BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	88.0 % (1112 of 1264)	89.3 % (585 of 655)	83.8 % (413 of 493)	98.3 % (114 of 116)
Backbone	92.8 % (594 of 640)	90.5 % (200 of 221)	92.7 % (292 of 315)	98.1 % (102 of 104)
Sidechain	84.8 % (613 of 723)	88.7 % (385 of 434)	78.0 % (216 of 277)	100.0 % (12 of 12)
Aromatic	40.5 % (51 of 126)	61.9 % (39 of 63)	13.6 % (8 of 59)	100.0 % (4 of 4)
Methyl	100.0 % (110 of 110)	100.0 % (55 of 55)	100.0 % (55 of 55)

1. entity

GPLGSPEFME GVLYKWTNYL TGWQPRWFVL DNGILSYYDS QDDVCKGSKG SIKMAVCEIK VHSADNTRME LIIPGEQHFY MKAVNAAERQ RWLVALGSSK ACLTDTRT

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	entity	[U-13C; U-15N]	500.0 ~ 800.0 uM
2	DTT	natural abundance	1 mM
3	TRIS	natural abundance	20 mM
4	sodium chloride	natural abundance	100 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

LACS Plot; CA

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

Referencing offset: -0.07 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -0.07 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: -0.11 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: 0.1 ppm, Outliers: 3 Detail

Protein Blocks Logo

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

Release date

2014-09-21

Citation

Solution structure of the human wild type FAPP1-PH domain
Lenoir, M., Overduin, M.
Not known

Related entities 1. human wild type FAPP1-PH domain, : 1 : 7 : 187 entities Detail

Interaction partners 1. human wild type FAPP1-PH domain, : 2 interactors Detail

More details for 2 interactors identified by 1 citations

Experiments performed 5 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19508_2mdx.nef
Input source #2: Coordindates	2mdx.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
GPLGSPEFMEGVLYKWTNYLTGWQPRWFVLDNGILSYYDSQDDVCKGSKGSIKMAVCEIKVHSADNTRMELIIPGEQHFYMKAVNAAERQRWLVALGSSK
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GPLGSPEFMEGVLYKWTNYLTGWQPRWFVLDNGILSYYDSQDDVCKGSKGSIKMAVCEIKVHSADNTRMELIIPGEQHFYMKAVNAAERQRWLVALGSSK

--------
ACLTDTRT
||||||||
ACLTDTRT

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	108	0	0	100.0

Content subtype: combined_19508_2mdx.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list	Warning	1083		99.1 (chain: A, length: 108)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1724 (1)	noe	97.2 (chain: A, length: 108)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	66 (1)	hbond	40.7 (chain: A, length: 108)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	128 (128)	.	75.0 (chain: A, length: 108)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 99.1%
- Total number of assignments
  - ¹H chemical shifts: 570
  - ¹³C chemical shifts: 400
  - ¹⁵N chemical shifts: 113
- 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	655	570	87.0
¹³C chemical shifts	493	400	81.1
¹⁵N chemical shifts	121	113	93.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	221	198	89.6
¹³C chemical shifts	216	198	91.7
¹⁵N chemical shifts	104	101	97.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	434	372	85.7
¹³C chemical shifts	277	202	72.9
¹⁵N chemical shifts	17	12	70.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	59	59	100.0
¹³C chemical shifts	59	59	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	36	57.1
¹³C chemical shifts	59	0	0.0
¹⁵N chemical shifts	4	4	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 97.2%
- Total number of restraints: 1714
- Weight of restraints: 1.0 (1714)
- Potential type of restraints: square-well-parabolic (1714)
- Range of distance target values: 1.41, 3.71 (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
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 40.7%
  - Total number of restraints: 66
  - Weight of restraints: 1.0 (66)
  - Potential type of restraints: square-well-parabolic (66)
  - Range of distance target values: 2.1, 3.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 75.0%
- Total number of restraints: 128
- Total number of restraints per polymer type: 128
- Weight of restraints: 1.0 (128)
- Potential type of restraints: square-well-parabolic (128)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords NMR, phosphoinositide, pleckstrin homology

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Found 1 Document (0.757 seconds)

BMRB: 19508

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. human wild type FAPP1-PH domain, : 1 : 7 : 187 entities Detail

Interaction partners 1. human wild type FAPP1-PH domain, : 2 interactors Detail

Experiments performed 5 experiments Detail

Instrument

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Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail