BMRBj - BMREntryMaster

Found 1 Document (1.323 seconds)

BMRB: 4565

1HOV

1H, 13C and 15N resonance assignments for a truncated and inhibited catalytic domain of matrix metalloproteinase-2

Authors

Feng, Y., Likos, J.J., Zhu, L., Woodward, H., McDonald, J., Stevens, A.M., Howard, S.C., Welsch, D.J.

Assembly

truncated catalytic domain of matrix metalloproteinase-2

Entity

1. mmp2 (polymer, Thiol state: not present), 163 monomers, 18471.20 Da Detail

MYNFFPRKPK WDKNQITYRI IGYTPDLDPE TVDDAFARAF QVWSDVTPLR FSRIHDGEAD IMINFGRWEH GDGYPFDGKD GLLAHAFAPG TGVGGDSHFD DDELWTNTSA NYSLFLVAAH EFGHAMGLEH SQDPGALMAP IYTYTKNFRL SQDDIKGIQE LYG

2. I52 (non-polymer), 574.732 Da

Total weight

19045.932 Da

Max. entity weight

18471.2 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.9 %, Completeness: 83.4 %, Completeness (bb): 94.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	83.4 % (1578 of 1891)	83.9 % (817 of 974)	82.5 % (617 of 748)	85.2 % (144 of 169)
Backbone	94.4 % (906 of 960)	94.9 % (316 of 333)	94.5 % (447 of 473)	92.9 % (143 of 154)
Sidechain	75.3 % (812 of 1078)	78.2 % (501 of 641)	73.5 % (310 of 422)	6.7 % (1 of 15)
Aromatic	32.7 % (85 of 260)	36.2 % (47 of 130)	29.4 % (37 of 126)	25.0 % (1 of 4)
Methyl	97.9 % (141 of 144)	98.6 % (71 of 72)	97.2 % (70 of 72)

1. mmp2

MYNFFPRKPK WDKNQITYRI IGYTPDLDPE TVDDAFARAF QVWSDVTPLR FSRIHDGEAD IMINFGRWEH GDGYPFDGKD GLLAHAFAPG TGVGGDSHFD DDELWTNTSA NYSLFLVAAH EFGHAMGLEH SQDPGALMAP IYTYTKNFRL SQDDIKGIQE LYG

Show sample condition

Sample

Pressure 1 atm, Temperature 303 K, pH 7.4 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	mmp2	[U-13C; U-15N]		0.35 mM

Release date

2000-06-18

Citation

1H, 13C and 15N resonance assignments for a truncated and inhibited catalytic domain of matrix metalloproteinase-2
Feng, Y., Likos, J.J., Zhu, L., Woodward, H., McDonald, J., Stevens, A.M., Howard, S.C., Welsch, D.J.
J. Biomol. NMR (2000), 17, 85-86, PubMed 10909870 , Abstract

Related entities 1. mmp2, : 1 : 277 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4565_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: bmr4565_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_set_1	Warning	1699		96.3 (chain: 1, length: 163)
1	Chemical shift references	chemical_shift_reference_set_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 163, Sequence coverage: 96.3%
- Total number of assignments
  - ¹³C chemical shifts: 610
  - ¹H chemical shifts: 945
  - ¹⁵N chemical shifts: 144
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Tautomeric state of HIS
- 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 (%)
¹³C chemical shifts	748	610	81.6
¹H chemical shifts	974	803	82.4
¹⁵N chemical shifts	176	144	81.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	326	308	94.5
¹H chemical shifts	333	315	94.6
¹⁵N chemical shifts	154	143	92.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	422	302	71.6
¹H chemical shifts	641	488	76.1
¹⁵N chemical shifts	22	1	4.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	76	71	93.4
¹H chemical shifts	76	71	93.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	126	28	22.2
¹H chemical shifts	130	37	28.5
¹⁵N chemical shifts	4	1	25.0

Keywords gelatinase, matrix metalloproteinase, mmp, mmp2, NMR, nuclear magnetic resonance, protein, protein-ligand interaction, resonance assignments

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Found 1 Document (1.323 seconds)

BMRB: 4565

Sample

Related entities 1. mmp2, : 1 : 277 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 4 contents Detail