BMRB Entry 19340

Name: Untangling the Solution Structure of C-Terminal Domain of AciniformSpidroin
Published: 2014-02-13

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PDB ID: 2mab
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19340
MolProbity Validation Chart

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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: Untangling the Solution Structure of C-Terminal Domain of AciniformSpidroin PubMed: 24422432

Deposition date: 2013-07-09 Original release date: 2014-02-13

Authors: Wang, Shujing; Yang, Daiwen

Citation: Wang, Shujing; Huang, Weidong; Yang, Daiwen. "Structure and function of C-terminal domain of aciniform spidroin." Biomacromolecules 15, 468-477 (2014).

Assembly members:
entity, polymer, 109 residues, 10887.300 Da.

Natural source: Common Name: Batik golden web spider Taxonomy ID: 171624 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Nephila Antipodiana

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

Entity Sequences (FASTA):
entity: PSFGLVLNSPNGLRSPQAKA RINNLASALSTAVGRNGVDV NAFTSGLRATLSNLGDSGMS PNEAKVEVLLEALTAALQLL SSSTLGAVDTTSIGLTSNSV SKAVAQALA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	330
15N chemical shifts	121
1H chemical shifts	737

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1

Entities:

Entity 1, entity_1 109 residues - 10887.300 Da.

1

PRO

SER

PHE

GLY

LEU

VAL

LEU

ASN

SER

PRO

2

ASN

GLY

LEU

ARG

SER

PRO

GLN

ALA

LYS

ALA

3

ARG

ILE

ASN

LEU

ALA

SER

ALA

LEU

SER

4

THR

ALA

VAL

GLY

ARG

ASN

GLY

VAL

ASP

VAL

5

ASN

ALA

PHE

THR

SER

GLY

LEU

ARG

ALA

THR

6

LEU

SER

ASN

LEU

GLY

ASP

SER

GLY

MET

SER

7

PRO

ASN

GLU

ALA

LYS

VAL

GLU

VAL

LEU

8

GLU

ALA

LEU

THR

ALA

LEU

GLN

LEU

9

SER

THR

LEU

GLY

ALA

VAL

ASP

THR

10

THR

SER

ILE

GLY

LEU

THR

SER

ASN

SER

VAL

11

SER

LYS

ALA

VAL

ALA

GLN

ALA

LEU

ALA

Samples:

sample_1: CTDtrQA, [U-100% 13C; U-100% 15N], 2 mM; sodium phosphate 10 mM; sodium azide 0.01%; D2O 5%; H2O 95%

sample_2: CTDtrQA 1 mM; CTDtrQA, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 10 mM; 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
3D MQ-(H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 13C,15N-filtered NOESY	sample_2	isotropic	sample_conditions_1
4D NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMRspy, Xu, Yingqi; Zheng, Yu; Fan, Jing-song; Yang, Daiwen. - data analysis

NMR spectrometers:

Bruker Avance 800 MHz

Biological Magnetic Resonance Data Bank