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BMRB: 25083

2MRL

Backbone 1H, 13C, and 15N Chemical Shift Assignments and NMR structure for potential drug target from Burkholderia thailandensis E264'

Authors

Barnwal, R., Varani, G.

Assembly

Putative uncharacterized protein BTH I2711

Entity

1. Putative uncharacterized protein BTH I2711 (polymer, Thiol state: not present), 72 monomers, 8120.198 Da Detail

MDRIFMTRTE ALEFLLKAHQ TAVDKIGHPS HKQTPADHAA IEALDRLLLD VRARRVDQFQ INASAAQIIV TD

Formula weight

8120.198 Da

Source organism

Burkholderia thailandensis

Exptl. method

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 92.2 %, Completeness (bb): 99.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	92.2 % (768 of 833)	87.7 % (377 of 430)	96.3 % (315 of 327)	100.0 % (76 of 76)
Backbone	99.8 % (427 of 428)	99.3 % (142 of 143)	100.0 % (215 of 215)	100.0 % (70 of 70)
Sidechain	86.6 % (412 of 476)	81.9 % (235 of 287)	93.4 % (171 of 183)	100.0 % (6 of 6)
Aromatic	71.7 % (33 of 46)	73.9 % (17 of 23)	69.6 % (16 of 23)
Methyl	97.0 % (97 of 100)	96.0 % (48 of 50)	98.0 % (49 of 50)

1. entity

MDRIFMTRTE ALEFLLKAHQ TAVDKIGHPS HKQTPADHAA IEALDRLLLD VRARRVDQFQ INASAAQIIV TD

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

LACS Plot; CA

Referencing offset: -1.03 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: -1.03 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: 0.11 ppm, Outliers: 2 Detail

LACS Plot; CO

Referencing offset: 0.17 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2MRL, Strand ID: A Detail

Release date

2014-07-15

Related entities 1. Putative uncharacterized protein BTH I2711, : 1 : 3 entities Detail

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

3 3D CBCA(CO)NH

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

4 3D HNCO

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

5 3D HNCACB

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

6 3D HBHA(CO)NH

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

7 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

8 3D H(CCO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

9 3D 1H-15N NOESY

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

10 3D 1H-13C NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	Putative uncharacterized protein (BTH_I2711)	[U-95% 13C; U-95% 15N]		7.2 mg/mL

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25083_2mrl.nef
Input source #2: Coordindates	2mrl.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	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

Sequence alignments

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

--------10--------20--------30--------40--------50--------60--------70--
MDRIFMTRTEALEFLLKAHQTAVDKIGHPSHKQTPADHAAIEALDRLLLDVRARRVDQFQINASAAQIIVTD
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MDRIFMTRTEALEFLLKAHQTAVDKIGHPSHKQTPADHAAIEALDRLLLDVRARRVDQFQINASAAQIIVTD

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	72	0	0	100.0

Content subtype: combined_25083_2mrl.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	769		100.0 (chain: A, length: 72)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	769 (1)	noe	93.1 (chain: A, length: 72)
2	Distance restraints	DYANA/DIANA_distance_constraints_4	Warning	44 (1)	hbond	25.0 (chain: A, length: 72)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	702 (702)	.	100.0 (chain: A, length: 72)
2	Dihedral angle restraints	DYANA/DIANA_dihedral_5	OK	124 (124)	.	98.6 (chain: A, length: 72)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 72, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 372
  - ¹³C chemical shifts: 321
  - ¹⁵N chemical shifts: 76
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 72, Sequence coverage: 93.1%
- Total number of restraints: 769
- Weight of restraints: 1.0 (769)
- Potential type of restraints: upper-bound-parabolic (769)
- Range of distance target values: 2.35, 5.5 (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
- Saveframe: DYANA/DIANA_distance_constraints_4
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 72, Sequence coverage: 25.0%
  - Total number of restraints: 44
  - Weight of restraints: 1.0 (44)
  - Potential type of restraints: upper-bound-parabolic (44)
  - Range of distance target values: 1.8, 3.0 (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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 72, Sequence coverage: 100.0%
- Total number of restraints: 702
- Total number of restraints per polymer type: 702
- Weight of restraints: 1.0 (702)
- Potential type of restraints: square-well-parabolic (702)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
- Saveframe: DYANA/DIANA_dihedral_5
  - Status: OK
  - Experiment type: .
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 72, Sequence coverage: 98.6%
  - Total number of restraints: 124
  - Total number of restraints per polymer type: 124
  - Weight of restraints: 1.0 (124)
  - Potential type of restraints: square-well-parabolic (124)
  - Plot of Phi-Psi angle restraints
  - Dihedral angle restraints per residue
    - Chain_ID: A

Keywords Burkholderia thailandensis, NMR Structure, drug target