BMRBj - BMREntryMaster

Found 1 Document (0.443 seconds)

BMRB: 19422

2MC0

Structural Basis of a Thiopeptide Antibiotic Multidrug Resistance System from Streptomyces lividans:Nosiheptide in Complex with TipAS

Authors

Habazettl, J., Allan, M.G., Jensen, P., Sass, H., Grzesiek, S.

Assembly

Nosiheptide in Complex with TipAS

Entity

1. TipAS (polymer, Thiol state: free and other bound), 144 monomers, 16562.92 Da Detail

MGINLTPEEK FEVFGDFDPD QYEEEVRERW GNTDAYRQSK EKTASYTKED WQRIQDEADE LTRRFVALMD AGEPADSEGA MDAAEDHRQG IARNHYDCGY EMHTCLGEMY VSDERFTRNI DAAKPGLAAY MRDAILANAV RHTP

2. nosiheptide (polymer, Thiol state: all free), 14 monomers, 1382.501 Da Detail

SXTXXXXCXX XXXX

Total weight

17945.422 Da

Max. entity weight

16562.92 Da

Source organism

Streptomyces lividans , Streptomyces actuosus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.8 %, Completeness: 95.1 %, Completeness (bb): 95.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	95.1 % (1571 of 1652)	95.9 % (825 of 860)	93.9 % (599 of 638)	95.5 % (147 of 154)
Backbone	95.6 % (834 of 872)	97.7 % (291 of 298)	93.8 % (405 of 432)	97.2 % (138 of 142)
Sidechain	94.6 % (868 of 918)	95.0 % (534 of 562)	94.5 % (325 of 344)	75.0 % (9 of 12)
Aromatic	98.6 % (144 of 146)	98.6 % (72 of 73)	98.6 % (70 of 71)	100.0 % (2 of 2)
Methyl	95.7 % (111 of 116)	96.6 % (56 of 58)	94.8 % (55 of 58)

1. TipAS

MGINLTPEEK FEVFGDFDPD QYEEEVRERW GNTDAYRQSK EKTASYTKED WQRIQDEADE LTRRFVALMD AGEPADSEGA MDAAEDHRQG IARNHYDCGY EMHTCLGEMY VSDERFTRNI DAAKPGLAAY MRDAILANAV RHTP

2. nosiheptide

SXTXXXXCXXX

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 15 N labeled TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
1	TipAS	[U-98% 15N]	1 mM
2	nosiheptide	natural abundance	2 mM
3	potassium phosphate	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 w/v
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS, nosiheptide in Deuterium

#	Name	Isotope labeling	Concentration
13	TipAS	[U-99% 13C; U-99% 15N]	1 mM
14	nosiheptide	natural abundance	2 mM
15	potassium phosphate	natural abundance	50 mM
16	sodium azide	natural abundance	0.02 w/v
17	D2O	natural abundance	100 %

Sample #4

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS, nosiheptide, in Pf1 phage

#	Name	Isotope labeling	Concentration
18	TipAS	[U-99% 13C; U-99% 15N]	0.8 mM
19	nosiheptide	natural abundance	1.6 mM
20	potassium phosphate	natural abundance	10 mM
21	Pf1 phage	natural abundance	10 mg/mL
22	H2O	natural abundance	95 %
23	D2O	natural abundance	5 %

Release date

2014-12-07

Citation

Structural Basis of a Thiopeptide Antibiotic Multidrug Resistance System from Streptomyces lividans
Habazettl, J., Allan, M., Jensen, P., Sass, J., Grzesiek, S.
Not known

Related entities 1. TipAS, : 1 : 3 entities Detail

Experiments performed 20 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 15 N labeled TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
1	TipAS	[U-98% 15N]	1 mM
2	nosiheptide	natural abundance	2 mM
3	potassium phosphate	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 w/v
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

2 2D 1H-13C HSQC aliphatic

Instrument

Bruker DRX - 800 MHz TCI probe head

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, Details 13C-15N TipAS, nosiheptide in Deuterium

