BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 18218

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18218
MolProbity Validation Chart

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Title: Backbone structure of human membrane protein HIGD1B   PubMed: 22609626

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

Authors: Klammt, Christian; 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, 99 residues, 11075.031 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: MSANRRWWVPPDDEDCVSEK LLRKTRESPLVPIGLGGCLV VAAYRIYRLRSRGSTKMSIH LIHTRVAAQACAVGAIMLGA VYTMYSDYVKRMAQDAGEK

Data sets:
Data typeCount
13C chemical shifts356
15N chemical shifts94
1H chemical shifts558

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1HIGD1B1

Entities:

Entity 1, HIGD1B 99 residues - 11075.031 Da.

1   METSERALAASNARGARGTRPTRPVALPRO
2   PROASPASPGLUASPCYSVALSERGLULYS
3   LEULEUARGLYSTHRARGGLUSERPROLEU
4   VALPROILEGLYLEUGLYGLYCYSLEUVAL
5   VALALAALATYRARGILETYRARGLEUARG
6   SERARGGLYSERTHRLYSMETSERILEHIS
7   LEUILEHISTHRARGVALALAALAGLNALA
8   CYSALAVALGLYALAILEMETLEUGLYALA
9   VALTYRTHRMETTYRSERASPTYRVALLYS
10   ARGMETALAGLNASPALAGLYGLULYS

Samples:

samples_CDL: HIGD1B, [U-15N; U13C1], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_N: HIGD1B, [U-15N], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_CN: HIGD1B, [U-15N; U-13C], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_CND: HIGD1B, [U-15N; U-13C; U-2H], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_CN-dLMPG: HIGD1B, [U-15N; U-13C], ?0.2 mM; MES-Bis-TRIS 20 mM; d27-LMPG, 95%-2H in alkyl chain, 2%; DSS 0.5 mM; H2O 95%; D2O 5%

samples_SL: HIGD1B, [U-15N], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

samples_DL: HIGD1B, [U-15N], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_ND: HIGD1B, [U-15N; U-2H], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 40 mM; pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_Nisotropicsample_conditions_1
2D 1H-15N HSQCsamples_CDLisotropicsample_conditions_1
2D HNCOsamples_CDLisotropicsample_conditions_1
2D 1H-15N HSQCsample_CNisotropicsample_conditions_1
3D HNCOsample_CNDisotropicsample_conditions_1
3D HNHAsample_CNDisotropicsample_conditions_1
3D HNCACBsample_CNDisotropicsample_conditions_1
3D 1H-15N NOESYsample_Nisotropicsample_conditions_1
3D 1H-15N NOESYsample_CN-dLMPGisotropicsample_conditions_1
3D 13C-15N HSQC-NOESY-HSQCsample_CNisotropicsample_conditions_1
3D 1H-15N NOESYsample_NDisotropicsample_conditions_1
2D 1H-15N HSQCsamples_SLisotropicsample_conditions_1
2D 1H-15N HSQCsamples_DLisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

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

PROSA, Guntert - processing

MCCL, (MCCL) Kwiatkowski, Maslennikov - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker DRX 700 MHz
  • Varian Uniform NMR System 500 MHz

Related Database Links:

PDB
DBJ BAA90725 BAA90726
GB AAH20667 EAW51575 EAW51576
REF NP_001258809 NP_057522 XP_001146933 XP_002827469 XP_002827470
SP Q9P298

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