BMRBj - BMREntryMaster

Found 1 Document (0.387 seconds)

BMRB: 30800

3HR6

Solution Structure of the Corynebacterium diphtheriae SpaA Pilin-Signal Peptide Complex

Authors

McConnell, S.A., Clubb, R.T.

Assembly

Putative surface-anchored fimbrial subunit, SpaA sorting signal peptide

Entity

1. Putative surface-anchored fimbrial subunit, SpaA sorting signal peptide, entity 1 (polymer, Thiol state: not present), 143 monomers, 15382.24 Da Detail

ERTSIAVHAL MGLPTGQPAN GTKLDSIGLP KVDGMSFTLY RVNEIDLTTQ AGWDAASKIK LEELYTNGHP TDKVTKVATK KTEGGVAKFD NLTPALYLVV QELNGAEAVV RSQPFLVAAP QTNPTGDGWL QDVHVYPKHQ ALS

2. Putative surface-anchored fimbrial subunit, SpaA sorting signal peptide, entity 2 (polymer, Thiol state: not present), 10 monomers, 1089.241 Da Detail

KNAGFELPLT

Total weight

16471.48 Da

Max. entity weight

15382.24 Da

Source organism

Corynebacterium diphtheriae NCTC 13129 , Corynebacterium diphtheriae

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 86.7 %, Completeness (bb): 92.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.7 % (1504 of 1735)	85.7 % (764 of 891)	88.0 % (600 of 682)	86.4 % (140 of 162)
Backbone	92.5 % (831 of 898)	94.8 % (293 of 309)	91.7 % (409 of 446)	90.2 % (129 of 143)
Sidechain	81.6 % (797 of 977)	80.4 % (468 of 582)	84.6 % (318 of 376)	57.9 % (11 of 19)
Aromatic	57.1 % (64 of 112)	60.7 % (34 of 56)	51.9 % (28 of 54)	100.0 % (2 of 2)
Methyl	90.8 % (178 of 196)	92.9 % (91 of 98)	88.8 % (87 of 98)

1. entity 1

ERTSIAVHAL MGLPTGQPAN GTKLDSIGLP KVDGMSFTLY RVNEIDLTTQ AGWDAASKIK LEELYTNGHP TDKVTKVATK KTEGGVAKFD NLTPALYLVV QELNGAEAVV RSQPFLVAAP QTNPTGDGWL QDVHVYPKHQ ALS

2. entity 2

KNAGFELPLT

Show sample condition

Sample #1

Solvent system 92% H2O, 8% D2O, Pressure 1 null, Temperature 298 K, pH 6.0, Details 1.2 mM [U-13C; U-15N] SpaA backbone pilin for protein, 1.2 mM SpaA sorting signal for peptide, 50 mM NaH2PO4, 100 mM NaCl, 0.01 % NaN3, 92% H2O, 8% D2O

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

Sample #2

Solvent system 100% D2O, Pressure 1 null, Temperature 298 K, pH 6.0, Details 1.2 mM [U-13C; U-15N] SpaA backbone pilin for protein, 1.2 mM SpaA sorting signal for peptide, 50 mM NaH2PO4, 100 mM NaCl, 0.01 % NaN3, 100% D2O

#	Name	Isotope labeling	Concentration
6	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
7	SpaA sorting signal for peptide	natural abundance	1.2 mM
8	NaH2PO4	natural abundance	50 mM
9	NaCl	natural abundance	100 mM
10	NaN3	natural abundance	0.01 %

Release date

2020-10-14

Citation

Sortase-assembled pili in Corynebacterium diphtheriae are built using a latch mechanism
McConnell, S.A., McAllister, R.A., Amer, B.A., Mahoney, B.J., Sue, C.K., Chang, C., Ton-That, H., Clubb, R.T.
Proc. Natl. Acad. Sci. U. S. A. (2021), 118, PubMed 33723052 , DOI 10.1073/pnas.2019649118 , Abstract

Related entities 1. Putative surface-anchored fimbrial subunit, SpaA sorting signal peptide, entity 1, : 1 : 1 : 1 : 3 entities Detail

Related entities 2. Putative surface-anchored fimbrial subunit, SpaA sorting signal peptide, entity 2, : 1 entities Detail

Experiments performed 24 experiments Detail

1 3D_15N-separated_NOESY

Instrument

Bruker AVANCE NEO - 800 MHz

Sample

State isotropic, Solvent system 92% H2O, 8% D2O, Pressure 1 null, Temperature 298 K, pH 6.0, Details 1.2 mM [U-13C; U-15N] SpaA backbone pilin for protein, 1.2 mM SpaA sorting signal for peptide, 50 mM NaH2PO4, 100 mM NaCl, 0.01 % NaN3, 92% H2O, 8% D2O

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

2 3D_(F1)_13C,15N-filtered_(F2)_15N-edited NOESY-HSQC

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

3 2D 1H-15N HSQC

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

4 2D 1H-13C HSQC

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 null, Temperature 298 K, pH 6.0, Details 1.2 mM [U-13C; U-15N] SpaA backbone pilin for protein, 1.2 mM SpaA sorting signal for peptide, 50 mM NaH2PO4, 100 mM NaCl, 0.01 % NaN3, 100% D2O

