BMRBj - BMREntryMaster

Found 1 Document (2.134 seconds)

BMRB: 6310

1XWN

1H,13C ans 15N assigned chemical shifts and secondary structures for hPPIL1 (peptidylprolyl isomerase -like 1)

Authors

Xu, C.

Assembly

hPPIL1 monomer

Entity

1. hPPIL1 monomer (polymer, Thiol state: all free), 174 monomers, 19309.74 Da Detail

MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLHHH HHHH

Formula weight

19309.74 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 93.7 %, Completeness: 78.4 %, Completeness (bb): 92.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	78.4 % (1577 of 2012)	74.9 % (781 of 1043)	80.5 % (635 of 789)	89.4 % (161 of 180)
Backbone	92.3 % (943 of 1022)	91.6 % (327 of 357)	92.6 % (465 of 502)	92.6 % (151 of 163)
Sidechain	67.9 % (777 of 1144)	66.2 % (454 of 686)	71.0 % (313 of 441)	58.8 % (10 of 17)
Aromatic	16.3 % (34 of 208)	25.0 % (26 of 104)	5.9 % (6 of 101)	66.7 % (2 of 3)
Methyl	98.2 % (167 of 170)	98.8 % (84 of 85)	97.6 % (83 of 85)

1. Homo sapiens peptidylprolyl isomerase (cyclophilin)-like 1

MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLHHH HHHH

Show sample condition

Sample

Temperature 295 (±1) K, pH 6.8 (±0.2)

#	Name	Concentration
1	Homo sapiens peptidylprolyl isomerase (cyclophilin)-like 1	0.5 mM
2	NaCl	50 mM
3	phosphate buffer	20 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	H2O	protons	external	indirect	0.0
¹H	H2O	protons	internal	direct	1.0
¹⁵N	H2O	protons	external	indirect	0.0

Referencing offset: -0.2 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	H2O	protons	external	indirect	0.0
¹H	H2O	protons	internal	direct	1.0
¹⁵N	H2O	protons	external	indirect	0.0

Referencing offset: -0.2 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	H2O	protons	external	indirect	0.0
¹H	H2O	protons	internal	direct	1.0
¹⁵N	H2O	protons	external	indirect	0.0

Referencing offset: 0.05 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	H2O	protons	external	indirect	0.0
¹H	H2O	protons	internal	direct	1.0
¹⁵N	H2O	protons	external	indirect	0.0

Referencing offset: 0.43 ppm, Outliers: 2 Detail

Release date

2005-03-17

Citation

Backbone and side chain assignments of human Peptidylprolyl Isomerase Like 1 (hPPIL1)
Xu, C., Xu, Y., Tang, Y., Wu, J., Shi, Y., Huang, Q., Zhang, Q.
J. Biomol. NMR (2005), 31, 179-180, PubMed 15772761 , DOI 10.1007/s10858-004-8238-0 , Abstract

Related entities 1. hPPIL1 monomer, : 1 : 22 : 237 entities Detail

Interaction partners 1. hPPIL1 monomer, : 23 interactors Detail

More details for 23 interactors identified by 8 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6310_3.str
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

Content subtype: bmr6310_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1684		92.0 (chain: 1, length: 174)

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 174, Sequence coverage: 92.0%
- Total number of assignments
  - ¹³C chemical shifts: 615
  - ¹H chemical shifts: 910
  - ¹⁵N chemical shifts: 159
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	348	318	91.4
¹H chemical shifts	357	321	89.9
¹⁵N chemical shifts	163	149	91.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	441	297	67.3
¹H chemical shifts	686	416	60.6
¹⁵N chemical shifts	24	10	41.7

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Found 1 Document (2.134 seconds)

BMRB: 6310

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. hPPIL1 monomer, : 1 : 22 : 237 entities Detail

Interaction partners 1. hPPIL1 monomer, : 23 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	789	615	77.9
¹H chemical shifts	1043	737	70.7
¹⁵N chemical shifts	187	159	85.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	101	0	0.0
¹H chemical shifts	104	16	15.4
¹⁵N chemical shifts	3	2	66.7