BMRB Entry 17446

Name: 1H 15N 13C Backbone Assignment of Sap97 N terminal region and PDZ1 domain
Published: 2012-08-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17446

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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:

1H 15N 13C Backbone Assignment of Sap97 N terminal region and PDZ1 domain

Deposition date:

2011-02-07

Original release date:

2012-08-14

Authors:

Phelan, Marie; Tully, Mark; Leyland, Mark; Lian, Lu-Yun

Citation:

Citation: Tully, Mark; Grossmann, J.; Phelan, Marie; Pandelaneni, Sravan; Leyland, Mark; Lian, Lu-Yun. "Conformational characterization of synapse-associated protein 97 by nuclear magnetic resonance and small-angle X-ray scattering shows compact and elongated forms" Biochemistry 51, 899-908 (2012).
PubMed: 22242544

Assembly members:

Assembly members:
SAP97NPDZ1, polymer, 214 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pLEIC-01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SAP97NPDZ1: SMSKQCEPVQPGNPWESGSL SSAAVTSESLPGGLSPPVEK YRYQDEEVLPSERISPQVPN EVLGPELVHVSEKSLSEIEN VHGFVSHSHISPIKANPPPV LVNTDSLETPTYVNGTDADY EYEEITLERGNSGLGFSIAG GTDNPHIGDDSSIFITKIIT GGAAAQDGRLRVNDCILRVN EADVRDVTHSKAVEALKEAG SIVRLYVKRRKPAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	567
15N chemical shifts	181
1H chemical shifts	630

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SAP97NPDZ1	1

Entities:

Entity 1, SAP97NPDZ1 214 residues - Formula weight is not available

1

SER

MET

SER

LYS

GLN

CYS

GLU

PRO

VAL

GLN

2

PRO

GLY

ASN

PRO

TRP

GLU

SER

GLY

SER

LEU

3

SER

ALA

VAL

THR

SER

GLU

SER

LEU

4

PRO

GLY

LEU

SER

PRO

VAL

GLU

LYS

5

TYR

ARG

TYR

GLN

ASP

GLU

VAL

LEU

PRO

6

SER

GLU

ARG

ILE

SER

PRO

GLN

VAL

PRO

ASN

7

GLU

VAL

LEU

GLY

PRO

GLU

LEU

VAL

HIS

VAL

8

SER

GLU

LYS

SER

LEU

SER

GLU

ILE

GLU

ASN

9

VAL

HIS

GLY

PHE

VAL

SER

HIS

SER

HIS

ILE

10

SER

PRO

ILE

LYS

ALA

ASN

PRO

VAL

11

LEU

VAL

ASN

THR

ASP

SER

LEU

GLU

THR

PRO

12

THR

TYR

VAL

ASN

GLY

THR

ASP

ALA

ASP

TYR

13

GLU

TYR

GLU

ILE

THR

LEU

GLU

ARG

GLY

14

ASN

SER

GLY

LEU

GLY

PHE

SER

ILE

ALA

GLY

15

GLY

THR

ASP

ASN

PRO

HIS

ILE

GLY

ASP

16

SER

ILE

PHE

ILE

THR

LYS

ILE

THR

17

GLY

ALA

GLN

ASP

GLY

ARG

LEU

18

ARG

VAL

ASN

ASP

CYS

ILE

LEU

ARG

VAL

ASN

19

GLU

ALA

ASP

VAL

ARG

ASP

VAL

THR

HIS

SER

20

LYS

ALA

VAL

GLU

ALA

LEU

LYS

GLU

ALA

GLY

21

SER

ILE

VAL

ARG

LEU

TYR

VAL

LYS

ARG

22

LYS

PRO

ALA

SER

Samples:

sample_1: SAP97NPDZ1, [U-98% 13C; U-98% 15N], 1 mM

sample_conditions_1: ionic strength: 100 mM; 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	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHANH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

Analysis v2.1.3, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

UNP	Q62696
AlphaFold	Q62696