FMO DATABASE

FMODB ID: Y79K2

Calculation Name: 7DR2-A-Other547

Preferred Name:

Target Type:

Ligand 3-letter code: CLA | CL0 | BCR | LMG | LHG | PQN | SF4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7DR2

Chain ID: A

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	139
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1077469.624595
FMO2-HF: Nuclear repulsion	1024547.936573
FMO2-HF: Total energy	-52921.688021
FMO2-MP2: Total energy	-53078.529254

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:78:THR)

Summations of interaction energy for fragment #1(A:78:THR)

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.
97.525	102.813	1.072	-2.603	-3.757	-0.015

Interaction energy analysis for fragmet #1(A:78:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.883 / 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	80	ASN	0	0.008	0.014	2.096	2.884	6.225	0.984	-1.852	-2.473	-0.012
4	A	81	LEU	0	0.007	0.023	3.792	5.002	5.219	0.007	-0.079	-0.146	-0.001
82	A	159	LYS	1	0.878	0.940	3.945	56.602	56.724	-0.001	-0.013	-0.108	0.000
84	A	161	TYR	0	-0.027	-0.049	2.751	-3.586	-2.116	0.084	-0.644	-0.909	-0.002
93	A	170	GLN	0	-0.009	-0.028	4.293	-3.933	-3.871	-0.001	-0.007	-0.054	0.000
94	A	171	PHE	0	-0.039	-0.022	4.314	-2.240	-2.164	-0.001	-0.008	-0.067	0.000
5	A	82	ASN	0	-0.022	-0.018	6.767	0.496	0.496	0.000	0.000	0.000	0.000
6	A	83	ALA	0	0.082	0.047	8.139	1.337	1.337	0.000	0.000	0.000	0.000
7	A	84	PRO	0	-0.036	-0.016	9.597	1.138	1.138	0.000	0.000	0.000	0.000
8	A	85	THR	0	0.033	0.021	13.473	0.036	0.036	0.000	0.000	0.000	0.000
9	A	86	PRO	0	-0.033	0.002	15.176	0.805	0.805	0.000	0.000	0.000	0.000
10	A	87	ILE	0	-0.010	-0.003	18.286	0.036	0.036	0.000	0.000	0.000	0.000
11	A	88	PHE	0	0.006	-0.016	21.419	0.238	0.238	0.000	0.000	0.000	0.000
12	A	89	GLY	0	-0.006	0.017	23.081	0.467	0.467	0.000	0.000	0.000	0.000
13	A	90	GLY	0	0.049	0.017	24.722	0.558	0.558	0.000	0.000	0.000	0.000
14	A	91	SER	0	-0.047	-0.028	24.452	-0.368	-0.368	0.000	0.000	0.000	0.000
15	A	92	THR	0	0.051	0.026	25.948	-0.309	-0.309	0.000	0.000	0.000	0.000
16	A	93	GLY	0	0.005	0.017	27.367	-0.054	-0.054	0.000	0.000	0.000	0.000
17	A	94	GLY	0	-0.002	-0.030	23.200	-0.351	-0.351	0.000	0.000	0.000	0.000
18	A	95	LEU	0	-0.090	-0.041	16.928	0.087	0.087	0.000	0.000	0.000	0.000
19	A	96	LEU	0	0.091	0.060	21.070	-0.056	-0.056	0.000	0.000	0.000	0.000
20	A	97	ARG	1	1.029	1.003	22.396	11.318	11.318	0.000	0.000	0.000	0.000
21	A	98	LYS	1	0.861	0.943	19.019	15.929	15.929	0.000	0.000	0.000	0.000
22	A	99	ALA	0	-0.051	-0.036	17.861	-0.441	-0.441	0.000	0.000	0.000	0.000
23	A	100	GLU	-1	-0.910	-0.950	17.632	-14.146	-14.146	0.000	0.000	0.000	0.000
24	A	101	VAL	0	-0.052	-0.015	19.939	0.378	0.378	0.000	0.000	0.000	0.000
