSERSER

Samples:

sample_1: MES-Bis-TRIS 20 mM; LMPG 3%; DSS 0.5 mM; D2O 5%; H2O 95%

sample_NC: MES-Bis-TRIS 20 mM; LMPG 3%; DSS 0.5 mM; D2O 5%; H2O 95%

sample_NCD: MES-Bis-TRIS 20 mM; LMPG 3%; DSS 0.5 mM; D2O 5%; H2O 95%

sample_ND: MES-Bis-TRIS 20 mM; LMPG 3%; DSS 0.5 mM; D2O 5%; H2O 95%

samples_CDL: MES-Bis-TRIS 20 mM; LMPG 3%; DSS 0.5 mM; D2O 5%; H2O 95%

samples_SL: MES-Bis-TRIS 20 mM; LMPG 3%; DSS 0.5 mM; D2O 5%; H2O 95%

samples_DL: MES-Bis-TRIS 20 mM; LMPG 3%; DSS 0.5 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 60 mM; pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsamples_CDLisotropicsample_conditions_1
2D HNCOsamples_CDLisotropicsample_conditions_1
3D HNCOsample_NCDisotropicsample_conditions_1
3D HNCAsample_NCDisotropicsample_conditions_1
3D HNCACBsample_NCDisotropicsample_conditions_1
2D 1H-15N HSQCsamples_SLisotropicsample_conditions_1
2D 1H-15N HSQCsamples_DLisotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_NDisotropicsample_conditions_1
3D 13C-15N HSQC-NOESY-HSQCsample_NCisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

PROSA, Guntert - processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure analysis, structure visualization

NMR spectrometers:

  • Bruker DRX 700 MHz

Related Database Links:

PDB
GB AAH15423 ACT64524 ACT64525 ADZ15768 AIC52948
REF NP_660292 NP_996832 XP_009426632 XP_011534707 XP_011534708
SP Q96BM0
TPE CAE00392

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