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Found 1 Document (1.096 seconds)

BMRB: 19551

2MPH

1H, 13C, and 15N Chemical Shift Assignments for human FK506 binding Protein 25

Authors

Shin, J., Prakash, A., Yoon, H.

Assembly

hFKBP25 monomer

Entity

1. hFKBP25 monomer (polymer, Thiol state: all free), 224 monomers, 25176.48 Da Detail

MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ EHGSDSFLAE HKLLGNIKNV AKTANKDHLV TAYNHLFETK RFKGTESISK VSEQVKNVKL NEDKPKETKS EETLDEGPPK YTKSVLKKGD KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ TSAKKKKNAK PLSFKVGVGK VIRGWDEALL TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NAKLTFEVEL VDID

Formula weight

25176.48 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

torsion angle dynamics, simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.6 %, Completeness: 95.7 %, Completeness (bb): 97.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	95.7 % (2577 of 2694)	98.0 % (1389 of 1418)	92.3 % (961 of 1041)	96.6 % (227 of 235)
Backbone	97.8 % (1293 of 1322)	97.8 % (441 of 451)	98.2 % (646 of 658)	96.7 % (206 of 213)
Sidechain	94.3 % (1492 of 1582)	98.0 % (948 of 967)	88.2 % (523 of 593)	95.5 % (21 of 22)
Aromatic	75.6 % (136 of 180)	100.0 % (90 of 90)	48.8 % (42 of 86)	100.0 % (4 of 4)
Methyl	99.1 % (232 of 234)	99.1 % (116 of 117)	99.1 % (116 of 117)

1. hFKBP25

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	human FK506 binding protein 25 (hFKBP25)	[U-13C; U-15N]	0.5 mM
2	D2O	[U-100% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium chloride	natural abundance	50 mM
5	sodium phosphate	natural abundance	20 mM
6	sodium azide	natural abundance	0.001 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
7	human FK506 binding protein 25 (hFKBP25)	[U-15N]	0.5 mM
8	D2O	[U-100% 2H]	10 %
9	H2O	natural abundance	90 %
10	sodium chloride	natural abundance	50 mM
11	sodium phosphate	natural abundance	20 mM
12	sodium azide	natural abundance	0.001 %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
13	human FK506 binding protein 25 (hFKBP25)	[U-13C]	0.5 mM
14	D2O	[U-100% 2H]	100 %
15	sodium chloride	natural abundance	50 mM
16	sodium phosphate	natural abundance	20 mM
17	sodium phosphate	natural abundance	0.001 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	0.0 ppm	internal	direct	1.0

Referencing offset: 0.04 ppm, Outliers: 4 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	0.0 ppm	internal	direct	1.0

Referencing offset: 0.04 ppm, Outliers: 4 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	0.0 ppm	internal	direct	1.0

Referencing offset: 0.07 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	0.0 ppm	internal	direct	1.0

Referencing offset: 0.29 ppm, Outliers: 1 Detail

Protein Blocks Logo

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

Release date

2014-02-11

Citation

(1)H, (13)C and (15)N resonance assignments of human FK506 binding protein 25
Prakash, A., Shin, J., Yoon, H.
Biomol. NMR Assign. (2015), 9, 43-46, PubMed 24414276 , DOI 10.1007/s12104-014-9541-7 , Abstract

Related entities 1. hFKBP25 monomer, : 2 : 16 entities Detail

Interaction partners 1. hFKBP25 monomer, : 9 interactors Detail

More details for 9 interactors identified by 6 citations

Experiments performed 13 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
7	human FK506 binding protein 25 (hFKBP25)	[U-15N]	0.5 mM
8	D2O	[U-100% 2H]	10 %
9	H2O	natural abundance	90 %
10	sodium chloride	natural abundance	50 mM
11	sodium phosphate	natural abundance	20 mM
12	sodium azide	natural abundance	0.001 %

2 3D HNCA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	human FK506 binding protein 25 (hFKBP25)	[U-13C; U-15N]	0.5 mM
2	D2O	[U-100% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium chloride	natural abundance	50 mM
5	sodium phosphate	natural abundance	20 mM
6	sodium azide	natural abundance	0.001 %

