BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	95.6 % (1399 of 1464)	94.7 % (731 of 772)	96.4 % (542 of 562)	96.9 % (126 of 130)
Backbone	97.3 % (697 of 716)	95.9 % (233 of 243)	98.3 % (351 of 357)	97.4 % (113 of 116)
Sidechain	94.4 % (815 of 863)	94.1 % (498 of 529)	95.0 % (304 of 320)	92.9 % (13 of 14)
Aromatic	86.5 % (90 of 104)	86.5 % (45 of 52)	86.0 % (43 of 50)	100.0 % (2 of 2)
Methyl	100.0 % (112 of 112)	100.0 % (56 of 56)	100.0 % (56 of 56)

1. entity 1

SASDIRMKKV MQYRRALTKV VKLKTHLFSE TVKVTCSKDG EEVQWFKGKS TAGAQDRKKP SGGFPVDKIT SVKSQADNTK VLVITVNNPQ PTTYNFTFKS PGERESWQEQ IQSLMKFMSM K

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7, Details 730 uM [U-100% 15N]; [U-100% 13C] C-terminal PH domain from TgAPH, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.78 ppm	internal	indirect	0.2514495
¹H	water	protons	4.78 ppm	internal	direct	1.0
¹⁵N	water	protons	4.78 ppm	internal	indirect	0.1013291

Referencing offset: -0.13 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.78 ppm	internal	indirect	0.2514495
¹H	water	protons	4.78 ppm	internal	direct	1.0
¹⁵N	water	protons	4.78 ppm	internal	indirect	0.1013291

Referencing offset: -0.13 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.78 ppm	internal	indirect	0.2514495
¹H	water	protons	4.78 ppm	internal	direct	1.0
¹⁵N	water	protons	4.78 ppm	internal	indirect	0.1013291

Referencing offset: -0.07 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.78 ppm	internal	indirect	0.2514495
¹H	water	protons	4.78 ppm	internal	direct	1.0
¹⁵N	water	protons	4.78 ppm	internal	indirect	0.1013291

Referencing offset: 0.13 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 6F8E, Strand ID: A Detail

Release date

2019-01-21

Citation

Structural Basis of Phosphatidic Acid Sensing by APH in Apicomplexan Parasites
Darvill, N., Dubois, D.J., Rouse, S.L., Hammoudi, P.M., Blake, T., Benjamin, S., Liu, B., Soldati-Favre, D., Matthews, S.
Structure (2018), 26, 1059-1071, PubMed 29910186 , DOI 10.1016/j.str.2018.05.001 , Abstract

Related entities 1. Uncharacterized protein, : 1 : 3 entities Detail

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker DRX - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7, Details 730 uM [U-100% 15N]; [U-100% 13C] C-terminal PH domain from TgAPH, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

2 3D CBCA(CO)NH

Instrument

Bruker DRX - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

3 3D HNCACB

Instrument

Bruker DRX - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

4 3D HNCO

Instrument

Bruker DRX - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

5 3D HN(CO)CA

Instrument

Bruker DRX - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

6 3D HBHA(CO)NH

Instrument

Bruker DRX - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

7 3D C(CO)NH

Instrument

Bruker DRX - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

8 3D H(CCO)NH

Instrument

Bruker DRX - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

9 3D 1H-15N NOESY

Instrument

Bruker DRX - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

10 3D 1H-13C NOESY

Instrument

Bruker DRX - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	C-terminal PH domain from TgAPH	[U-100% 15N]; [U-100% 13C]		730 uM
2	NaCl	natural abundance		150 mM

NMR combined restraints 2 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts	combined_34216_6f8e.nef
Input source #2: Coordindates	6f8e.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	Error

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

--------20--------30--------40--------50--------60--------70--------80--------90-------100-------110
SASDIRMKKVMQYRRALTKVVKLKTHLFSETVKVTCSKDGEEVQWFKGKSTAGAQDRKKPSGGFPVDKITSVKSQADNTKVLVITVNNPQPTTYNFTFKS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SASDIRMKKVMQYRRALTKVVKLKTHLFSETVKVTCSKDGEEVQWFKGKSTAGAQDRKKPSGGFPVDKITSVKSQADNTKVLVITVNNPQPTTYNFTFKS
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

-------120-------130-
PGERESWQEQIQSLMKFMSMK
|||||||||||||||||||||
PGERESWQEQIQSLMKFMSMK
-------110-------120-

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	121	0	0	100.0

Content subtype: combined_34216_6f8e.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1398		97.5 (chain: A, length: 121)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 121, Sequence coverage: 97.5%
- Total number of assignments
  - ¹H chemical shifts: 734
  - ¹³C chemical shifts: 538
  - ¹⁵N chemical shifts: 126
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	772	733	94.9
¹³C chemical shifts	562	538	95.7
¹⁵N chemical shifts	135	126	93.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	243	235	96.7
¹³C chemical shifts	242	236	97.5
¹⁵N chemical shifts	116	112	96.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	529	498	94.1
¹³C chemical shifts	320	302	94.4
¹⁵N chemical shifts	19	14	73.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	61	56	91.8
¹³C chemical shifts	61	56	91.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	52	45	86.5
¹³C chemical shifts	50	43	86.0
¹⁵N chemical shifts	2	2	100.0

Keywords LIPID BINDING PROTEIN, PH domain, membrane association, phosphatidic acid binding

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Found 1 Document (0.624 seconds)

BMRB: 34216

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Uncharacterized protein, : 1 : 3 entities Detail

Experiments performed 10 experiments Detail

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NMR combined restraints 2 contents Detail