FMO DATABASE

FMODB ID: 6G9YZ

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	OptH
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	-596022.006416
FMO2-HF: Nuclear repulsion	561243.955885
FMO2-HF: Total energy	-34778.050531
FMO2-MP2: Total energy	-34879.181555

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.
-12.222	-8.691	2.176	-2.828	-2.877	-0.017

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 : 0.107 / q_NPA : 0.035

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	-0.133	0.081	4.382	-0.517	-0.183	0.002	-0.152	-0.184	0.000
5	A	3	ALA	0	0.158	-0.045	3.819	-3.553	-2.465	0.008	-0.543	-0.553	0.002
6	A	3	ALA	0	-0.098	0.099	5.065	0.059	0.059	0.000	0.000	0.000	0.000
7	A	4	GLU	0	0.083	-0.131	3.398	-0.369	-0.167	0.022	-0.008	-0.216	0.000
8	A	4	GLU	-1	-0.960	-0.829	2.570	-4.862	-3.278	2.150	-1.984	-1.749	-0.019
9	A	5	PHE	0	0.119	-0.075	4.425	-0.453	-0.320	-0.001	-0.087	-0.045	0.000
10	A	5	PHE	0	-0.097	0.050	5.132	-0.190	-0.166	-0.001	-0.006	-0.017	0.000
11	A	6	ASP	0	0.078	-0.120	6.169	-0.105	-0.105	0.000	0.000	0.000	0.000
12	A	6	ASP	-1	-0.975	-0.851	8.006	1.521	1.521	0.000	0.000	0.000	0.000
13	A	7	LYS	0	0.043	-0.098	7.469	0.022	0.022	0.000	0.000	0.000	0.000
14	A	7	LYS	1	0.817	1.048	8.112	0.053	0.053	0.000	0.000	0.000	0.000
15	A	8	ALA	0	0.164	-0.065	8.166	0.140	0.140	0.000	0.000	0.000	0.000
16	A	8	ALA	0	-0.068	0.092	8.343	-0.069	-0.069	0.000	0.000	0.000	0.000
17	A	9	ALA	0	0.125	-0.082	9.972	0.002	0.002	0.000	0.000	0.000	0.000
18	A	9	ALA	0	-0.095	0.082	11.298	0.027	0.027	0.000	0.000	0.000	0.000
19	A	10	GLU	0	0.060	-0.150	12.120	-0.026	-0.026	0.000	0.000	0.000	0.000
20	A	10	GLU	-1	-0.971	-0.834	12.435	0.114	0.114	0.000	0.000	0.000	0.000
21	A	11	GLU	0	0.020	-0.106	12.537	0.050	0.050	0.000	0.000	0.000	0.000
22	A	11	GLU	-1	-0.980	-0.875	11.199	-0.433	-0.433	0.000	0.000	0.000	0.000
23	A	12	VAL	0	0.095	-0.078	13.758	0.040	0.040	0.000	0.000	0.000	0.000
24	A	12	VAL	0	-0.111	0.071	14.346	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	13	LYS	0	0.027	-0.144	15.714	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	13	LYS	1	0.818	1.058	16.437	-0.032	-0.032	0.000	0.000	0.000	0.000
27	A	14	ASN	0	0.002	-0.052	17.922	0.021	0.021	0.000	0.000	0.000	0.000
28	A	14	ASN	0	-0.141	0.049	17.997	0.014	0.014	0.000	0.000	0.000	0.000
29	A	15	LEU	0	0.096	-0.156	19.602	0.008	0.008	0.000	0.000	0.000	0.000
30	A	15	LEU	0	-0.117	0.114	17.908	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	16	LYS	0	0.088	-0.093	20.593	0.013	0.013	0.000	0.000	0.000	0.000
32	A	16	LYS	1	0.796	1.046	23.230	0.136	0.136	0.000	0.000	0.000	0.000
33	A	17	THR	0	0.013	-0.109	23.877	0.020	0.020	0.000	0.000	0.000	0.000
34	A	17	THR	0	-0.008	0.097	25.245	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	18	LYS	0	0.141	-0.070	24.199	-0.020	-0.020	0.000	0.000	0.000	0.000
36	A	18	LYS	1	0.812	1.053	26.706	0.138	0.138	0.000	0.000	0.000	0.000
37	A	19	PRO	0	-0.043	-0.097	21.610	0.006	0.006	0.000	0.000	0.000	0.000
38	A	20	ALA	0	0.087	-0.029	24.022	0.028	0.028	0.000	0.000	0.000	0.000
39	A	20	ALA	0	-0.053	0.129	24.721	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	21	ASP	0	0.085	-0.099	23.869	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	21	ASP	-1	-0.990	-0.873	26.869	-0.194	-0.194	0.000	0.000	0.000	0.000
42	A	22	ASP	0	0.092	-0.107	23.400	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	22	ASP	-1	-0.894	-0.817	23.061	-0.281	-0.281	0.000	0.000	0.000	0.000
44	A	23	GLU	0	0.061	-0.118	20.196	-0.040	-0.040	0.000	0.000	0.000	0.000
45	A	23	GLU	-1	-0.787	-0.697	20.422	-0.318	-0.318	0.000	0.000	0.000	0.000
46	A	24	MET	0	0.172	-0.056	19.209	-0.051	-0.051	0.000	0.000	0.000	0.000
47	A	24	MET	0	-0.182	0.066	21.580	0.012	0.012	0.000	0.000	0.000	0.000
48	A	25	LEU	0	0.078	-0.144	19.433	-0.022	-0.022	0.000	0.000	0.000	0.000
49	A	25	LEU	0	-0.116	0.135	21.952	0.001	0.001	0.000	0.000	0.000	0.000
50	A	26	PHE	0	0.228	-0.037	17.951	0.009	0.009	0.000	0.000	0.000	0.000
51	A	26	PHE	0	-0.084	0.092	13.624	0.010	0.010	0.000	0.000	0.000	0.000
52	A	27	ILE	0	0.135	-0.054	14.974	-0.087	-0.087	0.000	0.000	0.000	0.000
53	A	27	ILE	0	-0.045	0.113	14.462	0.006	0.006	0.000	0.000	0.000	0.000
54	A	28	TYR	0	0.096	-0.062	14.952	-0.050	-0.050	0.000	0.000	0.000	0.000
55	A	28	TYR	0	-0.135	0.048	19.009	0.023	0.023	0.000	0.000	0.000	0.000
56	A	29	SER	0	0.049	-0.087	16.037	0.002	0.002	0.000	0.000	0.000	0.000
57	A	29	SER	0	-0.104	0.045	16.870	-0.027	-0.027	0.000	0.000	0.000	0.000
58	A	30	HIS	0	0.139	-0.054	12.894	0.059	0.059	0.000	0.000	0.000	0.000
59	A	30	HIS	1	0.667	0.972	11.829	0.743	0.743	0.000	0.000	0.000	0.000
60	A	31	TYR	0	0.233	-0.018	11.869	-0.107	-0.107	0.000	0.000	0.000	0.000
61	A	31	TYR	0	-0.124	0.045	12.555	0.032	0.032	0.000	0.000	0.000	0.000
62	A	32	LYS	0	-0.021	-0.131	12.626	0.020	0.020	0.000	0.000	0.000	0.000
63	A	32	LYS	1	0.861	1.074	16.797	0.104	0.104	0.000	0.000	0.000	0.000
64	A	33	GLN	0	0.130	-0.071	13.773	0.117	0.117	0.000	0.000	0.000	0.000
65	A	33	GLN	0	-0.083	0.099	12.897	0.014	0.014	0.000	0.000	0.000	0.000
66	A	34	ALA	0	0.066	-0.162	9.478	0.050	0.050	0.000	0.000	0.000	0.000
67	A	34	ALA	0	-0.088	0.124	8.658	-0.064	-0.064	0.000	0.000	0.000	0.000
68	A	35	THR	0	-0.090	-0.119	9.693	0.104	0.104	0.000	0.000	0.000	0.000
69	A	35	THR	0	-0.053	0.070	10.729	0.025	0.025	0.000	0.000	0.000	0.000
70	A	36	VAL	0	-0.001	-0.096	12.108	0.133	0.133	0.000	0.000	0.000	0.000
71	A	36	VAL	0	-0.121	0.059	16.022	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	37	GLY	0	-0.011	-0.105	14.430	0.059	0.059	0.000	0.000	0.000	0.000
73	A	38	ASP	0	0.120	0.010	15.340	-0.033	-0.033	0.000	0.000	0.000	0.000
74	A	38	ASP	-1	-0.898	-0.797	17.691	-0.281	-0.281	0.000	0.000	0.000	0.000
75	A	39	ILE	0	0.050	-0.131	18.145	0.043	0.043	0.000	0.000	0.000	0.000
76	A	39	ILE	0	-0.110	0.097	20.960	0.001	0.001	0.000	0.000	0.000	0.000
77	A	40	ASN	0	0.040	-0.089	20.780	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	40	ASN	0	-0.039	0.087	21.008	-0.013	-0.013	0.000	0.000	0.000	0.000
79	A	41	THR	0	0.014	-0.083	23.306	0.024	0.024	0.000	0.000	0.000	0.000
80	A	41	THR	0	-0.020	0.060	22.989	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	42	GLU	0	0.105	-0.087	25.649	-0.016	-0.016	0.000	0.000	0.000	0.000
82	A	42	GLU	-1	-0.985	-0.836	29.861	-0.042	-0.042	0.000	0.000	0.000	0.000
83	A	43	ARG	0	0.076	-0.118	28.421	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	43	ARG	1	0.709	0.987	29.164	0.120	0.120	0.000	0.000	0.000	0.000
85	A	44	PRO	0	-0.048	-0.096	28.054	0.009	0.009	0.000	0.000	0.000	0.000
86	A	45	GLY	0	0.048	0.003	31.090	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	46	MET	0	0.032	0.002	34.779	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	46	MET	0	-0.089	0.056	35.799	0.000	0.000	0.000	0.000	0.000	0.000
89	A	47	LEU	0	0.057	-0.090	36.907	-0.006	-0.006	0.000	0.000	0.000	0.000
90	A	47	LEU	0	-0.035	0.120	38.017	0.000	0.000	0.000	0.000	0.000	0.000
91	A	48	ASP	0	0.088	-0.104	32.908	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	48	ASP	-1	-0.933	-0.825	30.814	-0.072	-0.072	0.000	0.000	0.000	0.000
93	A	49	PHE	0	0.086	-0.133	31.456	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	49	PHE	0	-0.014	0.132	32.628	0.000	0.000	0.000	0.000	0.000	0.000
95	A	50	LYS	0	0.128	-0.044	29.090	-0.013	-0.013	0.000	0.000	0.000	0.000
96	A	50	LYS	1	0.890	1.059	27.547	0.087	0.087	0.000	0.000	0.000	0.000
97	A	51	GLY	0	0.028	-0.070	27.277	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	52	LYS	0	0.120	-0.014	26.768	-0.014	-0.014	0.000	0.000	0.000	0.000
99	A	52	LYS	1	0.808	1.056	30.412	0.085	0.085	0.000	0.000	0.000	0.000
100	A	53	ALA	0	0.123	-0.061	27.190	-0.007	-0.007	0.000	0.000	0.000	0.000
101	A	53	ALA	0	-0.108	0.083	26.954	0.000	0.000	0.000	0.000	0.000	0.000
102	A	54	LYS	0	0.060	-0.117	23.136	-0.022	-0.022	0.000	0.000	0.000	0.000
103	A	54	LYS	1	0.824	1.030	22.697	0.159	0.159	0.000	0.000	0.000	0.000
104	A	55	TRP	0	0.088	-0.058	22.490	-0.027	-0.027	0.000	0.000	0.000	0.000
105	A	55	TRP	0	-0.070	0.083	25.634	-0.006	-0.006	0.000	0.000	0.000	0.000
106	A	56	ASP	0	0.082	-0.097	23.386	-0.013	-0.013	0.000	0.000	0.000	0.000
107	A	56	ASP	-1	-0.849	-0.766	26.126	-0.151	-0.151	0.000	0.000	0.000	0.000
108	A	57	ALA	0	0.161	-0.048	21.774	-0.011	-0.011	0.000	0.000	0.000	0.000
109	A	57	ALA	0	-0.080	0.094	20.935	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	58	TRP	0	0.121	-0.081	18.864	-0.050	-0.050	0.000	0.000	0.000	0.000
111	A	58	TRP	0	-0.144	0.082	16.985	0.037	0.037	0.000	0.000	0.000	0.000
112	A	59	ASN	0	0.110	-0.066	19.688	-0.024	-0.024	0.000	0.000	0.000	0.000
113	A	59	ASN	0	-0.116	0.043	23.916	0.015	0.015	0.000	0.000	0.000	0.000
114	A	60	GLN	0	-0.064	-0.155	21.751	0.006	0.006	0.000	0.000	0.000	0.000
115	A	60	GLN	0	-0.143	0.076	21.596	0.024	0.024	0.000	0.000	0.000	0.000
116	A	61	LEU	0	0.015	-0.124	17.186	-0.019	-0.019	0.000	0.000	0.000	0.000
117	A	61	LEU	0	-0.111	0.095	14.947	-0.018	-0.018	0.000	0.000	0.000	0.000
118	A	62	LYS	0	0.227	-0.039	17.138	-0.039	-0.039	0.000	0.000	0.000	0.000
119	A	62	LYS	1	0.828	1.036	21.011	0.178	0.178	0.000	0.000	0.000	0.000
120	A	63	GLY	0	-0.099	-0.137	18.012	-0.015	-0.015	0.000	0.000	0.000	0.000
121	A	64	THR	0	0.020	0.031	14.331	0.005	0.005	0.000	0.000	0.000	0.000
122	A	64	THR	0	-0.047	0.055	12.244	-0.032	-0.032	0.000	0.000	0.000	0.000
123	A	65	SER	0	0.065	-0.076	11.153	0.133	0.133	0.000	0.000	0.000	0.000
124	A	65	SER	0	-0.045	0.091	9.986	-0.105	-0.105	0.000	0.000	0.000	0.000
125	A	66	LYS	0	0.198	-0.046	9.188	-0.240	-0.240	0.000	0.000	0.000	0.000
126	A	66	LYS	1	0.918	1.071	8.736	-0.090	-0.090	0.000	0.000	0.000	0.000
127	A	67	GLU	0	0.117	-0.092	5.680	-0.303	-0.303	0.000	0.000	0.000	0.000
128	A	67	GLU	-1	-0.997	-0.845	4.441	-4.586	-4.517	0.000	-0.033	-0.036	0.000
129	A	68	ASP	0	0.088	-0.104	6.217	-1.013	-1.013	0.000	0.000	0.000	0.000
130	A	68	ASP	-1	-0.956	-0.848	10.420	-1.214	-1.214	0.000	0.000	0.000	0.000
131	A	69	ALA	0	0.091	-0.111	8.606	-0.222	-0.222	0.000	0.000	0.000	0.000
132	A	69	ALA	0	-0.122	0.093	9.248	0.062	0.062	0.000	0.000	0.000	0.000
133	A	70	MET	0	0.086	-0.137	5.495	0.547	0.563	-0.002	-0.001	-0.014	0.000
134	A	70	MET	0	-0.110	0.152	4.931	-0.166	-0.122	-0.001	-0.010	-0.032	0.000
135	A	71	LYS	0	0.129	-0.057	5.591	-0.152	-0.152	0.000	0.000	0.000	0.000
136	A	71	LYS	1	0.847	1.066	5.860	1.968	1.968	0.000	0.000	0.000	0.000
137	A	72	SER	0	0.037	-0.038	6.308	0.294	0.294	0.000	0.000	0.000	0.000
138	A	72	SER	0	-0.121	0.011	10.098	0.192	0.192	0.000	0.000	0.000	0.000
139	A	73	TYR	0	0.065	-0.088	9.298	0.268	0.268	0.000	0.000	0.000	0.000
140	A	73	TYR	0	-0.106	0.079	8.406	0.118	0.118	0.000	0.000	0.000	0.000
141	A	74	ILE	0	0.093	-0.128	7.462	0.509	0.509	0.000	0.000	0.000	0.000
142	A	74	ILE	0	-0.074	0.149	4.715	-0.001	0.036	-0.001	-0.004	-0.031	0.000
143	A	75	ASP	0	0.100	-0.064	8.812	0.299	0.299	0.000	0.000	0.000	0.000
144	A	75	ASP	-1	-0.965	-0.865	8.963	-1.959	-1.959	0.000	0.000	0.000	0.000
145	A	76	LYS	0	0.143	-0.067	10.793	0.195	0.195	0.000	0.000	0.000	0.000
146	A	76	LYS	1	0.781	1.040	13.246	0.620	0.620	0.000	0.000	0.000	0.000
147	A	77	VAL	0	0.065	-0.104	12.251	0.163	0.163	0.000	0.000	0.000	0.000
148	A	77	VAL	0	-0.041	0.121	10.855	0.014	0.014	0.000	0.000	0.000	0.000
149	A	78	GLU	0	0.040	-0.132	12.268	0.171	0.171	0.000	0.000	0.000	0.000
150	A	78	GLU	-1	-0.934	-0.822	10.191	-0.765	-0.765	0.000	0.000	0.000	0.000
151	A	79	GLU	0	0.039	-0.142	13.589	0.111	0.111	0.000	0.000	0.000	0.000
152	A	79	GLU	-1	-1.011	-0.855	15.879	-0.567	-0.567	0.000	0.000	0.000	0.000
153	A	80	LEU	0	0.026	-0.139	16.398	0.071	0.071	0.000	0.000	0.000	0.000
154	A	80	LEU	0	-0.074	0.101	17.096	0.012	0.012	0.000	0.000	0.000	0.000
155	A	81	LYS	0	0.046	-0.115	16.239	0.072	0.072	0.000	0.000	0.000	0.000
156	A	81	LYS	1	0.725	1.021	12.571	0.470	0.470	0.000	0.000	0.000	0.000
157	A	82	LYS	0	-0.017	-0.109	17.486	0.056	0.056	0.000	0.000	0.000	0.000
158	A	82	LYS	1	0.874	1.035	16.409	0.527	0.527	0.000	0.000	0.000	0.000
159	A	83	LYS	0	0.056	-0.088	19.871	0.041	0.041	0.000	0.000	0.000	0.000
160	A	83	LYS	1	0.747	1.024	21.219	0.307	0.307	0.000	0.000	0.000	0.000
161	A	84	TYR	0	0.024	-0.112	21.295	0.022	0.022	0.000	0.000	0.000	0.000
162	A	84	TYR	0	-0.123	0.031	21.437	0.005	0.005	0.000	0.000	0.000	0.000
163	A	85	GLY	0	0.066	-0.072	21.191	0.031	0.031	0.000	0.000	0.000	0.000
164	A	86	ILE	0	-0.080	-0.048	19.300	0.021	0.021	0.000	0.000	0.000	0.000
165	A	86	ILE	0	0.063	0.051	17.321	0.002	0.002	0.000	0.000	0.000	0.000

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