BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	78.8 % (495 of 628)	90.2 % (295 of 327)	61.4 % (151 of 246)	89.1 % (49 of 55)
Backbone	77.7 % (244 of 314)	96.2 % (102 of 106)	59.1 % (94 of 159)	98.0 % (48 of 49)
Sidechain	80.3 % (293 of 365)	87.3 % (193 of 221)	71.7 % (99 of 138)	16.7 % (1 of 6)
Aromatic	81.1 % (60 of 74)	94.6 % (35 of 37)	71.4 % (25 of 35)	0.0 % (0 of 2)
Methyl	84.2 % (32 of 38)	100.0 % (19 of 19)	68.4 % (13 of 19)

1. PEPTIDYL-PROLYL CIS/TRANS ISOMERASE

GSMVNTGLPA GWEVRHSNSK NLPYYFNPAT RESRWEPPAD TDMETLKMYM ATYH

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 283 K, pH 5.0, Details 1.8 MM [U-100% 13C, U-100% 15N] WW DOMAIN POLYPEPTIDE, 50 MM SODIUM PHOSPHATE, 50 MM SODIUM CHLORIDE, 0.02 % SODIUM AZIDE, 10% D2O, 90% H2O

#	Name	Isotope labeling	Concentration
1	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	[U-100% 13C; U-100% 15N]	1.8 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
5	H2O	natural abundance	90 %
6	D2O		10 %

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: -0.99 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: -0.99 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: 0.04 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2JV4, Strand ID: A Detail

Release date

2008-06-24

Citation

Structural characterisation of PinA WW domain and a comparison with other group IV WW domains, Pin1 and Ess1
Ng, C.A., Kato, Y., Tanokura, M., Brownlee, R.T.C.
Biochim. Biophys. Acta (2008), 1784, 1208-1214, PubMed 18503784 , DOI 10.1016/j.bbapap.2008.04.026 , Abstract

Related entities 1. PinA WW domain, : 1 : 23 entities Detail

Experiments performed 8 experiments Detail

1 3D HNHA

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 283 K, pH 5.0, Details 1.8 MM [U-100% 13C, U-100% 15N] WW DOMAIN POLYPEPTIDE, 50 MM SODIUM PHOSPHATE, 50 MM SODIUM CHLORIDE, 0.02 % SODIUM AZIDE, 10% D2O, 90% H2O

#	Name	Isotope labeling	Concentration
1	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	[U-100% 13C; U-100% 15N]	1.8 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
5	H2O	natural abundance	90 %
6	D2O		10 %

2 3D_13C- SEPARATED_ NOESY

Instrument

Varian INOVA - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	[U-100% 13C; U-100% 15N]	1.8 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
5	H2O	natural abundance	90 %
6	D2O		10 %

3 3D_15N- SEPARATED_ NOESY

Instrument

Varian INOVA - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	[U-100% 13C; U-100% 15N]	1.8 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
5	H2O	natural abundance	90 %
6	D2O		10 %

4 2D 1H-15N HSQC

Instrument

Varian INOVA - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	[U-100% 13C; U-100% 15N]	1.8 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
5	H2O	natural abundance	90 %
6	D2O		10 %

5 3D HNCACB

Instrument

Varian INOVA - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	[U-100% 13C; U-100% 15N]	1.8 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
5	H2O	natural abundance	90 %
6	D2O		10 %

6 3D HN(COCA)CB

Instrument

Varian INOVA - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	[U-100% 13C; U-100% 15N]	1.8 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
5	H2O	natural abundance	90 %
6	D2O		10 %

7 3D HCCH -COSY

Instrument

Varian INOVA - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	[U-100% 13C; U-100% 15N]	1.8 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
5	H2O	natural abundance	90 %
6	D2O		10 %

8 3D HCCH-TOCSY

Instrument

Varian INOVA - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	[U-100% 13C; U-100% 15N]	1.8 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
5	H2O	natural abundance	90 %
6	D2O		10 %

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_15466_2jv4.nef
Input source #2: Coordindates	2jv4.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

0--------10--------20--------30--------40--------50---
GSMVNTGLPAGWEVRHSNSKNLPYYFNPATRESRWEPPADTDMETLKMYMATYH
||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSMVNTGLPAGWEVRHSNSKNLPYYFNPATRESRWEPPADTDMETLKMYMATYH
--------10--------20--------30--------40--------50----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	54	0	0	100.0

Content subtype: combined_15466_2jv4.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	486		96.3 (chain: A, length: 54)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	582 (1)	noe	94.4 (chain: A, length: 54)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 54, Sequence coverage: 96.3%
- Total number of assignments
  - ¹H chemical shifts: 292
  - ¹³C chemical shifts: 145
  - ¹⁵N chemical shifts: 49
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
53	HIS	HD1	7.633
53	HIS	ND1	119.824

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	327	291	89.0
¹³C chemical shifts	246	145	58.9
¹⁵N chemical shifts	58	48	82.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	106	102	96.2
¹³C chemical shifts	108	47	43.5
¹⁵N chemical shifts	49	48	98.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	221	189	85.5
¹³C chemical shifts	138	98	71.0
¹⁵N chemical shifts	9	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	23	19	82.6
¹³C chemical shifts	23	13	56.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	37	35	94.6
¹³C chemical shifts	35	25	71.4
¹⁵N chemical shifts	2	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 54, Sequence coverage: 94.4%
- Total number of restraints: 582
- Weight of restraints: 1.0 (582)
- Potential type of restraints: upper-bound-parabolic (582)
- Range of distance target values: 2.32, 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

Keywords PPIASE DOMAIN, WW DOMAIN GROUP IV

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BMRB: 15466

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. PinA WW domain, : 1 : 23 entities Detail

Experiments performed 8 experiments Detail

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NMR combined restraints 3 contents Detail