25	A	102	GLU	-1	-0.899	-0.948	18.478	-13.914	-13.914	0.000	0.000	0.000	0.000
26	A	103	GLU	-1	-0.814	-0.886	15.182	-17.802	-17.802	0.000	0.000	0.000	0.000
27	A	104	PHE	0	0.005	-0.001	12.513	0.275	0.275	0.000	0.000	0.000	0.000
28	A	105	TYR	0	-0.008	-0.035	12.498	-1.815	-1.815	0.000	0.000	0.000	0.000
29	A	106	SER	0	-0.027	-0.028	9.790	0.351	0.351	0.000	0.000	0.000	0.000
30	A	107	ILE	0	-0.024	-0.002	10.411	-2.022	-2.022	0.000	0.000	0.000	0.000
31	A	108	THR	0	0.018	0.008	7.764	0.078	0.078	0.000	0.000	0.000	0.000
32	A	109	TRP	0	-0.010	-0.010	10.258	-0.697	-0.697	0.000	0.000	0.000	0.000
33	A	110	THR	0	0.019	0.010	12.089	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	111	GLY	0	0.050	0.029	14.434	0.711	0.711	0.000	0.000	0.000	0.000
35	A	112	LYS	1	0.802	0.873	16.128	18.697	18.697	0.000	0.000	0.000	0.000
36	A	113	SER	0	-0.028	-0.022	20.713	1.025	1.025	0.000	0.000	0.000	0.000
37	A	114	GLU	-1	-0.872	-0.928	21.860	-14.520	-14.520	0.000	0.000	0.000	0.000
38	A	115	THR	0	-0.008	-0.006	23.436	0.489	0.489	0.000	0.000	0.000	0.000
39	A	116	VAL	0	0.019	0.004	23.869	-0.591	-0.591	0.000	0.000	0.000	0.000
40	A	117	PHE	0	-0.032	-0.026	19.514	-0.064	-0.064	0.000	0.000	0.000	0.000
41	A	118	GLU	-1	-0.924	-0.955	24.847	-11.337	-11.337	0.000	0.000	0.000	0.000
42	A	119	LEU	0	-0.033	-0.011	20.839	-0.875	-0.875	0.000	0.000	0.000	0.000
43	A	120	PRO	0	-0.048	-0.042	20.430	0.424	0.424	0.000	0.000	0.000	0.000
44	A	121	THR	0	-0.039	-0.008	22.466	0.191	0.191	0.000	0.000	0.000	0.000
45	A	122	GLY	0	0.057	0.025	25.282	0.553	0.553	0.000	0.000	0.000	0.000
46	A	123	GLY	0	0.007	0.007	26.395	-0.474	-0.474	0.000	0.000	0.000	0.000
47	A	124	ALA	0	0.010	0.003	26.339	0.379	0.379	0.000	0.000	0.000	0.000
48	A	125	ALA	0	-0.025	-0.024	21.226	-0.451	-0.451	0.000	0.000	0.000	0.000
49	A	126	ILE	0	0.050	0.030	21.604	0.564	0.564	0.000	0.000	0.000	0.000
50	A	127	MET	0	-0.156	-0.037	19.018	-0.946	-0.946	0.000	0.000	0.000	0.000
51	A	128	ARG	1	0.935	0.955	16.396	17.053	17.053	0.000	0.000	0.000	0.000
52	A	129	ALA	0	0.068	0.043	17.786	-0.109	-0.109	0.000	0.000	0.000	0.000
53	A	130	GLY	0	-0.033	-0.024	13.950	-0.570	-0.570	0.000	0.000	0.000	0.000
54	A	131	GLU	-1	-0.853	-0.929	7.850	-34.256	-34.256	0.000	0.000	0.000	0.000
55	A	132	ASN	0	0.025	0.023	11.313	2.215	2.215	0.000	0.000	0.000	0.000
56	A	133	LEU	0	-0.016	-0.004	8.065	-0.538	-0.538	0.000	0.000	0.000	0.000
57	A	134	LEU	0	0.036	0.000	11.910	1.702	1.702	0.000	0.000	0.000	0.000
58	A	135	ARG	1	0.901	0.951	12.341	20.463	20.463	0.000	0.000	0.000	0.000
59	A	136	LEU	0	0.029	0.012	14.853	1.394	1.394	0.000	0.000	0.000	0.000
60	A	137	ALA	0	0.046	0.018	16.616	-0.554	-0.554	0.000	0.000	0.000	0.000
61	A	138	ARG	1	0.857	0.902	18.154	13.584	13.584	0.000	0.000	0.000	0.000
62	A	139	LYS	1	1.014	1.009	14.503	18.448	18.448	0.000	0.000	0.000	0.000
63	A	140	GLU	-1	-0.830	-0.903	16.619	-13.574	-13.574	0.000	0.000	0.000	0.000
64	A	141	GLN	0	0.040	0.018	18.908	-0.363	-0.363	0.000	0.000	0.000	0.000
65	A	142	CYS	0	-0.001	0.011	14.020	-0.510	-0.510	0.000	0.000	0.000	0.000
66	A	143	ILE	0	-0.016	-0.009	15.471	-0.420	-0.420	0.000	0.000	0.000	0.000
67	A	144	ALA	0	0.014	0.009	17.791	0.287	0.287	0.000	0.000	0.000	0.000
68	A	145	LEU	0	0.024	0.018	16.699	0.358	0.358	0.000	0.000	0.000	0.000
69	A	146	GLY	0	0.025	-0.003	17.171	0.145	0.145	0.000	0.000	0.000	0.000
70	A	147	ALA	0	-0.048	-0.028	17.791	0.345	0.345	0.000	0.000	0.000	0.000
71	A	148	GLN	0	-0.003	0.001	21.340	0.747	0.747	0.000	0.000	0.000	0.000
72	A	149	LEU	0	-0.015	-0.014	16.916	0.435	0.435	0.000	0.000	0.000	0.000
73	A	150	LYS	1	0.921	0.973	18.953	15.909	15.909	0.000	0.000	0.000	0.000
74	A	151	ASP	-1	-0.933	-0.967	20.986	-11.217	-11.217	0.000	0.000	0.000	0.000
75	A	152	LYS	1	0.940	0.974	24.505	11.556	11.556	0.000	0.000	0.000	0.000
76	A	153	PHE	0	0.030	0.005	21.751	0.279	0.279	0.000	0.000	0.000	0.000
77	A	154	LYS	1	0.872	0.947	22.738	11.870	11.870	0.000	0.000	0.000	0.000
78	A	155	ILE	0	-0.013	0.017	17.551	-0.341	-0.341	0.000	0.000	0.000	0.000
79	A	156	THR	0	-0.016	-0.031	16.958	0.115	0.115	0.000	0.000	0.000	0.000
80	A	157	ASP	-1	-0.788	-0.878	12.628	-21.478	-21.478	0.000	0.000	0.000	0.000
81	A	158	TYR	0	-0.026	0.007	11.414	-2.050	-2.050	0.000	0.000	0.000	0.000
83	A	160	ILE	0	-0.013	-0.011	8.992	-1.509	-1.509	0.000	0.000	0.000	0.000
85	A	162	ARG	1	0.771	0.882	8.228	23.271	23.271	0.000	0.000	0.000	0.000
86	A	163	VAL	0	0.026	0.026	8.639	-2.779	-2.779	0.000	0.000	0.000	0.000
87	A	164	TYR	0	0.045	0.030	7.537	0.310	0.310	0.000	0.000	0.000	0.000
88	A	165	PRO	0	0.009	0.013	9.530	0.882	0.882	0.000	0.000	0.000	0.000
89	A	166	SER	0	0.009	0.001	12.477	0.924	0.924	0.000	0.000	0.000	0.000
90	A	167	GLY	0	-0.025	-0.010	12.623	1.157	1.157	0.000	0.000	0.000	0.000
91	A	168	GLU	-1	-0.841	-0.904	12.656	-19.363	-19.363	0.000	0.000	0.000	0.000
92	A	169	VAL	0	-0.035	-0.025	9.198	-0.990	-0.990	0.000	0.000	0.000	0.000
95	A	172	LEU	0	0.009	-0.002	6.249	3.490	3.490	0.000	0.000	0.000	0.000
96	A	173	HIS	0	0.007	0.009	9.709	2.730	2.730	0.000	0.000	0.000	0.000
97	A	174	PRO	0	0.004	0.015	10.049	-2.267	-2.267	0.000	0.000	0.000	0.000
98	A	175	LYS	1	0.967	0.969	9.666	23.923	23.923	0.000	0.000	0.000	0.000
99	A	176	ASP	-1	-0.779	-0.861	11.115	-20.333	-20.333	0.000	0.000	0.000	0.000
100	A	177	GLY	0	-0.034	-0.007	10.560	0.159	0.159	0.000	0.000	0.000	0.000
101	A	178	VAL	0	-0.023	-0.018	11.458	0.489	0.489	0.000	0.000	0.000	0.000
102	A	179	PHE	0	0.009	-0.012	14.565	-0.441	-0.441	0.000	0.000	0.000	0.000
