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Biological Magnetic Resonance Data Bank


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BMRB Entry 15578

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15578
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Title: Evidence of reciprocical reorientation of the catalytic and hemopexin-like domains of full-length MMP-12   PubMed: 18465858

Deposition date: 2007-12-03 Original release date: 2008-06-27

Authors: Bertini, Ivano; Calderone, Vito; Fragai, Marco; Jaiswal, Rahul; Luchinat, Claudio; Melikian, Maxime; Mylonas, Efstratios; Svergun, Dmitri

Citation: Bertini, I.; Calderone, V.; Fragai, M.; Jaiswal, R.; Luchinat, C.; Melikian, M.; Mylonas, E.; Svergun, D.. "Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12"  J. Am. Chem. Soc. 130, 7011-7021 (2008).

Assembly members:
FL_MMP12, polymer, 366 residues, Formula weight is not available
CD, non-polymer, 112.411 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo Sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
FL_MMP12: MGPVWRKHYITYRINNYTPD MNREDVDYAIRKAFQVWSNV TPLKFSKINTGMADILVVFA RGAHGDDHAFDGKGGILAHA FGPGSGIGGDAHFDEDEFWT THSGGTNLFLTAVHAIGHSL GLGHSSDPKAVMFPTYKYVD INTFRLSADDIRGIQSLYGD PKENQRLPNPDNSEPALCDP NLSFDAVTTVGNKIFFFKDR FFWLKVSERPKTSVNLISSL WPTLPSGIEAAYEIEARNQV FLFKDDKYWLISNLRPEPNY PKSIHSFGFPNFVKKIDAAV FNPRFYRTYFFVDNQYWRYD ERRQMMDPGYPKLITKNFQG IGPKIDAVFYSKNKYYYFFQ GSNQFEYDFLLQRITKTLKS NSWFGC

Data sets:
Data typeCount
13C chemical shifts1326
15N chemical shifts375
1H chemical shifts1992
heteronuclear NOE values227
T1 relaxation values297
T2 relaxation values314

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Full_Length Protein1
2Cadmium ion2

Entities:

Entity 1, Full_Length Protein 366 residues - Formula weight is not available

1   METGLYPROVALTRPARGLYSHISTYRILE
2   THRTYRARGILEASNASNTYRTHRPROASP
3   METASNARGGLUASPVALASPTYRALAILE
4   ARGLYSALAPHEGLNVALTRPSERASNVAL
5   THRPROLEULYSPHESERLYSILEASNTHR
6   GLYMETALAASPILELEUVALVALPHEALA
7   ARGGLYALAHISGLYASPASPHISALAPHE
8   ASPGLYLYSGLYGLYILELEUALAHISALA
9   PHEGLYPROGLYSERGLYILEGLYGLYASP
10   ALAHISPHEASPGLUASPGLUPHETRPTHR
11   THRHISSERGLYGLYTHRASNLEUPHELEU
12   THRALAVALHISALAILEGLYHISSERLEU
13   GLYLEUGLYHISSERSERASPPROLYSALA
14   VALMETPHEPROTHRTYRLYSTYRVALASP
15   ILEASNTHRPHEARGLEUSERALAASPASP
16   ILEARGGLYILEGLNSERLEUTYRGLYASP
17   PROLYSGLUASNGLNARGLEUPROASNPRO
18   ASPASNSERGLUPROALALEUCYSASPPRO
19   ASNLEUSERPHEASPALAVALTHRTHRVAL
20   GLYASNLYSILEPHEPHEPHELYSASPARG
21   PHEPHETRPLEULYSVALSERGLUARGPRO
22   LYSTHRSERVALASNLEUILESERSERLEU
23   TRPPROTHRLEUPROSERGLYILEGLUALA
24   ALATYRGLUILEGLUALAARGASNGLNVAL
25   PHELEUPHELYSASPASPLYSTYRTRPLEU
26   ILESERASNLEUARGPROGLUPROASNTYR
27   PROLYSSERILEHISSERPHEGLYPHEPRO
28   ASNPHEVALLYSLYSILEASPALAALAVAL
29   PHEASNPROARGPHETYRARGTHRTYRPHE
30   PHEVALASPASNGLNTYRTRPARGTYRASP
31   GLUARGARGGLNMETMETASPPROGLYTYR
32   PROLYSLEUILETHRLYSASNPHEGLNGLY
33   ILEGLYPROLYSILEASPALAVALPHETYR
34   SERLYSASNLYSTYRTYRTYRPHEPHEGLN
35   GLYSERASNGLNPHEGLUTYRASPPHELEU
36   LEUGLNARGILETHRLYSTHRLEULYSSER
37   ASNSERTRPPHEGLYCYS

Entity 2, Cadmium ion - Cd - 112.411 Da.

1   CD

Samples:

sample_1: Full_Length Protein, [U-13C; U-15N], mM; Cadmium ion mM; NaCl 300 mM

sample_conditions_1: ionic strength: 300 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-15N HSQC T1sample_1isotropicsample_conditions_1
2D 1H-15N HSQC T2sample_1isotropicsample_conditions_1
2D 1H-15N HSQC NOEsample_1isotropicsample_conditions_1
2D 1H-15N HSQC T1sample_1isotropicsample_conditions_1
2D 1H-15N HSQC T2sample_1isotropicsample_conditions_1
2D 1H-15N HSQC NOEsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQC T1sample_1isotropicsample_conditions_1
2D 1H-15N HSQC T2sample_1isotropicsample_conditions_1
2D 1H-15N HSQC NOEsample_1isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_1isotropicsample_conditions_1

Software:

CARA -

NMR spectrometers:

  • Bruker AVANCE 900 MHz
  • Bruker DRX 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAG36675 BAJ20684
GB AAA58658 AAB36943 AAI12302 AAI43774 AAW29944
REF NP_002417 XP_003828422 XP_004052087 XP_508724
SP P39900

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts