BMRB Entry 5875

Name: 1H, 13C, and 15N Chemical Shift Assignments of the dimeric mutant of GB1
Published: 2003-12-05

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PDB ID: 1q1o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5875
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N Chemical Shift Assignments of the dimeric mutant of GB1

Deposition date:

2003-07-18

Original release date:

2003-12-05

Authors:

Byeon, In-Ja; Louis, John; Gronenborn, Angela

Citation:

Citation: Byeon, In-Ja; Louis, John; Gronenborn, Angela. "A Protein Contortionist: Core Mutations of GB1 that Induce Dimerization and Domain Swapping" J. Mol. Biol. 333, 141-152 (2003).
PubMed: 14516749

Assembly members:

Assembly members:
Immunoglobulin Binding domain 1 of Protein G, polymer, 56 residues, 6220.8 Da.

Natural source:

Natural source: Common Name: Streptococcus sp. (Lancefield Group G) Taxonomy ID: 1306 Superkingdom: Eubacteria Kingdom: not available Genus/species: Streptococcus Streptococcus sp. (Lancefield Group G)

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Immunoglobulin Binding domain 1 of Protein G: MQYKVILNGKTLKGETTTEA VDAATAEKVVKQFFNDNGVD GEWTYDDATKTFTVTE

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
13C chemical shifts	175
15N chemical shifts	61
1H chemical shifts	362

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GB1 subunit A	1
2	GB1 subunit B	1

Entities:

Entity 1, GB1 subunit A 56 residues - 6220.8 Da.

1

MET

GLN

TYR

LYS

VAL

ILE

LEU

ASN

GLY

LYS

2

THR

LEU

LYS

GLY

GLU

THR

GLU

ALA

3

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

4

LYS

GLN

PHE

ASN

ASP

ASN

GLY

VAL

ASP

5

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

6

THR

PHE

THR

VAL

THR

GLU

Samples:

sample_1: Immunoglobulin Binding domain 1 of Protein G, [U-95% 13C; U-95% 15N], 1.7 mM

Ex-cond_1: pH: 6.0; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	not available	not available	not available
2D 1H-1H TOCSY	not available	not available	not available
2D 1H-15N HSQC	not available	not available	not available
2D 1H-13C HSQC/HMQC	not available	not available	not available
3D HNCO	not available	not available	not available
3D HNCACB	not available	not available	not available
3D CBCA(CO)NH	not available	not available	not available
3D H(CCO)NH-TOCSY	not available	not available	not available
3D C(CCO)NH-TOCSY	not available	not available	not available
3D HNHB	not available	not available	not available
3D HACAHB-COSY	not available	not available	not available
2D 13C'-{13CG} spin-echo difference	not available	not available	not available
2D 15N-{13C'} spin-echo difference	not available	not available	not available
2D 13C'-{13CG} spin-echo difference arom	not available	not available	not available
2D 15N-{13C'} spin-echo difference arom	not available	not available	not available
2D [13C-13C] long-range correlation experiment	not available	not available	not available
3D 15N-edited TOCSY	not available	not available	not available
3D 15N-edited NOESY	not available	not available	not available

Software:

NMRPipe v2.2 - processing

PIPP v4.3.2 - data analysis

NMR spectrometers:

Bruker DRX 800 MHz
Bruker DMX 750 MHz
Bruker DRX 600 MHz
Bruker DMX 600 MHz
Bruker DMX 500 MHz