Table 1 Crystallographic statistics of N-domain ACE in complex with Ac-SDKP fragments.

From: Structural basis of Ac-SDKP hydrolysis by Angiotensin-I converting enzyme

 

N-dom:Ac-SD

N-dom:KP

Resolution (Å)

1.8

1.8

Space group

P1

Cell dimensions and angles Number of molecules/asymmetric unit

a = 73, b = 77, c = 83 Å; α = 89, β = 64, γ = 75° 2

a = 73, b =102, c = 115 Å; α = 85, β = 86, γ = 82° 4

Total/Unique reflections

419,370 130,327

936,596 293,868

Completeness (%)a

90 (58)

97 (96)

R merge a , b

10.9 (64.9)

10.3 (70.2)

R pim a , c

7.1 (43.9)

6.8 (45.7)

I/σ(I)a

6.1 (1.6)

6.2 (1.5)

R cryst d

20.2

20.7

R free e

22.8

23.5

RMSD in bond lengths (Å)

0.010

0.007

RMSD in bond angles (°)

1.37

1.18

B- factor statistics (Å2)

Protein all atoms (per chain)

24.7/30.2

30.3/31.3/25.9/25.8

Protein main chain atoms (per chain)

23.8/29.4

29.6/30.7/25.2/25.2

Protein side chain atoms (per chain)

25.7/31.0

31.0/31.8/26.5/26.5

Peptide atoms (per chain)

42.0/39.9

25.9/26.0/25.6/24.1

Solvent atoms

32.2

32.1

Zn2+/Cl ions

17.8/19.1

20.6/20.8

Glycosylated carbohydrate atoms

64.3

56.1

Ramachandran statistics (Molprobity)

Favored

98.1%

98.1%

Outliers

0.3%

0.1%

PDB code

4ufa

4ufb

  1. aValues in parentheses refer to the highest resolution shell.
  2. bRmerge = ΣΣi|Ih − Ihi|/ΣΣiIh, where Ih is the mean intensity for reflection h.
  3. cRpim = Σh (1/nh − 1) Σl |Ihl − (Ih)|/ΣhΣl(Ih).
  4. dRcryst = ΣFo| − |Fc/Σ|Fo|, where Fo and Fc are measured and calculated structure factors, respectively.
  5. eRfree = ΣFo| − |Fc|/Σ|Fo|, calculated from 5% of the reflections selected randomly and omitted during refinement.