FMO DATABASE

FMODB ID: 7ML6K

Calculation Name: 2FDQ-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2FDQ

Chain ID: A

ChEMBL ID:

UniProt ID: P82934

Base Structure: X-ray

Registration Date: 2025-07-10

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	165
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-596359.444838
FMO2-HF: Nuclear repulsion	561578.828123
FMO2-HF: Total energy	-34780.616716
FMO2-MP2: Total energy	-34881.648765

3D Structure

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:SER)

Summations of interaction energy for fragment #1(A:1: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.
-12.442	-8.489	4.147	-4.27	-3.827	-0.029

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.096 / q_NPA : 0.047

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].
4	A	2	GLN	0	-0.112	0.082	4.195	-0.579	-0.307	0.001	-0.118	-0.155	0.000
5	A	3	ALA	0	0.149	-0.053	3.819	-3.082	-2.026	0.004	-0.490	-0.570	0.002
6	A	3	ALA	0	-0.089	0.088	5.076	0.173	0.173	0.000	0.000	0.000	0.000
7	A	4	GLU	0	0.070	-0.122	3.391	-0.883	-0.668	0.020	-0.020	-0.214	0.000
8	A	4	GLU	-1	-0.938	-0.836	2.336	-2.029	-0.404	4.102	-3.201	-2.526	-0.029
9	A	5	PHE	0	0.156	-0.040	4.423	-0.169	-0.055	-0.001	-0.077	-0.035	0.000
10	A	5	PHE	0	-0.111	0.076	5.190	-0.208	-0.188	-0.001	-0.006	-0.013	0.000
11	A	6	ASP	0	-0.003	-0.165	6.169	-0.044	-0.044	0.000	0.000	0.000	0.000
12	A	6	ASP	-1	-0.955	-0.848	7.988	1.098	1.098	0.000	0.000	0.000	0.000
13	A	7	LYS	0	0.040	-0.106	7.468	0.008	0.008	0.000	0.000	0.000	0.000
14	A	7	LYS	1	0.756	1.010	8.119	-0.240	-0.240	0.000	0.000	0.000	0.000
15	A	8	ALA	0	0.152	-0.051	8.176	0.144	0.144	0.000	0.000	0.000	0.000
16	A	8	ALA	0	-0.052	0.099	8.506	-0.086	-0.086	0.000	0.000	0.000	0.000
17	A	9	ALA	0	0.070	-0.061	9.983	0.017	0.017	0.000	0.000	0.000	0.000
18	A	9	ALA	0	-0.075	0.084	11.231	0.003	0.003	0.000	0.000	0.000	0.000
19	A	10	GLU	0	0.047	-0.136	12.130	-0.034	-0.034	0.000	0.000	0.000	0.000
20	A	10	GLU	-1	-0.881	-0.775	12.590	0.121	0.121	0.000	0.000	0.000	0.000
21	A	11	GLU	0	0.066	-0.117	12.539	0.041	0.041	0.000	0.000	0.000	0.000
22	A	11	GLU	-1	-0.900	-0.776	11.525	-0.085	-0.085	0.000	0.000	0.000	0.000
23	A	12	VAL	0	0.092	-0.070	13.756	0.051	0.051	0.000	0.000	0.000	0.000
24	A	12	VAL	0	-0.094	0.075	14.263	-0.011	-0.011	0.000	0.000	0.000	0.000
25	A	13	LYS	0	0.032	-0.138	15.727	-0.008	-0.008	0.000	0.000	0.000	0.000
26	A	13	LYS	1	0.735	0.982	16.583	-0.042	-0.042	0.000	0.000	0.000	0.000
27	A	14	ASN	0	0.001	-0.061	17.937	0.012	0.012	0.000	0.000	0.000	0.000
28	A	14	ASN	0	-0.174	0.030	17.261	0.023	0.023	0.000	0.000	0.000	0.000
29	A	15	LEU	0	0.087	-0.146	19.622	0.022	0.022	0.000	0.000	0.000	0.000
30	A	15	LEU	0	-0.110	0.108	17.992	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	16	LYS	0	0.098	-0.103	20.607	0.002	0.002	0.000	0.000	0.000	0.000
32	A	16	LYS	1	0.818	1.062	23.413	0.072	0.072	0.000	0.000	0.000	0.000
33	A	17	THR	0	-0.040	-0.086	23.895	0.017	0.017	0.000	0.000	0.000	0.000
34	A	17	THR	0	-0.001	0.084	25.303	0.003	0.003	0.000	0.000	0.000	0.000
35	A	18	LYS	0	0.154	-0.059	24.216	-0.022	-0.022	0.000	0.000	0.000	0.000
36	A	18	LYS	1	0.823	1.052	26.442	0.191	0.191	0.000	0.000	0.000	0.000
37	A	19	PRO	0	-0.034	-0.102	21.552	0.007	0.007	0.000	0.000	0.000	0.000
38	A	20	ALA	0	0.076	-0.020	24.095	0.027	0.027	0.000	0.000	0.000	0.000
39	A	20	ALA	0	-0.029	0.130	24.746	0.000	0.000	0.000	0.000	0.000	0.000
40	A	21	ASP	0	0.058	-0.087	23.910	-0.026	-0.026	0.000	0.000	0.000	0.000
41	A	21	ASP	-1	-0.978	-0.867	26.877	-0.246	-0.246	0.000	0.000	0.000	0.000
42	A	22	ASP	0	0.064	-0.119	23.436	-0.017	-0.017	0.000	0.000	0.000	0.000
43	A	22	ASP	-1	-0.898	-0.837	23.255	-0.327	-0.327	0.000	0.000	0.000	0.000
44	A	23	GLU	0	0.083	-0.110	20.237	-0.052	-0.052	0.000	0.000	0.000	0.000
45	A	23	GLU	-1	-0.794	-0.714	20.302	-0.323	-0.323	0.000	0.000	0.000	0.000
46	A	24	MET	0	0.211	-0.044	19.247	-0.064	-0.064	0.000	0.000	0.000	0.000
47	A	24	MET	0	-0.198	0.070	21.744	0.006	0.006	0.000	0.000	0.000	0.000
48	A	25	LEU	0	0.024	-0.149	19.465	-0.038	-0.038	0.000	0.000	0.000	0.000
49	A	25	LEU	0	-0.080	0.111	22.042	0.001	0.001	0.000	0.000	0.000	0.000
50	A	26	PHE	0	0.140	-0.057	17.995	-0.019	-0.019	0.000	0.000	0.000	0.000
51	A	26	PHE	0	-0.045	0.095	13.652	0.012	0.012	0.000	0.000	0.000	0.000
52	A	27	ILE	0	0.086	-0.063	15.015	-0.122	-0.122	0.000	0.000	0.000	0.000
53	A	27	ILE	0	-0.078	0.102	14.658	0.005	0.005	0.000	0.000	0.000	0.000
54	A	28	TYR	0	0.149	-0.057	14.979	-0.093	-0.093	0.000	0.000	0.000	0.000
55	A	28	TYR	0	-0.139	0.048	19.038	0.025	0.025	0.000	0.000	0.000	0.000
56	A	29	SER	0	0.025	-0.107	16.054	-0.042	-0.042	0.000	0.000	0.000	0.000
57	A	29	SER	0	-0.076	0.084	17.587	-0.018	-0.018	0.000	0.000	0.000	0.000
58	A	30	HIS	0	0.159	-0.076	12.897	0.034	0.034	0.000	0.000	0.000	0.000
59	A	30	HIS	1	0.739	1.005	11.844	0.963	0.963	0.000	0.000	0.000	0.000
60	A	31	TYR	0	0.220	-0.017	11.868	-0.205	-0.205	0.000	0.000	0.000	0.000
61	A	31	TYR	0	-0.112	0.057	12.308	0.035	0.035	0.000	0.000	0.000	0.000
62	A	32	LYS	0	0.000	-0.135	12.630	-0.066	-0.066	0.000	0.000	0.000	0.000
63	A	32	LYS	1	0.847	1.069	16.780	0.353	0.353	0.000	0.000	0.000	0.000
64	A	33	GLN	0	0.115	-0.062	13.766	0.098	0.098	0.000	0.000	0.000	0.000
65	A	33	GLN	0	-0.128	0.061	13.022	0.057	0.057	0.000	0.000	0.000	0.000
66	A	34	ALA	0	0.058	-0.141	9.534	0.002	0.002	0.000	0.000	0.000	0.000
67	A	34	ALA	0	-0.059	0.113	8.560	-0.054	-0.054	0.000	0.000	0.000	0.000
68	A	35	THR	0	-0.058	-0.121	9.678	-0.118	-0.118	0.000	0.000	0.000	0.000
69	A	35	THR	0	-0.027	0.076	10.731	0.032	0.032	0.000	0.000	0.000	0.000
70	A	36	VAL	0	0.011	-0.096	12.097	0.124	0.124	0.000	0.000	0.000	0.000
71	A	36	VAL	0	-0.101	0.090	16.050	0.014	0.014	0.000	0.000	0.000	0.000
72	A	37	GLY	0	0.001	-0.113	14.409	0.044	0.044	0.000	0.000	0.000	0.000
73	A	38	ASP	0	0.166	0.004	15.317	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	38	ASP	-1	-0.881	-0.777	17.422	-0.571	-0.571	0.000	0.000	0.000	0.000
75	A	39	ILE	0	0.004	-0.096	18.122	0.040	0.040	0.000	0.000	0.000	0.000
76	A	39	ILE	0	-0.105	0.087	20.747	0.002	0.002	0.000	0.000	0.000	0.000
77	A	40	ASN	0	0.045	-0.085	20.764	0.008	0.008	0.000	0.000	0.000	0.000
78	A	40	ASN	0	-0.054	0.068	20.540	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	41	THR	0	0.006	-0.076	23.286	0.026	0.026	0.000	0.000	0.000	0.000
80	A	41	THR	0	-0.029	0.050	23.188	0.000	0.000	0.000	0.000	0.000	0.000
81	A	42	GLU	0	0.120	-0.089	25.637	-0.020	-0.020	0.000	0.000	0.000	0.000
82	A	42	GLU	-1	-0.969	-0.830	29.912	-0.152	-0.152	0.000	0.000	0.000	0.000
83	A	43	ARG	0	0.053	-0.116	28.420	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	43	ARG	1	0.711	0.973	28.844	0.212	0.212	0.000	0.000	0.000	0.000
85	A	44	PRO	0	-0.044	-0.110	28.005	0.014	0.014	0.000	0.000	0.000	0.000
86	A	45	GLY	0	0.061	0.019	31.093	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	46	MET	0	0.057	0.023	34.784	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	46	MET	0	-0.086	0.078	35.834	0.003	0.003	0.000	0.000	0.000	0.000
89	A	47	LEU	0	0.063	-0.088	36.918	-0.009	-0.009	0.000	0.000	0.000	0.000
90	A	47	LEU	0	-0.034	0.112	38.092	0.000	0.000	0.000	0.000	0.000	0.000
91	A	48	ASP	0	0.093	-0.110	32.879	0.003	0.003	0.000	0.000	0.000	0.000
92	A	48	ASP	-1	-0.902	-0.808	30.757	-0.155	-0.155	0.000	0.000	0.000	0.000
93	A	49	PHE	0	0.087	-0.119	31.470	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	49	PHE	0	-0.014	0.124	32.663	0.001	0.001	0.000	0.000	0.000	0.000
95	A	50	LYS	0	0.154	-0.036	29.118	-0.017	-0.017	0.000	0.000	0.000	0.000
96	A	50	LYS	1	0.864	1.057	27.874	0.143	0.143	0.000	0.000	0.000	0.000
97	A	51	GLY	0	0.010	-0.098	27.294	-0.020	-0.020	0.000	0.000	0.000	0.000
98	A	52	LYS	0	0.092	-0.028	26.781	-0.025	-0.025	0.000	0.000	0.000	0.000
99	A	52	LYS	1	0.778	1.023	30.338	0.151	0.151	0.000	0.000	0.000	0.000
100	A	53	ALA	0	0.128	-0.045	27.207	-0.015	-0.015	0.000	0.000	0.000	0.000
101	A	53	ALA	0	-0.107	0.092	26.972	0.001	0.001	0.000	0.000	0.000	0.000
102	A	54	LYS	0	0.065	-0.110	23.158	-0.027	-0.027	0.000	0.000	0.000	0.000
103	A	54	LYS	1	0.805	1.023	22.739	0.259	0.259	0.000	0.000	0.000	0.000
104	A	55	TRP	0	0.078	-0.055	22.501	-0.044	-0.044	0.000	0.000	0.000	0.000
105	A	55	TRP	0	-0.065	0.081	25.545	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	56	ASP	0	0.097	-0.102	23.389	-0.031	-0.031	0.000	0.000	0.000	0.000
107	A	56	ASP	-1	-0.868	-0.759	26.211	-0.244	-0.244	0.000	0.000	0.000	0.000
108	A	57	ALA	0	0.170	-0.050	21.856	-0.018	-0.018	0.000	0.000	0.000	0.000
109	A	57	ALA	0	-0.087	0.095	21.051	0.000	0.000	0.000	0.000	0.000	0.000
110	A	58	TRP	0	0.146	-0.062	18.876	-0.058	-0.058	0.000	0.000	0.000	0.000
111	A	58	TRP	0	-0.133	0.075	17.126	0.062	0.062	0.000	0.000	0.000	0.000
112	A	59	ASN	0	0.103	-0.051	19.685	-0.047	-0.047	0.000	0.000	0.000	0.000
113	A	59	ASN	0	-0.104	0.048	23.931	0.010	0.010	0.000	0.000	0.000	0.000
114	A	60	GLN	0	-0.067	-0.138	21.751	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	60	GLN	0	-0.126	0.073	21.781	0.021	0.021	0.000	0.000	0.000	0.000
116	A	61	LEU	0	0.061	-0.104	17.171	0.001	0.001	0.000	0.000	0.000	0.000
117	A	61	LEU	0	-0.107	0.089	15.163	-0.025	-0.025	0.000	0.000	0.000	0.000
118	A	62	LYS	0	0.201	-0.034	17.126	-0.084	-0.084	0.000	0.000	0.000	0.000
119	A	62	LYS	1	0.786	1.018	20.900	0.377	0.377	0.000	0.000	0.000	0.000
120	A	63	GLY	0	-0.036	-0.129	17.986	0.004	0.004	0.000	0.000	0.000	0.000
121	A	64	THR	0	-0.001	0.007	14.308	-0.025	-0.025	0.000	0.000	0.000	0.000
122	A	64	THR	0	-0.083	0.021	12.179	-0.013	-0.013	0.000	0.000	0.000	0.000
123	A	65	SER	0	0.087	-0.030	11.252	0.125	0.125	0.000	0.000	0.000	0.000
124	A	65	SER	0	-0.056	0.068	10.258	-0.157	-0.157	0.000	0.000	0.000	0.000
125	A	66	LYS	0	0.186	-0.057	9.160	-0.165	-0.165	0.000	0.000	0.000	0.000
126	A	66	LYS	1	0.805	1.030	8.682	0.679	0.679	0.000	0.000	0.000	0.000
127	A	67	GLU	0	0.080	-0.091	5.661	-0.497	-0.497	0.000	0.000	0.000	0.000
128	A	67	GLU	-1	-0.942	-0.820	3.873	-8.865	-8.357	0.025	-0.344	-0.189	-0.002
129	A	68	ASP	0	0.122	-0.094	6.206	-0.941	-0.941	0.000	0.000	0.000	0.000
130	A	68	ASP	-1	-0.902	-0.807	10.400	-1.638	-1.638	0.000	0.000	0.000	0.000
131	A	69	ALA	0	0.144	-0.089	8.611	-0.124	-0.124	0.000	0.000	0.000	0.000
132	A	69	ALA	0	-0.141	0.108	9.547	0.074	0.074	0.000	0.000	0.000	0.000
133	A	70	MET	0	0.038	-0.167	5.427	0.938	0.953	-0.002	-0.002	-0.011	0.000
134	A	70	MET	0	-0.086	0.113	4.176	-0.124	-0.039	0.000	-0.005	-0.079	0.000
135	A	71	LYS	0	0.109	-0.039	5.637	0.104	0.104	0.000	0.000	0.000	0.000
136	A	71	LYS	1	0.765	1.027	5.627	2.189	2.189	0.000	0.000	0.000	0.000
137	A	72	SER	0	0.077	-0.045	6.333	0.415	0.415	0.000	0.000	0.000	0.000
138	A	72	SER	0	-0.128	0.015	10.061	0.196	0.196	0.000	0.000	0.000	0.000
139	A	73	TYR	0	0.069	-0.073	9.346	0.334	0.334	0.000	0.000	0.000	0.000
140	A	73	TYR	0	-0.115	0.051	8.818	0.106	0.106	0.000	0.000	0.000	0.000
141	A	74	ILE	0	0.101	-0.136	7.481	0.529	0.529	0.000	0.000	0.000	0.000
142	A	74	ILE	0	-0.048	0.119	4.571	-0.021	0.022	-0.001	-0.007	-0.035	0.000
143	A	75	ASP	0	0.036	-0.078	8.865	0.359	0.359	0.000	0.000	0.000	0.000
144	A	75	ASP	-1	-0.955	-0.858	9.348	-1.780	-1.780	0.000	0.000	0.000	0.000
145	A	76	LYS	0	0.141	-0.060	10.844	0.228	0.228	0.000	0.000	0.000	0.000
146	A	76	LYS	1	0.729	0.987	13.373	0.606	0.606	0.000	0.000	0.000	0.000
147	A	77	VAL	0	0.117	-0.087	12.314	0.157	0.157	0.000	0.000	0.000	0.000
148	A	77	VAL	0	-0.074	0.110	11.508	0.016	0.016	0.000	0.000	0.000	0.000
149	A	78	GLU	0	0.061	-0.122	12.295	0.152	0.152	0.000	0.000	0.000	0.000
150	A	78	GLU	-1	-0.931	-0.818	10.861	-0.341	-0.341	0.000	0.000	0.000	0.000
151	A	79	GLU	0	0.018	-0.144	13.611	0.119	0.119	0.000	0.000	0.000	0.000
152	A	79	GLU	-1	-0.935	-0.798	15.887	-0.560	-0.560	0.000	0.000	0.000	0.000
153	A	80	LEU	0	0.036	-0.122	16.459	0.071	0.071	0.000	0.000	0.000	0.000
154	A	80	LEU	0	-0.084	0.087	17.151	0.009	0.009	0.000	0.000	0.000	0.000
155	A	81	LYS	0	0.094	-0.091	16.233	0.056	0.056	0.000	0.000	0.000	0.000
156	A	81	LYS	1	0.697	0.953	12.218	0.239	0.239	0.000	0.000	0.000	0.000
157	A	82	LYS	0	-0.011	-0.110	17.504	0.058	0.058	0.000	0.000	0.000	0.000
158	A	82	LYS	1	0.837	1.036	14.886	0.449	0.449	0.000	0.000	0.000	0.000
159	A	83	LYS	0	0.046	-0.092	19.892	0.040	0.040	0.000	0.000	0.000	0.000
160	A	83	LYS	1	0.755	1.013	21.278	0.293	0.293	0.000	0.000	0.000	0.000
161	A	84	TYR	0	0.026	-0.114	21.316	0.017	0.017	0.000	0.000	0.000	0.000
162	A	84	TYR	0	-0.134	0.045	21.300	0.006	0.006	0.000	0.000	0.000	0.000
163	A	85	GLY	0	0.065	-0.078	21.204	0.028	0.028	0.000	0.000	0.000	0.000
164	A	86	ILE	0	-0.068	-0.041	19.282	0.002	0.002	0.000	0.000	0.000	0.000
165	A	86	ILE	0	0.055	0.039	17.261	0.005	0.005	0.000	0.000	0.000	0.000

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