#	Name	Isotope labeling	Concentration
13	TipAS	[U-99% 13C; U-99% 15N]	1 mM
14	nosiheptide	natural abundance	2 mM
15	potassium phosphate	natural abundance	50 mM
16	sodium azide	natural abundance	0.02 w/v
17	D2O	natural abundance	100 %

3 3D HNCO

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

4 3D CBCA(CO)NH

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

5 3D C(CO)NH

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

6 3D HBHA(CO)NH

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

7 3D HC(CO)NH TOCSY

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

8 3D HCCH-TOCSY

Instrument

Bruker DRX - 800 MHz TCI probe head

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, Details 13C-15N TipAS, nosiheptide in Deuterium

#	Name	Isotope labeling	Concentration
13	TipAS	[U-99% 13C; U-99% 15N]	1 mM
14	nosiheptide	natural abundance	2 mM
15	potassium phosphate	natural abundance	50 mM
16	sodium azide	natural abundance	0.02 w/v
17	D2O	natural abundance	100 %

9 3D HNHA

Instrument

Bruker DRX - 800 MHz TCI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 15 N labeled TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
1	TipAS	[U-98% 15N]	1 mM
2	nosiheptide	natural abundance	2 mM
3	potassium phosphate	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 w/v
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

10 3D 1H-15N NOESY

Instrument

Bruker DRX - 800 MHz TCI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 15 N labeled TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
1	TipAS	[U-98% 15N]	1 mM
2	nosiheptide	natural abundance	2 mM
3	potassium phosphate	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 w/v
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

11 3D 1H-13C NOESY aliphatic

Instrument

Bruker DRX - 800 MHz TCI probe head

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, Details 13C-15N TipAS, nosiheptide in Deuterium

#	Name	Isotope labeling	Concentration
13	TipAS	[U-99% 13C; U-99% 15N]	1 mM
14	nosiheptide	natural abundance	2 mM
15	potassium phosphate	natural abundance	50 mM
16	sodium azide	natural abundance	0.02 w/v
17	D2O	natural abundance	100 %

12 3D 1H-13C NOESY aromatic

Instrument

Bruker DRX - 800 MHz TCI probe head

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, Details 13C-15N TipAS, nosiheptide in Deuterium

#	Name	Isotope labeling	Concentration
13	TipAS	[U-99% 13C; U-99% 15N]	1 mM
14	nosiheptide	natural abundance	2 mM
15	potassium phosphate	natural abundance	50 mM
16	sodium azide	natural abundance	0.02 w/v
17	D2O	natural abundance	100 %

13 2D 1H-1H NOESY/filter against 13C-15N

Instrument

Bruker DRX - 800 MHz TCI probe head

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, Details 13C-15N TipAS, nosiheptide in Deuterium

#	Name	Isotope labeling	Concentration
13	TipAS	[U-99% 13C; U-99% 15N]	1 mM
14	nosiheptide	natural abundance	2 mM
15	potassium phosphate	natural abundance	50 mM
16	sodium azide	natural abundance	0.02 w/v
17	D2O	natural abundance	100 %

14 2D 1H-1H NOESY/filter against 13C-15N

Instrument

Bruker DRX - 800 MHz TCI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

15 2D 1H-1H TOCSY/filter against 13C-15N

Instrument

Bruker DRX - 800 MHz TCI probe head

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, Details 13C-15N TipAS, nosiheptide in Deuterium

#	Name	Isotope labeling	Concentration
13	TipAS	[U-99% 13C; U-99% 15N]	1 mM
14	nosiheptide	natural abundance	2 mM
15	potassium phosphate	natural abundance	50 mM
16	sodium azide	natural abundance	0.02 w/v
17	D2O	natural abundance	100 %

16 Doublet-separated 2D 1H-15N HSQC

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

17 Doublet-separated 2D 1H-15N HSQC

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS, nosiheptide, in Pf1 phage

#	Name	Isotope labeling	Concentration
18	TipAS	[U-99% 13C; U-99% 15N]	0.8 mM
19	nosiheptide	natural abundance	1.6 mM
20	potassium phosphate	natural abundance	10 mM
21	Pf1 phage	natural abundance	10 mg/mL
22	H2O	natural abundance	95 %
23	D2O	natural abundance	5 %

