BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	97.8 % (1316 of 1346)	97.6 % (691 of 708)	98.5 % (509 of 517)	95.9 % (116 of 121)
Backbone	96.8 % (672 of 694)	96.2 % (230 of 239)	97.7 % (334 of 342)	95.6 % (108 of 113)
Sidechain	98.7 % (750 of 760)	98.3 % (461 of 469)	99.3 % (281 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	100.0 % (98 of 98)	100.0 % (49 of 49)	100.0 % (49 of 49)

1. entity

GSHMEPARVR CSHLLVKHSQ SRRPSSWRQE KITRTKEEAL ELINGYIQKI KSGEEDFESL ASQFSDSSSA KARGDLGAFS RGQMQKPFED ASFALRTGEM SGPVFTDSGI HIILRTE

Show sample condition

Sample

Solvent system 94% H2O/6% D2O, Pressure 1 atm, Temperature 299 K, pH 6.6

#	Name	Isotope labeling	Type	Concentration
1	sodium sulfate	natural abundance	salt	100 mM
2	sodium phosphate	natural abundance	buffer	50 mM
3	D2O	[U-2H]	solvent	6 %
4	H2O	natural abundance	solvent	94 %
5	EDTA	natural abundance		5 mM
6	DTT	natural abundance		1 mM
7	NaN3	natural abundance		0.03 %

LACS Plot; CA

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

Referencing offset: -0.54 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -0.54 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.0 ppm, Outliers: 5 Detail

LACS Plot; CO

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

Referencing offset: -0.31 ppm, Outliers: 2 Detail

Protein Blocks Logo

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

Release date

2016-01-03

Citation

Allosteric Breakage of the Hydrogen Bond within the Dual-Histidine Motif in the Active Site of Human Pin1 PPIase
Wang, J., Tochio, N., Kawasaki, R., Tamari, Y., Xu, N., Uewaki, J., Utsunomiya-Tate, N., Tate, S.
Biochemistry (2015), 54, 5242-5253, PubMed 26226559 , DOI 10.1021/acs.biochem.5b00606 , Abstract

Related entities 1. Human Pin1 PPIase C113S mutant, : 1 : 1 : 55 : 121 entities Detail

Interaction partners 1. Human Pin1 PPIase C113S mutant, : 141 interactors Detail

More details for 141 interactors identified by 38 citations

Experiments performed 2 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_11588_2rur.nef
Input source #2: Coordindates	2rur.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
GSHMEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDSSSAKARGDLGAFSRGQMQKPFEDASFALRTGEM
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSHMEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDSSSAKARGDLGAFSRGQMQKPFEDASFALRTGEM

-------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_11588_2rur.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1334		98.3 (chain: A, length: 117)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	3722 (1)	noe	97.4 (chain: A, length: 117)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	104 (104)	.	61.5 (chain: A, length: 117)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_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: 697
  - ¹³C chemical shifts: 511
  - ¹⁵N chemical shifts: 126
- 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	708	697	98.4
¹³C chemical shifts	517	511	98.8
¹⁵N chemical shifts	131	126	96.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	239	232	97.1
¹³C chemical shifts	234	230	98.3
¹⁵N chemical shifts	113	108	95.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	469	465	99.1
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	52	52	100.0
¹³C chemical shifts	52	52	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: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 117, Sequence coverage: 97.4%
- Total number of restraints: 3580
- Weight of restraints: 1.0 (3580)
- Potential type of restraints: square-well-parabolic (3580)
- 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: 104
- Total number of restraints per polymer type: 104
- Weight of restraints: 1.0 (104)
- Potential type of restraints: square-well-parabolic (104)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Cys-113 mutation, Human Pin1 PPIase

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Found 1 Document (2.544 seconds)

BMRB: 11588

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Human Pin1 PPIase C113S mutant, : 1 : 1 : 55 : 121 entities Detail

Interaction partners 1. Human Pin1 PPIase C113S mutant, : 141 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail