Table 2.

Refinement statistics of BPPS structures

Structure	BPPS	BPPS–PPi	BPPS–1	BPPS–1	BPPS–2	BPPS–3	BPPS–BPP
Limiting resolution, Å	2.0	2.3	2.3	3.1	2.4	2.4	2.3
No. of reflections, work/test	89,853/3,756	61,228/3,269	57,096/2,410	24,228/2,072	53,718/2,862	53,674/2,864	58,692/2,465
R/Rfree	0.203/0.234	0.213/0.242	0.206/0.229	0.206/0.233	0.220/0.255	0.208/0.246	0.210/0.238
Protein atoms	8,549	8,699	8,717	4,405	8,719	8,742	8,751
Water molecules	588	290	269	26	226	222	348
Metal ions/ligand atoms	15/0	6/18	6/38	3/19	7/38	6/38	6/38
rms deviations
Bond lengths, Å	0.006	0.006	0.006	0.006	0.007	0.007	0.007
Bond angles, °	1.1	1.1	1.1	1.2	1.1	1.1	1.2
Proper dihedral angles, °	18.5	18.7	18.9	19.2	18.7	18.8	18.8
Improper dihedral angles, °	0.8	0.8	0.8	0.8	0.8	0.8	0.9
PDB ID code

^*Complexes: analogues 1–3 indicated in Fig. 1. All complexes are isomorphous with native BPPS in space group P2₁2₁2₁.

^† The structure of the BPPS–1 complex was also solved in space group P6₃22.

^‡ R = ∑||F_o|−|F_c∥/∑|F_o|, where |F_o| and |F_c| are the observed and calculated structure factor amplitudes, respectively. R_free is calculated in the same manner for reflections in the test set excluded from refinement.