18 J-resolved ct 13C-HSQC

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

19 J-resolved ct 13C-HSQC

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS, nosiheptide, in Pf1 phage

#	Name	Isotope labeling	Concentration
18	TipAS	[U-99% 13C; U-99% 15N]	0.8 mM
19	nosiheptide	natural abundance	1.6 mM
20	potassium phosphate	natural abundance	10 mM
21	Pf1 phage	natural abundance	10 mg/mL
22	H2O	natural abundance	95 %
23	D2O	natural abundance	5 %

20 3D CBCANH

Instrument

Bruker DRX - 600 MHz TXI probe head

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.9, Details 13C-15N TipAS in complex with nosiheptide

#	Name	Isotope labeling	Concentration
7	TipAS	[U-99% 13C; U-99% 15N]	1 mM
8	nosiheptide	natural abundance	2 mM
9	potassium phosphate	natural abundance	50 mM
10	sodium azide	natural abundance	0.02 w/v
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19422_2mc0.nef
Input source #2: Coordindates	2mc0.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	Error

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)
2:1:SER:C	2:2:BB9:N	unknown	unknown	n/a
2:2:BB9:C	2:3:THR:N	unknown	unknown	n/a
2:3:THR:C	2:4:DBU:N	unknown	unknown	n/a
2:4:DBU:C	2:5:BB9:N	unknown	unknown	n/a
2:5:BB9:C	2:6:3GL:N	unknown	unknown	n/a
2:6:3GL:C	2:7:BB9:N	unknown	unknown	n/a
2:7:BB9:C	2:8:CYS:N	unknown	unknown	n/a
2:8:CYS:C	2:9:BB9:N	unknown	unknown	n/a
2:9:BB9:C	2:10:MH6:N	unknown	unknown	n/a
2:10:MH6:C	2:11:BB9:N	unknown	unknown	n/a
2:11:BB9:C	2:12:ALA:N	unknown	unknown	n/a
2:12:ALA:C	2:13:NH2:N	unknown	unknown	n/a
2:1:SER:CB	2:10:MH6:CB	unknown	unknown	n/a
2:1:SER:CA	2:9:BB9:C	unknown	unknown	n/a
2:6:3GL:OE1	3:1:NO1:CF	unknown	unknown	n/a
2:6:3GL:C	2:7:BB9:SG	unknown	unknown	n/a
2:8:CYS:C	2:9:BB9:SG	unknown	unknown	n/a
2:10:MH6:C	2:11:BB9:SG	unknown	unknown	n/a
2:1:SER:C	2:2:BB9:SG	unknown	unknown	n/a
2:4:DBU:C	2:5:BB9:SG	unknown	unknown	n/a
2:8:CYS:SG	3:1:NO1:C	unknown	unknown	n/a
1:105:CYS:SG	2:12:ALA:CB	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	502	BB9	(2Z)-2-amino-3-sulfanylprop-2-enoic acid	Assigned chemical shifts, Coordinates
B	504	DBU	(2Z)-2-AMINOBUT-2-ENOIC ACID	Assigned chemical shifts, Coordinates
B	505	BB9	(2Z)-2-amino-3-sulfanylprop-2-enoic acid	Assigned chemical shifts, Coordinates
B	506	3GL	(2S,4S)-2-amino-4-hydroxy-pentanedioic acid	Assigned chemical shifts, Coordinates
B	507	BB9	(2Z)-2-amino-3-sulfanylprop-2-enoic acid	Assigned chemical shifts, Coordinates
B	509	BB9	(2Z)-2-amino-3-sulfanylprop-2-enoic acid	Assigned chemical shifts, Coordinates
B	510	MH6	3-hydroxy-2-iminopropanoic acid	Coordinates
B	511	BB9	(2Z)-2-amino-3-sulfanylprop-2-enoic acid	Assigned chemical shifts, Coordinates
B	513	NH2	AMINO GROUP	Coordinates
C	1	NO1	4-(hydroxymethyl)-3-methyl-1H-indole-2-carboxylic acid	Assigned chemical shifts

Sequence alignments

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

110-----120-------130-------140-------150-------160-------170-------180-------190-------200-------21
MGINLTPEEKFEVFGDFDPDQYEEEVRERWGNTDAYRQSKEKTASYTKEDWQRIQDEADELTRRFVALMDAGEPADSEGAMDAAEDHRQGIARNHYDCGY
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MGINLTPEEKFEVFGDFDPDQYEEEVRERWGNTDAYRQSKEKTASYTKEDWQRIQDEADELTRRFVALMDAGEPADSEGAMDAAEDHRQGIARNHYDCGY
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

0-------220-------230-------240-------250---
EMHTCLGEMYVSDERFTRNIDAAKPGLAAYMRDAILANAVRHTP
||||||||||||||||||||||||||||||||||||||||||||
EMHTCLGEMYVSDERFTRNIDAAKPGLAAYMRDAILANAVRHTP
-------110-------120-------130-------140----

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

-------510---
SXTXXXXCXXXAX
|||||||||||||
SXTXXXXCXXXAX
--------10---

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	144	0	0	100.0
B	B	13	0	0	100.0

Content subtype: combined_19422_2mc0.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	22		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Error	1612		99.3 (chain: A, length: 144), 76.9 (chain: B, length: 13), 100.0 (chain: C, length: 1)
1	Distance restraints	CNS/XPLOR_distance_constraints_5	Warning	3471 (1)	noe	99.3 (chain: A, length: 144), 15.4 (chain: B, length: 13)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	132 (1)	hbond	66.7 (chain: A, length: 144)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	260 (260)	.	99.3 (chain: A, length: 144)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Error
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 144, Sequence coverage: 99.3%
  - Entity_assembly_ID: B, Chain length: 13, Sequence coverage: 76.9%
  - Entity_assembly_ID: C, Chain length: 1, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 859
  - ¹³C chemical shifts: 600
  - ¹⁵N chemical shifts: 153
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: C
- Redox state of CYS
- 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: A
  - Chain_ID: B

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
138	ARG	HH11	7.306
138	ARG	HH21	6.276
173	ARG	HH11	6.577
173	ARG	HH21	6.514
202	ARG	HH11	6.84
202	ARG	HH21	6.546
212	HIS	HE2	11.623
212	HIS	NE2	187.999
241	ARG	HH21	7.278

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	848	819	96.6
¹³C chemical shifts	628	600	95.5
¹⁵N chemical shifts	163	152	93.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	292	290	99.3
¹³C chemical shifts	288	275	95.5
¹⁵N chemical shifts	139	138	99.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	556	529	95.1
¹³C chemical shifts	340	325	95.6
¹⁵N chemical shifts	24	14	58.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	61	96.8
¹³C chemical shifts	63	59	93.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	73	71	97.3
¹³C chemical shifts	71	69	97.2
¹⁵N chemical shifts	2	2	100.0

Comp_index_ID	Comp_ID
1	NO1

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_5
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 144, Sequence coverage: 99.3%
  - Entity_assembly_ID: B, Chain length: 13, Sequence coverage: 15.4%
- Total number of restraints: 3467
- Weight of restraints: 1.0 (3467)
- Potential type of restraints: lower-bound-parabolic (8), square-well-parabolic (3459)
- Range of distance target values: 1.6, 10.0 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
    None
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 144, Sequence coverage: 66.7%
  - Total number of restraints: 132
  - Weight of restraints: 1.0 (132)
  - Potential type of restraints: square-well-parabolic (132)
  - Range of distance target values: 1.9, 3.15 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
      None
    - Chain_ID: C
      None
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 144, Sequence coverage: 99.3%
- Total number of restraints: 260
- Total number of restraints per polymer type: 260
- Weight of restraints: 1.0 (260)
- Potential type of restraints: square-well-parabolic (260)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords multidrug recognition, protein/antibiotic, protein/thiopeptide, TipAS/nosiheptide

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.443 seconds)

BMRB: 19422

Sample #1

Sample #2

Sample #3

Sample #4

Related entities 1. TipAS, : 1 : 3 entities Detail

Experiments performed 20 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail