BMRB Entry 50953

Name: The 1H, 15N and 13C resonance assignments of the C-terminal domain of Serpine mRNA binding protein 1 (SERBP1)
Published: 2021-08-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50953

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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:

The 1H, 15N and 13C resonance assignments of the C-terminal domain of Serpine mRNA binding protein 1 (SERBP1)

Deposition date:

2021-05-26

Original release date:

2021-08-27

Authors:

Baudin, Antoine; Xu, Xiaoping; Libich, David

Citation:

Citation: Baudin, Antoine; Xu, Xiaoping; Libich, David. "The 1H, 15N and 13C resonance assignments of the C-terminal domain of Serpine mRNA binding protein 1 (SERBP1)" Biomol. NMR Assignments 15, 461-466 (2021).
PubMed: 34436734

Assembly members:

Assembly members:
entity_1, polymer, 212 residues, 23728.54 Da.

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 Vector: pAG8Ha-His

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GKREFDRHSGSDRSSFSHYS GLKHEDKRGGSGSHNWGTVK DELTESPKYIQKQISYNYSD LDQSNVTEETPEGEEHHPVA DTENKENEVEEVKEEGPKEM TLDEWKAIQNKDRAKVEFNI RKPNEGADGQWKKGFVLHKS KSEEAHAEDSVMDHHFRKPA NDITSQLEINFGDLGRPGRG GRGGRGGRGRGGRPNRGSRT DKSSASAPDVDD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	693
15N chemical shifts	188
1H chemical shifts	576

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SERBP1 189-408	1

Entities:

Entity 1, SERBP1 189-408 212 residues - 23728.54 Da.

1

GLY

LYS

ARG

GLU

PHE

ASP

ARG

HIS

SER

GLY

2

SER

ASP

ARG

SER

PHE

SER

HIS

TYR

SER

3

GLY

LEU

LYS

HIS

GLU

ASP

LYS

ARG

GLY

4

SER

GLY

SER

HIS

ASN

TRP

GLY

THR

VAL

LYS

5

ASP

GLU

LEU

THR

GLU

SER

PRO

LYS

TYR

ILE

6

GLN

LYS

GLN

ILE

SER

TYR

ASN

TYR

SER

ASP

7

LEU

ASP

GLN

SER

ASN

VAL

THR

GLU

THR

8

PRO

GLU

GLY

GLU

HIS

PRO

VAL

ALA

9

ASP

THR

GLU

ASN

LYS

GLU

ASN

GLU

VAL

GLU

10

GLU

VAL

LYS

GLU

GLY

PRO

LYS

GLU

MET

11

THR

LEU

ASP

GLU

TRP

LYS

ALA

ILE

GLN

ASN

12

LYS

ASP

ARG

ALA

LYS

VAL

GLU

PHE

ASN

ILE

13

ARG

LYS

PRO

ASN

GLU

GLY

ALA

ASP

GLY

GLN

14

TRP

LYS

GLY

PHE

VAL

LEU

HIS

LYS

SER

15

LYS

SER

GLU

ALA

HIS

ALA

GLU

ASP

SER

16

VAL

MET

ASP

HIS

PHE

ARG

LYS

PRO

ALA

17

ASN

ASP

ILE

THR

SER

GLN

LEU

GLU

ILE

ASN

18

PHE

GLY

ASP

LEU

GLY

ARG

PRO

GLY

ARG

GLY

19

GLY

ARG

GLY

ARG

GLY

ARG

GLY

ARG

20

GLY

ARG

PRO

ASN

ARG

GLY

SER

ARG

THR

21

ASP

LYS

SER

ALA

SER

ALA

PRO

ASP

VAL

22

ASP

Samples:

sample_1: SERBP1_189-400, [U-100% 13C; U-100% 15N], 82 uM; NaCl 60 mM

sample_conditions_1: ionic strength: 60 mM; pH: 6.9; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC/HMQC	sample_1	isotropic	sample_conditions_1
CBCA(CO)NH (H[N[co[{CA\|ca[C]}]]])	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
HN(CA)CO (H[N[ca[CO]]])	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
HNHA (H{[N]+[HA]})	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis v2.5 - chemical shift assignment, data analysis, peak picking

NMRPipe - processing

TOPSPIN v4.0.7 - collection

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks