BMRB Entry 19836

Name: NMR structure of E. coli Trigger Factor in complex with unfolded PhoA1-150
Published: 2014-05-20

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PDB ID: 2mly
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19836
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of E. coli Trigger Factor in complex with unfolded PhoA1-150 PubMed: 24812405

Deposition date: 2014-03-05 Original release date: 2014-05-20

Authors: Saio, Tomohide; Guan, Xiao; Rossi, Paolo; Economou, Anastassios; Kalodimos, Charalampos

Citation: Saio, Tomohide; Guan, Xiao; Rossi, Paolo; Economou, Anastassios; Kalodimos, Charalampos. "Structural basis for protein antiaggregation activity of the trigger factor chaperone" Science 344, 1250494-1250494 (2014).

Assembly members:
entity_1, polymer, 151 residues, 16862.254 Da.
entity_2, polymer, 443 residues, 48256.020 Da.

Natural source: Common Name: E. coli Taxonomy ID: 469008 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
entity_1: HMKQSTIALALLPLLFTPVT KARTPEMPVLENRAAQGDIT APGGARRLTGDQTAALRDSL SDKPAKNIILLIGDGMGDSE ITAARNYAEGAGGFFKGIDA LPLTGQYTHYALNKKTGKPD YVTDSAASATAWSTGVKTYN GALGVDIHEKD
entity_2: MNHKVHHHHHHMQVSVETTQ GLGRRVTITIAADSIETAVK SELVNVAKKVRIDGFRKGKV PMNIVAQRYGASVRQDVLGD LMSRNFIDAIIKEKINPAGA PTYVPGEYKLGEDFTYSVEF EVYPEVELQGLEAIEVEKPI VEVTDADVDGMLDTLRKQQA TWKEKDGAVEAEDRVTIDFT GSVDGEEFEGGKASDFVLAM GQGRMIPGFEDGIKGHKAGE EFTIDVTFPEEYHAENLKGK AAKFAINLKKVEERELPELT AEFIKRFGVEDGSVEGLRAE VRKNMERELKSAIRNRVKSQ AIEGLVKANDIDVPAALIDS EIDVLRRQAAQRFGGNEKQA LELPRELFEEQAKRRVVVGL LLGEVIRTNELKADEERVKG LIEEMASAYEDPKEVIEFYS KNKELMDNMRNVALEEQAVE AVLAKAKVTEKETTFNELMN QQA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_1_dup

Data type	Count
13C chemical shifts	565
15N chemical shifts	479
1H chemical shifts	1638

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 151 residues - 16862.254 Da.

1

HIS

MET

LYS

GLN

SER

THR

ILE

ALA

LEU

ALA

2

LEU

PRO

LEU

PHE

THR

PRO

VAL

THR

3

LYS

ALA

ARG

THR

PRO

GLU

MET

PRO

VAL

LEU

4

GLU

ASN

ARG

ALA

GLN

GLY

ASP

ILE

THR

5

ALA

PRO

GLY

ALA

ARG

LEU

THR

GLY

6

ASP

GLN

THR

ALA

LEU

ARG

ASP

SER

LEU

7

SER

ASP

LYS

PRO

ALA

LYS

ASN

ILE

LEU

8

LEU

ILE

GLY

ASP

GLY

MET

GLY

ASP

SER

GLU

9

ILE

THR

ALA

ARG

ASN

TYR

ALA

GLU

GLY

10

ALA

GLY

PHE

LYS

GLY

ILE

ASP

ALA

11

LEU

PRO

LEU

THR

GLY

GLN

TYR

THR

HIS

TYR

12

ALA

LEU

ASN

LYS

THR

GLY

LYS

PRO

ASP

13

TYR

VAL

THR

ASP

SER

ALA

SER

ALA

THR

14

ALA

TRP

SER

THR

GLY

VAL

LYS

THR

TYR

ASN

15

GLY

ALA

LEU

GLY

VAL

ASP

ILE

HIS

GLU

LYS

16

ASP

Entity 2, entity_2 443 residues - 48256.020 Da.

