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Biological Magnetic Resonance Data Bank


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BMRB Entry 34077

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34077
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Title: Solution structure of the cinaciguat bound human beta1 H-NOX.

Deposition date: 2016-12-13 Original release date: 2018-06-07

Authors: Matzapetakis, M.; Saraiva, I.

Citation: Matzapetakis, M.; Saraiva, I.. "Solution structure of the cinaciguat bound human beta1 H-NOX."  . ., .-..

Assembly members:
entity_1, polymer, 194 residues, 22460.486 Da.
entity_Z90, non-polymer, 565.699 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):
entity_1: MYGFVNHALELLVIRNYGPE VWEDIKKEAQLDEEGQFLVR IIYDDSKTYDLVAAASKVLN LNAGEILQMFGKMFFVFCQE SGYDTILRVLGSNVREFLQN LDALHDHLATIYPGMRAPSF RCTDAEKGKGLILHYYSERE GLQDIVIGIIKTVAQQIHGT EIDMKVIQQRNEECDHTQFL IEEKESKEHHHHHH

Data typeCount
13C chemical shifts890
15N chemical shifts365
1H chemical shifts1299

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_Z902

Entities:

Entity 1, entity_1 194 residues - 22460.486 Da.

1   METTYRGLYPHEVALASNHISALALEUGLU
2   LEULEUVALILEARGASNTYRGLYPROGLU
3   VALTRPGLUASPILELYSLYSGLUALAGLN
4   LEUASPGLUGLUGLYGLNPHELEUVALARG
5   ILEILETYRASPASPSERLYSTHRTYRASP
6   LEUVALALAALAALASERLYSVALLEUASN
7   LEUASNALAGLYGLUILELEUGLNMETPHE
8   GLYLYSMETPHEPHEVALPHECYSGLNGLU
9   SERGLYTYRASPTHRILELEUARGVALLEU
10   GLYSERASNVALARGGLUPHELEUGLNASN
11   LEUASPALALEUHISASPHISLEUALATHR
12   ILETYRPROGLYMETARGALAPROSERPHE
13   ARGCYSTHRASPALAGLULYSGLYLYSGLY
14   LEUILELEUHISTYRTYRSERGLUARGGLU
15   GLYLEUGLNASPILEVALILEGLYILEILE
16   LYSTHRVALALAGLNGLNILEHISGLYTHR
17   GLUILEASPMETLYSVALILEGLNGLNARG
18   ASNGLUGLUCYSASPHISTHRGLNPHELEU
19   ILEGLUGLULYSGLUSERLYSGLUHISHIS
20   HISHISHISHIS

Entity 2, entity_Z90 - C36 H39 N O5 - 565.699 Da.

1   Z90

Samples:

sample_1: beta1 H-NOX, [U-99% 13C; U-99% 15N], 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 110 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 110 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
H[C]_H{[c(0)]+[n(0)]}.through-spacesample_1isotropicsample_conditions_1
H[c(0)]_H[c(0)].through-spacesample_1isotropicsample_conditions_1
H_H{[n(0)]+[c(0)]}.through-spacesample_1isotropicsample_conditions_1
H[c(0)]_H[c(0)].relayedsample_1isotropicsample_conditions_1
3D HN(COCA)HAsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - chemical shift assignment

Analysis v2.4, CCPN - data analysis

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

TOPSPIN v3.2, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AvanceII 800 MHz
  • Bruker AvanceII 500 MHz