BMRB Entry 5654

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PDB ID: 1mpe
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5654
MolProbity Validation Chart

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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:

A Protein Contorsionist-Core Mutations Switch Monomeric Protein GB1 into an Intertwined Tetramer

Deposition date:

2002-11-06

Original release date:

2003-08-08

Authors:

Frank, M.; Dyda, F.; Dobrodumov, A.; Gronenborn, A.

Citation:

Citation: Frank, M.; Dyda, F.; Dobrodumov, A.; Gronenborn, A.. "Core Mutations Switch Monomeric Protein GB1 into an Intertwined Tetramer" Nat. Struct. Biol. 9, 877-885 (2002).
PubMed: 12379842

Assembly members:

Assembly members:
mmunoglobulin G binding protein G, polymer, 56 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Streptococcus Taxonomy ID: 1306 Superkingdom: Eubacteria Kingdom: not available Genus/species: Streptococcus sp.

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET11A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mmunoglobulin G binding protein G: MQYKVILNGKTLKGETTTEA VDAATFEKVVKQFFNDNGVD GEWTYDDATKTFTVTE

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1
coupling_constants
- coupling_constants_set_1

Data type	Count
13C chemical shifts	250
15N chemical shifts	61
1H chemical shifts	356
coupling constants	44

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Immunoglobulin G binding protein G chain A	1
2	Immunoglobulin G binding protein G chain B	1
3	Immunoglobulin G binding protein G chain C	1
4	Immunoglobulin G binding protein G chain D	1

Entities:

Entity 1, Immunoglobulin G binding protein G chain A 56 residues - Formula weight is not available

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

PHE

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: mmunoglobulin G binding protein G, [U-15N; U-13C], 3.5 mM; sodium phosphate 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: mmunoglobulin G binding protein G, [U-15N], 2.89 mM; sodium phosphate 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_3: mmunoglobulin G binding protein G, [U-15N; U-13C], 3.5 mM; sodium phosphate 50 mM; sodium azide 0.02%; D2O 100%

sample_4: mmunoglobulin G binding protein G 0.7 mM; mmunoglobulin G binding protein G, [U-15N; U-13C], 0.7 mM; sodium phosphate 50 mM; sodium azide 0.02%; D2O 100%

sample_cond_1: ionic strength: 50 mM; pH: 5.45; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	not available	not available	not available
HNHA	not available	not available	not available
3D 13C-separated NOESY	not available	not available	not available
4D 13C-separated NOESY	not available	not available	not available
4D 13C/15N-separated NOESY	not available	not available	not available
3D 12C-filtered 13C-separated NOESY	not available	not available	not available

Software:

NMRPipe v2.2 - processing

PIPP v4.3.2 - data analysis

xwinnmr v2.6 - collection

X-PLOR v4.0 - refinement

CNS v1.0 - structure solution

NMR spectrometers:

Bruker DMX 500 MHz