BMRB Entry 16099

Name: Solution NMR Structure of KAZAL-1 domain from Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A.
Published: 2010-09-17

Click here to enlarge.

PDB ID: 2kcx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16099
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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):

Entity Sequences (FASTA):
FSTL-3: SDSCDGVECGPGKACRMLGG RPRCECAPDCSGLPARLQVC GSDGATYRDECELRAARCRG HPDLSVMYRGRCRK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	284
15N chemical shifts	67
1H chemical shifts	437

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FSTL_3	1

Entities:

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

1

SER

ASP

SER

CYS

ASP

GLY

VAL

GLU

CYS

GLY

2

PRO

GLY

LYS

ALA

CYS

ARG

MET

LEU

GLY

3

ARG

PRO

ARG

CYS

GLU

CYS

ALA

PRO

ASP

CYS

4

SER

GLY

LEU

PRO

ALA

ARG

LEU

GLN

VAL

CYS

5

GLY

SER

ASP

GLY

ALA

THR

TYR

ARG

ASP

GLU

6

CYS

GLU

LEU

ARG

ALA

ARG

CYS

ARG

GLY

7

HIS

PRO

ASP

LEU

SER

VAL

MET

TYR

ARG

GLY

8

ARG

CYS

ARG

LYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC ali	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aro	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY sim	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HET_NOE	sample_2	isotropic	sample_conditions_1
2D N15 T1	sample_2	isotropic	sample_conditions_1
2D N15 T2 cpmg	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C NOESY aro	sample_1	isotropic	sample_conditions_1
3D NHCACO	sample_1	isotropic	sample_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

PDB	2KCX 3B4V 3SEK
DBJ	BAF84647
GB	AAC64321 AAH05839 AAQ89276 EAW61165 EAW61166
REF	NP_005851 XP_001117132 XP_003316016 XP_003788724 XP_004059654
SP	O95633
AlphaFold	O95633