BMRBj - BMREntryMaster

Found 1 Document (2.394 seconds)

BMRB: 3442

1YZI

Sequential assignment of proton resonances in the NMR spectrum of Zn-substituted alpha chains from human hemoglobin

Authors

Martineau, L., Craescu, C.T.

Assembly

hemoglobin A alpha chain

Entity

1. hemoglobin A alpha chain (polymer), 141 monomers, 15126.15 Da Detail

VLSPADKTNV KAAWGKVGAH AGEYGAEALE RMFLSFPTTK TYFPHFDLSH GSAQVKGHGK KVADALTNAV AHVDDMPNAL SALSDLHAHK LRVDPVNFKL LSHCLLVTLA AHLPAEFTPA VHASLDKFLA SVSTVLTSKY R

Formula weight

15126.15 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 75.2 %, Completeness: 63.7 %, Completeness (bb): 70.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	63.7 % (512 of 804)	63.7 % (512 of 804)
Backbone	70.6 % (199 of 282)	70.6 % (199 of 282)
Sidechain	60.0 % (313 of 522)	60.0 % (313 of 522)
Aromatic	83.6 % (61 of 73)	83.6 % (61 of 73)
Methyl	75.0 % (69 of 92)	75.0 % (69 of 92)

1. hemoglobin A alpha chain

VLSPADKTNV KAAWGKVGAH AGEYGAEALE RMFLSFPTTK TYFPHFDLSH GSAQVKGHGK KVADALTNAV AHVDDMPNAL SALSDLHAHK LRVDPVNFKL LSHCLLVTLA AHLPAEFTPA VHASLDKFLA SVSTVLTSKY R

Show sample condition

Sample

Temperature 310 K, pH 5.6

Release date

1995-07-30

Citation

Sequential assignment of proton resonances in the NMR spectrum of Zn-substituted alpha chains from human hemoglobin. Ligand-induced tertiary changes in the heme pocket
Martineau, L., Craescu, C.T.
Eur. J. Biochem. (1993), 214, 383-393, PubMed 8513788 , DOI 10.1111/j.1432-1033.1993.tb17934.x , Abstract

Related entities 1. hemoglobin A alpha chain, : 1 : 102 : 1 : 6 : 151 entities Detail

Interaction partners 1. hemoglobin A alpha chain, : 32 interactors Detail

More details for 32 interactors identified by 19 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr3442_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: bmr3442_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_data_set_one	Warning	647		73.0 (chain: 1, length: 141)

Assigned chemical shifts

Saveframe: chemical_shift_assignment_data_set_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 141, Sequence coverage: 73.0%
- Total number of assignments
  - ¹H chemical shifts: 647
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
20	HIS	HD1	7.28
20	HIS	HE2	8.51
87	HIS	HD1	9.92

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Found 1 Document (2.394 seconds)

BMRB: 3442

Sample

Related entities 1. hemoglobin A alpha chain, : 1 : 102 : 1 : 6 : 151 entities Detail

Interaction partners 1. hemoglobin A alpha chain, : 32 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail