FMO DATABASE

FMODB ID: 2G3MR

Calculation Name: 1G5C-A-Xray549

Preferred Name: Carbonic anhydrase

Target Type: SINGLE PROTEIN

Ligand Name: 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid | calcium ion | zinc ion

Ligand 3-letter code: EPE | CA | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1G5C

Chain ID: A

ChEMBL ID: CHEMBL3926

UniProt ID: Q50565

Base Structure: X-ray

Registration Date: 2025-10-11

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	169
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1529872.09593
FMO2-HF: Nuclear repulsion	1463995.507033
FMO2-HF: Total energy	-65876.588898
FMO2-MP2: Total energy	-66067.672539

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:2:ILE)

Summations of interaction energy for fragment #1(A:2:ILE)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-102.161	-97.252	12.022	-8.69	-8.241	-0.104

Interaction energy analysis for fragmet #1(A:2:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.839 / q_NPA : 0.903

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	4	LYS	1	0.977	0.971	3.442	54.638	56.612	0.002	-0.747	-1.229	-0.001
4	A	5	ASP	-1	-0.835	-0.887	1.774	-106.827	-104.740	11.069	-7.499	-5.657	-0.100
5	A	6	ILE	0	0.115	0.045	2.414	6.645	7.493	0.951	-0.444	-1.355	-0.003
6	A	7	LEU	0	-0.027	-0.021	5.503	5.850	5.850	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.887	0.939	5.687	42.486	42.486	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.921	-0.959	6.681	-34.536	-34.536	0.000	0.000	0.000	0.000
9	A	10	ASN	0	-0.039	-0.030	9.609	3.148	3.148	0.000	0.000	0.000	0.000
10	A	11	GLN	0	-0.064	-0.017	11.391	0.991	0.991	0.000	0.000	0.000	0.000
11	A	12	ASP	-1	-0.872	-0.926	13.729	-18.378	-18.378	0.000	0.000	0.000	0.000
12	A	13	PHE	0	-0.018	0.005	13.358	1.054	1.054	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.785	0.863	15.333	17.282	17.282	0.000	0.000	0.000	0.000
14	A	15	PHE	0	0.000	0.014	18.643	-0.153	-0.153	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.884	0.937	20.244	13.758	13.758	0.000	0.000	0.000	0.000
16	A	17	ASP	-1	-0.816	-0.897	23.742	-10.870	-10.870	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.004	0.008	23.351	-0.692	-0.692	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.024	-0.013	23.624	-0.085	-0.085	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.904	-0.934	18.981	-14.338	-14.338	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.038	-0.008	18.283	-1.016	-1.016	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.943	0.963	17.308	15.996	15.996	0.000	0.000	0.000	0.000
22	A	23	HIS	0	-0.018	-0.032	18.487	0.608	0.608	0.000	0.000	0.000	0.000
23	A	24	SER	0	0.015	0.030	22.405	0.217	0.217	0.000	0.000	0.000	0.000
24	A	25	PRO	0	0.063	0.024	24.961	-0.264	-0.264	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.775	0.926	22.632	12.181	12.181	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.101	0.064	28.412	0.190	0.190	0.000	0.000	0.000	0.000
27	A	28	CYS	0	-0.030	-0.012	31.964	0.006	0.006	0.000	0.000	0.000	0.000
28	A	29	ILE	0	0.012	0.011	34.700	0.186	0.186	0.000	0.000	0.000	0.000
29	A	30	ILE	0	0.013	0.007	38.226	-0.016	-0.016	0.000	0.000	0.000	0.000
30	A	31	THR	0	-0.012	-0.034	41.308	0.142	0.142	0.000	0.000	0.000	0.000
31	A	32	CYS	-1	-0.830	-0.776	44.261	-6.304	-6.304	0.000	0.000	0.000	0.000
32	A	33	MET	0	0.000	-0.024	46.015	-0.142	-0.142	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.773	-0.894	47.875	-5.943	-5.943	0.000	0.000	0.000	0.000
