BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	98.2 % (1321 of 1345)	98.7 % (698 of 707)	98.1 % (507 of 517)	95.9 % (116 of 121)
Backbone	97.3 % (675 of 694)	98.3 % (235 of 239)	97.1 % (332 of 342)	95.6 % (108 of 113)
Sidechain	98.6 % (748 of 759)	98.3 % (460 of 468)	98.9 % (280 of 283)	100.0 % (8 of 8)
Aromatic	100.0 % (96 of 96)	100.0 % (48 of 48)	100.0 % (47 of 47)	100.0 % (1 of 1)
Methyl	98.0 % (98 of 100)	98.0 % (49 of 50)	98.0 % (49 of 50)

1. entity 1

GSHMEPARVR CSHLLVKHSQ SRRPSSWRQE KITRTKEEAL ELINGYIQKI KSGEEDFESL ASQFSDCSSA KARGDLGAFS RGQMQKPFED AAFALRTGEM SGPVFTDSGI HIILRTE

Show sample condition

Sample

Solvent system 94% H2O/6% D2O, Pressure 1 atm, Temperature 299 K, pH 6.6, Details 1 mM [U-13C; U-15N] Pin1 PPIase S138A mutant, 50 mM sodium phosphate, 100 mM sodium sulfate, 5 mM EDTA, 1 mM DTT, 0.03 % sodium azide, 6 % [U-2H] D2O, 94% H2O/6% D2O

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.778 ppm	internal	indirect	0.2514495
¹H	water	protons	4.778 ppm	internal	direct	1.0
¹⁵N	water	protons	4.778 ppm	internal	indirect	0.1013291

Referencing offset: -0.58 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.778 ppm	internal	indirect	0.2514495
¹H	water	protons	4.778 ppm	internal	direct	1.0
¹⁵N	water	protons	4.778 ppm	internal	indirect	0.1013291

Referencing offset: -0.58 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.778 ppm	internal	indirect	0.2514495
¹H	water	protons	4.778 ppm	internal	direct	1.0
¹⁵N	water	protons	4.778 ppm	internal	indirect	0.1013291

Referencing offset: 0.0 ppm, Outliers: 3 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.778 ppm	internal	indirect	0.2514495
¹H	water	protons	4.778 ppm	internal	direct	1.0
¹⁵N	water	protons	4.778 ppm	internal	indirect	0.1013291

Referencing offset: -0.28 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 5GPH, Strand ID: A Detail

Release date

2016-10-31

Citation

Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1
Wang, J., Kawasaki, R., Uewaki, J.I., Rashid, A., Tochio, N., Tate, S.I.
Molecules (2017), 22, E992-E992, PubMed 28617332 , DOI 10.3390/molecules22060992 , Abstract

Related entities 1. Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (E.C.5.2.1.8), : 1 : 1 : 174 entities Detail

Interaction partners 1. Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (E.C.5.2.1.8), : 141 interactors Detail

More details for 141 interactors identified by 38 citations

Experiments performed 11 experiments Detail

1 3D HNCO

Instrument

Bruker AvanceII - 700 MHz

Sample

State isotropic, Solvent system 94% H2O/6% D2O, Pressure 1 atm, Temperature 299 K, pH 6.6, Details 1 mM [U-13C; U-15N] Pin1 PPIase S138A mutant, 50 mM sodium phosphate, 100 mM sodium sulfate, 5 mM EDTA, 1 mM DTT, 0.03 % sodium azide, 6 % [U-2H] D2O, 94% H2O/6% D2O

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

2 3D HN(CA)CO

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

3 3D HN(CO)CA

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

4 3D HNCA

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

5 3D CBCA(CO)NH

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

6 3D C(CO)NH

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

7 3D HBHA(CO)NH

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

8 3D 1H-15N NOESY

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

9 3D 1H-13C NOESY

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

10 2D 1H-15N HSQC

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

11 2D 1H-13C HSQC

Instrument

Bruker AvanceII - 700 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Pin1 PPIase S138A mutant	[U-13C; U-15N]	protein	1 mM
2	DTT	natural abundance		1 mM
3	EDTA	natural abundance		5 mM
4	sodium azide	natural abundance		0.03 %
5	sodium phosphate	natural abundance	buffer	50 mM
6	sodium sulfate	natural abundance	salt	100 mM
7	H2O	natural abundance	solvent	94 %
8	D2O	[U-2H]	solvent	6 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_36014_5gph.nef
Input source #2: Coordindates	5gph.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
GSHMEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDAAFALRTGEM
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSHMEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDAAFALRTGEM

-------110-------
SGPVFTDSGIHIILRTE
|||||||||||||||||
SGPVFTDSGIHIILRTE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	117	0	0	100.0

Content subtype: combined_36014_5gph.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1335		98.3 (chain: A, length: 117)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	4702 (1)	noe	97.4 (chain: A, length: 117)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	102 (102)	.	61.5 (chain: A, length: 117)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 117, Sequence coverage: 98.3%
- Total number of assignments
  - ¹H chemical shifts: 698
  - ¹³C chemical shifts: 510
  - ¹⁵N chemical shifts: 127
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	707	698	98.7
¹³C chemical shifts	517	510	98.6
¹⁵N chemical shifts	131	127	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	239	233	97.5
¹³C chemical shifts	234	229	97.9
¹⁵N chemical shifts	113	109	96.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	468	465	99.4
¹³C chemical shifts	283	281	99.3
¹⁵N chemical shifts	18	18	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	53	53	100.0
¹³C chemical shifts	53	53	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	48	100.0
¹³C chemical shifts	47	47	100.0
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 117, Sequence coverage: 97.4%
- Total number of restraints: 4511
- Weight of restraints: 1.0 (4511)
- Potential type of restraints: square-well-parabolic (4511)
- Range of distance target values: 2.6, 6.9 (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

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 117, Sequence coverage: 61.5%
- Total number of restraints: 102
- Total number of restraints per polymer type: 102
- Weight of restraints: 1.0 (102)
- Potential type of restraints: square-well-parabolic (102)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords MOLMOL, PPIase, Pin1, S138A

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Found 1 Document (2.404 seconds)

BMRB: 36014

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (E.C.5.2.1.8), : 1 : 1 : 174 entities Detail

Interaction partners 1. Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (E.C.5.2.1.8), : 141 interactors Detail

Experiments performed 11 experiments Detail

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NMR combined restraints 4 contents Detail