FMO DATABASE

FMODB ID: QNQYY

Calculation Name: 2CUW-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CUW

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SI58

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	154
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-475944.925734
FMO2-HF: Nuclear repulsion	444541.907216
FMO2-HF: Total energy	-31403.018518
FMO2-MP2: Total energy	-31495.18503

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:2:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-19.094	-9.888	11.3	-8.507	-11.995	-0.067

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / q_NPA : 0.001

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	3	ARG	1	0.826	1.015	4.144	-0.594	-0.237	0.000	-0.123	-0.234	0.000
4	A	4	TYR	0	0.039	-0.093	3.781	-1.202	0.756	0.005	-0.936	-1.027	0.002
5	A	4	TYR	0	-0.062	0.082	2.510	-2.529	-0.094	2.559	-1.479	-3.516	-0.010
6	A	5	GLN	0	0.153	-0.086	5.605	0.286	0.286	0.000	0.000	0.000	0.000
7	A	5	GLN	0	-0.134	0.040	9.601	0.059	0.059	0.000	0.000	0.000	0.000
8	A	6	ALA	0	0.071	-0.085	9.361	-0.067	-0.067	0.000	0.000	0.000	0.000
9	A	6	ALA	0	-0.084	0.087	11.253	-0.008	-0.008	0.000	0.000	0.000	0.000
10	A	7	THR	0	0.018	-0.080	11.978	0.062	0.062	0.000	0.000	0.000	0.000
11	A	7	THR	0	-0.116	0.015	14.716	-0.010	-0.010	0.000	0.000	0.000	0.000
12	A	8	LEU	0	0.082	-0.098	15.306	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	8	LEU	0	-0.101	0.088	15.688	0.005	0.005	0.000	0.000	0.000	0.000
14	A	9	LEU	0	0.090	-0.102	17.740	0.032	0.032	0.000	0.000	0.000	0.000
15	A	9	LEU	0	-0.047	0.132	20.686	0.004	0.004	0.000	0.000	0.000	0.000
16	A	10	ILE	0	0.067	-0.103	21.380	-0.026	-0.026	0.000	0.000	0.000	0.000
17	A	10	ILE	0	-0.119	0.099	21.402	0.002	0.002	0.000	0.000	0.000	0.000
18	A	11	GLU	0	0.091	-0.088	24.058	0.018	0.018	0.000	0.000	0.000	0.000
19	A	11	GLU	-1	-0.847	-0.755	26.339	-0.181	-0.181	0.000	0.000	0.000	0.000
20	A	12	LEU	0	0.076	-0.116	27.467	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	12	LEU	0	-0.032	0.140	31.228	0.001	0.001	0.000	0.000	0.000	0.000
22	A	13	LYS	0	0.095	-0.102	31.013	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	13	LYS	1	0.760	1.020	30.511	0.170	0.170	0.000	0.000	0.000	0.000
24	A	14	LYS	0	0.057	-0.119	32.479	0.007	0.007	0.000	0.000	0.000	0.000
25	A	14	LYS	1	0.758	1.033	29.891	0.176	0.176	0.000	0.000	0.000	0.000
26	A	15	GLY	0	0.025	-0.107	35.229	0.001	0.001	0.000	0.000	0.000	0.000
27	A	16	ILE	0	0.015	-0.017	35.958	0.009	0.009	0.000	0.000	0.000	0.000
28	A	16	ILE	0	-0.091	0.110	34.748	0.000	0.000	0.000	0.000	0.000	0.000
29	A	17	LEU	0	0.077	-0.122	37.338	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	17	LEU	0	-0.073	0.109	39.939	0.001	0.001	0.000	0.000	0.000	0.000
31	A	18	ASP	0	0.118	-0.111	35.899	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	18	ASP	-1	-0.860	-0.763	33.940	-0.120	-0.120	0.000	0.000	0.000	0.000
33	A	19	PRO	0	-0.042	-0.126	36.950	0.003	0.003	0.000	0.000	0.000	0.000