34	A	35	SER	0	0.000	-0.010	48.616	-0.108	-0.108	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.764	0.848	48.953	5.668	5.668	0.000	0.000	0.000	0.000
36	A	37	LEU	0	0.013	0.006	45.573	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.065	-0.024	43.879	-0.186	-0.186	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.876	-0.912	42.749	-7.057	-7.057	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.037	-0.020	43.284	-0.111	-0.111	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.031	0.013	41.844	-0.028	-0.028	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.847	-0.935	38.759	-7.610	-7.610	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.766	0.858	37.868	7.588	7.588	0.000	0.000	0.000	0.000
43	A	44	ALA	0	-0.017	0.002	41.245	-0.057	-0.057	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.025	-0.016	38.552	0.019	0.019	0.000	0.000	0.000	0.000
45	A	46	GLY	0	-0.033	-0.005	37.481	-0.179	-0.179	0.000	0.000	0.000	0.000
46	A	47	ILE	0	-0.021	0.009	34.547	-0.270	-0.270	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.023	0.000	33.688	0.257	0.257	0.000	0.000	0.000	0.000
48	A	49	ARG	1	0.887	0.928	28.137	10.235	10.235	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.021	0.003	28.831	-0.287	-0.287	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.832	-0.924	28.829	-10.078	-10.078	0.000	0.000	0.000	0.000
51	A	52	ALA	0	0.003	0.002	30.693	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.792	0.895	27.170	10.828	10.828	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.003	-0.013	33.502	0.195	0.195	0.000	0.000	0.000	0.000
54	A	55	ILE	0	-0.020	-0.006	37.307	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.882	0.945	39.968	7.432	7.432	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.034	-0.019	43.537	0.003	0.003	0.000	0.000	0.000	0.000
57	A	58	ALA	0	0.061	0.005	46.706	0.034	0.034	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.110	0.012	50.316	0.053	0.053	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.083	-0.043	46.142	0.084	0.084	0.000	0.000	0.000	0.000
60	A	61	ILE	0	0.066	0.059	47.170	-0.070	-0.070	0.000	0.000	0.000	0.000
61	A	62	VAL	0	-0.014	0.004	43.872	-0.122	-0.122	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.768	-0.876	45.654	-6.766	-6.766	0.000	0.000	0.000	0.000
63	A	64	ASP	-1	-0.868	-0.956	44.319	-7.007	-7.007	0.000	0.000	0.000	0.000
64	A	65	GLY	0	-0.059	-0.026	42.616	-0.206	-0.206	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.001	0.007	41.137	-0.275	-0.275	0.000	0.000	0.000	0.000
66	A	67	ILE	0	0.030	0.015	39.954	-0.255	-0.255	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.916	0.953	38.444	7.200	7.200	0.000	0.000	0.000	0.000
68	A	69	SER	0	-0.038	-0.022	36.766	-0.302	-0.302	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.030	0.012	35.360	-0.288	-0.288	0.000	0.000	0.000	0.000
70	A	71	ALA	0	0.007	0.010	34.269	-0.266	-0.266	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.050	-0.027	31.764	-0.342	-0.342	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.004	0.001	30.686	-0.394	-0.394	0.000	0.000	0.000	0.000
73	A	74	ILE	0	0.024	0.023	29.694	-0.378	-0.378	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.108	-0.073	28.391	-0.509	-0.509	0.000	0.000	0.000	0.000
75	A	76	ALA	0	-0.072	-0.031	26.726	-0.431	-0.431	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.061	-0.025	25.758	-0.462	-0.462	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.018	0.039	25.370	-0.297	-0.297	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.868	-0.960	26.374	-10.226	-10.226	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.039	-0.048	27.893	0.188	0.188	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.868	-0.919	30.633	-8.622	-8.622	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.023	-0.022	33.642	-0.070	-0.070	0.000	0.000	0.000	0.000
