BMRB Entry 4341

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4341

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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:

Assignment of the Backbone Resonances of Oxidized Fe-superoxide Dismutase, a 42 kDa Paramagnet-containing Enzyme

Deposition date:

1999-05-04

Original release date:

1999-11-30

Authors:

Vathyam, Surekha; Byrd, R.; Miller, Anne-Frances

Citation:

Citation: Vathyam, Surekha; Byrd, R.; Miller, Anne-Frances. "Assignment of the Backbone Resonances of Oxidized Fe-superoxide Dismutase, a 42 kDa Paramagnet-containing Enzyme" J. Biomol. NMR 14, 293-294 (1999).

Assembly members:

Assembly members:
Fe-superoxide dismutase, polymer, 192 residues, 21000 Da.
FE (III) ION, non-polymer, 55.845 Da.
WATER, water, 18.015 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fe-superoxide dismutase: SFELPALPYAKDALAPHISA ETIEYHYGKHHQTYVTNLNN LIKGTAFEGKSLEEIIRSSE GGVFNNAAQVWNHWFYWNCL APNAGGEPTGKVAEAIAASF GSFADFKAQFTDAAIKNFGS GWTWLVKNSDGKLAIVSTSN AGTPLTTDATPLLTVDVWEH AYYIDYRNARPGYLEHFWAL VNWEFVAKNLAA

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
13C chemical shifts	381
15N chemical shifts	117
1H chemical shifts	117

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Fe(II)SOD monomer 1	1
2	Fe(II)SOD monomer 2	1
3	Fe(II) monomer 1	2
4	Fe(II) monomer 2	2
5	H2O monomer 1	3
6	H2O monomer 2	3

Entities:

Entity 1, Fe(II)SOD monomer 1 192 residues - 21000 Da.

1

SER

PHE

GLU

LEU

PRO

ALA

LEU

PRO

TYR

ALA

2

LYS

ASP

ALA

LEU

ALA

PRO

HIS

ILE

SER

ALA

3

GLU

THR

ILE

GLU

TYR

HIS

TYR

GLY

LYS

HIS

4

HIS

GLN

THR

TYR

VAL

THR

ASN

LEU

ASN

5

LEU

ILE

LYS

GLY

THR

ALA

PHE

GLU

GLY

LYS

6

SER

LEU

GLU

ILE

ARG

SER

GLU

7

GLY

VAL

PHE

ASN

ALA

GLN

VAL

8

TRP

ASN

HIS

TRP

PHE

TYR

TRP

ASN

CYS

LEU

9

ALA

PRO

ASN

ALA

GLY

GLU

PRO

THR

GLY

10

LYS

VAL

ALA

GLU

ALA

ILE

ALA

SER

PHE

11

GLY

SER

PHE

ALA

ASP

PHE

LYS

ALA

GLN

PHE

12

THR

ASP

ALA

ILE

LYS

ASN

PHE

GLY

SER

13

GLY

TRP

THR

TRP

LEU

VAL

LYS

ASN

SER

ASP

14

GLY

LYS

LEU

ALA

ILE

VAL

SER

THR

SER

ASN

15

ALA

GLY

THR

PRO

LEU

THR

ASP

ALA

THR

16

PRO

LEU

THR

VAL

ASP

VAL

TRP

GLU

HIS

17

ALA

TYR

ILE

ASP

TYR

ARG

ASN

ALA

ARG

18

PRO

GLY

TYR

LEU

GLU

HIS

PHE

TRP

ALA

LEU

19

VAL

ASN

TRP

GLU

PHE

VAL

ALA

LYS

ASN

LEU

20

ALA

Entity 2, Fe(II) monomer 1 - Fe - 55.845 Da.

1

FE

Entity 3, H2O monomer 1 - 18.015 Da.

1

HOH

Samples:

sample_1: Fe-superoxide dismutase, [U-99% 2H, U-99% 13C, U-99% 15N], 1.57 mM

Ex-cond_1: pH: 6.46 na; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
HNCA	sample_1	not available	Ex-cond_1
HN(CO)CA	sample_1	not available	Ex-cond_1
HN(CA)CB	sample_1	not available	Ex-cond_1
HN(COCA)CB	sample_1	not available	Ex-cond_1
HN(CO)CACB	sample_1	not available	Ex-cond_1
HNCO	sample_1	not available	Ex-cond_1
HSQC	sample_1	not available	Ex-cond_1

Software:

nmrPipe v1.6 - processed NMR data

ANSIG v3.3 - made peak assignments

NMR spectrometers:

Varian Unity-Plus 500 MHz

BMRB	4315
PDB	1ISA 1ISB 1ISC 1ZA5 2BKB 2NYB
DBJ	BAA15422 BAA84485 BAA84490 BAB35788 BAG77304
EMBL	CAP76155 CAQ32133 CAQ88908 CAQ98565 CAR03017
GB	AAA24637 AAC74728 AAG56645 AAN43263 AAN80510
REF	NP_310392 NP_416173 NP_707556 WP_000007270 WP_000007272
SP	P0AGD3 P0AGD4 P0AGD5 P0AGD6
AlphaFold	P0AGD3 P0AGD4 P0AGD5 P0AGD6