BMRB Entry 5759

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5759

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Title:
A model for effector activity in a highly specific biological electron transfer complex: The cytochrome P450cam-putidaredoxin couple
Deposition date:
2003-03-31
Original release date:
2004-04-07
Authors:
Pochapsky, Susan; Pochapsky, Thomas; Wei, Julie
Citation:

Citation: Pochapsky, Susan; Pochapsky, Thomas; Wei, Julie. "A Model for Effector Activity in a Highly Specific Biological Electron Transfer Complex: The Cytochrome P450cam-Putidaredoxin Couple"  Biochemistry 42, 5649-5656 (2003).
PubMed: 12741821

Assembly members:

Assembly members:
cytochrome P450cam, polymer, 414 residues, Formula weight is not available
HEM, non-polymer, 616.487 Da.

Natural source:

Natural source:   Common Name: Pseudomonas putida   Taxonomy ID: 303   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Pseudomonas putida

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cytochrome P450cam: TTETIQSNANLAPLPPHVPE HLVFDFDMYNPSNLSAGVQE AWAVLQESNVPDLVWTRCNG GHWIATRGQLIREAYEDYRH FSSECPFIPREAGEAYDFIP TSMDPPEQRQFRALANQVVG MPVVDKLENRIQELACSLIE SLRPQGQCNFTEDYAEPFPI RIFMLLAGLPEEDIPHLKYL TDQMTRPDGSMTFAEAKEAL YDYLIPIIEQRRQKPGTDAI SIVANGQVNGRPITSDEAKR MCGLLLVGGLDTVVNFLSFS MEFLAKSPEHRQELIERPER IPAACEELLRRFSLVADGRI LTSDYEFHGVQLKKGDQILL PQMLSGLDERENAAPMHVDF SRQKVSHTTFGHGSHLCLGQ HLARREIIVTLKEWLTRIPD FSIAPGAQIQHKSGIVSGVQ ALPLVWDPATTKAV

Data sets:
Data typeCount
13C chemical shifts404
1H chemical shifts143
15N chemical shifts143

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cytochrome P450cam1
2Heme2

Entities:

Entity 1, cytochrome P450cam 414 residues - Formula weight is not available

1   THRTHRGLUTHRILEGLNSERASNALAASN
2   LEUALAPROLEUPROPROHISVALPROGLU
3   HISLEUVALPHEASPPHEASPMETTYRASN
4   PROSERASNLEUSERALAGLYVALGLNGLU
5   ALATRPALAVALLEUGLNGLUSERASNVAL
6   PROASPLEUVALTRPTHRARGCYSASNGLY
7   GLYHISTRPILEALATHRARGGLYGLNLEU
8   ILEARGGLUALATYRGLUASPTYRARGHIS
9   PHESERSERGLUCYSPROPHEILEPROARG
10   GLUALAGLYGLUALATYRASPPHEILEPRO
11   THRSERMETASPPROPROGLUGLNARGGLN
12   PHEARGALALEUALAASNGLNVALVALGLY
13   METPROVALVALASPLYSLEUGLUASNARG
14   ILEGLNGLULEUALACYSSERLEUILEGLU
15   SERLEUARGPROGLNGLYGLNCYSASNPHE
16   THRGLUASPTYRALAGLUPROPHEPROILE
17   ARGILEPHEMETLEULEUALAGLYLEUPRO
18   GLUGLUASPILEPROHISLEULYSTYRLEU
19   THRASPGLNMETTHRARGPROASPGLYSER
20   METTHRPHEALAGLUALALYSGLUALALEU
21   TYRASPTYRLEUILEPROILEILEGLUGLN
22   ARGARGGLNLYSPROGLYTHRASPALAILE
23   SERILEVALALAASNGLYGLNVALASNGLY
24   ARGPROILETHRSERASPGLUALALYSARG
25   METCYSGLYLEULEULEUVALGLYGLYLEU
26   ASPTHRVALVALASNPHELEUSERPHESER
27   METGLUPHELEUALALYSSERPROGLUHIS
28   ARGGLNGLULEUILEGLUARGPROGLUARG
29   ILEPROALAALACYSGLUGLULEULEUARG
30   ARGPHESERLEUVALALAASPGLYARGILE
31   LEUTHRSERASPTYRGLUPHEHISGLYVAL
32   GLNLEULYSLYSGLYASPGLNILELEULEU
33   PROGLNMETLEUSERGLYLEUASPGLUARG
34   GLUASNALAALAPROMETHISVALASPPHE
35   SERARGGLNLYSVALSERHISTHRTHRPHE
36   GLYHISGLYSERHISLEUCYSLEUGLYGLN
37   HISLEUALAARGARGGLUILEILEVALTHR
38   LEULYSGLUTRPLEUTHRARGILEPROASP
39   PHESERILEALAPROGLYALAGLNILEGLN
40   HISLYSSERGLYILEVALSERGLYVALGLN
41   ALALEUPROLEUVALTRPASPPROALATHR
42   THRLYSALAVAL

Entity 2, Heme - C34 H32 Fe N4 O4 - 616.487 Da.

1   HEM

Samples:

sample_1: cytochrome P450cam, [U-15N; U-13C, U-85% 2H], 0.2 – 0.6 mM; TrisCl, [U-2H], 50 mM; KCl 150 mM; camphor, [U-2H], 1 mM; H2O 90%; D2O 10%

condition_1: pH: 7.4; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
Experiments were run with 16 scans per t1 point, 512 (1H) x 32 (13C) x 32 (15N)sample_1not availablecondition_1
complex points, and 1 second recycle delays. Spectral widths were 10000 Hzsample_1not availablecondition_1
(1H) and 2600 Hz (15N). 13C spectral widths were 4524 Hz (HNCA and HN(CO)CA),sample_1not availablecondition_1
12064 Hz (HNCACB) and 3000 Hz (HNCO). The implementations of triple resonancesample_1not availablecondition_1
experiments used were TROSY versions of the sensitivity-enhanced gradientsample_1not availablecondition_1
coherence selection experiments as described by Muhandiram & Kay (J. Magn.sample_1not availablecondition_1
Reson. Series B, vol.103, 203-216, 1994).sample_1not availablecondition_1
A 3D 1H, 15N-TROSY-NOESY spectrum and 2D 1H, 15N-TROSY-HSQC spectrum weresample_1not availablecondition_1
acquired with a 2H, 15N-labeled mos sample. The HSQC was acquired withsample_1not availablecondition_1
spectral widths of 8000 Hz (1H) and 2200 Hz (15N), 640 x 128 complex points, 8sample_1not availablecondition_1
scans per t1 point and a 1 second recycle delay. The spectral widths for thesample_1not availablecondition_1
3D NOESY experiment were 10000 Hz (1H), 10000 Hz (1H) and 2000 Hz (15N), withsample_1not availablecondition_1
512 x 128 x 32 complex points, respectively. The mixing time was 150 ms,sample_1not availablecondition_1
recycle delay was 1 sec and 16 scans per t1 point were acquired.sample_1not availablecondition_1

Software:

No software information available

NMR spectrometers:

  • Varian UNITY-INOVA 500 MHz
  • Varian UNITY-INOVA 600 MHz

Related Database Links:

BMRB 16753 17415 19038
PDB
DBJ BAN13286
GB AAA25760
REF WP_032492633 YP_009083112
SP P00183
AlphaFold P00183

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