FMO DATABASE

FMODB ID: 3M4NL

Calculation Name: 3CO1-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3CO1

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UPY8

Base Structure: X-ray

Registration Date: 2025-10-05

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	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1270278.582626
FMO2-HF: Nuclear repulsion	1215659.569264
FMO2-HF: Total energy	-54619.013362
FMO2-MP2: Total energy	-54775.626723

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:-1:GLY)

Summations of interaction energy for fragment #1(A:-1:GLY)

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.
3.564	4.307	-0.002	-0.282	-0.457	-0.001

Interaction energy analysis for fragmet #1(A:-1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.855 / q_NPA : 0.914

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	1	MET	0	-0.038	-0.017	3.824	-5.623	-4.904	-0.001	-0.279	-0.438	-0.001
87	A	85	MET	0	-0.006	0.006	4.609	-3.759	-3.735	-0.001	-0.003	-0.019	0.000
4	A	2	ALA	0	-0.003	-0.002	6.603	0.564	0.564	0.000	0.000	0.000	0.000
5	A	3	VAL	0	-0.007	0.006	9.143	1.004	1.004	0.000	0.000	0.000	0.000
6	A	4	ASN	0	-0.006	0.000	12.113	0.504	0.504	0.000	0.000	0.000	0.000
7	A	5	VAL	0	0.010	0.010	15.224	0.511	0.511	0.000	0.000	0.000	0.000
8	A	6	TYR	0	-0.030	-0.042	17.919	0.415	0.415	0.000	0.000	0.000	0.000
9	A	7	SER	0	-0.021	-0.021	21.907	0.041	0.041	0.000	0.000	0.000	0.000
10	A	8	THR	0	0.012	0.001	24.293	0.250	0.250	0.000	0.000	0.000	0.000
11	A	9	SER	0	-0.010	0.009	20.295	-0.187	-0.187	0.000	0.000	0.000	0.000
12	A	10	VAL	0	0.026	0.016	22.611	0.407	0.407	0.000	0.000	0.000	0.000
13	A	11	THR	0	-0.058	-0.045	20.953	-0.724	-0.724	0.000	0.000	0.000	0.000
14	A	12	SER	0	0.028	0.022	22.933	0.481	0.481	0.000	0.000	0.000	0.000
15	A	13	GLU	-1	-0.890	-0.932	24.955	-10.905	-10.905	0.000	0.000	0.000	0.000
16	A	14	ASN	0	-0.027	-0.020	26.742	-0.631	-0.631	0.000	0.000	0.000	0.000
17	A	15	LEU	0	0.064	0.043	24.966	0.307	0.307	0.000	0.000	0.000	0.000
18	A	16	SER	0	-0.001	-0.019	28.601	0.181	0.181	0.000	0.000	0.000	0.000
19	A	17	ARG	1	0.911	0.934	30.144	8.521	8.521	0.000	0.000	0.000	0.000
20	A	18	HIS	0	-0.020	-0.006	30.963	-0.033	-0.033	0.000	0.000	0.000	0.000
21	A	19	ASP	-1	-0.747	-0.852	28.838	-10.051	-10.051	0.000	0.000	0.000	0.000
22	A	20	MET	0	-0.026	0.010	24.670	-0.580	-0.580	0.000	0.000	0.000	0.000
23	A	21	LEU	0	-0.047	-0.028	25.761	-0.414	-0.414	0.000	0.000	0.000	0.000
24	A	22	ALA	0	0.016	0.019	27.248	-0.191	-0.191	0.000	0.000	0.000	0.000
25	A	23	TRP	0	0.096	0.050	18.330	0.006	0.006	0.000	0.000	0.000	0.000
26	A	24	VAL	0	-0.038	-0.019	22.542	-0.609	-0.609	0.000	0.000	0.000	0.000
27	A	25	ASN	0	-0.052	-0.023	23.189	-0.538	-0.538	0.000	0.000	0.000	0.000
28	A	26	ASP	-1	-0.852	-0.933	24.212	-11.669	-11.669	0.000	0.000	0.000	0.000
29	A	27	SER	0	-0.079	-0.048	18.880	-0.530	-0.530	0.000	0.000	0.000	0.000
30	A	28	LEU	0	-0.053	-0.037	17.842	-0.713	-0.713	0.000	0.000	0.000	0.000
31	A	29	HIS	0	-0.008	0.013	21.139	-0.067	-0.067	0.000	0.000	0.000	0.000
32	A	30	LEU	0	-0.084	-0.028	23.025	0.299	0.299	0.000	0.000	0.000	0.000
33	A	31	ASN	0	0.026	0.000	26.423	0.341	0.341	0.000	0.000	0.000	0.000
34	A	32	TYR	0	-0.059	-0.039	25.431	0.196	0.196	0.000	0.000	0.000	0.000
35	A	33	THR	0	0.040	0.012	29.855	0.112	0.112	0.000	0.000	0.000	0.000
36	A	34	LYS	1	0.928	0.964	32.144	8.966	8.966	0.000	0.000	0.000	0.000
37	A	35	ILE	0	0.041	0.019	28.251	-0.190	-0.190	0.000	0.000	0.000	0.000
38	A	36	GLU	-1	-0.871	-0.943	28.676	-9.364	-9.364	0.000	0.000	0.000	0.000
39	A	37	GLN	0	0.052	0.037	29.146	0.062	0.062	0.000	0.000	0.000	0.000
40	A	38	LEU	0	0.019	0.014	23.242	-0.230	-0.230	0.000	0.000	0.000	0.000
41	A	39	CYS	0	-0.066	-0.021	25.127	-0.402	-0.402	0.000	0.000	0.000	0.000
42	A	40	SER	0	0.017	0.004	26.167	-0.232	-0.232	0.000	0.000	0.000	0.000
43	A	41	GLY	0	0.019	0.009	22.664	-0.170	-0.170	0.000	0.000	0.000	0.000
44	A	42	ALA	0	-0.002	-0.013	20.845	-0.816	-0.816	0.000	0.000	0.000	0.000
45	A	43	ALA	0	0.052	0.028	19.972	-0.714	-0.714	0.000	0.000	0.000	0.000
46	A	44	TYR	0	0.044	0.017	18.383	-0.591	-0.591	0.000	0.000	0.000	0.000
47	A	45	CYS	0	-0.064	-0.021	16.116	-1.227	-1.227	0.000	0.000	0.000	0.000
48	A	46	GLN	0	0.063	0.035	15.008	-0.626	-0.626	0.000	0.000	0.000	0.000
49	A	47	PHE	0	0.062	0.026	14.895	-0.891	-0.891	0.000	0.000	0.000	0.000
50	A	48	MET	0	-0.026	-0.009	10.937	-0.936	-0.936	0.000	0.000	0.000	0.000
51	A	49	ASP	-1	-0.842	-0.918	10.373	-26.943	-26.943	0.000	0.000	0.000	0.000
52	A	50	MET	0	-0.006	0.016	10.412	-1.439	-1.439	0.000	0.000	0.000	0.000
53	A	51	LEU	0	-0.001	0.023	9.675	-0.624	-0.624	0.000	0.000	0.000	0.000
54	A	52	PHE	0	0.008	-0.025	5.687	-3.306	-3.306	0.000	0.000	0.000	0.000
55	A	53	PRO	0	0.073	0.048	6.467	0.537	0.537	0.000	0.000	0.000	0.000
56	A	54	GLY	0	0.000	0.013	7.157	-4.191	-4.191	0.000	0.000	0.000	0.000
57	A	55	CYS	0	-0.105	-0.041	7.649	0.584	0.584	0.000	0.000	0.000	0.000
58	A	56	VAL	0	0.033	0.012	9.154	1.965	1.965	0.000	0.000	0.000	0.000
59	A	57	HIS	0	-0.009	-0.004	12.991	1.433	1.433	0.000	0.000	0.000	0.000
60	A	58	LEU	0	0.089	0.032	14.991	1.443	1.443	0.000	0.000	0.000	0.000
61	A	59	ARG	1	0.996	0.997	17.238	17.662	17.662	0.000	0.000	0.000	0.000
62	A	60	LYS	1	0.862	0.937	17.987	17.293	17.293	0.000	0.000	0.000	0.000
63	A	61	VAL	0	-0.027	0.013	18.850	0.572	0.572	0.000	0.000	0.000	0.000
64	A	62	LYS	1	0.874	0.931	21.887	11.435	11.435	0.000	0.000	0.000	0.000
65	A	63	PHE	0	0.064	0.004	19.622	0.277	0.277	0.000	0.000	0.000	0.000
66	A	64	GLN	0	-0.047	-0.014	25.435	0.269	0.269	0.000	0.000	0.000	0.000
67	A	65	ALA	0	-0.016	0.004	27.781	0.333	0.333	0.000	0.000	0.000	0.000
68	A	66	LYS	1	0.951	0.965	29.627	8.901	8.901	0.000	0.000	0.000	0.000
69	A	67	LEU	0	0.007	0.017	32.323	0.235	0.235	0.000	0.000	0.000	0.000
70	A	68	GLU	-1	-0.803	-0.912	31.424	-9.793	-9.793	0.000	0.000	0.000	0.000
71	A	69	HIS	0	0.051	0.013	30.371	-0.350	-0.350	0.000	0.000	0.000	0.000
72	A	70	GLU	-1	-0.814	-0.908	28.573	-10.703	-10.703	0.000	0.000	0.000	0.000
73	A	71	TYR	0	0.022	0.018	26.773	-0.590	-0.590	0.000	0.000	0.000	0.000
74	A	72	ILE	0	0.010	0.004	25.615	-0.629	-0.629	0.000	0.000	0.000	0.000
75	A	73	HIS	0	-0.083	-0.043	23.810	-0.309	-0.309	0.000	0.000	0.000	0.000
76	A	74	ASN	0	0.006	-0.007	22.226	-0.939	-0.939	0.000	0.000	0.000	0.000
77	A	75	PHE	0	0.038	0.007	20.857	-0.916	-0.916	0.000	0.000	0.000	0.000
78	A	76	LYS	1	0.896	0.960	20.819	12.364	12.364	0.000	0.000	0.000	0.000
79	A	77	VAL	0	-0.024	-0.010	17.311	-0.845	-0.845	0.000	0.000	0.000	0.000
80	A	78	LEU	0	0.033	0.018	15.999	-1.237	-1.237	0.000	0.000	0.000	0.000
81	A	79	GLN	0	-0.001	-0.002	16.079	-0.412	-0.412	0.000	0.000	0.000	0.000
82	A	80	ALA	0	-0.039	-0.020	15.459	-0.687	-0.687	0.000	0.000	0.000	0.000
83	A	81	ALA	0	0.028	0.017	12.038	-1.380	-1.380	0.000	0.000	0.000	0.000
84	A	82	PHE	0	0.040	-0.002	11.411	-2.009	-2.009	0.000	0.000	0.000	0.000
85	A	83	LYS	1	0.948	0.984	12.443	17.723	17.723	0.000	0.000	0.000	0.000
86	A	84	LYS	1	0.811	0.904	7.063	33.977	33.977	0.000	0.000	0.000	0.000
88	A	86	GLY	0	0.008	0.014	8.731	-0.897	-0.897	0.000	0.000	0.000	0.000
89	A	87	VAL	0	-0.032	-0.012	11.339	1.241	1.241	0.000	0.000	0.000	0.000
90	A	88	ASP	-1	-0.845	-0.904	13.911	-17.307	-17.307	0.000	0.000	0.000	0.000
91	A	89	LYS	1	0.870	0.960	17.328	15.252	15.252	0.000	0.000	0.000	0.000
92	A	90	ILE	0	0.019	0.003	19.345	-0.234	-0.234	0.000	0.000	0.000	0.000
93	A	91	ILE	0	0.022	0.018	18.427	0.434	0.434	0.000	0.000	0.000	0.000
94	A	92	PRO	0	0.004	0.017	22.612	0.329	0.329	0.000	0.000	0.000	0.000
95	A	93	VAL	0	0.025	-0.008	23.895	0.452	0.452	0.000	0.000	0.000	0.000
96	A	94	GLU	-1	-0.914	-0.960	26.507	-9.861	-9.861	0.000	0.000	0.000	0.000
97	A	95	LYS	1	0.809	0.894	29.595	10.259	10.259	0.000	0.000	0.000	0.000
98	A	96	LEU	0	0.003	0.019	24.487	0.272	0.272	0.000	0.000	0.000	0.000
