Table 1.
StralSV profiles of B1 MBL active site, functional residues For each five B1 MBL proteins, residues within 4 Å of either the zinc ions or ligand were identified (red denotes metal coordination residues, while bold denotes those in close proximity to the ligand).
| NDM-1 (3q6x_A) | IMP-1 (1dd6_A) | ccrA (1a8t_A) | VIM-2 (2yz3_A) | BcII (3fcz_A) | NDM-1 StralSV profile | Uniqueness, by% shared |
|---|---|---|---|---|---|---|
| L65 | E23 | A27 | Q40 | G59 | GDLAEVYCNIQRSWTF | 15.5 |
| M67 | V25 | I29 | F24 | F61 | FIDMNHAE | 14.1 |
| F70 | W28 | W32 | A45 | - | WFAGKP | 24 |
| V73 | V31 | V35 | Y47 | V67 | VILYPMDKAGQTRHF | 46.4 |
| A74 | P32 | P36 | P48 | P68 | PTDAVISGQLRWCFYHX | 7.9 |
| S75 | K33 | S37 | S49 | S69 | SGLAYVKDNEIMRTQHFPC | 22.9 |
| N76 | H34 | N38 | N50 | S70 | NSFTYVAHGQELWIXPMDCRK | 26.8 |
| W93 | F51 | I55 | W67 | W87 | WIFSTYKPQAVLDGERM | 35.8 |
| A116 | S73 | F78 | A90 | A112 | VIFLASYNWMGTHCQDX | 5.5 |
| H120 | H77 | H82 | H94 | H116 | HGVPAIYNLTRWDMQEFS | 53.4 |
| H122 | H79 | H84 | H96 | H118 | HGETASNQCKVL | 64.4 |
| Q123 | S80 | G85 | D97 | A119 | ALGSDPNFKTYEQVWHIMR | 1.6 |
| D124 | D81 | D86 | D98 | D120 | DSNTAKVEIFLPCQGH | 73.2 |
| K125 | S82 | C87 | R99 | R121 | HGRCSANTVFKLYDIME | 1.3 |
| Q147 | E104 | D109 | R121 | E144 | EDLQVKGAHNPSRFTXMYI | 7.5 |
| M154 | K111 | L116 | N128 | Y167 | YKLNMPGF | 6 |
| H189 | H139 | H145 | H159 | H196 | HEDKVR | 96.9 |
| D202 | K152 | N158 | S172 | N215 | NRKQADSEHG | 5.6 |
| C208 | C158 | C164 | C178 | C221 | DCSXEKMGR | 28 |
| K211 | K161 | K167 | Y181 | K224 | KFYLVHPGR | 68.6 |
| D212 | P162 | D168 | E182 | S225 | SDTEIVA | 24.8 |
| A215 | - | T171 | R185 | A228 | ARSTN | 78.9 |
| S217 | G164 | S173 | S187 | D230 | DSEG | 38.9 |
| L218 | L165 | I174 | A188 | L231 | LIA | 74.8 |
| G219 | G166 | G175 | G189 | G232 | GL | 99.2 |
| N220 | N167 | N176 | N190 | N233 | NKYAPR | 85.3 |
| E227 | E174 | T183 | A197 | N240 | ENKTDIALXPSQ | 31.6 |
| Y229 | W176 | W185 | W199 | W242 | WYMVGLARISTHFN | 27.7 |
| G237 | K184 | K193 | Q207 | S250 | KLRQISEGATVYNC | 2.9 |
| S249 | S196 | G205 | G219 | S262 | GSPAYVDE | 24.3 |
| H250 | H197 | H206 | H220 | H263 | HD | 99.1 |
| S251 | S198 | G207 | G221 | G264 | GSDNL | 15.6 |
| A252 | E199 | N208 | L222 | E265 | EODIALPWVNGY | 6.9 |
These structures were selected because unlike the references structures used to build the MBL library they are ligand bound, with the exception of BcII (3fcz_A). Structural alignments were then used to identify residue-residue correspondences for five B1 MBL proteins for those given residues. For NDM-1, the corresponding StralSV profile is provided, showing several positions in NDM-1, that are either around the binding pocket or are associated with resistance, are rare or uncommon for their corresponding locations in other MBLs, such as 125 K, 123Q, 237 G, 252A, 154 M (full StralSV output is provided in Additional file 4). Note that the residue numbering is according to the PDB structure provided in parentheses: 3q6x_A, 1dd6_A, 1a8t_A, 2yz3_A and 3fcz_A for NDM-1, IMP-1, ccrA, VIM-2 and BcII, respectively. The residue numbering for VIM-2 (2yz3_A) and ccrA (1a8t_A) are different from the residue numbering for the reference VIM-2 and reference ccrA used throughout the rest of this paper