BMRB Entry 7167

Name: 1H, 15N, 13C resonance assignments for regeneration-induced CNPase homolog (RICH) protein
Published: 2006-10-02

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PDB ID: 2i3e
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7167
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 15N, 13C resonance assignments for regeneration-induced CNPase homolog (RICH) protein

Deposition date:

2006-06-14

Original release date:

2006-10-02

Authors:

Denisov, Alexey; Kozlov, Guennadi; Gehring, Kalle

Citation:

Citation: Denisov, Alexey; Kozlov, Guennadi; Gravel, Michel; Sprules, Tara; Braun, Peter; Gehring, Kalle. "1H, 13C and 15N resonance assignments of the catalytic domain of the goldfish RICH protein" J. Biomol. NMR 36, 75-75 (2006).
PubMed: 17031527

Assembly members:

Assembly members:
RICH protein, polymer, 222 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Goldfish Taxonomy ID: 7957 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Carassius auratus

Experimental source:

Experimental source: Production method: recombinant technology Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RICH protein: GSHMELPLFFGWFLLPEEEE RIKCATMDFLKTLDTLEAFK EHISEFTGEAEKEVDLEQYF QNPLQLHCTTKFCDYGKAEG AKEYAELQVVKESLTKSYEL SVTALIVTPRTFGARVALTE AQVKLWPEGADKEGVAPALL PSVEALPAGSRAHVTLGCSA GVETVQTGLDLLEILALQKE GKEGTQVEMDLGTLTYLSEG RWFLALREPINADTTFTSFS ED

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	633
15N chemical shifts	212
1H chemical shifts	1087

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RICH protein	1

Entities:

Entity 1, RICH protein 222 residues - Formula weight is not available

1

GLY

SER

HIS

MET

GLU

LEU

PRO

LEU

PHE

2

GLY

TRP

PHE

LEU

PRO

GLU

3

ARG

ILE

LYS

CYS

ALA

THR

MET

ASP

PHE

LEU

4

LYS

THR

LEU

ASP

THR

LEU

GLU

ALA

PHE

LYS

5

GLU

HIS

ILE

SER

GLU

PHE

THR

GLY

GLU

ALA

6

GLU

LYS

GLU

VAL

ASP

LEU

GLU

GLN

TYR

PHE

7

GLN

ASN

PRO

LEU

GLN

LEU

HIS

CYS

THR

8

LYS

PHE

CYS

ASP

TYR

GLY

LYS

ALA

GLU

GLY

9

ALA

LYS

GLU

TYR

ALA

GLU

LEU

GLN

VAL

10

LYS

GLU

SER

LEU

THR

LYS

SER

TYR

GLU

LEU

11

SER

VAL

THR

ALA

LEU

ILE

VAL

THR

PRO

ARG

12

THR

PHE

GLY

ALA

ARG

VAL

ALA

LEU

THR

GLU

13

ALA

GLN

VAL

LYS

LEU

TRP

PRO

GLU

GLY

ALA

14

ASP

LYS

GLU

GLY

VAL

ALA

PRO

ALA

LEU

15

PRO

SER

VAL

GLU

ALA

LEU

PRO

ALA

GLY

SER

16

ARG

ALA

HIS

VAL

THR

LEU

GLY

CYS

SER

ALA

17

GLY

VAL

GLU

THR

VAL

GLN

THR

GLY

LEU

ASP

18

LEU

GLU

ILE

LEU

ALA

LEU

GLN

LYS

GLU

19

GLY

LYS

GLU

GLY

THR

GLN

VAL

GLU

MET

ASP

20

LEU

GLY

THR

LEU

THR

TYR

LEU

SER

GLU

GLY

21

ARG

TRP

PHE

LEU

ALA

LEU

ARG

GLU

PRO

ILE

22

ASN

ALA

ASP

THR

PHE

THR

SER

PHE

SER

23

GLU

ASP

Samples:

sample_1: RICH protein, [U-99% 13C; U-99% 15N], 1 mM; MES buffer 50 mM; NaCl 150 mM; D2O 10%; H2O 90%

conditions_1: pH: 6.0; temperature: 307 K

Experiments:

Name	Sample	Sample state	Sample conditions
HSQC	sample_1	not available	conditions_1
HNCACB	sample_1	not available	conditions_1
3D-NOESY-HSQC	sample_1	not available	conditions_1
HNCA	sample_1	not available	conditions_1
HNCO	sample_1	not available	conditions_1
CBCACOHN	sample_1	not available	conditions_1

Software:

XEASY v1.3.13 -

NMRPipe -

NMR spectrometers:

Varian Unity Inova 800 MHz
Bruker DRX 600 MHz

PDB	2I3E
GB	AAA84448