BMRB Entry 27170

Name: Sequence specific 1H, 13C and 15N resonance assignments of a cataract-related variant G57W of human Gamma S-Crystallin
Published: 2017-08-04

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27170

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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:

Sequence specific 1H, 13C and 15N resonance assignments of a cataract-related variant G57W of human Gamma S-Crystallin

Deposition date:

2017-07-10

Original release date:

2017-08-04

Authors:

Khandekar Bari, Jishan; Sharma, Shrikant; Chary, Kandala V.R.

Citation:

Citation: Khandekar Bari, Jishan; Sharma, Shrikant; Chary, Kandala V.R.. "Sequence specific 1H, 13C and 15N resonance assignments of a cataract-related variant G57W of human Gamma S-Crystallin" Biomol. NMR Assignments 12, 51-55 (2018).
PubMed: 28936763

Assembly members:

Assembly members:
G57W_mutant_of_human_Gamma_S-Crystallin, polymer, 184 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
G57W_mutant_of_human_Gamma_S-Crystallin: MSKTGTKITFYEDKNFQGRR YDCDCDCADFHTYLSRCNSI KVEGGTWAVYERPNFAWYMY ILPQGEYPEYQRWMGLNDRL SSCRAVHLPSGGQYKIQIFE KGDFSGQMYETTEDCPSIME QFHMREIHSCKVLEGVWIFY ELPNYRGRQYLLDKKEYRKP IDWGAASPAVQSFRRIVE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	630
15N chemical shifts	177
1H chemical shifts	1139

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Polypeptide chain	1

Entities:

Entity 1, Polypeptide chain 184 residues - Formula weight is not available

1

MET

SER

LYS

THR

GLY

THR

LYS

ILE

THR

PHE

2

TYR

GLU

ASP

LYS

ASN

PHE

GLN

GLY

ARG

3

TYR

ASP

CYS

ASP

CYS

ASP

CYS

ALA

ASP

PHE

4

HIS

THR

TYR

LEU

SER

ARG

CYS

ASN

SER

ILE

5

LYS

VAL

GLU

GLY

THR

TRP

ALA

VAL

TYR

6

GLU

ARG

PRO

ASN

PHE

ALA

TRP

TYR

MET

TYR

7

ILE

LEU

PRO

GLN

GLY

GLU

TYR

PRO

GLU

TYR

8

GLN

ARG

TRP

MET

GLY

LEU

ASN

ASP

ARG

LEU

9

SER

CYS

ARG

ALA

VAL

HIS

LEU

PRO

SER

10

GLY

GLN

TYR

LYS

ILE

GLN

ILE

PHE

GLU

11

LYS

GLY

ASP

PHE

SER

GLY

GLN

MET

TYR

GLU

12

THR

GLU

ASP

CYS

PRO

SER

ILE

MET

GLU

13

GLN

PHE

HIS

MET

ARG

GLU

ILE

HIS

SER

CYS

14

LYS

VAL

LEU

GLU

GLY

VAL

TRP

ILE

PHE

TYR

15

GLU

LEU

PRO

ASN

TYR

ARG

GLY

ARG

GLN

TYR

16

LEU

ASP

LYS

GLU

TYR

ARG

LYS

PRO

17

ILE

ASP

TRP

GLY

ALA

SER

PRO

ALA

VAL

18

GLN

SER

PHE

ARG

ILE

VAL

GLU

Samples:

sample_1: G57W mutant of human Gamma S-Crystallin, [U-100% 13C; U-100% 15N], 1.2 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 77 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 15N-1H HSQC-NOESY	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Ascend 700 MHz

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