FMO DATABASE

FMODB ID: N8M6Q

Calculation Name: 7O3C-F-Other547

Preferred Name:

Target Type:

Ligand 3-letter code: CDL | HEA | HEM | HEC | PC1 | TGL | 3PE | FES | CUA | CU | MG | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7O3C

Chain ID: F

ChEMBL ID:

UniProt ID:

Base Structure: ElectronMicroscopy

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	102
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-824259.976903
FMO2-HF: Nuclear repulsion	779934.37613
FMO2-HF: Total energy	-44325.600772
FMO2-MP2: Total energy	-44455.926846

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:9:SER)

Summations of interaction energy for fragment #1(A:9:SER)

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.
91.537	94.943	1.243	-1.76	-2.89	-0.007

Interaction energy analysis for fragmet #1(A:9:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.862 / q_NPA : 0.922

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	11	LYS	1	0.968	0.990	3.870	39.147	40.603	-0.010	-0.642	-0.804	-0.001
4	A	12	TRP	0	0.091	0.036	3.847	1.608	1.930	-0.001	-0.044	-0.277	0.000
5	A	13	LEU	0	-0.035	-0.003	2.594	1.533	2.984	1.255	-1.050	-1.656	-0.006
6	A	14	ASP	-1	-0.816	-0.905	4.466	-24.379	-24.202	-0.001	-0.024	-0.153	0.000
7	A	15	GLY	0	0.040	0.016	6.931	3.993	3.993	0.000	0.000	0.000	0.000
8	A	16	PHE	0	-0.003	-0.004	7.829	3.046	3.046	0.000	0.000	0.000	0.000
9	A	17	ARG	1	0.971	0.990	5.896	36.170	36.170	0.000	0.000	0.000	0.000
10	A	18	LYS	1	0.996	1.007	10.050	23.817	23.817	0.000	0.000	0.000	0.000
11	A	19	TRP	0	-0.056	-0.029	12.144	1.485	1.485	0.000	0.000	0.000	0.000
12	A	20	TYR	0	0.032	0.001	12.697	1.411	1.411	0.000	0.000	0.000	0.000
13	A	21	TYR	0	-0.080	-0.060	14.110	1.222	1.222	0.000	0.000	0.000	0.000
14	A	22	ASN	0	-0.005	-0.005	15.996	1.708	1.708	0.000	0.000	0.000	0.000
15	A	23	ALA	0	-0.044	-0.023	17.333	0.932	0.932	0.000	0.000	0.000	0.000
16	A	24	ALA	0	-0.010	-0.003	17.995	0.722	0.722	0.000	0.000	0.000	0.000
17	A	25	GLY	0	-0.004	0.006	19.817	0.650	0.650	0.000	0.000	0.000	0.000
18	A	26	PHE	0	0.055	0.023	18.040	0.449	0.449	0.000	0.000	0.000	0.000
19	A	27	ASN	0	0.021	0.014	20.532	0.695	0.695	0.000	0.000	0.000	0.000
20	A	28	LYS	1	0.883	0.957	22.340	13.764	13.764	0.000	0.000	0.000	0.000
21	A	29	LEU	0	0.038	0.020	25.596	0.483	0.483	0.000	0.000	0.000	0.000
22	A	30	GLY	0	-0.001	0.001	26.264	0.378	0.378	0.000	0.000	0.000	0.000
23	A	31	LEU	0	-0.019	0.003	24.718	0.238	0.238	0.000	0.000	0.000	0.000
24	A	32	MET	0	0.012	0.018	22.238	-0.421	-0.421	0.000	0.000	0.000	0.000
25	A	33	ARG	1	0.860	0.929	16.141	16.659	16.659	0.000	0.000	0.000	0.000
26	A	34	ASP	-1	-0.769	-0.890	20.230	-14.207	-14.207	0.000	0.000	0.000	0.000
27	A	35	ASP	-1	-0.759	-0.821	22.487	-11.046	-11.046	0.000	0.000	0.000	0.000
28	A	36	THR	0	-0.116	-0.063	21.887	0.255	0.255	0.000	0.000	0.000	0.000
29	A	37	LEU	0	-0.045	-0.005	20.590	-0.101	-0.101	0.000	0.000	0.000	0.000
30	A	38	HIS	0	0.053	0.026	24.484	0.316	0.316	0.000	0.000	0.000	0.000
31	A	39	GLU	-1	-0.887	-0.931	27.243	-9.343	-9.343	0.000	0.000	0.000	0.000
32	A	40	THR	0	0.022	-0.005	27.696	0.061	0.061	0.000	0.000	0.000	0.000
33	A	41	GLU	-1	-0.861	-0.930	30.648	-8.757	-8.757	0.000	0.000	0.000	0.000
34	A	42	ASP	-1	-0.785	-0.875	26.938	-10.739	-10.739	0.000	0.000	0.000	0.000
35	A	43	VAL	0	-0.024	-0.015	25.689	-0.083	-0.083	0.000	0.000	0.000	0.000
36	A	44	LYS	1	0.867	0.923	28.291	8.867	8.867	0.000	0.000	0.000	0.000
37	A	45	GLU	-1	-0.712	-0.810	31.310	-8.663	-8.663	0.000	0.000	0.000	0.000
38	A	46	ALA	0	-0.031	-0.019	26.863	0.046	0.046	0.000	0.000	0.000	0.000
39	A	47	ILE	0	-0.033	-0.033	28.828	0.026	0.026	0.000	0.000	0.000	0.000
40	A	48	ARG	1	0.828	0.887	30.603	8.623	8.623	0.000	0.000	0.000	0.000
41	A	49	ARG	1	0.746	0.841	30.317	9.622	9.622	0.000	0.000	0.000	0.000
42	A	50	LEU	0	-0.056	-0.005	27.468	-0.168	-0.168	0.000	0.000	0.000	0.000
43	A	51	PRO	0	0.011	0.014	30.171	0.279	0.279	0.000	0.000	0.000	0.000
44	A	52	GLU	-1	-0.882	-0.962	33.029	-7.925	-7.925	0.000	0.000	0.000	0.000
45	A	53	ASP	-1	-0.922	-0.949	32.913	-8.736	-8.736	0.000	0.000	0.000	0.000
46	A	54	LEU	0	0.024	-0.001	27.302	-0.163	-0.163	0.000	0.000	0.000	0.000
47	A	55	TYR	0	-0.008	0.006	30.550	-0.177	-0.177	0.000	0.000	0.000	0.000
48	A	56	ASN	0	0.015	-0.004	32.841	0.045	0.045	0.000	0.000	0.000	0.000
49	A	57	ASP	-1	-0.912	-0.952	30.338	-9.700	-9.700	0.000	0.000	0.000	0.000
50	A	58	ARG	1	0.908	0.962	27.872	10.380	10.380	0.000	0.000	0.000	0.000
51	A	59	MET	0	-0.019	-0.012	30.458	-0.139	-0.139	0.000	0.000	0.000	0.000
52	A	60	PHE	0	-0.039	-0.010	33.334	0.142	0.142	0.000	0.000	0.000	0.000
53	A	61	ARG	1	0.839	0.881	27.001	11.144	11.144	0.000	0.000	0.000	0.000
54	A	62	ILE	0	0.025	0.011	29.454	-0.064	-0.064	0.000	0.000	0.000	0.000
55	A	63	LYS	1	0.959	0.973	31.526	7.993	7.993	0.000	0.000	0.000	0.000
56	A	64	ARG	1	0.908	0.963	28.896	10.339	10.339	0.000	0.000	0.000	0.000
57	A	65	ALA	0	0.022	0.009	29.611	0.041	0.041	0.000	0.000	0.000	0.000
58	A	66	LEU	0	0.006	0.019	31.505	0.046	0.046	0.000	0.000	0.000	0.000
59	A	67	ASP	-1	-0.805	-0.870	34.460	-7.998	-7.998	0.000	0.000	0.000	0.000
60	A	68	LEU	0	-0.055	-0.024	31.159	0.105	0.105	0.000	0.000	0.000	0.000
61	A	69	THR	0	-0.019	-0.034	30.858	0.095	0.095	0.000	0.000	0.000	0.000
62	A	70	MET	0	-0.056	-0.004	33.868	0.152	0.152	0.000	0.000	0.000	0.000
63	A	71	ARG	1	0.822	0.868	36.912	8.446	8.446	0.000	0.000	0.000	0.000
64	A	72	HIS	0	-0.018	0.005	34.666	-0.122	-0.122	0.000	0.000	0.000	0.000
65	A	73	GLN	0	-0.072	-0.035	34.112	-0.112	-0.112	0.000	0.000	0.000	0.000
66	A	74	ILE	0	-0.018	-0.016	28.007	-0.305	-0.305	0.000	0.000	0.000	0.000
67	A	75	LEU	0	-0.002	0.006	28.419	0.314	0.314	0.000	0.000	0.000	0.000
68	A	76	PRO	0	0.041	0.022	29.713	-0.265	-0.265	0.000	0.000	0.000	0.000
69	A	77	LYS	1	0.945	0.970	22.885	12.786	12.786	0.000	0.000	0.000	0.000
70	A	78	ASP	-1	-0.860	-0.929	26.015	-10.688	-10.688	0.000	0.000	0.000	0.000
71	A	79	GLN	0	-0.025	-0.037	27.151	-0.181	-0.181	0.000	0.000	0.000	0.000
72	A	80	TRP	0	-0.082	-0.027	22.700	-0.461	-0.461	0.000	0.000	0.000	0.000
73	A	81	THR	0	-0.028	-0.033	21.290	0.076	0.076	0.000	0.000	0.000	0.000
74	A	82	LYS	1	0.905	0.959	20.004	12.252	12.252	0.000	0.000	0.000	0.000
75	A	83	TYR	0	-0.046	-0.049	9.761	0.415	0.415	0.000	0.000	0.000	0.000
76	A	84	GLU	-1	-0.909	-0.932	14.272	-20.457	-20.457	0.000	0.000	0.000	0.000
77	A	85	GLU	-1	-0.860	-0.951	16.852	-14.327	-14.327	0.000	0.000	0.000	0.000
78	A	86	ASP	-1	-0.834	-0.891	18.047	-14.376	-14.376	0.000	0.000	0.000	0.000
79	A	87	LYS	1	0.876	0.935	17.996	14.994	14.994	0.000	0.000	0.000	0.000
80	A	88	PHE	0	-0.005	-0.017	13.900	0.175	0.175	0.000	0.000	0.000	0.000
81	A	89	TYR	0	0.040	-0.022	19.760	0.074	0.074	0.000	0.000	0.000	0.000
82	A	90	LEU	0	-0.002	0.007	22.728	0.379	0.379	0.000	0.000	0.000	0.000
83	A	91	GLU	-1	-0.923	-0.978	17.400	-15.653	-15.653	0.000	0.000	0.000	0.000
84	A	92	PRO	0	0.020	0.016	20.455	0.047	0.047	0.000	0.000	0.000	0.000
85	A	93	TYR	0	0.037	0.016	21.955	0.207	0.207	0.000	0.000	0.000	0.000
86	A	94	LEU	0	0.003	-0.005	22.076	0.244	0.244	0.000	0.000	0.000	0.000
87	A	95	LYS	1	0.878	0.945	16.421	15.948	15.948	0.000	0.000	0.000	0.000
88	A	96	GLU	-1	-0.800	-0.862	22.547	-10.777	-10.777	0.000	0.000	0.000	0.000
89	A	97	VAL	0	-0.001	0.013	25.862	0.240	0.240	0.000	0.000	0.000	0.000
90	A	98	ILE	0	-0.029	-0.023	22.717	0.149	0.149	0.000	0.000	0.000	0.000
91	A	99	ARG	1	0.807	0.881	24.586	10.891	10.891	0.000	0.000	0.000	0.000
92	A	100	GLU	-1	-0.765	-0.867	26.116	-9.066	-9.066	0.000	0.000	0.000	0.000
93	A	101	ARG	1	0.725	0.823	26.671	10.859	10.859	0.000	0.000	0.000	0.000
94	A	102	LYS	1	0.869	0.932	24.299	11.795	11.795	0.000	0.000	0.000	0.000
95	A	103	GLU	-1	-0.917	-0.943	28.520	-9.249	-9.249	0.000	0.000	0.000	0.000
96	A	104	ARG	1	0.958	0.969	30.867	9.173	9.173	0.000	0.000	0.000	0.000
97	A	105	GLU	-1	-0.869	-0.922	29.381	-9.989	-9.989	0.000	0.000	0.000	0.000
98	A	106	GLU	-1	-0.911	-0.958	30.048	-9.056	-9.056	0.000	0.000	0.000	0.000
99	A	107	TRP	0	0.016	0.012	32.320	0.146	0.146	0.000	0.000	0.000	0.000
100	A	108	ALA	0	-0.031	-0.019	35.651	0.178	0.178	0.000	0.000	0.000	0.000
101	A	109	LYS	1	0.856	0.933	29.954	9.856	9.856	0.000	0.000	0.000	0.000
102	A	110	LYS	0	-0.129	-0.046	34.237	1.099	1.099	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:SER)