103	A	180	PRO	0	-0.008	-0.004	15.309	0.762	0.762	0.000	0.000	0.000	0.000
104	A	181	GLU	-1	-0.848	-0.933	18.044	-15.414	-15.414	0.000	0.000	0.000	0.000
105	A	182	LYS	1	0.916	0.974	20.360	13.849	13.849	0.000	0.000	0.000	0.000
106	A	183	VAL	0	0.003	-0.009	20.818	-0.585	-0.585	0.000	0.000	0.000	0.000
107	A	184	ASN	0	-0.004	-0.015	18.334	-0.104	-0.104	0.000	0.000	0.000	0.000
108	A	185	PRO	0	0.012	0.008	21.227	0.211	0.211	0.000	0.000	0.000	0.000
109	A	186	GLY	0	0.058	0.025	20.675	-0.579	-0.579	0.000	0.000	0.000	0.000
110	A	187	ARG	1	0.773	0.892	17.781	15.917	15.917	0.000	0.000	0.000	0.000
111	A	188	VAL	0	0.039	0.022	20.142	0.646	0.646	0.000	0.000	0.000	0.000
112	A	189	ALA	0	-0.011	-0.006	22.747	-0.215	-0.215	0.000	0.000	0.000	0.000
113	A	190	VAL	0	0.012	-0.010	22.003	0.508	0.508	0.000	0.000	0.000	0.000
114	A	191	GLY	0	0.042	0.024	24.911	-0.098	-0.098	0.000	0.000	0.000	0.000
115	A	192	SER	0	-0.077	-0.025	27.594	0.394	0.394	0.000	0.000	0.000	0.000
116	A	193	ASN	0	0.064	0.026	29.996	0.367	0.367	0.000	0.000	0.000	0.000
117	A	194	LYS	1	0.904	0.954	31.972	9.610	9.610	0.000	0.000	0.000	0.000
118	A	195	ARG	1	0.879	0.927	36.146	8.545	8.545	0.000	0.000	0.000	0.000
119	A	196	ARG	1	0.968	0.983	37.717	6.989	6.989	0.000	0.000	0.000	0.000
120	A	197	ILE	0	0.064	0.021	36.591	0.080	0.080	0.000	0.000	0.000	0.000
121	A	198	GLY	0	0.016	0.005	39.628	0.036	0.036	0.000	0.000	0.000	0.000
122	A	199	GLN	0	-0.035	-0.016	42.047	0.038	0.038	0.000	0.000	0.000	0.000
123	A	200	ASN	0	-0.015	0.006	37.753	-0.136	-0.136	0.000	0.000	0.000	0.000
124	A	201	PRO	0	-0.001	0.011	40.538	0.211	0.211	0.000	0.000	0.000	0.000
125	A	202	ASP	-1	-0.847	-0.928	43.002	-6.796	-6.796	0.000	0.000	0.000	0.000
126	A	203	PRO	0	0.026	-0.010	42.864	0.014	0.014	0.000	0.000	0.000	0.000
127	A	204	ALA	0	-0.028	-0.008	44.761	0.053	0.053	0.000	0.000	0.000	0.000
128	A	205	LYS	1	0.914	0.947	46.849	6.552	6.552	0.000	0.000	0.000	0.000
129	A	206	LEU	0	-0.013	0.003	40.851	0.054	0.054	0.000	0.000	0.000	0.000
130	A	207	LYS	1	0.973	0.999	44.295	6.111	6.111	0.000	0.000	0.000	0.000
131	A	208	PHE	0	-0.018	-0.018	45.402	0.100	0.100	0.000	0.000	0.000	0.000
132	A	209	LYS	1	0.949	0.985	41.875	7.180	7.180	0.000	0.000	0.000	0.000
133	A	210	GLY	0	0.025	0.013	39.260	-0.055	-0.055	0.000	0.000	0.000	0.000
134	A	211	GLN	0	-0.050	-0.015	37.505	0.030	0.030	0.000	0.000	0.000	0.000
135	A	212	GLU	-1	-0.857	-0.938	32.747	-9.276	-9.276	0.000	0.000	0.000	0.000
136	A	213	THR	0	-0.048	-0.036	36.998	-0.009	-0.009	0.000	0.000	0.000	0.000
137	A	214	PHE	0	-0.037	-0.015	32.821	0.210	0.210	0.000	0.000	0.000	0.000
138	A	215	ASP	-1	-0.904	-0.944	31.956	-9.977	-9.977	0.000	0.000	0.000	0.000
139	A	216	SER	-1	-0.937	-0.947	33.699	-8.331	-8.331	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:78:THR)