34	A	20	GLN	0	0.045	0.009	35.416	0.007	0.007	0.000	0.000	0.000	0.000
35	A	20	GLN	0	-0.055	0.086	32.328	0.003	0.003	0.000	0.000	0.000	0.000
36	A	21	GLY	0	0.056	-0.081	35.599	0.002	0.002	0.000	0.000	0.000	0.000
37	A	22	ARG	0	0.077	0.014	36.285	0.002	0.002	0.000	0.000	0.000	0.000
38	A	22	ARG	1	0.689	0.966	36.628	0.104	0.104	0.000	0.000	0.000	0.000
39	A	23	ALA	0	0.151	-0.073	39.602	0.004	0.004	0.000	0.000	0.000	0.000
40	A	23	ALA	0	-0.089	0.092	39.232	0.000	0.000	0.000	0.000	0.000	0.000
41	A	24	VAL	0	0.058	-0.101	36.712	0.006	0.006	0.000	0.000	0.000	0.000
42	A	24	VAL	0	-0.079	0.092	35.067	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	25	GLU	0	0.078	-0.142	38.256	0.002	0.002	0.000	0.000	0.000	0.000
44	A	25	GLU	-1	-0.861	-0.778	38.129	-0.096	-0.096	0.000	0.000	0.000	0.000
45	A	26	GLY	0	-0.035	-0.094	39.951	0.003	0.003	0.000	0.000	0.000	0.000
46	A	27	VAL	0	0.159	0.056	41.507	0.003	0.003	0.000	0.000	0.000	0.000
47	A	27	VAL	0	-0.103	0.079	40.532	0.000	0.000	0.000	0.000	0.000	0.000
48	A	28	LEU	0	0.047	-0.103	39.713	0.005	0.005	0.000	0.000	0.000	0.000
49	A	28	LEU	0	-0.063	0.091	36.271	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	29	LYS	0	0.052	-0.104	40.931	0.001	0.001	0.000	0.000	0.000	0.000
51	A	29	LYS	1	0.751	1.022	41.649	0.077	0.077	0.000	0.000	0.000	0.000
52	A	30	ASP	0	0.107	-0.092	44.283	0.002	0.002	0.000	0.000	0.000	0.000
53	A	30	ASP	-1	-1.020	-0.863	45.257	-0.055	-0.055	0.000	0.000	0.000	0.000
54	A	31	LEU	0	-0.016	-0.119	43.005	0.004	0.004	0.000	0.000	0.000	0.000
55	A	31	LEU	0	-0.104	0.084	40.875	0.000	0.000	0.000	0.000	0.000	0.000
56	A	32	GLY	0	-0.007	-0.116	44.252	0.001	0.001	0.000	0.000	0.000	0.000
57	A	33	HIS	0	0.013	-0.011	40.742	0.001	0.001	0.000	0.000	0.000	0.000
58	A	33	HIS	0	-0.113	0.085	39.901	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	34	PRO	0	0.036	-0.128	40.956	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	35	VAL	0	0.034	-0.003	38.634	0.000	0.000	0.000	0.000	0.000	0.000
61	A	35	VAL	0	-0.023	0.124	37.159	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	36	GLU	0	0.072	-0.103	39.402	0.004	0.004	0.000	0.000	0.000	0.000
63	A	36	GLU	-1	-1.025	-0.868	38.967	-0.096	-0.096	0.000	0.000	0.000	0.000
64	A	37	GLU	0	0.053	-0.114	37.187	0.005	0.005	0.000	0.000	0.000	0.000
65	A	37	GLU	-1	-0.878	-0.791	35.158	-0.127	-0.127	0.000	0.000	0.000	0.000
66	A	38	VAL	0	-0.015	-0.140	34.194	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	38	VAL	0	-0.058	0.112	33.214	0.000	0.000	0.000	0.000	0.000	0.000
68	A	39	ARG	0	0.095	-0.086	32.153	0.007	0.007	0.000	0.000	0.000	0.000
69	A	39	ARG	1	0.704	0.946	29.497	0.154	0.154	0.000	0.000	0.000	0.000
70	A	40	VAL	0	0.027	-0.129	30.367	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	40	VAL	0	-0.099	0.110	30.792	0.002	0.002	0.000	0.000	0.000	0.000
72	A	41	GLY	0	0.001	-0.108	27.249	0.003	0.003	0.000	0.000	0.000	0.000
73	A	42	LYS	0	0.069	0.005	25.078	0.013	0.013	0.000	0.000	0.000	0.000
74	A	42	LYS	1	0.754	0.980	24.341	0.189	0.189	0.000	0.000	0.000	0.000
