BMRB Entry 16099

Title:
Solution NMR Structure of KAZAL-1 domain from Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A.
Deposition date:
2008-12-30
Original release date:
2010-09-17
Authors:
Rossi, Paolo; Chiang, Yiwen; Montelione, Gaetano; Anderson, Stephen
Citation:

Citation: Rossi, Paolo; Chiang, Yiwen; Montelione, Gaetano; Anderson, Stephen. "Solution NMR Structure of Kazal-1 Domain of Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A."  .

Assembly members:

Assembly members:
FSTL-3, polymer, 74 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts284
15N chemical shifts67
1H chemical shifts437

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FSTL_31

Entities:

Entity 1, FSTL_3 74 residues - Formula weight is not available

1   SERASPSERCYSASPGLYVALGLUCYSGLY
2   PROGLYLYSALACYSARGMETLEUGLYGLY
3   ARGPROARGCYSGLUCYSALAPROASPCYS
4   SERGLYLEUPROALAARGLEUGLNVALCYS
5   GLYSERASPGLYALATHRTYRARGASPGLU
6   CYSGLULEUARGALAALAARGCYSARGGLY
7   HISPROASPLEUSERVALMETTYRARGGLY
8   ARGCYSARGLYS

Samples:

sample_1: FSTL-3, [U-100% 13C; U-100% 15N], 0.6 mM; MES 20 mM; sodium chloride 200 mM; H2O 90%; D2O 10%

sample_2: FSTL-3, [U-100% 15N], 0.2 mM; MES 20 mM; sodium chloride 200 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC alisample_1isotropicsample_conditions_1
2D 1H-13C HSQC arosample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY simsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HET_NOEsample_2isotropicsample_conditions_1
2D N15 T1sample_2isotropicsample_conditions_1
2D N15 T2 cpmgsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C NOESY arosample_1isotropicsample_conditions_1
3D NHCACOsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

PSVS v1.3, Bhattacharya and Montelione - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v2.113, Goddard - data analysis

TOPSPIN v2.1, Bruker Biospin - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

Molmol, Koradi, Billeter and Wuthrich - visualization

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - refinement

MolProbity, Richardson - refinement

PDBStat, Tejero, Montelione - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAF84647
GB AAC64321 AAH05839 AAQ89276 EAW61165 EAW61166
REF NP_005851 XP_001117132 XP_003316016 XP_003788724 XP_004059654
SP O95633
AlphaFold O95633

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