BMRB Entry 15437

Name: Assignment, structure, and dynamics of de novo designed protein S836
Published: 2008-01-28

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PDB ID: 2jua
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15437
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Assignment, structure, and dynamics of de novo designed protein S836

Deposition date:

2007-08-16

Original release date:

2008-01-28

Authors:

Go, Abigail; Kim, Seho; Baum, Jean; Hecht, Michael

Citation:

Citation: Go, Abigail; Kim, Seho; Hecht, Michael; Baum, Jean. "NMR assignment of S836: a de novo protein from a designed superfamily" Biomol. NMR Assignments 1, 213-215 (2007).
PubMed: 19636868

Assembly members:

Assembly members:
S836, polymer, 102 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet3A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S836: MYGKLNDLLEDLQEVLKHVN QHWQGGQKNMNKVDHHLQNV IEDIHDFMQGGGSGGKLQEM MKEFQQVLDEIKQQLQGGDN SLHNVHENIKEIFHHLEELV HR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- NOE_list_1
- NOE_list_2
heteronucl_T1_relaxation
- T1_list_1
- T1_list_2
heteronucl_T2_relaxation
- T2_list_1
- T2_list_2

Data type	Count
13C chemical shifts	414
15N chemical shifts	121
1H chemical shifts	719
heteronuclear NOE values	198
T1 relaxation values	198
T2 relaxation values	198

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	S836 monomer	1

Entities:

Entity 1, S836 monomer 102 residues - Formula weight is not available

1

MET

TYR

GLY

LYS

LEU

ASN

ASP

LEU

GLU

2

ASP

LEU

GLN

GLU

VAL

LEU

LYS

HIS

VAL

ASN

3

GLN

HIS

TRP

GLN

GLY

GLN

LYS

ASN

MET

4

ASN

LYS

VAL

ASP

HIS

LEU

GLN

ASN

VAL

5

ILE

GLU

ASP

ILE

HIS

ASP

PHE

MET

GLN

GLY

6

GLY

SER

GLY

LYS

LEU

GLN

GLU

MET

7

MET

LYS

GLU

PHE

GLN

VAL

LEU

ASP

GLU

8

ILE

LYS

GLN

LEU

GLN

GLY

ASP

ASN

9

SER

LEU

HIS

ASN

VAL

HIS

GLU

ASN

ILE

LYS

10

GLU

ILE

PHE

HIS

LEU

GLU

LEU

VAL

11

HIS

ARG

Samples:

sample_1: S836, [U-15N], 1 – 2 mM; D2O, [U-2H], 10%; acetic acid - sodium acetate 50 mM

sample_2: S836, [U-13C; U-15N], 2 mM; D2O, [U-2H], 10%; acetic acid - sodium acetate, [U-13C], 50 mM

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D (HCA)CO(CA)NH	sample_2	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

AQUA, Rullmann, Doreleijers and Kaptein - validation

ProcheckNMR, Laskowski and MacArthur - validation

Molmol, Koradi, Billeter and Wuthrich - structural visualization

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 500 MHz