82	A	83	ILE	0	0.005	0.005	36.657	0.198	0.198	0.000	0.000	0.000	0.000
83	A	84	ILE	0	0.003	0.011	39.483	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.025	-0.012	41.817	0.075	0.075	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.081	0.058	44.576	0.016	0.016	0.000	0.000	0.000	0.000
86	A	87	HIS	1	0.754	0.816	48.167	6.066	6.066	0.000	0.000	0.000	0.000
87	A	88	THR	0	0.045	0.019	50.565	0.066	0.066	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.896	-0.937	54.039	-5.497	-5.497	0.000	0.000	0.000	0.000
89	A	90	CYS	0	-0.056	-0.014	52.433	-0.061	-0.061	0.000	0.000	0.000	0.000
90	A	91	GLY	0	0.018	0.005	54.745	0.006	0.006	0.000	0.000	0.000	0.000
91	A	92	MET	0	0.048	0.013	53.367	0.074	0.074	0.000	0.000	0.000	0.000
92	A	93	ALA	0	-0.014	0.018	56.628	0.034	0.034	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.865	0.920	58.727	5.235	5.235	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.007	0.019	57.716	0.033	0.033	0.000	0.000	0.000	0.000
95	A	96	ASP	-1	-0.838	-0.918	61.872	-4.669	-4.669	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.850	-0.947	63.513	-5.001	-5.001	0.000	0.000	0.000	0.000
97	A	98	ASP	-1	-0.893	-0.938	65.466	-4.561	-4.561	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.078	-0.041	66.304	0.022	0.022	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.028	-0.016	60.920	-0.023	-0.023	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.040	0.016	64.579	-0.011	-0.011	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.066	-0.026	66.636	0.034	0.034	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.981	0.978	63.507	4.940	4.940	0.000	0.000	0.000	0.000
103	A	104	MET	0	-0.024	-0.002	60.923	-0.015	-0.015	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.843	0.879	65.213	4.591	4.591	0.000	0.000	0.000	0.000
105	A	106	GLU	-1	-1.023	-0.998	68.530	-4.620	-4.620	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.087	-0.053	64.213	0.021	0.021	0.000	0.000	0.000	0.000
107	A	108	GLY	0	-0.036	-0.006	66.444	-0.039	-0.039	0.000	0.000	0.000	0.000
108	A	109	VAL	0	-0.049	-0.022	62.479	-0.034	-0.034	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.945	-0.974	63.919	-4.969	-4.969	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.777	-0.873	65.192	-4.694	-4.694	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.917	-0.949	62.065	-5.268	-5.268	0.000	0.000	0.000	0.000
112	A	113	VAL	0	0.055	0.029	59.715	-0.061	-0.061	0.000	0.000	0.000	0.000
113	A	114	ILE	0	-0.043	-0.023	61.420	-0.072	-0.072	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.962	-0.963	63.371	-4.851	-4.851	0.000	0.000	0.000	0.000
115	A	116	ASN	0	-0.025	-0.014	59.225	-0.005	-0.005	0.000	0.000	0.000	0.000
116	A	117	PHE	0	0.022	0.001	55.865	-0.070	-0.070	0.000	0.000	0.000	0.000
117	A	118	SER	0	-0.040	-0.036	59.391	-0.018	-0.018	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.022	-0.014	59.546	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	120	ASP	-1	-0.939	-0.972	55.389	-5.740	-5.740	0.000	0.000	0.000	0.000
120	A	121	VAL	0	-0.103	-0.056	54.479	-0.120	-0.120	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.068	-0.011	56.727	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	123	ASN	0	-0.031	-0.018	59.829	0.006	0.006	0.000	0.000	0.000	0.000
123	A	124	PRO	0	-0.044	-0.016	55.835	0.024	0.024	0.000	0.000	0.000	0.000
