BMRBj - BMREntryMaster

Found 1 Document (1.456 seconds)

BMRB: 4131

1BFX

1H, 15N, 13C chemical shifts of recombinant rat ferrocytochrome b5, B conformation

Authors

Dangi, B., Sarma, S., Yan, C., Banville, D.L., Guiles, R.D.

Assembly

rat ferrocytochrome b5 B form

Entity

1. cytochrome b5 (polymer), 94 monomers, 10794.75 Da Detail

DKDVKYYTLE EIQKHKDSKS TWVILHHKVY DLTKFLEEHP GGEEVLREQA GGDATENFED VGHSTDAREL SKTYIIGELH PDDRSKIAKP SETL

2. HEME C (non-polymer), 618.503 Da

Total weight

11413.253 Da

Max. entity weight

10794.75 Da

Source organism

Rattus rattus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.9 %, Completeness: 75.5 %, Completeness (bb): 94.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	75.5 % (829 of 1098)	76.4 % (437 of 572)	70.1 % (302 of 431)	94.7 % (90 of 95)
Backbone	94.4 % (527 of 558)	97.4 % (186 of 191)	90.9 % (251 of 276)	98.9 % (90 of 91)
Sidechain	59.7 % (375 of 628)	65.9 % (251 of 381)	51.0 % (124 of 243)	0.0 % (0 of 4)
Aromatic	14.8 % (13 of 88)	29.5 % (13 of 44)	0.0 % (0 of 43)	0.0 % (0 of 1)
Methyl	77.7 % (73 of 94)	87.2 % (41 of 47)	68.1 % (32 of 47)

1. cytochrome b5

DKDVKYYTLE EIQKHKDSKS TWVILHHKVY DLTKFLEEHP GGEEVLREQA GGDATENFED VGHSTDAREL SKTYIIGELH PDDRSKIAKP SETL

Show sample condition

Sample

Temperature 313 (±1) K, pH 7.0 (±0.2), Details 4mM 15N, 13C labeled in 100 mM phosphate pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	rat ferrocytochrome b5 B form	[U-15N,; U-13C]		4 mM
2	phosphate			100 mM

Release date

1998-08-11

Citation 1

The origin of differences in the physical properties of the equilibrium forms of cytochrome b5 revealed through high-resolution NMR structures and backbone dynamic analyses
Dangi, B., Sarma, S., Yan, C., Banville, D.L., Guiles, R.D.
Biochemistry (1998), 37, 8289-8302, PubMed 9622481 , DOI 10.1021/bi9801964 , Abstract

Show more 1 citaion

Citation 2

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data
Wishart, D.S., Sykes, B.D.
J. Biomol. NMR (1994), 4, 171-180, PubMed 8019132 , Abstract

Hide non-primary 1 citaion

Entries sharing articles BMRB: 4, Swiss-Prot: 1 entries Detail

  BMRB: 4573 released on 2004-05-14
    Title 1HN,15N,13CO,13Ca,13Cb chemical shifts of 7,8-dihydroneopterin aldolase (DHNA) from Staphylococcus aureus
  BMRB: 4467 released on 2000-12-14
    Title Sequence-specific 1H, 13C, and 15N Assignments of the MAR-binding Domain of Chicken MeCP2/ARBP
  BMRB: 4376 released on 1999-10-12
    Title Chemical shift assignments, 3JHNHA coupling constants, secondary structure and 15N{1H} Heteronuclear NOE values of the N-domain of VAT (VCP like ATPase of Thermoplasma). A group II AAA ATPase.
  BMRB: 4130 released on 1998-08-11
    Title 1H, 15N, 13C Chemical Shifts of Recombinant Rat Ferrocytochrome b5, A conformation
  Swiss-Prot: P00173 released on 1986-07-21
    Title CYB5_RAT Entity Cytochrome b5

Related entities 1. cytochrome b5, : 1 : 14 : 3 : 3 : 221 entities Detail

Interaction partners 1. cytochrome b5, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 1 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4131_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: bmr4131_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_one	Warning	901		98.9 (chain: 1, length: 94)
1	Chemical shift references	chemical_shift_reference_one	Warning	1		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 94, Sequence coverage: 98.9%
- Total number of assignments
  - ¹H chemical shifts: 514
  - ¹⁵N chemical shifts: 90
  - ¹³C chemical shifts: 297
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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 (%)
¹H chemical shifts	381	244	64.0
¹⁵N chemical shifts	7	0	0.0
¹³C chemical shifts	243	119	49.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	40	85.1
¹³C chemical shifts	47	31	66.0

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Found 1 Document (1.456 seconds)

BMRB: 4131

Sample

Entries sharing articles BMRB: 4, Swiss-Prot: 1 entries Detail

Related entities 1. cytochrome b5, : 1 : 14 : 3 : 3 : 221 entities Detail

Interaction partners 1. cytochrome b5, : 1 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 4 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	572	434	75.9
¹⁵N chemical shifts	98	90	91.8
¹³C chemical shifts	431	297	68.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	191	190	99.5
¹⁵N chemical shifts	91	90	98.9
¹³C chemical shifts	188	178	94.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	44	11	25.0
¹⁵N chemical shifts	1	0	0.0
¹³C chemical shifts	43	0	0.0