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BMRB Entry 16386

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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/BMR16386
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Title: Solution NMR Structure of the EGF-like 1 Domain of Human Fibulin-4. Northeast Structural Genomics Target HR6275.

Deposition date: 2009-06-30 Original release date: 2009-08-06

Authors: Rossi, Paolo; Chiang, Yiwen; Anderson, Stephen; Montelione, Gaetano

Citation: Rossi, Paolo; Chiang, Yiwen; Anderson, Stephen; Montelione, Gaetano. "Solution NMR Structure of the EGF-like 1 Domain of Human Fibulin-4. Northeast Structural Genomics Target HR6275."  Not known ., .-..

Assembly members:
EGF-like 1 Domain, polymer, 71 residues, 7576.472 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):
EGF-like 1 Domain: SDVNECLTIPEACKGEMKCI NHYGGYLCLPRSAAVINDLH GEGPPPPVPPAQHPNPCPPG YEPDDQDSCVD

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts67
1H chemical shifts407

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EGF-like 1 Domain1

Entities:

Entity 1, EGF-like 1 Domain 71 residues - 7576.472 Da.

1   SERASPVALASNGLUCYSLEUTHRILEPRO
2   GLUALACYSLYSGLYGLUMETLYSCYSILE
3   ASNHISTYRGLYGLYTYRLEUCYSLEUPRO
4   ARGSERALAALAVALILEASNASPLEUHIS
5   GLYGLUGLYPROPROPROPROVALPROPRO
6   ALAGLNHISPROASNPROCYSPROPROGLY
7   TYRGLUPROASPASPGLNASPSERCYSVAL
8   ASP

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.6 mM; sodium chloride 150 mM; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%

sample_2: entity, [U-100% 15N], 0.3 mM; sodium chloride 150 mM; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HMQCsample_1isotropicsample_conditions_1
2D 1H-15N het_NOEsample_1isotropicsample_conditions_1
1D 15N_T1 seriessample_1isotropicsample_conditions_1
1D 15N_T2 seriessample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

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

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

TOPSPIN v2.1, Bruker Biospin - collection

PSVS v1.3, Bhattacharya and Montelione - validation

SPARKY v2.113, Goddard - data analysis

PINE, Bahrami, Markley, Assadi, and Eghbalnia - data analysis

Molmol, Koradi, Billeter and Wuthrich - visualization

PyMol, DeLano Scientific - visualization

PDBStat v5.1, Tejero, Montelione - PDB processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA92880 BAD92358 BAF84768 BAG37622 BAG50843
EMBL CAA10791 CAG46732
GB AAC03101 AAF65188 AAG45245 AAH10456 AAQ89258
REF NP_001231778 NP_058634 XP_001118071 XP_003274253 XP_003909598
SP O55058 O95967

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