FMO DATABASE

FMODB ID: 7M7KK

Calculation Name: 1A32-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1A32

Chain ID: A

ChEMBL ID:

UniProt ID: P05766

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

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	-543710.522217
FMO2-HF: Nuclear repulsion	508712.619338
FMO2-HF: Total energy	-34997.902879
FMO2-MP2: Total energy	-35101.81489

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:2:LEU)

Summations of interaction energy for fragment #1(A:2: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.
2.81	4.315	-0.011	-0.796	-0.699	0.004

Interaction energy analysis for fragmet #1(A:2:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.180 / q_NPA : 0.019

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	3	THR	0	-0.020	0.074	4.094	-0.078	0.315	0.000	-0.164	-0.229	0.000
5	A	4	GLN	0	0.084	-0.111	3.885	-2.670	-1.746	-0.005	-0.602	-0.317	0.004
6	A	4	GLN	0	0.005	0.112	7.603	0.080	0.080	0.000	0.000	0.000	0.000
7	A	5	GLU	0	0.015	-0.070	6.671	-0.314	-0.314	0.000	0.000	0.000	0.000
8	A	5	GLU	-1	-0.846	-0.782	7.035	0.018	0.018	0.000	0.000	0.000	0.000
9	A	6	ARG	0	0.189	-0.079	5.743	-0.111	-0.111	0.000	0.000	0.000	0.000
10	A	6	ARG	1	0.738	1.016	4.743	0.748	0.788	-0.001	-0.005	-0.034	0.000
11	A	7	LYS	0	0.125	-0.081	5.143	-0.051	-0.025	-0.002	-0.007	-0.017	0.000
12	A	7	LYS	1	0.833	1.049	4.164	3.606	3.679	-0.001	-0.018	-0.054	0.000
13	A	8	ARG	0	0.050	-0.095	5.681	0.181	0.230	-0.002	0.000	-0.048	0.000
14	A	8	ARG	1	0.820	1.020	9.545	0.974	0.974	0.000	0.000	0.000	0.000
15	A	9	GLU	0	0.135	-0.092	9.342	0.102	0.102	0.000	0.000	0.000	0.000
16	A	9	GLU	-1	-0.907	-0.778	9.476	-0.497	-0.497	0.000	0.000	0.000	0.000
17	A	10	ILE	0	0.044	-0.078	8.005	0.323	0.323	0.000	0.000	0.000	0.000
18	A	10	ILE	0	-0.094	0.072	5.549	-0.057	-0.057	0.000	0.000	0.000	0.000
19	A	11	ILE	0	0.106	-0.063	9.238	0.174	0.174	0.000	0.000	0.000	0.000
20	A	11	ILE	0	-0.125	0.053	8.867	-0.064	-0.064	0.000	0.000	0.000	0.000
21	A	12	GLU	0	0.070	-0.116	10.978	0.104	0.104	0.000	0.000	0.000	0.000
22	A	12	GLU	-1	-0.965	-0.821	13.599	-0.541	-0.541	0.000	0.000	0.000	0.000
23	A	13	GLN	0	0.127	-0.089	12.784	0.135	0.135	0.000	0.000	0.000	0.000
24	A	13	GLN	0	-0.133	0.073	12.153	-0.050	-0.050	0.000	0.000	0.000	0.000
25	A	14	PHE	0	0.034	-0.064	13.368	0.115	0.115	0.000	0.000	0.000	0.000
26	A	14	PHE	0	-0.118	0.056	11.301	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	15	LYS	0	0.094	-0.072	14.620	0.003	0.003	0.000	0.000	0.000	0.000
28	A	15	LYS	1	0.729	0.966	15.816	0.550	0.550	0.000	0.000	0.000	0.000
29	A	16	VAL	0	0.096	-0.096	16.726	0.040	0.040	0.000	0.000	0.000	0.000
30	A	16	VAL	0	-0.106	0.096	19.413	0.002	0.002	0.000	0.000	0.000	0.000
31	A	17	HIS	0	0.052	-0.081	20.063	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	17	HIS	0	-0.104	0.061	21.919	-0.007	-0.007	0.000	0.000	0.000	0.000
33	A	18	GLU	0	0.138	-0.045	22.814	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	18	GLU	-1	-0.995	-0.871	24.880	-0.311	-0.311	0.000	0.000	0.000	0.000
35	A	19	ASN	0	0.046	-0.099	22.991	0.005	0.005	0.000	0.000	0.000	0.000
36	A	19	ASN	0	-0.136	0.041	22.157	-0.016	-0.016	0.000	0.000	0.000	0.000
