FMO DATABASE

FMODB ID: LGM49

Calculation Name: 2OPC-A-Xray547

Preferred Name:

Target Type:

Ligand Name: imidazole | cobalt (ii) ion

Ligand 3-letter code: IMD | CO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2OPC

Chain ID: A

ChEMBL ID:

UniProt ID: Q6R661

Base Structure: X-ray

Registration Date: 2025-10-04

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-956327.71113
FMO2-HF: Nuclear repulsion	910178.106292
FMO2-HF: Total energy	-46149.604838
FMO2-MP2: Total energy	-46284.319585

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:36:GLU)

Summations of interaction energy for fragment #1(A:36:GLU)

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.
-37.748	-31.866	9.066	-6.718	-8.229	0.051

Interaction energy analysis for fragmet #1(A:36:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.021 / q_NPA : -0.022

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	38	TYR	0	0.000	-0.003	1.906	-5.877	-2.507	3.881	-2.794	-4.457	-0.011
4	A	39	THR	0	0.045	0.028	3.677	5.231	5.460	-0.001	0.069	-0.297	0.000
108	A	143	LYS	1	0.866	0.943	1.941	-56.454	-54.539	5.186	-3.829	-3.271	0.061
110	A	145	LYS	1	0.896	0.944	3.897	17.716	18.084	0.000	-0.164	-0.204	0.001
5	A	40	ARG	1	0.788	0.873	5.533	-15.869	-15.869	0.000	0.000	0.000	0.000
6	A	41	PHE	0	-0.002	-0.008	8.049	-1.323	-1.323	0.000	0.000	0.000	0.000
7	A	42	TYR	0	0.061	0.019	10.363	0.766	0.766	0.000	0.000	0.000	0.000
8	A	43	ARG	1	0.922	0.970	13.633	-3.243	-3.243	0.000	0.000	0.000	0.000
9	A	44	SER	0	0.026	0.015	16.704	-0.224	-0.224	0.000	0.000	0.000	0.000
10	A	45	PRO	0	0.053	0.008	19.387	0.030	0.030	0.000	0.000	0.000	0.000
11	A	46	THR	0	-0.024	-0.010	21.884	-0.050	-0.050	0.000	0.000	0.000	0.000
12	A	47	ALA	0	-0.040	0.003	16.345	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	48	SER	0	-0.058	-0.058	17.462	-0.296	-0.296	0.000	0.000	0.000	0.000
14	A	49	VAL	0	-0.004	0.004	12.056	0.336	0.336	0.000	0.000	0.000	0.000
15	A	50	ILE	0	0.017	0.002	13.490	-0.444	-0.444	0.000	0.000	0.000	0.000
16	A	51	LEU	0	-0.006	0.002	9.621	0.371	0.371	0.000	0.000	0.000	0.000
17	A	52	SER	0	-0.008	-0.023	10.789	-0.702	-0.702	0.000	0.000	0.000	0.000
18	A	53	GLY	0	0.033	0.023	12.208	-0.237	-0.237	0.000	0.000	0.000	0.000
19	A	54	LEU	0	-0.017	0.006	15.139	0.008	0.008	0.000	0.000	0.000	0.000
20	A	55	VAL	0	0.031	0.015	15.446	0.091	0.091	0.000	0.000	0.000	0.000
21	A	56	LYS	1	0.920	0.987	15.353	-0.491	-0.491	0.000	0.000	0.000	0.000
22	A	57	VAL	0	0.000	-0.009	13.481	-0.196	-0.196	0.000	0.000	0.000	0.000
23	A	58	LYS	1	0.951	0.998	16.805	-0.831	-0.831	0.000	0.000	0.000	0.000
24	A	59	TRP	0	0.033	0.010	15.398	-0.126	-0.126	0.000	0.000	0.000	0.000
25	A	60	ASP	-1	-0.797	-0.890	20.394	1.165	1.165	0.000	0.000	0.000	0.000
26	A	61	ASN	0	-0.020	-0.018	23.438	-0.069	-0.069	0.000	0.000	0.000	0.000
27	A	62	GLU	-1	-0.901	-0.962	23.672	1.390	1.390	0.000	0.000	0.000	0.000
28	A	63	GLN	0	0.013	0.011	24.124	0.100	0.100	0.000	0.000	0.000	0.000
29	A	64	MET	0	-0.099	-0.020	19.419	0.222	0.222	0.000	0.000	0.000	0.000
30	A	65	THR	0	-0.022	-0.025	20.085	0.115	0.115	0.000	0.000	0.000	0.000