3 3D HN(CO)CA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	human FK506 binding protein 25 (hFKBP25)	[U-13C; U-15N]	0.5 mM
2	D2O	[U-100% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium chloride	natural abundance	50 mM
5	sodium phosphate	natural abundance	20 mM
6	sodium azide	natural abundance	0.001 %

4 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	human FK506 binding protein 25 (hFKBP25)	[U-13C; U-15N]	0.5 mM
2	D2O	[U-100% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium chloride	natural abundance	50 mM
5	sodium phosphate	natural abundance	20 mM
6	sodium azide	natural abundance	0.001 %

5 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	human FK506 binding protein 25 (hFKBP25)	[U-13C; U-15N]	0.5 mM
2	D2O	[U-100% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium chloride	natural abundance	50 mM
5	sodium phosphate	natural abundance	20 mM
6	sodium azide	natural abundance	0.001 %

6 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	human FK506 binding protein 25 (hFKBP25)	[U-13C; U-15N]	0.5 mM
2	D2O	[U-100% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium chloride	natural abundance	50 mM
5	sodium phosphate	natural abundance	20 mM
6	sodium azide	natural abundance	0.001 %

7 3D HN(CA)CO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	human FK506 binding protein 25 (hFKBP25)	[U-13C; U-15N]	0.5 mM
2	D2O	[U-100% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium chloride	natural abundance	50 mM
5	sodium phosphate	natural abundance	20 mM
6	sodium azide	natural abundance	0.001 %

8 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	human FK506 binding protein 25 (hFKBP25)	[U-13C; U-15N]	0.5 mM
2	D2O	[U-100% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium chloride	natural abundance	50 mM
5	sodium phosphate	natural abundance	20 mM
6	sodium azide	natural abundance	0.001 %

9 3D H(CCO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	human FK506 binding protein 25 (hFKBP25)	[U-13C; U-15N]	0.5 mM
2	D2O	[U-100% 2H]	10 %
3	H2O	natural abundance	90 %
4	sodium chloride	natural abundance	50 mM
5	sodium phosphate	natural abundance	20 mM
6	sodium azide	natural abundance	0.001 %

10 3D HNHA

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
7	human FK506 binding protein 25 (hFKBP25)	[U-15N]	0.5 mM
8	D2O	[U-100% 2H]	10 %
9	H2O	natural abundance	90 %
10	sodium chloride	natural abundance	50 mM
11	sodium phosphate	natural abundance	20 mM
12	sodium azide	natural abundance	0.001 %

11 3D HCCH-TOCSY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
13	human FK506 binding protein 25 (hFKBP25)	[U-13C]	0.5 mM
14	D2O	[U-100% 2H]	100 %
15	sodium chloride	natural abundance	50 mM
16	sodium phosphate	natural abundance	20 mM
17	sodium phosphate	natural abundance	0.001 %

12 3D 1H-13C NOESY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
13	human FK506 binding protein 25 (hFKBP25)	[U-13C]	0.5 mM
14	D2O	[U-100% 2H]	100 %
15	sodium chloride	natural abundance	50 mM
16	sodium phosphate	natural abundance	20 mM
17	sodium phosphate	natural abundance	0.001 %

13 3D 1H-15N NOESY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
7	human FK506 binding protein 25 (hFKBP25)	[U-15N]	0.5 mM
8	D2O	[U-100% 2H]	10 %
9	H2O	natural abundance	90 %
10	sodium chloride	natural abundance	50 mM
11	sodium phosphate	natural abundance	20 mM
12	sodium azide	natural abundance	0.001 %

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_19551_2mph.nef
Input source #2: Coordindates	2mph.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--------90-------100
MAAAVPQRAWTVEQLRSEQLPKKDIIKFLQEHGSDSFLAEHKLLGNIKNVAKTANKDHLVTAYNHLFETKRFKGTESISKVSEQVKNVKLNEDKPKETKS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MAAAVPQRAWTVEQLRSEQLPKKDIIKFLQEHGSDSFLAEHKLLGNIKNVAKTANKDHLVTAYNHLFETKRFKGTESISKVSEQVKNVKLNEDKPKETKS