37	A	20	ASP	0	0.203	-0.035	24.128	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	20	ASP	-1	-0.964	-0.869	25.191	-0.194	-0.194	0.000	0.000	0.000	0.000
39	A	21	THR	0	-0.114	-0.086	25.560	0.007	0.007	0.000	0.000	0.000	0.000
40	A	21	THR	0	-0.071	0.037	27.827	0.004	0.004	0.000	0.000	0.000	0.000
41	A	22	GLY	0	0.107	-0.079	27.925	0.012	0.012	0.000	0.000	0.000	0.000
42	A	23	SER	0	0.008	-0.020	28.759	0.015	0.015	0.000	0.000	0.000	0.000
43	A	23	SER	0	-0.040	0.095	31.848	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	24	PRO	0	-0.001	-0.124	32.019	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	25	GLU	0	0.043	-0.040	35.141	0.001	0.001	0.000	0.000	0.000	0.000
46	A	25	GLU	-1	-0.745	-0.713	35.681	-0.097	-0.097	0.000	0.000	0.000	0.000
47	A	26	VAL	0	0.114	-0.072	32.907	0.006	0.006	0.000	0.000	0.000	0.000
48	A	26	VAL	0	-0.046	0.137	31.208	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	27	GLN	0	0.104	-0.089	34.197	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	27	GLN	0	-0.065	0.087	31.076	0.008	0.008	0.000	0.000	0.000	0.000
51	A	28	ILE	0	0.053	-0.113	34.909	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	28	ILE	0	-0.089	0.109	38.407	0.001	0.001	0.000	0.000	0.000	0.000
53	A	29	ALA	0	0.133	-0.086	37.714	0.007	0.007	0.000	0.000	0.000	0.000
54	A	29	ALA	0	-0.053	0.131	36.881	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	30	ILE	0	0.082	-0.085	35.184	0.005	0.005	0.000	0.000	0.000	0.000
56	A	30	ILE	0	-0.079	0.104	32.308	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	31	LEU	0	0.096	-0.099	36.666	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	31	LEU	0	-0.130	0.066	37.078	0.001	0.001	0.000	0.000	0.000	0.000
59	A	32	THR	0	0.016	-0.103	39.020	0.004	0.004	0.000	0.000	0.000	0.000
60	A	32	THR	0	-0.049	0.064	41.342	0.003	0.003	0.000	0.000	0.000	0.000
61	A	33	GLU	0	0.112	-0.089	39.932	0.007	0.007	0.000	0.000	0.000	0.000
62	A	33	GLU	-1	-0.940	-0.795	39.008	-0.113	-0.113	0.000	0.000	0.000	0.000
63	A	34	GLN	0	0.057	-0.093	39.517	0.002	0.002	0.000	0.000	0.000	0.000
64	A	34	GLN	0	-0.056	0.069	35.592	0.003	0.003	0.000	0.000	0.000	0.000
65	A	35	ILE	0	0.069	-0.096	40.554	0.001	0.001	0.000	0.000	0.000	0.000
66	A	35	ILE	0	-0.141	0.059	42.590	0.002	0.002	0.000	0.000	0.000	0.000
67	A	36	ASN	0	0.045	-0.106	43.816	0.005	0.005	0.000	0.000	0.000	0.000
68	A	36	ASN	0	-0.095	0.087	43.843	0.004	0.004	0.000	0.000	0.000	0.000
69	A	37	ASN	0	0.131	-0.083	43.200	0.006	0.006	0.000	0.000	0.000	0.000
70	A	37	ASN	0	-0.082	0.097	41.377	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	38	LEU	0	0.110	-0.086	44.158	0.002	0.002	0.000	0.000	0.000	0.000
72	A	38	LEU	0	-0.105	0.103	43.099	0.000	0.000	0.000	0.000	0.000	0.000
73	A	39	ASN	0	0.053	-0.107	45.515	0.003	0.003	0.000	0.000	0.000	0.000
74	A	39	ASN	0	-0.152	0.037	47.400	0.004	0.004	0.000	0.000	0.000	0.000
75	A	40	GLU	0	0.077	-0.117	47.828	0.006	0.006	0.000	0.000	0.000	0.000
76	A	40	GLU	-1	-0.911	-0.783	45.960	-0.097	-0.097	0.000	0.000	0.000	0.000
77	A	41	HIS	0	0.096	-0.080	47.385	0.003	0.003	0.000	0.000	0.000	0.000
78	A	41	HIS	0	-0.123	0.058	46.617	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	42	LEU	0	0.046	-0.117	48.696	0.002	0.002	0.000	0.000	0.000	0.000
