BMRB Entry 18726

Name: Repetitive domain (RP) of aciniform spidroin 1 from Nephila antipodiana
Published: 2013-01-15

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PDB ID: 2lyi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18726
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Repetitive domain (RP) of aciniform spidroin 1 from Nephila antipodiana

Deposition date:

2012-09-18

Original release date:

2013-01-15

Authors:

Wang, Shujing; Huang, Weidong; Yang, Daiwen

Citation:

Citation: Wang, Shujing; Huang, Weidong; Yang, Daiwen. "NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana" J. Biomol. NMR 54, 415-420 (2012).
PubMed: 23129012

Assembly members:

Assembly members:
AcSp1-RP, polymer, 167 residues, 17079.383 Da.

Natural source:

Natural source: Common Name: Spiders Taxonomy ID: 171624 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Nephila antipodiana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-32a(+)(derived)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AcSp1-RP: MHHHHHHSGSLGDQLTSTLA SALTKTNTLKAVSASKPSAN VAVAIVTSGLKKALGALRIN AGVSSQLTSAVSQAVANVRP GSSPAVYAKAIAAPSVQILV SSGSVNNNNAKQVASTLSEN LVREMANTARRYRVNVPEAS VQADVSLVTSMTSTFVISSQ TSVQMGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	487
15N chemical shifts	165
1H chemical shifts	1070

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AcSp1-RP	1

Entities:

Entity 1, AcSp1-RP 167 residues - 17079.383 Da.

1

MET

HIS

SER

GLY

SER

2

LEU

GLY

ASP

GLN

LEU

THR

SER

THR

LEU

ALA

3

SER

ALA

LEU

THR

LYS

THR

ASN

THR

LEU

LYS

4

ALA

VAL

SER

ALA

SER

LYS

PRO

SER

ALA

ASN

5

VAL

ALA

VAL

ALA

ILE

VAL

THR

SER

GLY

LEU

6

LYS

ALA

LEU

GLY

ALA

LEU

ARG

ILE

ASN

7

ALA

GLY

VAL

SER

GLN

LEU

THR

SER

ALA

8

VAL

SER

GLN

ALA

VAL

ALA

ASN

VAL

ARG

PRO

9

GLY

SER

PRO

ALA

VAL

TYR

ALA

LYS

ALA

10

ILE

ALA

PRO

SER

VAL

GLN

ILE

LEU

VAL

11

SER

GLY

SER

VAL

ASN

ALA

12

LYS

GLN

VAL

ALA

SER

THR

LEU

SER

GLU

ASN

13

LEU

VAL

ARG

GLU

MET

ALA

ASN

THR

ALA

ARG

14

ARG

TYR

ARG

VAL

ASN

VAL

PRO

GLU

ALA

SER

15

VAL

GLN

ALA

ASP

VAL

SER

LEU

VAL

THR

SER

16

MET

THR

SER

THR

PHE

VAL

ILE

SER

GLN

17

THR

SER

VAL

GLN

MET

GLY

Samples:

sample_1: AcSp1-RP, [U-100% 13C; U-100% 15N], 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.0; 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 aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
4D time shared 13C/15N-edited NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

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

NMRspy, Yu Zheng, Daiwen Yang - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 800 MHz