BMRB Entry 15603

Name: SOLUTION NMR STRUCTURE OF LIPOPROTEIN SPR FROM ESCHERICHIA COLI K12. NORTHEAST STRUCTURAL GENOMICS TARGET ER541-37-162
Published: 2008-03-04

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PDB ID: 2k1g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15603
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

SOLUTION NMR STRUCTURE OF LIPOPROTEIN SPR FROM ESCHERICHIA COLI K12. NORTHEAST STRUCTURAL GENOMICS TARGET ER541-37-162

Deposition date:

2007-12-20

Original release date:

2008-03-04

Authors:

Aramini, James; Zhao, Li; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, GVT; Huang, Yuanpeng; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation:

Citation: Aramini, James; Rossi, Paolo; Huang, Yuanpeng; Zhao, Li; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Locke, Jessica; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Inouye, Masayori; Montelione, Gaetano. "Solution NMR Structure of the NlpC/P60 Domain of Lipoprotein Spr from Escherichia coli: Structural Evidence for a Novel Cysteine Peptidase Catalytic Triad" Biochemistry 47, 9715-9717 (2008).
PubMed: 18715016

Assembly members:

Assembly members:
ER541-37-162, polymer, 136 residues, 15724.854 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 Host organism: Escherichia coli Vector: ER541-37-162-21.1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ER541-37-162: MNVDVKSRIMDQYADWKGVR YRLGGSTKKGIDCSGFVQRT FREQFGLELPRSTYEQQEMG KSVSRSNLRTGDLVLFRAGS TGRHVGIYIGNNQFVHASTS SGVIISSMNEPYWKKRYNEA RRVLSRSLEHHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	580
15N chemical shifts	135
1H chemical shifts	897

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 136 residues - 15724.854 Da.

C-terminal LEHHHHHH purifcation tag starting at residue 163.

1

MET

ASN

VAL

ASP

VAL

LYS

SER

ARG

ILE

MET

2

ASP

GLN

TYR

ALA

ASP

TRP

LYS

GLY

VAL

ARG

3

TYR

ARG

LEU

GLY

SER

THR

LYS

GLY

4

ILE

ASP

CYS

SER

GLY

PHE

VAL

GLN

ARG

THR

5

PHE

ARG

GLU

GLN

PHE

GLY

LEU

GLU

LEU

PRO

6

ARG

SER

THR

TYR

GLU

GLN

GLU

MET

GLY

7

LYS

SER

VAL

SER

ARG

SER

ASN

LEU

ARG

THR

8

GLY

ASP

LEU

VAL

LEU

PHE

ARG

ALA

GLY

SER

9

THR

GLY

ARG

HIS

VAL

GLY

ILE

TYR

ILE

GLY

10

ASN

GLN

PHE

VAL

HIS

ALA

SER

THR

SER

11

SER

GLY

VAL

ILE

SER

MET

ASN

GLU

12

PRO

TYR

TRP

LYS

ARG

TYR

ASN

GLU

ALA

13

ARG

VAL

LEU

SER

ARG

SER

LEU

GLU

HIS

14

HIS

Samples:

sample_1: ER541-37-162, [U-100% 13C; U-100% 15N], 1.07 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_2: ER541-37-162, [U-100% 13C; U-100% 15N], 1.07 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_3: ER541-37-162, [U-5% 13C; U-100% 15N], 1.03 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; 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 (aliph)	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D simultaneous CN NOESY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D simultaneous CN NOESY	sample_2	isotropic	sample_conditions_1
3D CCcoNH TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY aliphatic	sample_1	isotropic	sample_conditions_1
HNHA	sample_1	isotropic	sample_conditions_1
2D 1H-13C high res. (L/V stereospecific assignment) (aliph)	sample_3	isotropic	sample_conditions_1
2D 1H-15N hetNOE	sample_3	isotropic	sample_conditions_1
2D 1H-13C high res. (L/V stereospecific assignment) (arom)	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC (arom)	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

VNMR v6.1C, Varian - collection

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF validation

PSVS v1.3, Bhattacharya and Montelione - structure validation

PDBStat v5.0, Tejero and Montelione - PDB analysis

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz

PDB	2K1G
DBJ	BAA13140 BAA15983 BAB36490 BAG77968 BAI26300
EMBL	CAP76677 CAQ32581 CAQ89766 CAQ99102 CAR03606
GB	AAC75236 AAG57313 AAN43781 AAN81166 AAP17598
REF	NP_311094 NP_416680 NP_708074 WP_000241007 WP_000241008
SP	P0AFV4 P0AFV5 P0AFV6 P0AFV7
AlphaFold	P0AFV4 P0AFV5 P0AFV6 P0AFV7