80	A	42	LEU	0	-0.099	0.082	48.645	0.000	0.000	0.000	0.000	0.000	0.000
81	A	43	ARG	0	0.031	-0.119	51.218	0.004	0.004	0.000	0.000	0.000	0.000
82	A	43	ARG	1	0.863	1.080	50.965	0.073	0.073	0.000	0.000	0.000	0.000
83	A	44	VAL	0	0.055	-0.111	52.625	0.005	0.005	0.000	0.000	0.000	0.000
84	A	44	VAL	0	-0.055	0.136	51.522	0.000	0.000	0.000	0.000	0.000	0.000
85	A	45	HIS	0	0.032	-0.100	51.689	0.003	0.003	0.000	0.000	0.000	0.000
86	A	45	HIS	0	-0.023	0.133	49.833	0.003	0.003	0.000	0.000	0.000	0.000
87	A	46	LYS	0	0.131	-0.114	53.097	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	46	LYS	1	0.848	1.057	56.676	0.062	0.062	0.000	0.000	0.000	0.000
89	A	47	LYS	0	0.076	-0.079	55.595	0.002	0.002	0.000	0.000	0.000	0.000
90	A	47	LYS	1	0.841	1.046	52.970	0.073	0.073	0.000	0.000	0.000	0.000
91	A	48	ASP	0	0.070	-0.105	51.140	0.001	0.001	0.000	0.000	0.000	0.000
92	A	48	ASP	-1	-0.804	-0.746	48.816	-0.083	-0.083	0.000	0.000	0.000	0.000
93	A	49	HIS	0	0.066	-0.093	50.762	0.003	0.003	0.000	0.000	0.000	0.000
94	A	49	HIS	0	-0.030	0.132	51.874	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	50	HIS	0	0.058	-0.110	47.206	0.003	0.003	0.000	0.000	0.000	0.000
96	A	50	HIS	0	0.026	0.140	45.421	0.003	0.003	0.000	0.000	0.000	0.000
97	A	51	SER	0	0.051	-0.113	45.344	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	51	SER	0	-0.019	0.061	45.947	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	52	ARG	0	0.055	-0.088	46.094	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	52	ARG	1	0.781	1.008	50.098	0.068	0.068	0.000	0.000	0.000	0.000
101	A	53	ARG	0	0.032	-0.115	46.822	0.001	0.001	0.000	0.000	0.000	0.000
102	A	53	ARG	1	0.824	1.057	46.134	0.069	0.069	0.000	0.000	0.000	0.000
103	A	54	GLY	0	0.004	-0.093	42.845	0.000	0.000	0.000	0.000	0.000	0.000
104	A	55	LEU	0	0.190	0.013	43.107	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	55	LEU	0	-0.091	0.130	45.179	0.000	0.000	0.000	0.000	0.000	0.000
106	A	56	LEU	0	0.055	-0.111	45.054	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	56	LEU	0	-0.058	0.108	47.091	0.000	0.000	0.000	0.000	0.000	0.000
108	A	57	LYS	0	0.063	-0.094	42.350	0.004	0.004	0.000	0.000	0.000	0.000
109	A	57	LYS	1	0.876	1.065	41.384	0.079	0.079	0.000	0.000	0.000	0.000
110	A	58	MET	0	0.078	-0.099	40.628	0.001	0.001	0.000	0.000	0.000	0.000
111	A	58	MET	0	-0.072	0.129	39.720	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	59	VAL	0	0.105	-0.092	41.636	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	59	VAL	0	-0.090	0.111	45.773	0.001	0.001	0.000	0.000	0.000	0.000
114	A	60	GLY	0	-0.005	-0.119	44.280	0.003	0.003	0.000	0.000	0.000	0.000
115	A	61	LYS	0	0.055	0.000	39.426	0.006	0.006	0.000	0.000	0.000	0.000
116	A	61	LYS	1	0.843	1.048	33.832	0.124	0.124	0.000	0.000	0.000	0.000
117	A	62	ARG	0	0.102	-0.096	40.458	0.000	0.000	0.000	0.000	0.000	0.000
118	A	62	ARG	1	0.847	1.066	41.433	0.084	0.084	0.000	0.000	0.000	0.000
119	A	63	ARG	0	0.060	-0.098	41.669	0.001	0.001	0.000	0.000	0.000	0.000
120	A	63	ARG	1	0.888	1.058	45.194	0.061	0.061	0.000	0.000	0.000	0.000
121	A	64	ARG	0	0.128	-0.046	41.740	0.004	0.004	0.000	0.000	0.000	0.000
122	A	64	ARG	1	0.836	1.056	38.755	0.075	0.075	0.000	0.000	0.000	0.000