75	A	43	VAL	0	0.060	-0.099	21.474	-0.014	-0.014	0.000	0.000	0.000	0.000
76	A	43	VAL	0	-0.051	0.118	19.946	0.001	0.001	0.000	0.000	0.000	0.000
77	A	44	LEU	0	0.024	-0.138	18.899	0.038	0.038	0.000	0.000	0.000	0.000
78	A	44	LEU	0	-0.066	0.095	18.240	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	45	GLU	0	0.107	-0.072	15.225	-0.048	-0.048	0.000	0.000	0.000	0.000
80	A	45	GLU	-1	-0.905	-0.773	15.017	-0.395	-0.395	0.000	0.000	0.000	0.000
81	A	46	ILE	0	0.041	-0.132	13.629	0.071	0.071	0.000	0.000	0.000	0.000
82	A	46	ILE	0	-0.053	0.127	12.353	0.000	0.000	0.000	0.000	0.000	0.000
83	A	47	VAL	0	0.139	-0.084	9.957	-0.183	-0.183	0.000	0.000	0.000	0.000
84	A	47	VAL	0	-0.106	0.092	8.913	0.032	0.032	0.000	0.000	0.000	0.000
85	A	48	PHE	0	-0.016	-0.118	8.450	0.304	0.304	0.000	0.000	0.000	0.000
86	A	48	PHE	0	-0.093	0.088	8.115	-0.071	-0.071	0.000	0.000	0.000	0.000
87	A	49	PRO	0	-0.002	-0.102	4.486	-0.494	-0.436	-0.001	-0.039	-0.017	0.000
88	A	50	ALA	0	0.034	-0.027	2.945	1.309	1.924	0.013	-0.225	-0.403	0.000
89	A	50	ALA	0	-0.055	0.099	4.531	0.140	0.198	-0.001	-0.020	-0.037	0.000
90	A	51	GLU	0	0.146	-0.081	1.965	-9.924	-10.273	6.536	-3.350	-2.837	-0.039
91	A	51	GLU	-1	-1.026	-0.868	5.550	0.045	0.045	0.000	0.000	0.000	0.000
92	A	52	ASN	0	0.032	-0.070	3.167	-1.490	-0.279	0.234	-0.454	-0.990	-0.003
93	A	52	ASN	0	-0.052	0.061	4.900	0.379	0.379	0.000	0.000	0.000	0.000
94	A	53	LEU	0	0.167	-0.066	3.905	0.093	0.119	-0.001	0.014	-0.039	0.000
95	A	53	LEU	0	-0.097	0.104	6.377	0.031	0.031	0.000	0.000	0.000	0.000
96	A	54	LEU	0	0.064	-0.088	6.569	0.223	0.223	0.000	0.000	0.000	0.000
97	A	54	LEU	0	-0.045	0.089	9.142	0.030	0.030	0.000	0.000	0.000	0.000
98	A	55	GLU	0	0.164	-0.061	7.793	0.250	0.250	0.000	0.000	0.000	0.000
99	A	55	GLU	-1	-0.847	-0.771	6.636	-2.026	-2.026	0.000	0.000	0.000	0.000
100	A	56	ALA	0	0.114	-0.111	6.959	0.292	0.292	0.000	0.000	0.000	0.000
101	A	56	ALA	0	-0.079	0.095	6.033	-0.067	-0.067	0.000	0.000	0.000	0.000
102	A	57	GLU	0	0.092	-0.121	8.003	0.249	0.249	0.000	0.000	0.000	0.000
103	A	57	GLU	-1	-0.961	-0.810	11.043	-0.774	-0.774	0.000	0.000	0.000	0.000
104	A	58	GLU	0	0.054	-0.141	11.265	0.172	0.172	0.000	0.000	0.000	0.000
105	A	58	GLU	-1	-1.014	-0.834	11.668	-0.848	-0.848	0.000	0.000	0.000	0.000
106	A	59	LYS	0	0.073	-0.110	10.850	0.202	0.202	0.000	0.000	0.000	0.000
107	A	59	LYS	1	0.710	0.999	6.662	1.711	1.711	0.000	0.000	0.000	0.000
108	A	60	ALA	0	0.082	-0.093	11.875	0.154	0.154	0.000	0.000	0.000	0.000
109	A	60	ALA	0	-0.064	0.098	11.601	-0.010	-0.010	0.000	0.000	0.000	0.000
110	A	61	LYS	0	0.074	-0.100	13.380	0.100	0.100	0.000	0.000	0.000	0.000
111	A	61	LYS	1	0.794	1.008	15.287	0.637	0.637	0.000	0.000	0.000	0.000
112	A	62	ALA	0	0.081	-0.096	15.614	0.084	0.084	0.000	0.000	0.000	0.000
113	A	62	ALA	0	-0.096	0.105	15.301	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	63	MET	0	0.057	-0.121	15.624	0.080	0.080	0.000	0.000	0.000	0.000
115	A	63	MET	0	-0.117	0.092	11.974	0.029	0.029	0.000	0.000	0.000	0.000
