FMO DATABASE

FMODB ID: N69JQ

Calculation Name: 7O3C-e-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: e

ChEMBL ID:

UniProt ID:

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-06

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	104
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-801516.049311
FMO2-HF: Nuclear repulsion	760126.235022
FMO2-HF: Total energy	-41389.814289
FMO2-MP2: Total energy	-41512.022396

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:6:GLU)

Summations of interaction energy for fragment #1(A:6: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.
-18.057	-14.842	0.099	-1.484	-1.83	-0.007

Interaction energy analysis for fragmet #1(A:6:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.104 / q_NPA : -0.060

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	8	ASP	-1	-0.836	-0.910	3.193	-10.494	-8.226	0.088	-1.134	-1.223	-0.005
5	A	10	GLU	-1	-0.974	-0.993	3.577	-3.985	-3.124	0.012	-0.345	-0.528	-0.002
6	A	11	PHE	0	0.027	0.010	4.608	1.541	1.627	-0.001	-0.005	-0.079	0.000
4	A	9	GLU	-1	-0.872	-0.944	6.009	-3.043	-3.043	0.000	0.000	0.000	0.000
7	A	12	ASP	-1	-0.814	-0.927	6.396	-2.864	-2.864	0.000	0.000	0.000	0.000
8	A	13	ALA	0	-0.001	0.009	9.503	0.687	0.687	0.000	0.000	0.000	0.000
9	A	14	ARG	1	0.897	0.964	6.920	1.360	1.360	0.000	0.000	0.000	0.000
10	A	15	TRP	0	-0.037	-0.011	9.487	0.692	0.692	0.000	0.000	0.000	0.000
11	A	16	VAL	0	0.004	-0.001	12.587	0.270	0.270	0.000	0.000	0.000	0.000
12	A	17	THR	0	-0.058	-0.035	13.899	0.213	0.213	0.000	0.000	0.000	0.000
13	A	18	TYR	0	-0.080	-0.063	14.653	0.131	0.131	0.000	0.000	0.000	0.000
14	A	19	PHE	0	0.009	0.000	16.110	0.137	0.137	0.000	0.000	0.000	0.000
15	A	20	ASN	0	-0.027	-0.036	18.262	0.105	0.105	0.000	0.000	0.000	0.000
16	A	21	LYS	1	0.840	0.962	18.624	0.126	0.126	0.000	0.000	0.000	0.000
17	A	22	PRO	0	-0.006	-0.021	21.894	0.000	0.000	0.000	0.000	0.000	0.000
18	A	23	ASP	-1	-0.915	-0.959	23.382	-0.032	-0.032	0.000	0.000	0.000	0.000
19	A	24	ILE	0	-0.052	-0.013	21.042	0.038	0.038	0.000	0.000	0.000	0.000
20	A	25	ASP	-1	-0.781	-0.884	24.590	0.054	0.054	0.000	0.000	0.000	0.000
21	A	26	ALA	0	0.051	0.002	24.923	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	27	TRP	0	-0.031	-0.040	24.810	0.001	0.001	0.000	0.000	0.000	0.000
23	A	28	GLU	-1	-0.816	-0.888	19.544	0.248	0.248	0.000	0.000	0.000	0.000
24	A	29	LEU	0	0.045	0.019	20.335	0.005	0.005	0.000	0.000	0.000	0.000
25	A	30	ARG	1	0.898	0.975	20.366	-0.056	-0.056	0.000	0.000	0.000	0.000
26	A	31	LYS	1	0.858	0.932	19.330	-0.302	-0.302	0.000	0.000	0.000	0.000
27	A	32	GLY	0	0.013	0.009	16.456	0.050	0.050	0.000	0.000	0.000	0.000
28	A	33	MET	0	0.042	0.017	15.963	-0.053	-0.053	0.000	0.000	0.000	0.000
29	A	34	ASN	0	-0.071	-0.042	17.379	-0.023	-0.023	0.000	0.000	0.000	0.000
30	A	35	THR	0	-0.042	-0.027	13.025	0.120	0.120	0.000	0.000	0.000	0.000
31	A	36	LEU	0	-0.010	0.012	12.485	0.048	0.048	0.000	0.000	0.000	0.000
32	A	37	VAL	0	0.003	-0.015	13.535	-0.168	-0.168	0.000	0.000	0.000	0.000
33	A	38	GLY	0	-0.023	-0.005	15.196	-0.048	-0.048	0.000	0.000	0.000	0.000
34	A	39	TYR	0	0.002	0.006	8.949	-0.005	-0.005	0.000	0.000	0.000	0.000
35	A	40	ASP	-1	-0.968	-0.984	11.009	-1.251	-1.251	0.000	0.000	0.000	0.000
36	A	41	LEU	0	0.004	-0.003	9.022	-0.452	-0.452	0.000	0.000	0.000	0.000
37	A	42	VAL	0	-0.008	0.001	12.421	0.371	0.371	0.000	0.000	0.000	0.000
38	A	43	PRO	0	-0.021	-0.020	13.428	-0.264	-0.264	0.000	0.000	0.000	0.000
39	A	44	GLU	-1	-0.845	-0.915	12.714	-2.194	-2.194	0.000	0.000	0.000	0.000
40	A	45	PRO	0	0.046	-0.005	15.281	0.164	0.164	0.000	0.000	0.000	0.000
41	A	46	LYS	1	0.903	0.961	15.693	1.370	1.370	0.000	0.000	0.000	0.000
42	A	47	ILE	0	0.002	0.003	11.530	0.210	0.210	0.000	0.000	0.000	0.000
43	A	48	ILE	0	-0.011	0.000	16.130	0.206	0.206	0.000	0.000	0.000	0.000
44	A	49	ASP	-1	-0.779	-0.889	19.394	-0.857	-0.857	0.000	0.000	0.000	0.000
45	A	50	ALA	0	-0.028	-0.013	18.010	0.116	0.116	0.000	0.000	0.000	0.000
46	A	51	ALA	0	-0.003	0.004	19.080	0.114	0.114	0.000	0.000	0.000	0.000
47	A	52	LEU	0	0.018	0.003	20.877	0.101	0.101	0.000	0.000	0.000	0.000
48	A	53	ARG	1	0.852	0.915	23.508	0.535	0.535	0.000	0.000	0.000	0.000
49	A	54	ALA	0	-0.022	-0.008	22.179	0.060	0.060	0.000	0.000	0.000	0.000
50	A	55	CYS	0	-0.060	-0.015	24.261	0.056	0.056	0.000	0.000	0.000	0.000
51	A	56	ARG	1	0.925	0.942	26.443	0.304	0.304	0.000	0.000	0.000	0.000
52	A	57	ARG	1	0.856	0.961	23.154	0.356	0.356	0.000	0.000	0.000	0.000
53	A	58	LEU	0	-0.025	-0.013	27.485	0.030	0.030	0.000	0.000	0.000	0.000
54	A	59	ASN	0	-0.062	-0.024	30.938	0.004	0.004	0.000	0.000	0.000	0.000
55	A	60	ASP	-1	-0.785	-0.852	29.576	-0.174	-0.174	0.000	0.000	0.000	0.000
56	A	61	PHE	0	0.046	0.016	30.719	-0.023	-0.023	0.000	0.000	0.000	0.000
57	A	62	ALA	0	0.020	0.014	30.690	-0.024	-0.024	0.000	0.000	0.000	0.000
58	A	63	SER	0	-0.086	-0.083	25.880	-0.021	-0.021	0.000	0.000	0.000	0.000
59	A	64	ALA	0	0.063	0.021	25.982	-0.038	-0.038	0.000	0.000	0.000	0.000
60	A	65	VAL	0	0.014	0.003	26.576	-0.046	-0.046	0.000	0.000	0.000	0.000
61	A	66	ARG	1	0.943	0.974	25.845	0.171	0.171	0.000	0.000	0.000	0.000
62	A	67	ILE	0	-0.037	-0.017	20.866	-0.027	-0.027	0.000	0.000	0.000	0.000
63	A	68	LEU	0	-0.028	-0.007	22.790	-0.077	-0.077	0.000	0.000	0.000	0.000
64	A	69	GLU	-1	-0.899	-0.957	25.267	-0.345	-0.345	0.000	0.000	0.000	0.000
65	A	70	VAL	0	-0.023	-0.015	20.515	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	71	VAL	0	0.000	-0.001	19.521	-0.085	-0.085	0.000	0.000	0.000	0.000
67	A	72	LYS	1	0.793	0.898	21.667	0.515	0.515	0.000	0.000	0.000	0.000
68	A	73	ASP	-1	-0.857	-0.928	22.721	-0.505	-0.505	0.000	0.000	0.000	0.000
69	A	74	LYS	1	0.909	0.955	15.464	0.858	0.858	0.000	0.000	0.000	0.000
70	A	75	ALA	0	-0.034	-0.006	19.093	-0.108	-0.108	0.000	0.000	0.000	0.000
71	A	76	GLY	0	-0.002	0.014	21.162	-0.016	-0.016	0.000	0.000	0.000	0.000
72	A	77	PRO	0	-0.040	-0.041	22.642	0.045	0.045	0.000	0.000	0.000	0.000
73	A	78	HIS	0	0.000	0.023	19.361	0.136	0.136	0.000	0.000	0.000	0.000
74	A	79	LYS	1	0.843	0.900	24.278	0.654	0.654	0.000	0.000	0.000	0.000
75	A	80	GLU	-1	-0.832	-0.925	23.186	-0.897	-0.897	0.000	0.000	0.000	0.000
76	A	81	ILE	0	0.002	0.004	19.169	-0.028	-0.028	0.000	0.000	0.000	0.000
77	A	82	TYR	0	0.047	0.019	22.418	-0.016	-0.016	0.000	0.000	0.000	0.000
78	A	83	PRO	0	0.019	0.000	24.854	0.010	0.010	0.000	0.000	0.000	0.000
79	A	84	TYR	0	-0.043	-0.010	19.802	-0.015	-0.015	0.000	0.000	0.000	0.000
80	A	85	VAL	0	0.060	0.021	20.297	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	86	ILE	0	-0.017	-0.006	22.986	0.029	0.029	0.000	0.000	0.000	0.000
82	A	87	GLN	0	-0.092	-0.057	26.195	0.044	0.044	0.000	0.000	0.000	0.000
83	A	88	GLU	-1	-0.870	-0.923	21.718	-1.141	-1.141	0.000	0.000	0.000	0.000
84	A	89	LEU	0	0.003	0.001	21.745	0.031	0.031	0.000	0.000	0.000	0.000
85	A	90	ARG	1	0.891	0.977	25.103	0.617	0.617	0.000	0.000	0.000	0.000
86	A	91	PRO	0	0.054	0.007	27.128	0.048	0.048	0.000	0.000	0.000	0.000
87	A	92	THR	0	-0.018	-0.016	25.002	0.048	0.048	0.000	0.000	0.000	0.000
88	A	93	LEU	0	-0.005	-0.011	27.641	0.043	0.043	0.000	0.000	0.000	0.000
89	A	94	ASN	0	-0.038	-0.027	30.632	0.014	0.014	0.000	0.000	0.000	0.000
90	A	95	GLU	-1	-0.895	-0.927	28.808	-0.474	-0.474	0.000	0.000	0.000	0.000
91	A	96	LEU	0	-0.067	-0.042	27.732	0.033	0.033	0.000	0.000	0.000	0.000
92	A	97	GLY	0	-0.034	-0.004	32.435	0.028	0.028	0.000	0.000	0.000	0.000
93	A	98	ILE	0	-0.059	-0.017	28.469	0.023	0.023	0.000	0.000	0.000	0.000
94	A	99	SER	0	0.016	0.007	32.652	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	100	THR	0	-0.038	-0.045	29.913	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	101	PRO	0	0.026	-0.011	28.661	0.024	0.024	0.000	0.000	0.000	0.000
97	A	102	GLU	-1	-0.861	-0.915	30.912	-0.467	-0.467	0.000	0.000	0.000	0.000
98	A	103	GLU	-1	-0.886	-0.914	34.183	-0.361	-0.361	0.000	0.000	0.000	0.000
99	A	104	LEU	0	-0.068	-0.030	33.707	0.021	0.021	0.000	0.000	0.000	0.000
100	A	105	GLY	0	-0.026	0.000	36.849	0.020	0.020	0.000	0.000	0.000	0.000
101	A	106	LEU	0	-0.049	-0.042	32.713	0.021	0.021	0.000	0.000	0.000	0.000
102	A	107	ASP	-1	-0.896	-0.936	32.971	-0.322	-0.322	0.000	0.000	0.000	0.000
103	A	108	LYS	1	0.811	0.899	33.939	0.211	0.211	0.000	0.000	0.000	0.000
104	A	109	VAL	-1	-0.880	-0.926	37.167	-0.176	-0.176	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:GLU)