99	A	97	VAL	0	0.010	-0.001	27.599	0.216	0.216	0.000	0.000	0.000	0.000
100	A	98	LYS	1	0.865	0.945	29.872	9.506	9.506	0.000	0.000	0.000	0.000
101	A	99	GLY	0	0.039	0.020	31.803	0.287	0.287	0.000	0.000	0.000	0.000
102	A	100	LYS	1	0.848	0.931	32.876	9.507	9.507	0.000	0.000	0.000	0.000
103	A	101	PHE	0	0.055	0.026	32.150	-0.348	-0.348	0.000	0.000	0.000	0.000
104	A	102	GLN	0	-0.020	-0.018	31.726	-0.078	-0.078	0.000	0.000	0.000	0.000
105	A	103	ASP	-1	-0.767	-0.880	30.018	-10.054	-10.054	0.000	0.000	0.000	0.000
106	A	104	ASN	0	-0.038	-0.049	27.466	-0.818	-0.818	0.000	0.000	0.000	0.000
107	A	105	PHE	0	-0.038	-0.009	26.931	-0.437	-0.437	0.000	0.000	0.000	0.000
108	A	106	GLU	-1	-0.845	-0.922	27.540	-10.459	-10.459	0.000	0.000	0.000	0.000
109	A	107	PHE	0	-0.031	-0.015	19.916	-0.443	-0.443	0.000	0.000	0.000	0.000
110	A	108	ILE	0	0.018	0.003	21.902	-0.614	-0.614	0.000	0.000	0.000	0.000
111	A	109	GLN	0	0.002	-0.019	22.917	-0.668	-0.668	0.000	0.000	0.000	0.000
112	A	110	TRP	0	-0.035	-0.028	16.545	0.004	0.004	0.000	0.000	0.000	0.000
113	A	111	PHE	0	0.020	-0.006	15.628	-0.598	-0.598	0.000	0.000	0.000	0.000
114	A	112	LYS	1	0.805	0.893	18.127	13.500	13.500	0.000	0.000	0.000	0.000
115	A	113	LYS	1	0.930	0.971	18.857	11.897	11.897	0.000	0.000	0.000	0.000
116	A	114	PHE	0	-0.020	-0.004	11.902	-0.692	-0.692	0.000	0.000	0.000	0.000
117	A	115	PHE	0	0.017	0.000	14.364	-1.444	-1.444	0.000	0.000	0.000	0.000
118	A	116	ASP	-1	-0.796	-0.896	14.448	-16.197	-16.197	0.000	0.000	0.000	0.000
119	A	117	ALA	0	-0.047	-0.012	14.999	-0.147	-0.147	0.000	0.000	0.000	0.000
120	A	118	ASN	0	-0.055	-0.050	10.248	-3.783	-3.783	0.000	0.000	0.000	0.000
121	A	119	TYR	0	-0.056	-0.033	10.034	-2.007	-2.007	0.000	0.000	0.000	0.000
122	A	120	ASP	-1	-0.823	-0.900	8.814	-27.850	-27.850	0.000	0.000	0.000	0.000
123	A	121	GLY	0	0.005	0.005	11.433	0.797	0.797	0.000	0.000	0.000	0.000
124	A	122	LYS	1	0.708	0.857	8.191	30.276	30.276	0.000	0.000	0.000	0.000
125	A	123	ASP	-1	-0.859	-0.917	13.209	-15.840	-15.840	0.000	0.000	0.000	0.000
126	A	124	TYR	0	-0.083	-0.078	13.494	-0.804	-0.804	0.000	0.000	0.000	0.000
127	A	125	ASN	0	0.044	0.021	16.049	1.405	1.405	0.000	0.000	0.000	0.000
128	A	126	PRO	0	0.010	0.001	18.562	-0.393	-0.393	0.000	0.000	0.000	0.000
129	A	127	LEU	0	-0.013	-0.015	20.066	0.364	0.364	0.000	0.000	0.000	0.000
130	A	128	LEU	0	-0.018	-0.007	16.755	0.164	0.164	0.000	0.000	0.000	0.000
131	A	129	ALA	0	-0.067	-0.030	17.808	-0.397	-0.397	0.000	0.000	0.000	0.000
132	A	130	ARG	0	-0.052	-0.006	19.505	0.516	0.516	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:-1:GLY)