BMRB Entry 25397

Name: NMR structure of N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 7.2
Published: 2015-08-17

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PDB ID: 2mx8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25397
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 7.2

Deposition date: 2014-12-17 Original release date: 2015-08-17

Authors: Otikovs, Martins; Jaudzems, Kristaps; Chen, Gefei; Nordling, Kerstin; Rising, Anna; Johansson, Jan

Citation: Otikovs, Martins; Jaudzems, Kristaps; Chen, Gefei; Nordling, Kerstin; Rising, Anna; Johansson, Jan. "NMR structure of N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 7.2" To be Published ., .-..

Assembly members:
entity, polymer, 133 residues, 14067.897 Da.

Natural source: Common Name: spiders Taxonomy ID: 182803 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Araneus ventricosus

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

Entity Sequences (FASTA):
entity: GSGNSQPIWTNPNAAMTMTN NLVQCASRSGVLTADQMDDM GMMADSVNSQMQKMGPNPPQ HRLRAMNTAMAAEVAEVVAT SPPQSYSAVLNTIGACLRES MMQATGSVDNAFTNEVMQLV KMLSADSANEVST

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	504
15N chemical shifts	140
1H chemical shifts	857

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 133 residues - 14067.897 Da.

Residues 1-4 are from a non-native affinity tag

1

GLY

SER

GLY

ASN

SER

GLN

PRO

ILE

TRP

THR

2

ASN

PRO

ASN

ALA

MET

THR

MET

THR

ASN

3

ASN

LEU

VAL

GLN

CYS

ALA

SER

ARG

SER

GLY

4

VAL

LEU

THR

ALA

ASP

GLN

MET

ASP

MET

5

GLY

MET

ALA

ASP

SER

VAL

ASN

SER

GLN

6

MET

GLN

LYS

MET

GLY

PRO

ASN

PRO

GLN

7

HIS

ARG

LEU

ARG

ALA

MET

ASN

THR

ALA

MET

8

ALA

GLU

VAL

ALA

GLU

VAL

ALA

THR

9

SER

PRO

GLN

SER

TYR

SER

ALA

VAL

LEU

10

ASN

THR

ILE

GLY

ALA

CYS

LEU

ARG

GLU

SER

11

MET

GLN

ALA

THR

GLY

SER

VAL

ASP

ASN

12

ALA

PHE

THR

ASN

GLU

VAL

MET

GLN

LEU

VAL

13

LYS

MET

LEU

SER

ALA

ASP

SER

ALA

ASN

GLU

14

VAL

SER

THR

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.95 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 0.03%; protease inhibitor cocktail 0.01 tablet/100mL

sample_conditions_1: ionic strength: 0.085 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ v2.1b, Varian - collection

TOPSPIN v3.1, Bruker Biospin - processing

CARA v1.9.0, Keller and Wuthrich - chemical shift assignment

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

UNIO v2.0.2, T. Herrmann, F. Fiorito, J. Volk - data analysis, peak picking, structure solution

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	25398
PDB	2MX8 2MX9
GB	AFV31615

Biological Magnetic Resonance Data Bank