#	Name	Isotope labeling	Concentration
6	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
7	SpaA sorting signal for peptide	natural abundance	1.2 mM
8	NaH2PO4	natural abundance	50 mM
9	NaCl	natural abundance	100 mM
10	NaN3	natural abundance	0.01 %

5 2D 1H-13C HSQC aromatic

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
6	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
7	SpaA sorting signal for peptide	natural abundance	1.2 mM
8	NaH2PO4	natural abundance	50 mM
9	NaCl	natural abundance	100 mM
10	NaN3	natural abundance	0.01 %

6 3D HNCACB

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

7 1H-15N heteronoe

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

8 3D CBCA(CO)NH

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

9 T2/R2 relaxation

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

10 T1/R1 relaxation

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

11 3D HN(CA)CO

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

12 3D HNCA

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

13 3D HNCO

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

14 3D HCCH-COSY

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
6	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
7	SpaA sorting signal for peptide	natural abundance	1.2 mM
8	NaH2PO4	natural abundance	50 mM
9	NaCl	natural abundance	100 mM
10	NaN3	natural abundance	0.01 %

15 3D HNHA

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

16 3D HBHA(CO)NH

Instrument

Bruker AVANCE NEO - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

17 3D 1H-15N TOCSY

Instrument

Bruker AVANCE NEO - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

18 3D H(CCO)NH

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

19 2D (F1,F2) 13C-filtered NOESY

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
6	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
7	SpaA sorting signal for peptide	natural abundance	1.2 mM
8	NaH2PO4	natural abundance	50 mM
9	NaCl	natural abundance	100 mM
10	NaN3	natural abundance	0.01 %

20 2D (F1) 13C,15N-filtered TOCSY

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
6	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
7	SpaA sorting signal for peptide	natural abundance	1.2 mM
8	NaH2PO4	natural abundance	50 mM
9	NaCl	natural abundance	100 mM
10	NaN3	natural abundance	0.01 %

21 3D_(F1)_13C,15N-filtered_(F2)_13C-edited NOESY-HSQC

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
6	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
7	SpaA sorting signal for peptide	natural abundance	1.2 mM
8	NaH2PO4	natural abundance	50 mM
9	NaCl	natural abundance	100 mM
10	NaN3	natural abundance	0.01 %

22 3D_13C-separated_NOESY_aliphatic_D2O

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
6	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
7	SpaA sorting signal for peptide	natural abundance	1.2 mM
8	NaH2PO4	natural abundance	50 mM
9	NaCl	natural abundance	100 mM
10	NaN3	natural abundance	0.01 %

23 3D_13C-separated_NOESY_aromatic_D2O

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
6	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
7	SpaA sorting signal for peptide	natural abundance	1.2 mM
8	NaH2PO4	natural abundance	50 mM
9	NaCl	natural abundance	100 mM
10	NaN3	natural abundance	0.01 %

24 3D_13C-separated_NOESY_aliphatic_H2O

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	SpaA backbone pilin for protein	[U-13C; U-15N]	1.2 mM
2	SpaA sorting signal for peptide	natural abundance	1.2 mM
3	NaH2PO4	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	NaN3	natural abundance	0.01 %

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30800_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr30800_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1691		99.3 (chain: 1, length: 143), 100.0 (chain: 2, length: 10)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 143, Sequence coverage: 99.3%
  - Entity_assembly_ID: 2, Chain length: 10, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 954
  - ¹³C chemical shifts: 600
  - ¹⁵N chemical shifts: 137
- Completeness of assignments
  - Entity_assemble_ID: 1
  - Entity_assemble_ID: 2
- Peptide bond of PRO
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
  - Chain_ID: 2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	829	715	86.2
¹³C chemical shifts	635	600	94.5
¹⁵N chemical shifts	152	137	90.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	289	276	95.5
¹³C chemical shifts	286	281	98.3
¹⁵N chemical shifts	134	126	94.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	540	439	81.3
¹³C chemical shifts	349	319	91.4
¹⁵N chemical shifts	18	11	61.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	94	89	94.7
¹³C chemical shifts	94	90	95.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	51	31	60.8
¹³C chemical shifts	49	28	57.1
¹⁵N chemical shifts	2	2	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	62	49	79.0
¹³C chemical shifts	47	0	0.0
¹⁵N chemical shifts	10	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	20	18	90.0
¹³C chemical shifts	20	0	0.0
¹⁵N chemical shifts	9	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	42	31	73.8
¹³C chemical shifts	27	0	0.0
¹⁵N chemical shifts	1	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	6	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	3	60.0
¹³C chemical shifts	5	0	0.0

Keywords CELL ADHESION, Gram-positive bacteria, backbone pilin, lysine isopeptide bond, pili, sortase

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Found 1 Document (0.387 seconds)

BMRB: 30800

Sample #1

Sample #2

Related entities 1. Putative surface-anchored fimbrial subunit, SpaA sorting signal peptide, entity 1, : 1 : 1 : 1 : 3 entities Detail

Related entities 2. Putative surface-anchored fimbrial subunit, SpaA sorting signal peptide, entity 2, : 1 entities Detail

Experiments performed 24 experiments Detail

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Chemical shift validation 4 contents Detail