BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	78.4 % (145 of 185)	92.7 % (89 of 96)	58.9 % (43 of 73)	81.3 % (13 of 16)
Backbone	71.9 % (69 of 96)	96.9 % (31 of 32)	52.0 % (26 of 50)	85.7 % (12 of 14)
Sidechain	84.8 % (89 of 105)	90.6 % (58 of 64)	76.9 % (30 of 39)	50.0 % (1 of 2)
Aromatic	85.7 % (24 of 28)	100.0 % (14 of 14)	69.2 % (9 of 13)	100.0 % (1 of 1)
Methyl	100.0 % (6 of 6)	100.0 % (3 of 3)	100.0 % (3 of 3)

1. entity 1

AACHNHAPXM PPXYWEGEC

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 (±0) atm, Temperature 298 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

Sample #2

Solvent system 100% D2O, Pressure 1 (±0) atm, Temperature 298 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

Sample #3

Solvent system 100% D2O, Pressure 1 (±0) atm, Temperature 298 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 100% D2O

#	Name	Isotope labeling	Type	Concentration
3	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

Protein Blocks Logo

Calculated from 20 models in PDB: 6VLJ, Strand ID: A Detail

Release date

2020-01-23

Citation 1

Structural characterization of four prochlorosins: a novel class of lantipeptides produced by planktonic marine cyanobacteria
Tang, W., van der Donk, W.A.
Biochemistry (2012), 51, 4271-4279, PubMed 22574919 , DOI 10.1021/bi300255s , Abstract

Show more 3 citaions

Citation 2

Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobacteria
Li, B., Sher, D., Kelly, L., Shi, Y., Huang, K., Knerr, P.J., Joewono, I., Rusch, D., Chisholm, S.W., van der Donk, W.A.
Proc. Natl. Acad. Sci. U. S. A. (2010), 107, 10430-10435, PubMed 20479271 , DOI 10.1073/pnas.0913677107 , Abstract

Citation 3

Evolutionary radiation of lanthipeptides in marine cyanobacteria
Cubillos-Ruiz, A., Berta-Thompson, J.W., Becker, J.W., van der Donk, W.A., Chisholm, S.W.
Proc. Natl. Acad. Sci. U. S. A. (2017), 114, E5424-E5433, PubMed 28630351 , DOI 10.1073/pnas.1700990114 , Abstract

Citation 4

Structural determinants of macrocyclization in substrate-controlled lanthipeptide biosynthetic pathways
Bobeica, S.C., Zhu, L., Acedo, J.Z., Tang, W., van der Donk, W.A.
Chem. Sci. (2020), 11, 12854-12870, PubMed 34094481 , DOI 10.1039/d0sc01651a , Abstract

Hide non-primary 3 citaions

Entries sharing articles BMRB: 4 entries Detail

  BMRB: 30789 released on 2020-09-02
    Title Solution NMR structure of Prochlorosin 2.11 (Pcn2.11) produced by Prochlorococcus MIT 9313
  BMRB: 30714 released on 2020-01-20
    Title Solution NMR structure of Prochlorosin 2.1 produced by Prochlorococcus MIT 9313
  BMRB: 30713 released on 2020-01-14
    Title Solution NMR structure of Prochlorosin 2.10 produced by Prochlorococcus MIT 9313
  BMRB: 30712 released on 2020-01-12
    Title Solution NMR of Prochlorosin 1.1 produced by Prochlorococcus MIT 9313

Related entities 1. Prochlorosin 2.8, : 1 : 1 entities Detail

Experiments performed 8 experiments Detail

1 2D 1H-1H TOCSY

Instrument

Agilent VNMRS - 750 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 (±0) atm, Temperature 298 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

2 2D 1H-1H NOESY

Instrument

Agilent VNMRS - 750 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 (±0) atm, Temperature 298 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

3 2D 1H-1H TOCSY

Instrument

Agilent VNMRS - 750 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±0) atm, Temperature 298 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

4 2D 1H-1H NOESY

Instrument

Agilent VNMRS - 750 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±0) atm, Temperature 298 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

5 2D 1H-13C HSQC

Instrument

Agilent VNMRS - 750 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±0) atm, Temperature 298 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

6 2D 1H-15N HSQC

Instrument

Agilent VNMRS - 750 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±0) atm, Temperature 298 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

7 2D 1H-1H TOCSY

Instrument

Agilent VNMRS - 750 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±0) atm, Temperature 310 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 100% D2O

#	Name	Isotope labeling	Type	Concentration
3	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

8 2D 1H-1H NOESY

Instrument

Agilent VNMRS - 750 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±0) atm, Temperature 310 (±0.1) K, pH 6.0 (±0.1), Details 33 mM Prochlorosin 2.8, 100% D2O

#	Name	Isotope labeling	Type	Concentration
3	Prochlorosin 2.8	natural abundance		33 (±0.3) mM

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_30718_6vlj.nef
Input source #2: Coordindates	6vlj.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:3:CYS:SG	1:9:DAL:CB	unknown	unknown	n/a
1:8:PRO:C	1:9:DAL:N	unknown	unknown	n/a
1:9:DAL:C	1:10:MET:N	unknown	unknown	n/a
1:12:PRO:C	1:13:DAL:N	unknown	unknown	n/a
1:13:DAL:CB	1:19:CYS:SG	unknown	unknown	n/a
1:13:DAL:C	1:14:TYR:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	9	DAL	D-ALANINE	Assigned chemical shifts, Distance restraints, Coordinates
A	13	DAL	D-ALANINE	Assigned chemical shifts, Distance restraints, Coordinates

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10---------
AACHNHAPXMPPXYWEGEC
|||||||||||||||||||
AACHNHAPXMPPXYWEGEC

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	19	0	0	100.0

Content subtype: combined_30718_6vlj.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	6		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	153		100.0 (chain: A, length: 19)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	175 (1)	noe	100.0 (chain: A, length: 19)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 19, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 97
  - ¹³C chemical shifts: 41
  - ¹⁵N chemical shifts: 15
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	102	95	93.1
¹³C chemical shifts	77	41	53.2
¹⁵N chemical shifts	18	15	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	36	35	97.2
¹³C chemical shifts	36	11	30.6
¹⁵N chemical shifts	16	14	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	66	60	90.9
¹³C chemical shifts	41	30	73.2
¹⁵N chemical shifts	2	1	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	5	83.3
¹³C chemical shifts	6	3	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	14	100.0
¹³C chemical shifts	13	9	69.2
¹⁵N chemical shifts	1	1	100.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 19, Sequence coverage: 100.0%
- Total number of restraints: 175
- Weight of restraints: 1.0 (175)
- Potential type of restraints: square-well-parabolic (175)
- Range of distance target values: 3.15, 4.4 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords RiPP, UNKNOWN FUNCTION, cyclic peptide, lanthipeptide, posttranslational modification

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BMRB: 30718

Sample #1

Sample #2

Sample #3

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. Prochlorosin 2.8, : 1 : 1 entities Detail

Experiments performed 8 experiments Detail

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NMR combined restraints 3 contents Detail