BMRB Entry 25485

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25485
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
NMR Solution Structure of the PRO Form of Human Matrilysin (proMMP-7)
Deposition date:
2015-02-11
Original release date:
2015-11-09
Authors:
Fulcher, Yan
Citation:

Citation: Prior, Stephen; Fulcher, Yan; Koppisetti, Rama; Jurkevich, A.; Van Doren, Steven. "Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors"  Structure 23, 2099-2110 (2015).
PubMed: 26439767

Assembly members:

Assembly members:
proMMP-7(E195A), polymer, 247 residues, 27589.332 Da.
CALCIUM ION, non-polymer, 40.078 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28-a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
proMMP-7(E195A): PQEAGGMSELQWEQAQDYLK RFYLYDSETKNANSLEAKLK EMQKFFGLPITGMLNSRVIE IMQKPRCGVPDVAEYSLFPN SPKWTSKVVTYRIVSYTRDL PHITVDRLVSKALNMWGKEI PLHFRKVVWGTADIMIGFAR GAHGDSYPFDGPGNTLAHAF APGTGLGGDAHFDEDERWTD GSSLGINFLYAATHALGHSL GMGHSSDPNAVMYPTYGNGD PQNFKLSQDDIKGIQKLYGK RSNSRKK

Data sets:
Data typeCount
13C chemical shifts1003
15N chemical shifts237
1H chemical shifts1506

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2CALCIUM ION_12
3CALCIUM ION_22
4ZINC ION_13
5ZINC ION_23

Entities:

Entity 1, entity_1 247 residues - 27589.332 Da.

1   PROGLNGLUALAGLYGLYMETSERGLULEU
2   GLNTRPGLUGLNALAGLNASPTYRLEULYS
3   ARGPHETYRLEUTYRASPSERGLUTHRLYS
4   ASNALAASNSERLEUGLUALALYSLEULYS
5   GLUMETGLNLYSPHEPHEGLYLEUPROILE
6   THRGLYMETLEUASNSERARGVALILEGLU
7   ILEMETGLNLYSPROARGCYSGLYVALPRO
8   ASPVALALAGLUTYRSERLEUPHEPROASN
9   SERPROLYSTRPTHRSERLYSVALVALTHR
10   TYRARGILEVALSERTYRTHRARGASPLEU
11   PROHISILETHRVALASPARGLEUVALSER
12   LYSALALEUASNMETTRPGLYLYSGLUILE
13   PROLEUHISPHEARGLYSVALVALTRPGLY
14   THRALAASPILEMETILEGLYPHEALAARG
15   GLYALAHISGLYASPSERTYRPROPHEASP
16   GLYPROGLYASNTHRLEUALAHISALAPHE
17   ALAPROGLYTHRGLYLEUGLYGLYASPALA
18   HISPHEASPGLUASPGLUARGTRPTHRASP
19   GLYSERSERLEUGLYILEASNPHELEUTYR
20   ALAALATHRHISALALEUGLYHISSERLEU
21   GLYMETGLYHISSERSERASPPROASNALA
22   VALMETTYRPROTHRTYRGLYASNGLYASP
23   PROGLNASNPHELYSLEUSERGLNASPASP
24   ILELYSGLYILEGLNLYSLEUTYRGLYLYS
25   ARGSERASNSERARGLYSLYS

Entity 2, CALCIUM ION_1 - Ca - 40.078 Da.

1   CA

Entity 3, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: proMMP-7(E195A), [U-100% 13C; U-100% 15N], 0.4 mM; imidazole, pH 6.6 20 mM; CaCl2 10 mM; ZnCl2 20 uM; beta-mercaptoethanol 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: proMMP-7(E195A), [U-10% 13C; U-100% 15N], 0.4 mM; imidazole, pH 6.6 20 mM; CaCl2 10 mM; ZnCl2 20 uM; beta-mercaptoethanol 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_3: proMMP-7(E195A), [U-100% 15N, U-100% 13CH3 (ILV)], 0.4 mM; imidazole, pH 6.6 20 mM; CaCl2 10 mM; ZnCl2 20 uM; beta-mercaptoethanol 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.6; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCnot availableisotropicsample_conditions_1
2D 1H-13C HSQCnot availableisotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
(Hb)Cb(CgCd)Hdsample_1isotropicsample_conditions_1
(Hb)Cb(CgCd)Hesample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection, processing

Analysis v2.4, CCPN - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

PSVS, Bhattacharya and Montelione - Validation

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

NCBI NP_002414.1
BMRB 25488 25489
PDB
DBJ BAD96700 BAG56875 BAI46673
EMBL CAA30678 CAA77942
GB AAC37543 AAH03635 AAV40839 AAX36381 AAX36443
REF NP_002414 XP_002822443 XP_003828431 XP_004052078 XP_508721
SP P09237
AlphaFold P09237 P09237

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks