BMRBj - BMREntryMaster

Found 1 Document (0.547 seconds)

BMRB: 17553

2LBB

Solution structure of acyl CoA binding protein from Babesia bovis T2Bo. Seattle Structure Genomics Center for Infectious Disease (SSGCID)

Authors

Yang, F., Barnwal, R., Varani, G.

Assembly

acyl CoA binding protein

Entity

1. acyl CoA binding protein (polymer, Thiol state: all free), 88 monomers, 10074.35 Da Detail

MSADDFDAAV KYVSNTTTMM ASNDDKLCFY KYYKQATVGD CNKPKPGMLQ LQEKYKWEAW NALRGMSTES AKEAYVKLLD TLAPSWRN

Formula weight

10074.35 Da

Source organism

Babesia bovis T2Bo

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 89.7 %, Completeness (bb): 98.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	89.7 % (931 of 1038)	86.3 % (466 of 540)	92.0 % (370 of 402)	99.0 % (95 of 96)
Backbone	98.5 % (514 of 522)	95.5 % (168 of 176)	100.0 % (261 of 261)	100.0 % (85 of 85)
Sidechain	83.5 % (502 of 601)	81.9 % (298 of 364)	85.8 % (194 of 226)	90.9 % (10 of 11)
Aromatic	69.2 % (72 of 104)	71.2 % (37 of 52)	65.3 % (32 of 49)	100.0 % (3 of 3)
Methyl	94.7 % (72 of 76)	94.7 % (36 of 38)	94.7 % (36 of 38)

1. entity

MSADDFDAAV KYVSNTTTMM ASNDDKLCFY KYYKQATVGD CNKPKPGMLQ LQEKYKWEAW NALRGMSTES AKEAYVKLLD TLAPSWRN

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-95% 15N]	0.8 mM
2	BIS-TRIS	natural abundance	20 mM
3	sodium chloride	natural abundance	100 mM
4	DTT	natural abundance	5 mM
5	EDTA	natural abundance	2 mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
11	entity	natural abundance	1 mM
12	BIS-TRIS	natural abundance	20 mM
13	sodium chloride	natural abundance	100 mM
14	DTT	natural abundance	5 mM
15	EDTA	natural abundance	2 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.12 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.12 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.0 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.4 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 2LBB, Strand ID: A Detail

Release date

2011-04-10

Citation

Solution structure of acyl CoA binding protein from Babesia bovis T2Bo
Yang, F., Barnwal, R., Varani, G.
Not known

Related entities 1. acyl CoA binding protein, : 1 : 126 entities Detail

Experiments performed 13 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-95% 15N]	0.8 mM
2	BIS-TRIS	natural abundance	20 mM
3	sodium chloride	natural abundance	100 mM
4	DTT	natural abundance	5 mM
5	EDTA	natural abundance	2 mM

2 2D 1H-13C HSQC

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

3 2D 1H-1H NOESY

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
11	entity	natural abundance	1 mM
12	BIS-TRIS	natural abundance	20 mM
13	sodium chloride	natural abundance	100 mM
14	DTT	natural abundance	5 mM
15	EDTA	natural abundance	2 mM

4 3D CBCA(CO)NH

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

5 3D HNCO

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

6 3D HNCA

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

7 3D HNCACB

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

8 3D HBHA(CO)NH

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

9 3D HCCH-TOCSY

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

10 3D 1H-15N NOESY

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-95% 15N]	0.8 mM
2	BIS-TRIS	natural abundance	20 mM
3	sodium chloride	natural abundance	100 mM
4	DTT	natural abundance	5 mM
5	EDTA	natural abundance	2 mM

11 3D 1H-13C NOESY

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

12 3D HCACO

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

13 3D 1H-13C NOESY aromatic

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-95% 13C; U-95% 15N]	0.8 mM
7	BIS-TRIS	natural abundance	20 mM
8	sodium chloride	natural abundance	100 mM
9	DTT	natural abundance	5 mM
10	EDTA	natural abundance	2 mM

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_17553_2lbb.nef
Input source #2: Coordindates	2lbb.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--------80--------
MAHHHHHHMSADDFDAAVKYVSNTTTMMASNDDKLCFYKYYKQATVGDCNKPKPGMLQLQEKYKWEAWNALRGMSTESAKEAYVKLLDTLAPSWRN
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MAHHHHHHMSADDFDAAVKYVSNTTTMMASNDDKLCFYKYYKQATVGDCNKPKPGMLQLQEKYKWEAWNALRGMSTESAKEAYVKLLDTLAPSWRN
--------10--------20--------30--------40--------50--------60--------70--------80--------90------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	96	0	0	100.0

Content subtype: combined_17553_2lbb.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	935		91.7 (chain: A, length: 96)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	2465 (1)	noe	91.7 (chain: A, length: 96)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 96, Sequence coverage: 91.7%
- Total number of assignments
  - ¹H chemical shifts: 471
  - ¹³C chemical shifts: 367
  - ¹⁵N chemical shifts: 97
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	586	471	80.4
¹³C chemical shifts	440	367	83.4
¹⁵N chemical shifts	106	97	91.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	192	174	90.6
¹³C chemical shifts	192	175	91.1
¹⁵N chemical shifts	93	85	91.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	394	297	75.4
¹³C chemical shifts	248	192	77.4
¹⁵N chemical shifts	13	12	92.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	45	38	84.4
¹³C chemical shifts	45	38	84.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	64	35	54.7
¹³C chemical shifts	61	32	52.5
¹⁵N chemical shifts	3	3	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 96, Sequence coverage: 91.7%
- Total number of restraints: 2465
- Weight of restraints: 1.0 (2465)
- Potential type of restraints: upper-bound-parabolic (2465)
- Range of distance target values: 2.36, 6.19 (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 acyl CoA binding protein

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Found 1 Document (0.547 seconds)

BMRB: 17553

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. acyl CoA binding protein, : 1 : 126 entities Detail

Experiments performed 13 experiments Detail

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NMR combined restraints 3 contents Detail