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Biological Magnetic Resonance Data Bank


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BMRB Entry 7414

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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/BMR7414
MolProbity Validation Chart

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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:
HPX_DOMAIN, polymer, 194 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):
HPX_DOMAIN: MEPALCDPNLSFDAVTTVGN KIFFFKDRFFWLKVSERPKT SVNLISSLWPTLPSGIEAAY EIEARNQVFLFKDDKYWLIS NLRPEPNYPKSIHSFGFPNF VKKIDAAVFNPRFYRTYFFV DNQYWRYDERRQMMDPGYPK LITKNFQGIGPKIDAVFYSK NKYYYFFQGSNQFEYDFLLQ RITKTLKSNSWFGC

Data sets:
Data typeCount
13C chemical shifts760
15N chemical shifts200
1H chemical shifts1213
heteronuclear NOE values125
T1 relaxation values160
T2 relaxation values152

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Hemopexin-like Domain1
2Cadmium ion2

Entities:

Entity 1, Hemopexin-like Domain 194 residues - Formula weight is not available

1   METGLUPROALALEUCYSASPPROASNLEU
2   SERPHEASPALAVALTHRTHRVALGLYASN
3   LYSILEPHEPHEPHELYSASPARGPHEPHE
4   TRPLEULYSVALSERGLUARGPROLYSTHR
5   SERVALASNLEUILESERSERLEUTRPPRO
6   THRLEUPROSERGLYILEGLUALAALATYR
7   GLUILEGLUALAARGASNGLNVALPHELEU
8   PHELYSASPASPLYSTYRTRPLEUILESER
9   ASNLEUARGPROGLUPROASNTYRPROLYS
10   SERILEHISSERPHEGLYPHEPROASNPHE
11   VALLYSLYSILEASPALAALAVALPHEASN
12   PROARGPHETYRARGTHRTYRPHEPHEVAL
13   ASPASNGLNTYRTRPARGTYRASPGLUARG
14   ARGGLNMETMETASPPROGLYTYRPROLYS
15   LEUILETHRLYSASNPHEGLNGLYILEGLY
16   PROLYSILEASPALAVALPHETYRSERLYS
17   ASNLYSTYRTYRTYRPHEPHEGLNGLYSER
18   ASNGLNPHEGLUTYRASPPHELEULEUGLN
19   ARGILETHRLYSTHRLEULYSSERASNSER
20   TRPPHEGLYCYS

Entity 2, Cadmium ion - Cd - 112.411 Da.

1   CD

Samples:

sample_1: Full_Length Protein, [U-13C; U-15N], 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:

No software information available

NMR spectrometers:

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

Related Database Links:

BMRB 15578
PDB
DBJ BAG36675 BAJ20684
GB AAA58658 AAB36943 AAI12302 AAI43774 AAW29944
REF NP_002417 XP_003828422 XP_004052087 XP_508724
SP P39900

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