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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).

From: Computational analysis of pathogen-borne metallo β-lactamases reveals discriminating structural features between B1 types

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
  1. 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