116	A	64	GLY	0	0.031	-0.101	17.019	0.052	0.052	0.000	0.000	0.000	0.000
117	A	65	ALA	0	0.091	-0.010	19.337	0.047	0.047	0.000	0.000	0.000	0.000
118	A	65	ALA	0	-0.091	0.095	20.595	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	66	LEU	0	0.001	-0.116	20.377	0.034	0.034	0.000	0.000	0.000	0.000
120	A	66	LEU	0	-0.118	0.090	18.965	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	67	LEU	0	0.009	-0.101	21.828	0.032	0.032	0.000	0.000	0.000	0.000
122	A	67	LEU	0	-0.054	0.083	19.409	0.000	0.000	0.000	0.000	0.000	0.000
123	A	68	ALA	0	0.166	-0.102	23.154	0.023	0.023	0.000	0.000	0.000	0.000
124	A	68	ALA	0	-0.091	0.119	24.182	-0.002	-0.002	0.000	0.000	0.000	0.000
125	A	69	ASN	0	0.102	-0.075	25.444	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	69	ASN	0	-0.123	0.068	29.917	0.002	0.002	0.000	0.000	0.000	0.000
127	A	70	PRO	0	0.055	-0.084	27.882	0.003	0.003	0.000	0.000	0.000	0.000
128	A	71	VAL	0	0.078	0.002	29.786	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	71	VAL	0	-0.083	0.105	33.698	0.001	0.001	0.000	0.000	0.000	0.000
130	A	72	MET	0	0.163	-0.067	32.397	0.001	0.001	0.000	0.000	0.000	0.000
131	A	72	MET	0	-0.115	0.088	31.591	0.004	0.004	0.000	0.000	0.000	0.000
132	A	73	GLU	0	-0.005	-0.130	28.535	0.009	0.009	0.000	0.000	0.000	0.000
133	A	73	GLU	-1	-0.847	-0.781	27.615	-0.183	-0.183	0.000	0.000	0.000	0.000
134	A	74	VAL	0	0.044	-0.093	26.302	0.003	0.003	0.000	0.000	0.000	0.000
135	A	74	VAL	0	-0.048	0.097	25.999	0.000	0.000	0.000	0.000	0.000	0.000
136	A	75	TYR	0	0.041	-0.077	21.807	0.019	0.019	0.000	0.000	0.000	0.000
137	A	75	TYR	0	-0.033	0.091	18.398	-0.015	-0.015	0.000	0.000	0.000	0.000
138	A	76	ALA	0	0.110	-0.129	20.712	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	76	ALA	0	-0.057	0.133	21.277	0.007	0.007	0.000	0.000	0.000	0.000
140	A	77	LEU	0	0.101	-0.086	16.052	0.029	0.029	0.000	0.000	0.000	0.000
141	A	77	LEU	0	-0.148	0.098	12.757	-0.017	-0.017	0.000	0.000	0.000	0.000
142	A	78	GLU	0	0.121	-0.094	16.664	-0.042	-0.042	0.000	0.000	0.000	0.000
143	A	78	GLU	-1	-1.020	-0.869	18.367	-0.301	-0.301	0.000	0.000	0.000	0.000
144	A	79	ALA	0	0.085	-0.109	14.684	0.019	0.019	0.000	0.000	0.000	0.000
145	A	79	ALA	0	-0.083	0.095	14.048	0.008	0.008	0.000	0.000	0.000	0.000
146	A	80	LEU	0	0.051	-0.133	10.852	0.032	0.032	0.000	0.000	0.000	0.000
147	A	80	LEU	0	-0.097	0.132	8.522	-0.003	-0.003	0.000	0.000	0.000	0.000
148	A	81	LYS	0	0.022	-0.092	8.480	0.007	0.007	0.000	0.000	0.000	0.000
149	A	81	LYS	1	0.836	1.046	9.075	0.555	0.555	0.000	0.000	0.000	0.000
150	A	82	GLU	0	0.154	-0.094	4.561	-0.245	-0.205	-0.001	-0.017	-0.020	0.000
151	A	82	GLU	-1	-0.935	-0.778	2.536	-6.281	-3.646	1.959	-1.868	-2.726	-0.017
152	A	83	LEU	0	0.007	-0.169	4.402	0.160	0.247	-0.001	-0.006	-0.079	0.000
153	A	83	LEU	0	-0.093	0.111	6.078	0.070	0.070	0.000	0.000	0.000	0.000
154	A	84	PRO	0	0.020	-0.058	4.600	0.299	0.374	-0.001	-0.004	-0.070	0.000

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