FMO DATABASE

FMODB ID: K2N93

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	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	154
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-476548.682495
FMO2-HF: Nuclear repulsion	445147.469594
FMO2-HF: Total energy	-31401.212901
FMO2-MP2: Total energy	-31493.460941

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.
-18.48	-9.111	15.653	-10.341	-14.683	-0.08

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 : 0.031 / q_NPA : 0.010

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	0.867	1.051	4.218	-0.755	-0.323	0.000	-0.158	-0.273	0.000
4	A	4	TYR	0	0.042	-0.110	3.711	-1.763	0.762	-0.001	-1.267	-1.257	0.006
5	A	4	TYR	0	-0.005	0.150	2.146	-2.541	-0.774	3.651	-1.504	-3.914	-0.012
6	A	5	GLN	0	0.179	-0.066	5.354	0.198	0.243	-0.002	-0.002	-0.042	0.000
7	A	5	GLN	0	-0.141	0.056	9.354	0.083	0.083	0.000	0.000	0.000	0.000
8	A	6	ALA	0	0.058	-0.103	9.064	-0.055	-0.055	0.000	0.000	0.000	0.000
9	A	6	ALA	0	-0.073	0.098	10.962	-0.008	-0.008	0.000	0.000	0.000	0.000
10	A	7	THR	0	0.008	-0.095	11.535	0.061	0.061	0.000	0.000	0.000	0.000
11	A	7	THR	0	-0.103	0.052	14.616	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	8	LEU	0	0.069	-0.112	14.977	-0.011	-0.011	0.000	0.000	0.000	0.000
13	A	8	LEU	0	-0.095	0.099	15.234	0.004	0.004	0.000	0.000	0.000	0.000
14	A	9	LEU	0	0.072	-0.118	17.448	0.028	0.028	0.000	0.000	0.000	0.000
15	A	9	LEU	0	-0.026	0.154	20.022	0.001	0.001	0.000	0.000	0.000	0.000
16	A	10	ILE	0	0.116	-0.100	21.131	-0.019	-0.019	0.000	0.000	0.000	0.000
17	A	10	ILE	0	-0.142	0.110	21.505	0.001	0.001	0.000	0.000	0.000	0.000
18	A	11	GLU	0	0.059	-0.115	23.813	0.019	0.019	0.000	0.000	0.000	0.000
19	A	11	GLU	-1	-1.006	-0.850	24.812	-0.220	-0.220	0.000	0.000	0.000	0.000
20	A	12	LEU	0	0.107	-0.124	27.051	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	12	LEU	0	-0.059	0.134	30.815	0.002	0.002	0.000	0.000	0.000	0.000
22	A	13	LYS	0	0.047	-0.105	30.596	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	13	LYS	1	0.837	1.041	29.591	0.186	0.186	0.000	0.000	0.000	0.000
24	A	14	LYS	0	0.080	-0.121	31.766	0.007	0.007	0.000	0.000	0.000	0.000
25	A	14	LYS	1	0.896	1.103	30.273	0.173	0.173	0.000	0.000	0.000	0.000
26	A	15	GLY	0	-0.015	-0.103	34.741	0.000	0.000	0.000	0.000	0.000	0.000
27	A	16	ILE	0	0.037	-0.030	35.220	0.009	0.009	0.000	0.000	0.000	0.000
28	A	16	ILE	0	-0.090	0.137	33.916	0.000	0.000	0.000	0.000	0.000	0.000
29	A	17	LEU	0	0.061	-0.117	36.553	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	17	LEU	0	-0.080	0.110	39.179	0.001	0.001	0.000	0.000	0.000	0.000
31	A	18	ASP	0	0.113	-0.114	35.601	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	18	ASP	-1	-0.855	-0.753	33.529	-0.124	-0.124	0.000	0.000	0.000	0.000
33	A	19	PRO	0	-0.011	-0.103	36.466	0.003	0.003	0.000	0.000	0.000	0.000
34	A	20	GLN	0	0.068	0.009	34.902	0.006	0.006	0.000	0.000	0.000	0.000
35	A	20	GLN	0	-0.039	0.094	32.223	0.001	0.001	0.000	0.000	0.000	0.000
36	A	21	GLY	0	0.083	-0.072	35.174	0.003	0.003	0.000	0.000	0.000	0.000
37	A	22	ARG	0	0.051	-0.033	35.808	0.002	0.002	0.000	0.000	0.000	0.000
38	A	22	ARG	1	0.762	1.040	36.278	0.103	0.103	0.000	0.000	0.000	0.000
39	A	23	ALA	0	0.149	-0.077	39.163	0.004	0.004	0.000	0.000	0.000	0.000
40	A	23	ALA	0	-0.098	0.096	38.575	0.000	0.000	0.000	0.000	0.000	0.000
41	A	24	VAL	0	0.051	-0.110	36.218	0.007	0.007	0.000	0.000	0.000	0.000
42	A	24	VAL	0	-0.053	0.097	34.500	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	25	GLU	0	0.048	-0.135	37.734	0.003	0.003	0.000	0.000	0.000	0.000
44	A	25	GLU	-1	-0.873	-0.767	37.733	-0.094	-0.094	0.000	0.000	0.000	0.000
45	A	26	GLY	0	-0.034	-0.118	39.480	0.003	0.003	0.000	0.000	0.000	0.000
46	A	27	VAL	0	0.171	0.059	40.943	0.003	0.003	0.000	0.000	0.000	0.000
47	A	27	VAL	0	-0.103	0.076	39.924	0.000	0.000	0.000	0.000	0.000	0.000
48	A	28	LEU	0	0.042	-0.120	39.214	0.005	0.005	0.000	0.000	0.000	0.000
49	A	28	LEU	0	-0.048	0.107	35.820	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	29	LYS	0	0.058	-0.116	40.326	0.002	0.002	0.000	0.000	0.000	0.000
51	A	29	LYS	1	0.756	1.084	41.428	0.072	0.072	0.000	0.000	0.000	0.000
52	A	30	ASP	0	0.094	-0.092	43.625	0.002	0.002	0.000	0.000	0.000	0.000
53	A	30	ASP	-1	-0.989	-0.845	44.999	-0.054	-0.054	0.000	0.000	0.000	0.000
54	A	31	LEU	0	-0.049	-0.139	42.557	0.004	0.004	0.000	0.000	0.000	0.000
55	A	31	LEU	0	-0.120	0.087	40.380	0.000	0.000	0.000	0.000	0.000	0.000
56	A	32	GLY	0	-0.014	-0.115	43.555	0.001	0.001	0.000	0.000	0.000	0.000
57	A	33	HIS	0	-0.001	-0.027	40.128	0.001	0.001	0.000	0.000	0.000	0.000
58	A	33	HIS	0	-0.108	0.094	39.229	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	34	PRO	0	0.058	-0.143	40.152	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	35	VAL	0	0.043	-0.014	38.227	0.001	0.001	0.000	0.000	0.000	0.000
61	A	35	VAL	0	-0.008	0.127	36.766	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	36	GLU	0	0.056	-0.139	38.806	0.004	0.004	0.000	0.000	0.000	0.000
63	A	36	GLU	-1	-1.027	-0.848	38.480	-0.094	-0.094	0.000	0.000	0.000	0.000
64	A	37	GLU	0	0.095	-0.115	36.846	0.004	0.004	0.000	0.000	0.000	0.000
65	A	37	GLU	-1	-0.974	-0.828	34.915	-0.127	-0.127	0.000	0.000	0.000	0.000
66	A	38	VAL	0	-0.035	-0.153	33.882	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	38	VAL	0	-0.054	0.113	33.106	0.000	0.000	0.000	0.000	0.000	0.000
68	A	39	ARG	0	0.050	-0.096	31.750	0.007	0.007	0.000	0.000	0.000	0.000
69	A	39	ARG	1	0.799	1.017	29.128	0.155	0.155	0.000	0.000	0.000	0.000
70	A	40	VAL	0	0.059	-0.135	30.114	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	40	VAL	0	-0.077	0.115	30.113	0.002	0.002	0.000	0.000	0.000	0.000
72	A	41	GLY	0	0.005	-0.090	26.955	0.000	0.000	0.000	0.000	0.000	0.000
73	A	42	LYS	0	0.038	-0.012	24.720	0.015	0.015	0.000	0.000	0.000	0.000
74	A	42	LYS	1	0.811	1.030	24.007	0.186	0.186	0.000	0.000	0.000	0.000
75	A	43	VAL	0	0.062	-0.097	20.930	-0.016	-0.016	0.000	0.000	0.000	0.000
