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Found 1 Document (2.541 seconds)

BMRB: 17953

4A1M

NMR Structure of protoporphyrin-IX bound murine p22HBP

Authors

Goodfellow, B.JAMES., Dias, J.S., Macedo, A.L., Ferreira, G.C., Peterson, F.C., Volkman, B.F., Duarte, I.C.N.

Assembly

NMR Structure of protoporphyrin-IX bound murine p22HBP

Entity

1. NMR Structure of protoporphyrin-IX bound murine p22HBP (polymer, Thiol state: all free), 195 monomers, 21735.11 Da Detail

MKNSTHHHHH HNSLFGSVET WPWQVLSTGG KEDVSYEERA CEGGKFATVE VTDKPVDEAL REAMPKIMKY VGGTNDKGVG MGMTVPVSFA VFPNEDGSLQ KKLKVWFRIP NQFQGSPPAP SDESVKIEER EGITVYSTQF GGYAKEADYV AHATQLRTTL EGTPATYQGD VYYCAGYDPP MKPYGRRNEV WLVKA

Formula weight

21735.11 Da

Source organism

Mus musculus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.3 %, Completeness: 78.6 %, Completeness (bb): 86.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	78.6 % (1760 of 2240)	78.9 % (918 of 1163)	76.2 % (669 of 878)	86.9 % (173 of 199)
Backbone	86.7 % (992 of 1144)	88.9 % (352 of 396)	84.5 % (478 of 566)	89.0 % (162 of 182)
Sidechain	72.6 % (923 of 1272)	73.8 % (566 of 767)	70.9 % (346 of 488)	64.7 % (11 of 17)
Aromatic	51.3 % (116 of 226)	59.3 % (67 of 113)	41.3 % (45 of 109)	100.0 % (4 of 4)
Methyl	90.2 % (157 of 174)	89.7 % (78 of 87)	90.8 % (79 of 87)

1. HEME-BINDING PROTEIN 1

Show sample condition

Sample

Solvent system 10% water/90% D2O, Pressure 1.000 atm, Temperature 303.000 K, pH 8.000, Details HBP 1mM

#	Name	Isotope labeling	Type	Concentration
1	HEME-BINDING_PROTEIN_1	[U-13C; U-15N]		1 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	0.0 ppm	external	direct	1.0

Referencing offset: -0.3 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	0.0 ppm	external	direct	1.0

Referencing offset: -0.3 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	0.0 ppm	external	direct	1.0

Referencing offset: -0.11 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	0.0 ppm	external	direct	1.0

Referencing offset: 0.18 ppm, Outliers: 6 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 4A1M, Strand ID: A Detail

Release date

2012-09-23

Related entities 1. NMR Structure of protoporphyrin-IX bound murine p22HBP, : 1 : 3 : 29 entities Detail

Interaction partners 1. NMR Structure of protoporphyrin-IX bound murine p22HBP, : 7 interactors Detail

More details for 7 interactors identified by 3 citations

Experiments performed 2 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_17953_4a1m.nef
Input source #2: Coordindates	4a1m.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-----
MKNSTHHHHHHNSLFGSVETWPWQVLSTGGKEDVSYEERACEGGKFATVEVTDKPVDEALREAMPKIMKYVGGTNDKGVGMGMTVPVSFAVFPNEDGSLQ
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MKNSTHHHHHHNSLFGSVETWPWQVLSTGGKEDVSYEERACEGGKFATVEVTDKPVDEALREAMPKIMKYVGGTNDKGVGMGMTVPVSFAVFPNEDGSLQ
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

--100-------110-------120-------130-------140-------150-------160-------170-------180-------190
KKLKVWFRIPNQFQGSPPAPSDESVKIEEREGITVYSTQFGGYAKEADYVAHATQLRTTLEGTPATYQGDVYYCAGYDPPMKPYGRRNEVWLVKA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
KKLKVWFRIPNQFQGSPPAPSDESVKIEEREGITVYSTQFGGYAKEADYVAHATQLRTTLEGTPATYQGDVYYCAGYDPPMKPYGRRNEVWLVKA
-------110-------120-------130-------140-------150-------160-------170-------180-------190-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	195	0	0	100.0

Content subtype: combined_17953_4a1m.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list	Warning	1686		90.3 (chain: A, length: 195)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	2777 (1)	noe	86.2 (chain: A, length: 195)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 195, Sequence coverage: 90.3%
- Total number of assignments
  - ¹H chemical shifts: 881
  - ¹⁵N chemical shifts: 166
  - ¹³C chemical shifts: 639
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
147	HIS	HD1	6.456

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1163	880	75.7
¹⁵N chemical shifts	206	166	80.6
¹³C chemical shifts	878	639	72.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	396	343	86.6
¹⁵N chemical shifts	182	154	84.6
¹³C chemical shifts	390	312	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	767	537	70.0
¹⁵N chemical shifts	24	12	50.0
¹³C chemical shifts	488	327	67.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	93	75	80.6
¹³C chemical shifts	93	83	89.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	113	66	58.4
¹⁵N chemical shifts	4	4	100.0
¹³C chemical shifts	109	45	41.3

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 195, Sequence coverage: 86.2%
- Total number of restraints: 2776
- Weight of restraints: 1.0 (2776)
- Potential type of restraints: upper-bound-parabolic (2776)
- Range of distance target values: 2.31, 6.18 (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 Heme-binding, HEME-BINDING PROTEIN, NMR, p22HBP

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Found 1 Document (2.541 seconds)

BMRB: 17953

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. NMR Structure of protoporphyrin-IX bound murine p22HBP, : 1 : 3 : 29 entities Detail

Interaction partners 1. NMR Structure of protoporphyrin-IX bound murine p22HBP, : 7 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail