FMO DATABASE

FMODB ID: Y9732

Calculation Name: 1G7E-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1G7E

Chain ID: A

ChEMBL ID:

UniProt ID: P52555

Base Structure: SolutionNMR

Registration Date: 2025-09-03

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	122
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1070283.139079
FMO2-HF: Nuclear repulsion	1022376.136645
FMO2-HF: Total energy	-47907.002434
FMO2-MP2: Total energy	-48049.32468

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:33:LEU)

Summations of interaction energy for fragment #1(A:33:LEU)

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.
-162.136	-154.255	18.274	-12.346	-13.809	-0.125

Interaction energy analysis for fragmet #1(A:33:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.773 / q_NPA : 0.892

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	35	THR	0	-0.033	-0.031	2.695	-2.921	0.349	0.764	-1.797	-2.237	-0.014
4	A	36	LYS	1	0.854	0.921	4.505	27.565	27.763	-0.001	-0.014	-0.183	0.000
11	A	43	THR	0	-0.038	-0.029	2.567	3.924	4.509	0.413	-0.307	-0.691	-0.002
12	A	44	VAL	0	0.036	0.026	4.766	5.527	5.657	-0.001	-0.004	-0.124	0.000
63	A	95	ASP	-1	-0.812	-0.901	2.589	-65.526	-62.322	0.979	-1.992	-2.193	-0.026
66	A	98	ASP	-1	-0.864	-0.943	1.926	-114.368	-114.103	10.508	-6.083	-4.690	-0.073
67	A	99	LYS	1	0.769	0.869	2.026	51.249	51.381	5.613	-2.141	-3.604	-0.010
68	A	100	LEU	0	0.076	0.060	4.815	5.368	5.465	-0.001	-0.008	-0.087	0.000
5	A	37	GLY	0	0.019	-0.003	5.834	2.806	2.806	0.000	0.000	0.000	0.000
6	A	38	ALA	0	-0.042	0.008	9.117	2.041	2.041	0.000	0.000	0.000	0.000
7	A	39	LEU	0	0.053	0.032	9.923	-1.099	-1.099	0.000	0.000	0.000	0.000
8	A	40	PRO	0	0.005	0.017	8.026	-1.629	-1.629	0.000	0.000	0.000	0.000
9	A	41	LEU	0	-0.026	-0.015	8.959	0.088	0.088	0.000	0.000	0.000	0.000
10	A	42	ASP	-1	-0.752	-0.884	6.052	-43.887	-43.887	0.000	0.000	0.000	0.000
13	A	45	THR	0	0.016	0.003	6.862	3.261	3.261	0.000	0.000	0.000	0.000
14	A	46	PHE	0	-0.004	-0.008	8.692	3.640	3.640	0.000	0.000	0.000	0.000
15	A	47	TYR	0	-0.014	-0.021	8.481	1.442	1.442	0.000	0.000	0.000	0.000
16	A	48	LYS	1	0.864	0.950	12.137	20.650	20.650	0.000	0.000	0.000	0.000
17	A	49	VAL	0	-0.052	-0.047	12.770	1.648	1.648	0.000	0.000	0.000	0.000
18	A	50	ILE	0	0.017	0.019	14.728	1.049	1.049	0.000	0.000	0.000	0.000
19	A	51	PRO	0	-0.006	0.009	15.977	0.958	0.958	0.000	0.000	0.000	0.000
20	A	52	LYS	1	0.711	0.857	18.237	14.915	14.915	0.000	0.000	0.000	0.000
21	A	53	SER	0	0.069	0.024	18.095	-0.804	-0.804	0.000	0.000	0.000	0.000
22	A	54	LYS	1	0.824	0.922	20.161	12.179	12.179	0.000	0.000	0.000	0.000
23	A	55	PHE	0	-0.034	-0.029	18.918	0.419	0.419	0.000	0.000	0.000	0.000
24	A	56	VAL	0	0.055	0.043	14.904	-0.629	-0.629	0.000	0.000	0.000	0.000
25	A	57	LEU	0	-0.037	0.002	15.791	0.393	0.393	0.000	0.000	0.000	0.000
26	A	58	VAL	0	0.034	0.010	11.181	-1.189	-1.189	0.000	0.000	0.000	0.000
27	A	59	LYS	1	0.756	0.875	12.051	23.050	23.050	0.000	0.000	0.000	0.000
28	A	60	PHE	0	0.037	0.009	9.549	-2.161	-2.161	0.000	0.000	0.000	0.000
29	A	61	ASP	-1	-0.741	-0.870	12.760	-18.697	-18.697	0.000	0.000	0.000	0.000
30	A	62	THR	0	0.040	0.023	12.799	-1.589	-1.589	0.000	0.000	0.000	0.000
31	A	63	GLN	0	-0.014	-0.012	11.402	0.454	0.454	0.000	0.000	0.000	0.000
32	A	64	TYR	0	0.011	0.000	11.993	-0.923	-0.923	0.000	0.000	0.000	0.000
33	A	65	PRO	0	-0.053	-0.018	13.569	1.017	1.017	0.000	0.000	0.000	0.000
34	A	66	TYR	0	0.048	0.028	16.763	0.286	0.286	0.000	0.000	0.000	0.000
35	A	67	GLY	0	0.023	0.003	18.504	-0.594	-0.594	0.000	0.000	0.000	0.000
36	A	68	GLU	-1	-0.828	-0.913	18.957	-11.519	-11.519	0.000	0.000	0.000	0.000
37	A	69	LYS	1	0.775	0.853	12.248	20.826	20.826	0.000	0.000	0.000	0.000
38	A	70	GLN	0	0.001	0.013	14.755	-0.318	-0.318	0.000	0.000	0.000	0.000
39	A	71	ASP	-1	-0.767	-0.869	16.535	-12.677	-12.677	0.000	0.000	0.000	0.000
40	A	72	GLU	-1	-0.812	-0.903	19.960	-11.714	-11.714	0.000	0.000	0.000	0.000
41	A	73	PHE	0	0.027	-0.008	13.179	0.238	0.238	0.000	0.000	0.000	0.000
42	A	74	LYS	1	0.879	0.956	16.499	13.587	13.587	0.000	0.000	0.000	0.000
43	A	75	ARG	1	0.875	0.926	17.702	12.067	12.067	0.000	0.000	0.000	0.000
44	A	76	LEU	0	-0.057	-0.019	18.374	0.333	0.333	0.000	0.000	0.000	0.000
45	A	77	ALA	0	0.019	0.009	15.198	0.062	0.062	0.000	0.000	0.000	0.000
46	A	78	GLU	-1	-0.917	-0.957	17.317	-14.343	-14.343	0.000	0.000	0.000	0.000
47	A	79	ASN	0	-0.012	-0.005	18.829	0.339	0.339	0.000	0.000	0.000	0.000
48	A	80	SER	0	-0.055	-0.049	17.611	-0.124	-0.124	0.000	0.000	0.000	0.000
49	A	81	ALA	0	0.002	0.005	17.107	-0.420	-0.420	0.000	0.000	0.000	0.000
50	A	82	SER	0	-0.025	-0.007	18.071	-0.110	-0.110	0.000	0.000	0.000	0.000
51	A	83	SER	0	-0.069	-0.045	17.492	-0.354	-0.354	0.000	0.000	0.000	0.000
52	A	84	ASP	-1	-0.903	-0.936	19.335	-12.369	-12.369	0.000	0.000	0.000	0.000
53	A	85	ASP	-1	-0.792	-0.871	22.471	-12.816	-12.816	0.000	0.000	0.000	0.000
54	A	86	LEU	0	-0.053	-0.034	20.365	-0.345	-0.345	0.000	0.000	0.000	0.000
55	A	87	LEU	0	0.053	0.016	14.957	-0.432	-0.432	0.000	0.000	0.000	0.000
56	A	88	VAL	0	-0.020	-0.010	14.974	-0.061	-0.061	0.000	0.000	0.000	0.000
57	A	89	ALA	0	0.024	0.009	9.695	-0.601	-0.601	0.000	0.000	0.000	0.000
58	A	90	GLU	-1	-0.792	-0.868	9.649	-23.180	-23.180	0.000	0.000	0.000	0.000
59	A	91	VAL	0	0.012	0.028	5.410	-2.503	-2.503	0.000	0.000	0.000	0.000
60	A	92	GLY	0	0.021	0.017	7.891	2.986	2.986	0.000	0.000	0.000	0.000
61	A	93	ILE	0	0.000	-0.003	8.774	-2.748	-2.748	0.000	0.000	0.000	0.000
62	A	94	SER	0	-0.020	-0.043	8.451	3.020	3.020	0.000	0.000	0.000	0.000
64	A	96	TYR	0	-0.034	-0.059	5.608	-7.475	-7.475	0.000	0.000	0.000	0.000
65	A	97	GLY	0	0.026	0.025	7.583	-1.319	-1.319	0.000	0.000	0.000	0.000
69	A	101	ASN	0	-0.043	-0.064	6.116	-1.465	-1.465	0.000	0.000	0.000	0.000
70	A	102	MET	0	-0.077	0.016	7.106	1.104	1.104	0.000	0.000	0.000	0.000
71	A	103	GLU	-1	-0.812	-0.881	9.104	-22.959	-22.959	0.000	0.000	0.000	0.000
72	A	104	LEU	0	-0.018	-0.031	11.029	2.475	2.475	0.000	0.000	0.000	0.000
73	A	105	SER	0	-0.090	-0.049	12.359	1.573	1.573	0.000	0.000	0.000	0.000
74	A	106	GLU	-1	-0.856	-0.908	13.979	-18.935	-18.935	0.000	0.000	0.000	0.000
75	A	107	LYS	1	0.889	0.959	15.080	17.656	17.656	0.000	0.000	0.000	0.000
76	A	108	TYR	0	0.004	-0.008	15.244	1.316	1.316	0.000	0.000	0.000	0.000
77	A	109	LYS	1	0.800	0.880	18.705	15.297	15.297	0.000	0.000	0.000	0.000
78	A	110	LEU	0	-0.054	-0.016	15.784	0.587	0.587	0.000	0.000	0.000	0.000
79	A	111	ASP	-1	-0.776	-0.883	15.369	-16.671	-16.671	0.000	0.000	0.000	0.000
80	A	112	LYS	1	0.914	0.961	14.002	15.176	15.176	0.000	0.000	0.000	0.000
81	A	113	GLU	-1	-0.794	-0.858	16.341	-14.527	-14.527	0.000	0.000	0.000	0.000
82	A	114	SER	0	-0.096	-0.081	18.560	0.102	0.102	0.000	0.000	0.000	0.000
83	A	115	TYR	0	-0.018	-0.013	16.335	-0.020	-0.020	0.000	0.000	0.000	0.000
84	A	116	PRO	0	-0.054	-0.009	17.515	-0.954	-0.954	0.000	0.000	0.000	0.000
85	A	117	VAL	0	0.007	-0.019	16.575	0.930	0.930	0.000	0.000	0.000	0.000
86	A	118	PHE	0	-0.028	-0.016	16.409	-1.216	-1.216	0.000	0.000	0.000	0.000
87	A	119	TYR	0	0.027	0.017	15.757	0.538	0.538	0.000	0.000	0.000	0.000
88	A	120	LEU	0	-0.047	-0.010	17.254	-0.670	-0.670	0.000	0.000	0.000	0.000
89	A	121	PHE	0	0.061	0.016	15.007	0.262	0.262	0.000	0.000	0.000	0.000
90	A	122	ARG	1	0.804	0.871	19.328	13.061	13.061	0.000	0.000	0.000	0.000