76	A	43	VAL	0	-0.015	0.131	19.168	0.002	0.002	0.000	0.000	0.000	0.000
77	A	44	LEU	0	0.008	-0.148	18.515	0.039	0.039	0.000	0.000	0.000	0.000
78	A	44	LEU	0	-0.077	0.097	17.846	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	45	GLU	0	0.115	-0.090	14.948	-0.060	-0.060	0.000	0.000	0.000	0.000
80	A	45	GLU	-1	-0.918	-0.803	14.703	-0.370	-0.370	0.000	0.000	0.000	0.000
81	A	46	ILE	0	0.027	-0.156	13.138	0.085	0.085	0.000	0.000	0.000	0.000
82	A	46	ILE	0	-0.076	0.137	11.978	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	47	VAL	0	0.150	-0.080	9.467	-0.199	-0.199	0.000	0.000	0.000	0.000
84	A	47	VAL	0	-0.116	0.091	8.376	0.041	0.041	0.000	0.000	0.000	0.000
85	A	48	PHE	0	-0.039	-0.135	7.976	0.339	0.339	0.000	0.000	0.000	0.000
86	A	48	PHE	0	-0.079	0.100	7.419	-0.042	-0.042	0.000	0.000	0.000	0.000
87	A	49	PRO	0	-0.026	-0.111	3.954	-0.570	-0.396	-0.001	-0.094	-0.079	0.000
88	A	50	ALA	0	0.065	-0.001	2.413	1.316	2.362	0.152	-0.470	-0.728	0.001
89	A	50	ALA	0	-0.063	0.087	3.974	0.124	0.229	0.000	-0.045	-0.060	0.000
90	A	51	GLU	0	0.138	-0.100	2.070	-8.330	-9.183	8.147	-3.545	-3.750	-0.046
91	A	51	GLU	-1	-1.029	-0.840	5.475	-0.197	-0.197	0.000	0.000	0.000	0.000
92	A	52	ASN	0	0.043	-0.075	2.971	-2.389	-0.873	0.358	-0.714	-1.160	-0.007
93	A	52	ASN	0	-0.051	0.074	5.313	0.261	0.261	0.000	0.000	0.000	0.000
94	A	53	LEU	0	0.176	-0.095	4.049	-0.053	-0.017	-0.002	0.008	-0.043	0.000
95	A	53	LEU	0	-0.095	0.113	6.041	0.029	0.029	0.000	0.000	0.000	0.000
96	A	54	LEU	0	0.047	-0.102	6.224	0.191	0.191	0.000	0.000	0.000	0.000
97	A	54	LEU	0	-0.046	0.099	8.941	0.029	0.029	0.000	0.000	0.000	0.000
98	A	55	GLU	0	0.197	-0.080	7.362	0.276	0.276	0.000	0.000	0.000	0.000
99	A	55	GLU	-1	-0.960	-0.825	6.403	-1.820	-1.820	0.000	0.000	0.000	0.000
100	A	56	ALA	0	0.082	-0.112	6.554	0.305	0.305	0.000	0.000	0.000	0.000
101	A	56	ALA	0	-0.070	0.101	5.480	-0.058	-0.058	0.000	0.000	0.000	0.000
102	A	57	GLU	0	0.137	-0.122	7.392	0.240	0.240	0.000	0.000	0.000	0.000
103	A	57	GLU	-1	-0.988	-0.825	10.846	-0.784	-0.784	0.000	0.000	0.000	0.000
104	A	58	GLU	0	0.021	-0.135	10.727	0.173	0.173	0.000	0.000	0.000	0.000
105	A	58	GLU	-1	-1.021	-0.847	11.004	-0.928	-0.928	0.000	0.000	0.000	0.000
106	A	59	LYS	0	0.065	-0.119	10.536	0.214	0.214	0.000	0.000	0.000	0.000
107	A	59	LYS	1	0.844	1.067	7.461	1.296	1.296	0.000	0.000	0.000	0.000
108	A	60	ALA	0	0.076	-0.092	11.186	0.156	0.156	0.000	0.000	0.000	0.000
109	A	60	ALA	0	-0.060	0.097	11.257	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	61	LYS	0	0.068	-0.109	12.779	0.112	0.112	0.000	0.000	0.000	0.000
111	A	61	LYS	1	0.834	1.061	14.929	0.588	0.588	0.000	0.000	0.000	0.000
112	A	62	ALA	0	0.088	-0.101	14.989	0.093	0.093	0.000	0.000	0.000	0.000
113	A	62	ALA	0	-0.093	0.110	15.060	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	63	MET	0	0.058	-0.117	15.351	0.087	0.087	0.000	0.000	0.000	0.000
115	A	63	MET	0	-0.119	0.096	11.674	0.029	0.029	0.000	0.000	0.000	0.000
116	A	64	GLY	0	0.019	-0.094	16.724	0.060	0.060	0.000	0.000	0.000	0.000
117	A	65	ALA	0	0.101	-0.016	19.018	0.050	0.050	0.000	0.000	0.000	0.000
118	A	65	ALA	0	-0.088	0.091	20.276	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	66	LEU	0	0.040	-0.126	20.051	0.037	0.037	0.000	0.000	0.000	0.000
120	A	66	LEU	0	-0.152	0.093	18.974	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	67	LEU	0	0.012	-0.112	20.965	0.035	0.035	0.000	0.000	0.000	0.000
122	A	67	LEU	0	-0.076	0.074	18.582	0.001	0.001	0.000	0.000	0.000	0.000
123	A	68	ALA	0	0.138	-0.079	22.509	0.026	0.026	0.000	0.000	0.000	0.000
124	A	68	ALA	0	-0.105	0.114	23.836	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	69	ASN	0	0.099	-0.088	25.019	0.000	0.000	0.000	0.000	0.000	0.000
126	A	69	ASN	0	-0.122	0.074	29.418	0.005	0.005	0.000	0.000	0.000	0.000
127	A	70	PRO	0	0.018	-0.093	27.932	0.004	0.004	0.000	0.000	0.000	0.000
128	A	71	VAL	0	0.033	-0.028	29.515	-0.005	-0.005	0.000	0.000	0.000	0.000
129	A	71	VAL	0	-0.073	0.096	33.689	0.001	0.001	0.000	0.000	0.000	0.000
130	A	72	MET	0	0.157	-0.060	31.951	0.003	0.003	0.000	0.000	0.000	0.000
131	A	72	MET	0	-0.136	0.081	31.149	0.005	0.005	0.000	0.000	0.000	0.000
132	A	73	GLU	0	0.000	-0.171	28.046	0.009	0.009	0.000	0.000	0.000	0.000
133	A	73	GLU	-1	-0.866	-0.792	27.313	-0.190	-0.190	0.000	0.000	0.000	0.000
134	A	74	VAL	0	0.039	-0.085	26.068	0.001	0.001	0.000	0.000	0.000	0.000
135	A	74	VAL	0	-0.035	0.082	25.884	0.001	0.001	0.000	0.000	0.000	0.000
136	A	75	TYR	0	0.056	-0.070	21.588	0.018	0.018	0.000	0.000	0.000	0.000
137	A	75	TYR	0	-0.053	0.089	18.415	-0.020	-0.020	0.000	0.000	0.000	0.000
138	A	76	ALA	0	0.087	-0.155	20.391	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	76	ALA	0	-0.058	0.148	20.996	0.007	0.007	0.000	0.000	0.000	0.000
140	A	77	LEU	0	0.082	-0.107	15.818	0.024	0.024	0.000	0.000	0.000	0.000
141	A	77	LEU	0	-0.128	0.100	12.620	-0.015	-0.015	0.000	0.000	0.000	0.000
142	A	78	GLU	0	0.121	-0.090	16.708	-0.024	-0.024	0.000	0.000	0.000	0.000
143	A	78	GLU	-1	-1.013	-0.861	17.633	-0.312	-0.312	0.000	0.000	0.000	0.000
144	A	79	ALA	0	0.067	-0.115	14.219	0.015	0.015	0.000	0.000	0.000	0.000
145	A	79	ALA	0	-0.077	0.103	13.822	0.010	0.010	0.000	0.000	0.000	0.000
146	A	80	LEU	0	0.061	-0.139	10.352	0.021	0.021	0.000	0.000	0.000	0.000
147	A	80	LEU	0	-0.096	0.146	8.322	-0.012	-0.012	0.000	0.000	0.000	0.000
148	A	81	LYS	0	0.014	-0.090	8.062	-0.018	-0.018	0.000	0.000	0.000	0.000
149	A	81	LYS	1	0.879	1.062	8.768	0.429	0.429	0.000	0.000	0.000	0.000
150	A	82	GLU	0	0.169	-0.121	4.219	-0.250	-0.184	-0.001	-0.021	-0.044	0.000
151	A	82	GLU	-1	-0.994	-0.815	2.259	-4.405	-2.128	3.354	-2.517	-3.114	-0.022
152	A	83	LEU	0	-0.023	-0.153	4.426	0.172	0.271	-0.001	-0.008	-0.089	0.000
153	A	83	LEU	0	-0.120	0.090	6.122	0.080	0.080	0.000	0.000	0.000	0.000
154	A	84	PRO	0	0.001	-0.087	4.601	0.114	0.248	-0.001	-0.004	-0.130	0.000

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