31	A	66	MET	0	-0.021	-0.022	19.032	-0.076	-0.076	0.000	0.000	0.000	0.000
32	A	67	PRO	0	-0.013	0.010	15.036	0.034	0.034	0.000	0.000	0.000	0.000
33	A	68	LEU	0	-0.062	-0.024	17.755	-0.273	-0.273	0.000	0.000	0.000	0.000
34	A	69	PHE	0	0.023	-0.011	14.196	0.173	0.173	0.000	0.000	0.000	0.000
35	A	70	LYS	1	0.862	0.941	19.301	-0.392	-0.392	0.000	0.000	0.000	0.000
36	A	71	TRP	0	-0.029	-0.010	18.536	0.060	0.060	0.000	0.000	0.000	0.000
37	A	72	ILE	0	-0.044	-0.048	18.022	0.127	0.127	0.000	0.000	0.000	0.000
38	A	73	GLY	0	0.016	0.030	20.120	0.010	0.010	0.000	0.000	0.000	0.000
39	A	74	GLY	0	-0.016	-0.007	20.759	-0.141	-0.141	0.000	0.000	0.000	0.000
40	A	75	GLU	-1	-0.921	-0.953	24.559	-0.356	-0.356	0.000	0.000	0.000	0.000
41	A	76	GLN	0	-0.055	-0.040	23.177	-0.161	-0.161	0.000	0.000	0.000	0.000
42	A	77	ALA	0	-0.001	0.003	26.911	0.046	0.046	0.000	0.000	0.000	0.000
43	A	78	GLU	-1	-0.937	-0.962	26.739	-1.007	-1.007	0.000	0.000	0.000	0.000
44	A	79	GLU	-1	-0.868	-0.927	25.016	-0.635	-0.635	0.000	0.000	0.000	0.000
45	A	80	LEU	0	0.012	0.017	20.597	-0.141	-0.141	0.000	0.000	0.000	0.000
46	A	81	HIS	0	-0.014	-0.025	20.665	0.101	0.101	0.000	0.000	0.000	0.000
47	A	82	PHE	0	0.005	-0.010	14.815	-0.319	-0.319	0.000	0.000	0.000	0.000
48	A	83	CYS	-1	-0.793	-0.804	14.141	-1.371	-1.371	0.000	0.000	0.000	0.000
49	A	84	VAL	0	-0.013	-0.006	12.926	-0.358	-0.358	0.000	0.000	0.000	0.000
50	A	85	HIS	0	-0.046	-0.024	8.962	-0.511	-0.511	0.000	0.000	0.000	0.000
51	A	86	ILE	0	0.021	0.001	9.308	0.581	0.581	0.000	0.000	0.000	0.000
52	A	87	ALA	0	-0.020	-0.007	6.295	-1.079	-1.079	0.000	0.000	0.000	0.000
53	A	88	HIS	0	-0.027	-0.029	8.383	-0.138	-0.138	0.000	0.000	0.000	0.000
54	A	89	SER	0	0.006	-0.004	9.660	0.243	0.243	0.000	0.000	0.000	0.000
55	A	90	SER	0	0.023	0.001	11.311	-0.322	-0.322	0.000	0.000	0.000	0.000
56	A	91	GLY	0	0.034	0.016	14.706	-0.233	-0.233	0.000	0.000	0.000	0.000
57	A	92	PRO	0	0.026	-0.003	15.589	0.011	0.011	0.000	0.000	0.000	0.000
58	A	93	LYS	1	0.959	0.984	13.403	1.566	1.566	0.000	0.000	0.000	0.000
59	A	94	LEU	0	0.093	0.066	9.932	-0.589	-0.589	0.000	0.000	0.000	0.000
60	A	95	ASN	0	-0.009	0.001	7.693	1.188	1.188	0.000	0.000	0.000	0.000
61	A	96	ARG	1	0.889	0.948	7.723	2.245	2.245	0.000	0.000	0.000	0.000
62	A	97	ALA	0	0.023	0.030	7.791	1.157	1.157	0.000	0.000	0.000	0.000
63	A	98	ARG	1	0.814	0.889	9.390	0.132	0.132	0.000	0.000	0.000	0.000
64	A	99	SER	0	0.003	-0.047	12.303	0.131	0.131	0.000	0.000	0.000	0.000
65	A	100	LEU	0	0.000	0.004	14.265	0.222	0.222	0.000	0.000	0.000	0.000
66	A	101	GLY	0	-0.010	-0.005	16.677	0.131	0.131	0.000	0.000	0.000	0.000
67	A	102	THR	0	0.010	-0.004	17.008	-0.098	-0.098	0.000	0.000	0.000	0.000
68	A	103	VAL	0	-0.018	-0.025	16.421	0.263	0.263	0.000	0.000	0.000	0.000
69	A	104	ASN	0	0.047	0.003	19.286	-0.149	-0.149	0.000	0.000	0.000	0.000
70	A	105	SER	0	0.081	0.024	21.466	0.103	0.103	0.000	0.000	0.000	0.000
71	A	106	ASN	0	-0.016	0.013	23.445	0.072	0.072	0.000	0.000	0.000	0.000
72	A	107	MET	0	-0.114	-0.015	21.745	0.103	0.103	0.000	0.000	0.000	0.000