91	A	123	ASP	-1	-0.775	-0.871	20.339	-14.272	-14.272	0.000	0.000	0.000	0.000
92	A	124	GLY	0	-0.013	-0.014	21.125	0.510	0.510	0.000	0.000	0.000	0.000
93	A	125	ASP	-1	-0.848	-0.917	19.637	-15.893	-15.893	0.000	0.000	0.000	0.000
94	A	126	PHE	0	-0.090	-0.051	14.297	-0.351	-0.351	0.000	0.000	0.000	0.000
95	A	127	GLU	-1	-0.822	-0.904	18.268	-13.148	-13.148	0.000	0.000	0.000	0.000
96	A	128	ASN	0	-0.122	-0.083	20.981	-0.514	-0.514	0.000	0.000	0.000	0.000
97	A	129	PRO	0	-0.004	0.031	18.209	0.378	0.378	0.000	0.000	0.000	0.000
98	A	130	VAL	0	-0.021	-0.018	20.935	0.499	0.499	0.000	0.000	0.000	0.000
99	A	131	PRO	0	0.007	0.010	21.369	-0.600	-0.600	0.000	0.000	0.000	0.000
100	A	132	TYR	0	-0.050	-0.031	21.282	0.953	0.953	0.000	0.000	0.000	0.000
101	A	133	SER	0	0.009	-0.006	20.929	-0.740	-0.740	0.000	0.000	0.000	0.000
102	A	134	GLY	0	0.018	0.005	21.703	0.722	0.722	0.000	0.000	0.000	0.000
103	A	135	ALA	0	0.021	0.018	21.432	-0.616	-0.616	0.000	0.000	0.000	0.000
104	A	136	VAL	0	-0.008	-0.001	16.813	0.082	0.082	0.000	0.000	0.000	0.000
105	A	137	LYS	1	0.815	0.893	20.181	11.619	11.619	0.000	0.000	0.000	0.000
106	A	138	VAL	0	0.013	-0.001	22.485	-0.068	-0.068	0.000	0.000	0.000	0.000
107	A	139	GLY	0	0.035	0.012	23.744	0.048	0.048	0.000	0.000	0.000	0.000
108	A	140	ALA	0	-0.027	-0.015	24.855	0.234	0.234	0.000	0.000	0.000	0.000
109	A	141	ILE	0	0.036	0.023	19.278	0.055	0.055	0.000	0.000	0.000	0.000
110	A	142	GLN	0	0.011	0.005	23.316	0.121	0.121	0.000	0.000	0.000	0.000
111	A	143	ARG	1	0.932	0.959	25.535	10.092	10.092	0.000	0.000	0.000	0.000
112	A	144	TRP	0	-0.024	-0.008	20.562	0.179	0.179	0.000	0.000	0.000	0.000
113	A	145	LEU	0	0.018	0.012	20.668	0.131	0.131	0.000	0.000	0.000	0.000
114	A	146	LYS	1	0.946	0.994	25.136	10.189	10.189	0.000	0.000	0.000	0.000
115	A	147	GLY	0	-0.054	-0.029	28.260	0.360	0.360	0.000	0.000	0.000	0.000
116	A	148	GLN	0	0.041	0.016	25.687	0.398	0.398	0.000	0.000	0.000	0.000
117	A	149	GLY	0	-0.012	0.009	28.592	-0.026	-0.026	0.000	0.000	0.000	0.000
118	A	150	VAL	0	-0.007	-0.015	23.703	-0.193	-0.193	0.000	0.000	0.000	0.000
119	A	151	TYR	0	-0.019	-0.004	27.078	0.327	0.327	0.000	0.000	0.000	0.000
120	A	152	LEU	0	-0.011	-0.016	21.226	-0.245	-0.245	0.000	0.000	0.000	0.000
121	A	153	GLY	0	0.026	0.004	22.986	-0.038	-0.038	0.000	0.000	0.000	0.000
122	A	154	MET	-1	-0.929	-0.944	23.814	-10.932	-10.932	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:33:LEU)