123	A	65	LEU	0	0.055	-0.117	38.917	0.005	0.005	0.000	0.000	0.000	0.000
124	A	65	LEU	0	-0.053	0.110	35.841	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	66	LEU	0	0.103	-0.099	39.821	0.000	0.000	0.000	0.000	0.000	0.000
126	A	66	LEU	0	-0.085	0.110	42.590	0.001	0.001	0.000	0.000	0.000	0.000
127	A	67	ALA	0	0.112	-0.082	42.861	0.002	0.002	0.000	0.000	0.000	0.000
128	A	67	ALA	0	-0.095	0.091	44.114	0.000	0.000	0.000	0.000	0.000	0.000
129	A	68	TYR	0	0.103	-0.074	39.955	0.006	0.006	0.000	0.000	0.000	0.000
130	A	68	TYR	0	-0.121	0.065	34.965	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	69	LEU	0	0.099	-0.100	40.317	0.004	0.004	0.000	0.000	0.000	0.000
132	A	69	LEU	0	-0.122	0.100	38.780	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	70	ARG	0	0.147	-0.079	41.112	0.002	0.002	0.000	0.000	0.000	0.000
134	A	70	ARG	1	0.783	1.011	45.681	0.043	0.043	0.000	0.000	0.000	0.000
135	A	71	ASN	0	0.007	-0.081	43.757	0.003	0.003	0.000	0.000	0.000	0.000
136	A	71	ASN	0	-0.116	0.070	43.696	0.000	0.000	0.000	0.000	0.000	0.000
137	A	72	LYS	0	0.112	-0.058	39.989	0.005	0.005	0.000	0.000	0.000	0.000
138	A	72	LYS	1	0.848	1.044	35.368	0.056	0.056	0.000	0.000	0.000	0.000
139	A	73	ASP	0	0.104	-0.119	41.119	0.003	0.003	0.000	0.000	0.000	0.000
140	A	73	ASP	-1	-0.903	-0.806	40.374	-0.058	-0.058	0.000	0.000	0.000	0.000
141	A	74	VAL	0	0.122	-0.082	42.334	-0.005	-0.005	0.000	0.000	0.000	0.000
142	A	74	VAL	0	-0.063	0.110	46.694	0.000	0.000	0.000	0.000	0.000	0.000
143	A	75	ALA	0	0.066	-0.109	44.674	0.000	0.000	0.000	0.000	0.000	0.000
144	A	75	ALA	0	-0.042	0.120	44.196	0.000	0.000	0.000	0.000	0.000	0.000
145	A	76	ARG	0	0.114	-0.092	40.665	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	76	ARG	1	0.787	0.993	34.782	0.082	0.082	0.000	0.000	0.000	0.000
147	A	77	TYR	0	0.071	-0.091	42.015	-0.006	-0.006	0.000	0.000	0.000	0.000
148	A	77	TYR	0	-0.133	0.086	43.645	0.002	0.002	0.000	0.000	0.000	0.000
149	A	78	ARG	0	0.108	-0.078	43.736	-0.003	-0.003	0.000	0.000	0.000	0.000
150	A	78	ARG	1	0.873	1.065	47.333	0.046	0.046	0.000	0.000	0.000	0.000
151	A	79	GLU	0	0.115	-0.085	43.499	0.001	0.001	0.000	0.000	0.000	0.000
152	A	79	GLU	-1	-0.924	-0.804	42.759	-0.073	-0.073	0.000	0.000	0.000	0.000
153	A	80	ILE	0	0.086	-0.072	41.420	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	80	ILE	0	-0.116	0.076	39.478	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	81	VAL	0	0.065	-0.111	42.688	-0.004	-0.004	0.000	0.000	0.000	0.000
156	A	81	VAL	0	-0.131	0.071	45.376	0.000	0.000	0.000	0.000	0.000	0.000
157	A	82	GLU	0	0.108	-0.109	45.989	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	82	GLU	-1	-1.010	-0.845	47.205	-0.061	-0.061	0.000	0.000	0.000	0.000
159	A	83	LYS	0	0.061	-0.082	43.850	0.001	0.001	0.000	0.000	0.000	0.000
160	A	83	LYS	1	0.747	0.990	42.826	0.076	0.076	0.000	0.000	0.000	0.000
161	A	84	LEU	0	-0.026	-0.126	43.877	-0.004	-0.004	0.000	0.000	0.000	0.000
162	A	84	LEU	0	-0.088	0.084	40.625	-0.001	-0.001	0.000	0.000	0.000	0.000
163	A	85	GLY	0	0.032	-0.095	44.830	0.000	0.000	0.000	0.000	0.000	0.000
164	A	86	LEU	0	-0.108	-0.052	47.549	0.004	0.004	0.000	0.000	0.000	0.000
165	A	86	LEU	0	-0.020	0.007	44.116	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LEU)