-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200
EETLDEGPPKYTKSVLKKGDKTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGK
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
EETLDEGPPKYTKSVLKKGDKTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGK

-------210-------220----
KGQPDAKIPPNAKLTFEVELVDID
||||||||||||||||||||||||
KGQPDAKIPPNAKLTFEVELVDID

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	224	0	0	100.0

Content subtype: combined_19551_2mph.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	2568		99.6 (chain: A, length: 224)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	7986 (1)	noe	99.6 (chain: A, length: 224)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	134 (1)	hbond	43.3 (chain: A, length: 224)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	281 (281)	.	81.2 (chain: A, length: 224)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_5	OK	128 (128)	.	57.1 (chain: A, length: 224)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 224, Sequence coverage: 99.6%
- Total number of assignments
  - ¹H chemical shifts: 1394
  - ¹³C chemical shifts: 945
  - ¹⁵N chemical shifts: 229
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
147	THR	HG1	5.368
183	SER	HG	5.098

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1418	1392	98.2
¹³C chemical shifts	1041	945	90.8
¹⁵N chemical shifts	240	229	95.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	451	444	98.4
¹³C chemical shifts	448	436	97.3
¹⁵N chemical shifts	213	206	96.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	967	948	98.0
¹³C chemical shifts	593	509	85.8
¹⁵N chemical shifts	27	23	85.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	119	118	99.2
¹³C chemical shifts	119	118	99.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	89	98.9
¹³C chemical shifts	86	33	38.4
¹⁵N chemical shifts	4	4	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 224, Sequence coverage: 99.6%
- Total number of restraints: 7986
- Weight of restraints: 1.0 (7986)
- Potential type of restraints: square-well-parabolic (7986)
- Range of distance target values: 2.4, 4.9 (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: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 224, Sequence coverage: 43.3%
  - Total number of restraints: 134
  - Weight of restraints: 1.0 (134)
  - Potential type of restraints: square-well-parabolic (134)
  - Range of distance target values: 2.0, 3.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 224, Sequence coverage: 81.2%
- Total number of restraints: 281
- Total number of restraints per polymer type: 281
- Weight of restraints: 1.0 (281)
- Potential type of restraints: square-well-parabolic (281)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_5

Status: OK
Experiment type: .

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 224, Sequence coverage: 57.1%

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MAAAVPQRAWTVEQLRSEQLPKKDIIKFLQEHGSDSFLAEHKLLGNIKNVAKTANKDHLVTAYNHLFETKRFKGTESISKVSEQVKNVKLNEDKPKETKS
   || ||||||||||| || | ||  || ||||||||||||||| ||||||||  | ||||||||  |||||                           
...AV.QRAWTVEQLRS.QL.K.DI..FL.EHGSDSFLAEHKLLG.IKNVAKTA..D.LVTAYNHL..TKRFK...........................

-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200
EETLDEGPPKYTKSVLKKGDKTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGK
           || || |||||   | | ||||||||| |||     |||        ||   |||| ||  |||| ||| |||||||| ||  | ||| 
...........TK.VL.KGDKT...K.G.VVHCWYTGT.QDG.....NIQ........AK...FKVG.GK..RGWD.ALL.MSKGEKAR.EI..E.AYG.

-------210-------220----
KGQPDAKIPPNAKLTFEVELVDID
 |   ||   ||| ||||||||||
.G...AK...NAK.TFEVELVDID

Total number of restraints: 128
Potential type of restraints: undefined (128)
Range of observed RDC values: 100.0, -100.0 (Hz)
RDC restraints per residue
- Chain_ID: A
  None

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Found 1 Document (1.096 seconds)

BMRB: 19551

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. hFKBP25 monomer, : 2 : 16 entities Detail

Interaction partners 1. hFKBP25 monomer, : 9 interactors Detail

Experiments performed 13 experiments Detail

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NMR combined restraints 6 contents Detail