124	A	125	VAL	0	-0.016	-0.005	54.777	-0.139	-0.139	0.000	0.000	0.000	0.000
125	A	126	GLY	0	0.027	0.030	55.777	0.109	0.109	0.000	0.000	0.000	0.000
126	A	127	ASP	-1	-0.887	-0.959	56.161	-5.343	-5.343	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-0.860	-0.948	52.980	-5.697	-5.697	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.848	-0.915	52.036	-5.912	-5.912	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.915	-0.965	51.892	-5.585	-5.585	0.000	0.000	0.000	0.000
130	A	131	ASN	0	0.009	0.004	50.700	-0.120	-0.120	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.007	0.011	46.480	-0.139	-0.139	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.025	-0.010	47.499	-0.141	-0.141	0.000	0.000	0.000	0.000
133	A	134	GLU	-1	-0.814	-0.888	48.558	-6.218	-6.218	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.026	0.000	46.618	-0.083	-0.083	0.000	0.000	0.000	0.000
135	A	136	VAL	0	0.003	-0.005	43.453	-0.149	-0.149	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.891	0.939	44.094	5.981	5.981	0.000	0.000	0.000	0.000
137	A	138	ARG	1	0.835	0.914	45.673	6.229	6.229	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.017	-0.011	39.776	-0.105	-0.105	0.000	0.000	0.000	0.000
139	A	140	LYS	1	0.869	0.908	39.732	7.529	7.529	0.000	0.000	0.000	0.000
140	A	141	SER	0	-0.036	-0.016	42.151	0.038	0.038	0.000	0.000	0.000	0.000
141	A	142	SER	0	-0.021	0.005	40.984	0.029	0.029	0.000	0.000	0.000	0.000
142	A	143	PRO	0	-0.009	-0.009	40.041	-0.164	-0.164	0.000	0.000	0.000	0.000
143	A	144	LEU	0	-0.035	-0.023	36.691	-0.211	-0.211	0.000	0.000	0.000	0.000
144	A	145	ILE	0	-0.011	0.002	35.749	-0.318	-0.318	0.000	0.000	0.000	0.000
145	A	146	PRO	0	-0.021	-0.001	32.306	0.147	0.147	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.904	-0.963	35.365	-7.708	-7.708	0.000	0.000	0.000	0.000
147	A	148	SER	0	-0.080	-0.038	31.543	0.047	0.047	0.000	0.000	0.000	0.000
148	A	149	ILE	0	-0.085	-0.025	31.537	-0.331	-0.331	0.000	0.000	0.000	0.000
149	A	150	GLY	0	0.064	0.056	34.121	0.246	0.246	0.000	0.000	0.000	0.000
150	A	151	VAL	0	-0.076	-0.055	36.144	-0.043	-0.043	0.000	0.000	0.000	0.000
151	A	152	HIS	0	0.019	0.002	36.811	0.488	0.488	0.000	0.000	0.000	0.000
152	A	153	GLY	0	0.023	-0.003	41.340	-0.008	-0.008	0.000	0.000	0.000	0.000
153	A	154	LEU	0	-0.023	-0.010	41.907	0.129	0.129	0.000	0.000	0.000	0.000
154	A	155	ILE	0	-0.008	0.000	45.935	0.023	0.023	0.000	0.000	0.000	0.000
155	A	156	ILE	0	-0.016	-0.009	45.345	-0.011	-0.011	0.000	0.000	0.000	0.000
156	A	157	ASP	-1	-0.834	-0.918	48.675	-5.680	-5.680	0.000	0.000	0.000	0.000
157	A	158	ILE	0	-0.015	-0.014	50.207	-0.097	-0.097	0.000	0.000	0.000	0.000
158	A	159	ASN	0	-0.042	-0.019	52.044	0.026	0.026	0.000	0.000	0.000	0.000
159	A	160	THR	0	-0.081	-0.061	52.250	-0.057	-0.057	0.000	0.000	0.000	0.000
160	A	161	GLY	0	0.033	0.027	48.077	-0.072	-0.072	0.000	0.000	0.000	0.000
161	A	162	ARG	1	0.913	0.959	47.156	5.843	5.843	0.000	0.000	0.000	0.000
162	A	163	LEU	0	0.044	0.023	42.925	0.087	0.087	0.000	0.000	0.000	0.000
163	A	164	LYS	1	0.761	0.859	47.422	5.911	5.911	0.000	0.000	0.000	0.000
164	A	165	PRO	0	0.014	0.012	45.678	-0.047	-0.047	0.000	0.000	0.000	0.000
165	A	166	LEU	0	-0.074	-0.036	47.179	0.166	0.166	0.000	0.000	0.000	0.000
166	A	167	TYR	0	-0.059	-0.056	42.426	0.206	0.206	0.000	0.000	0.000	0.000
167	A	168	LEU	0	-0.059	-0.022	41.732	-0.070	-0.070	0.000	0.000	0.000	0.000
168	A	169	ASP	-1	-0.760	-0.850	39.001	-7.601	-7.601	0.000	0.000	0.000	0.000
169	A	170	GLU	-2	-1.842	-1.899	34.633	-16.685	-16.685	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ILE)