1

MET

ASN

HIS

LYS

VAL

HIS

2

HIS

MET

GLN

VAL

SER

VAL

GLU

THR

GLN

3

GLY

LEU

GLY

ARG

VAL

THR

ILE

THR

ILE

4

ALA

ASP

SER

ILE

GLU

THR

ALA

VAL

LYS

5

SER

GLU

LEU

VAL

ASN

VAL

ALA

LYS

VAL

6

ARG

ILE

ASP

GLY

PHE

ARG

LYS

GLY

LYS

VAL

7

PRO

MET

ASN

ILE

VAL

ALA

GLN

ARG

TYR

GLY

8

ALA

SER

VAL

ARG

GLN

ASP

VAL

LEU

GLY

ASP

9

LEU

MET

SER

ARG

ASN

PHE

ILE

ASP

ALA

ILE

10

ILE

LYS

GLU

LYS

ILE

ASN

PRO

ALA

GLY

ALA

11

PRO

THR

TYR

VAL

PRO

GLY

GLU

TYR

LYS

LEU

12

GLY

GLU

ASP

PHE

THR

TYR

SER

VAL

GLU

PHE

13

GLU

VAL

TYR

PRO

GLU

VAL

GLU

LEU

GLN

GLY

14

LEU

GLU

ALA

ILE

GLU

VAL

GLU

LYS

PRO

ILE

15

VAL

GLU

VAL

THR

ASP

ALA

ASP

VAL

ASP

GLY

16

MET

LEU

ASP

THR

LEU

ARG

LYS

GLN

ALA

17

THR

TRP

LYS

GLU

LYS

ASP

GLY

ALA

VAL

GLU

18

ALA

GLU

ASP

ARG

VAL

THR

ILE

ASP

PHE

THR

19

GLY

SER

VAL

ASP

GLY

GLU

PHE

GLU

GLY

20

GLY

LYS

ALA

SER

ASP

PHE

VAL

LEU

ALA

MET

21

GLY

GLN

GLY

ARG

MET

ILE

PRO

GLY

PHE

GLU

22

ASP

GLY

ILE

LYS

GLY

HIS

LYS

ALA

GLY

GLU

23

GLU

PHE

THR

ILE

ASP

VAL

THR

PHE

PRO

GLU

24

GLU

TYR

HIS

ALA

GLU

ASN

LEU

LYS

GLY

LYS

25

ALA

LYS

PHE

ALA

ILE

ASN

LEU

LYS

26

VAL

GLU

ARG

GLU

LEU

PRO

GLU

LEU

THR

27

ALA

GLU

PHE

ILE

LYS

ARG

PHE

GLY

VAL

GLU

28

ASP

GLY

SER

VAL

GLU

GLY

LEU

ARG

ALA

GLU

29

VAL

ARG

LYS

ASN

MET

GLU

ARG

GLU

LEU

LYS

30

SER

ALA

ILE

ARG

ASN

ARG

VAL

LYS

SER

GLN

31

ALA

ILE

GLU

GLY

LEU

VAL

LYS

ALA

ASN

ASP

32

ILE

ASP

VAL

PRO

ALA

LEU

ILE

ASP

SER

33

GLU

ILE

ASP

VAL

LEU

ARG

GLN

ALA

34

GLN

ARG

PHE

GLY

ASN

GLU

LYS

GLN

ALA

35

LEU

GLU

LEU

PRO

ARG

GLU

LEU

PHE

GLU

36

GLN

ALA

LYS

ARG

VAL

GLY

LEU

37

LEU

GLY

GLU

VAL

ILE

ARG

THR

ASN

GLU

38

LEU

LYS

ALA

ASP

GLU

ARG

VAL

LYS

GLY

39

LEU

ILE

GLU

MET

ALA

SER

ALA

TYR

GLU

40

ASP

PRO

LYS

GLU

VAL

ILE

GLU

PHE

TYR

SER

41

LYS

ASN

LYS

GLU

LEU

MET

ASP

ASN

MET

ARG

42

ASN

VAL

ALA

LEU

GLU

GLN

ALA

VAL

GLU

43

ALA

VAL

LEU

ALA

LYS

ALA

LYS

VAL

THR

GLU

44

LYS

GLU

THR

PHE

ASN

GLU

LEU

MET

ASN

45

GLN

ALA

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.5 mM; entity_2, [U-100% 13C; U-100% 15N], 0.5 mM; potassium chloride 100 mM; BME 3 mM; potassium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-13C HMQC-NOESY_HMQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HMQC	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

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

SPARKY v3.113, Goddard - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

OLIVIA v1.16, Olivia, Yokochi Masashi - chemical shift assignment

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN v3.1, Bruker Biospin - collection

VNMRJ, Varian - collection

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TALOSN, Shen and Bax - geometry optimization

PSVS v1.5, Bhattacharya and Montelione - validation

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz
Varian INOVA 600 MHz
Varian INOVA 800 MHz

PDB	1AJA 1AJB 1AJC 1AJD 1ALH 1ALI 1ALJ 1ALK 1ANI 1ANJ 1B8J 1ED8 1ED9 1ELX 1ELY 1ELZ 1EW8 1EW9 1HJK 1HQA 1KH4 1KH5 1KH7 1KH9 1KHJ 1KHK 1KHL 1KHN 1URA 1URB 1Y6V 1Y7A 2ANH 2G9Y 2GA3 2MLY 3BDF 3BDG 3BDH 3CMR 3DPC 3DYC 3TG0 4KM4 4YR1 1W26 2MLX 2MLY 2MLZ 2VRH
DBJ	BAB33856 BAE76164 BAG75928 BAI23756 BAI29227 BAB33913 BAD98926 BAE76216 BAG75986 BAI23810
EMBL	CAA28257 CAP74918 CAQ30851 CAQ97255 CAR01727 CAP74970 CAQ30908 CAQ97312 CAR01780 CAR06670
GB	AAA24359 AAA24363 AAA24364 AAA24365 AAA24366 AAA62791 AAB40192 AAC73539 AAG54786 AAN42037
REF	NP_308460 NP_414917 NP_706185 WP_000089619 WP_000089625 NP_286178 NP_308517 NP_414970 NP_706330 NP_752485
SP	P00634 A1A8A5 A7ZIJ4 A7ZX94 B1J012 B1LJJ3
BMRB	19835 19837

Biological Magnetic Resonance Data Bank