BMRB Entry 7162

Name: 1H and 15N assignments for the b&#039; domain of ERp57
Published: 2006-10-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR7162

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H and 15N assignments for the b' domain of ERp57

Deposition date:

2006-06-09

Original release date:

2006-10-30

Authors:

Kozlov, Guennadi; Maattanen, Pekka; Schrag, Joseph; Pollock, Stephanie; Cygler, Miroslaw; Nagar, Bhushan; Thomas, David; Gehring, Kalle

Citation:

Citation: Kozlov, Guennadi; Maattanen, Pekka; Schrag, Joseph; Pollock, Stephanie; Cygler, Miroslaw; Nagar, Bhushan; Thomas, David; Gehring, Kalle. "Crystal structure of the bb' domains of the protein disulfide isomerase, ERp57" Structure 14, 1331-1339 (2006).
PubMed: 16905107

Assembly members:

Assembly members:
b' domain, polymer, 145 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
b' domain: GPLGSFGICPHMTEDNKDLI QGKDLLIAYYDVDYEKNAKG SNYWRNRVMMVAKKFLDAGH KLNFAVASRKTFSHELSDFG LESTAGEIPVVAIRTAKGEK FVMQEEFSRDGKALERFLQD YFDGNLKRYLKSEPIPESND GAAAS

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
15N chemical shifts	123
1H chemical shifts	123

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	b' domain of ERp57	1

Entities:

Entity 1, b' domain of ERp57 145 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

PHE

GLY

ILE

CYS

PRO

2

HIS

MET

THR

GLU

ASP

ASN

LYS

ASP

LEU

ILE

3

GLN

GLY

LYS

ASP

LEU

ILE

ALA

TYR

4

ASP

VAL

ASP

TYR

GLU

LYS

ASN

ALA

LYS

GLY

5

SER

ASN

TYR

TRP

ARG

ASN

ARG

VAL

MET

6

VAL

ALA

LYS

PHE

LEU

ASP

ALA

GLY

HIS

7

LYS

LEU

ASN

PHE

ALA

VAL

ALA

SER

ARG

LYS

8

THR

PHE

SER

HIS

GLU

LEU

SER

ASP

PHE

GLY

9

LEU

GLU

SER

THR

ALA

GLY

GLU

ILE

PRO

VAL

10

VAL

ALA

ILE

ARG

THR

ALA

LYS

GLY

GLU

LYS

11

PHE

VAL

MET

GLN

GLU

PHE

SER

ARG

ASP

12

GLY

LYS

ALA

LEU

GLU

ARG

PHE

LEU

GLN

ASP

13

TYR

PHE

ASP

GLY

ASN

LEU

LYS

ARG

TYR

LEU

14

LYS

SER

GLU

PRO

ILE

PRO

GLU

SER

ASN

ASP

15

GLY

ALA

SER

Samples:

sample_1: b' domain 1 mM; phosphate buffer 50 mM; NaCl 100 mM; DTT 1 mM

sample_2: b' domain, [U-15N], 1 mM; phosphate buffer 50 mM; NaCl 100 mM; DTT 1 mM

sample_3: b' domain, [U-13C; U-15N], 1 mM; phosphate buffer 50 mM; NaCl 100 mM; DTT 1 mM

conditions_1: pH: 6.8; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
HNCACB	sample_3	not available	conditions_1
CBCA(CO)NH	sample_3	not available	conditions_1
15N-NOESY	sample_2	not available	conditions_1

Software:

No software information available

NMR spectrometers:

Bruker Avance 600 MHz
Varian Inova 800 MHz

BMRB	17224
PDB	2H8L 3F8U
DBJ	BAA03759 BAA11928 BAG52144 BAG52151 BAG56782
EMBL	CAA89996 CAH90193
GB	AAB37397 AAC50331 AAC51518 AAH14433 AAH36000
PRF	2201310A 2209333A
REF	NP_001127250 NP_001162437 NP_001164786 NP_001182041 NP_001182645
SP	P30101 Q4VIT4 Q5RDG4
AlphaFold	P30101 Q4VIT4 Q5RDG4