73	A	108	ASP	-1	-0.767	-0.877	23.889	-0.007	-0.007	0.000	0.000	0.000	0.000
74	A	109	GLN	0	-0.029	-0.018	25.776	0.146	0.146	0.000	0.000	0.000	0.000
75	A	110	HIS	0	-0.031	-0.031	27.287	0.121	0.121	0.000	0.000	0.000	0.000
76	A	111	TRP	0	-0.030	-0.019	19.902	-0.018	-0.018	0.000	0.000	0.000	0.000
77	A	112	ALA	0	0.053	0.028	22.922	-0.009	-0.009	0.000	0.000	0.000	0.000
78	A	113	GLN	0	0.041	0.009	21.610	0.090	0.090	0.000	0.000	0.000	0.000
79	A	114	ALA	0	0.030	0.026	17.936	-0.107	-0.107	0.000	0.000	0.000	0.000
80	A	115	GLN	0	-0.013	-0.011	20.012	0.069	0.069	0.000	0.000	0.000	0.000
81	A	116	ARG	1	0.851	0.923	21.313	-0.317	-0.317	0.000	0.000	0.000	0.000
82	A	117	ASN	0	0.005	0.009	18.005	-0.178	-0.178	0.000	0.000	0.000	0.000
83	A	118	SER	0	0.054	0.032	22.228	-0.040	-0.040	0.000	0.000	0.000	0.000
84	A	119	GLY	0	0.019	0.002	21.280	-0.056	-0.056	0.000	0.000	0.000	0.000
85	A	120	ALA	0	-0.005	-0.018	22.242	0.103	0.103	0.000	0.000	0.000	0.000
86	A	121	THR	0	-0.053	-0.028	18.281	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	122	ARG	1	0.890	0.955	18.042	-0.432	-0.432	0.000	0.000	0.000	0.000
88	A	123	ARG	1	0.988	0.990	19.416	-0.611	-0.611	0.000	0.000	0.000	0.000
89	A	124	THR	0	-0.004	-0.005	20.432	-0.062	-0.062	0.000	0.000	0.000	0.000
90	A	125	ILE	0	-0.051	-0.029	15.032	-0.019	-0.019	0.000	0.000	0.000	0.000
91	A	126	GLU	-1	-0.894	-0.946	17.215	1.085	1.085	0.000	0.000	0.000	0.000
92	A	127	GLY	0	0.045	0.016	16.593	0.358	0.358	0.000	0.000	0.000	0.000
93	A	128	PHE	0	-0.014	-0.005	15.418	0.259	0.259	0.000	0.000	0.000	0.000
94	A	129	HIS	0	0.001	-0.008	12.519	0.139	0.139	0.000	0.000	0.000	0.000
95	A	130	LEU	0	-0.032	-0.001	11.463	0.918	0.918	0.000	0.000	0.000	0.000
96	A	131	PHE	0	-0.023	-0.010	7.762	0.684	0.684	0.000	0.000	0.000	0.000
97	A	132	GLU	-1	-0.855	-0.922	10.857	3.818	3.818	0.000	0.000	0.000	0.000
98	A	133	ASN	0	-0.071	-0.053	11.271	1.606	1.606	0.000	0.000	0.000	0.000
99	A	134	ASP	-1	-0.824	-0.878	9.380	11.357	11.357	0.000	0.000	0.000	0.000
100	A	135	ILE	0	-0.023	-0.001	12.395	-0.695	-0.695	0.000	0.000	0.000	0.000
101	A	136	PRO	0	0.054	0.022	16.032	0.008	0.008	0.000	0.000	0.000	0.000
102	A	137	ASN	0	-0.026	-0.034	18.496	-0.301	-0.301	0.000	0.000	0.000	0.000
103	A	138	PHE	0	-0.026	0.011	16.696	-0.200	-0.200	0.000	0.000	0.000	0.000
104	A	139	PRO	0	0.007	-0.005	16.491	0.202	0.202	0.000	0.000	0.000	0.000
105	A	140	ASP	-1	-0.810	-0.896	13.601	4.523	4.523	0.000	0.000	0.000	0.000
106	A	141	TYR	0	-0.053	-0.035	6.169	2.110	2.110	0.000	0.000	0.000	0.000
107	A	142	ILE	0	0.021	0.029	10.398	0.045	0.045	0.000	0.000	0.000	0.000
109	A	144	ILE	0	0.021	-0.001	7.399	-2.068	-2.068	0.000	0.000	0.000	0.000
111	A	146	LEU	0	0.013	0.011	8.424	0.271	0.271	0.000	0.000	0.000	0.000
112	A	147	VAL	0	-0.032	-0.006	9.227	-1.556	-1.556	0.000	0.000	0.000	0.000
113	A	148	PRO	0	0.047	0.012	11.830	0.670	0.670	0.000	0.000	0.000	0.000
114	A	149	LYS	1	0.815	0.886	15.114	1.440	1.440	0.000	0.000	0.000	0.000
115	A	150	THR	-1	-0.916	-0.942	16.276	-2.546	-2.546	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:36:GLU)