FMO DATABASE

FMODB ID: RYR98

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

Total energy (hartree)

FMO2-HF: Electronic energy	-476816.146429
FMO2-HF: Nuclear repulsion	445413.35582
FMO2-HF: Total energy	-31402.790609
FMO2-MP2: Total energy	-31495.010455

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.
-20.581	-10.38	12.965	-9.845	-13.32	-0.078

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 : 0.008 / q_NPA : -0.004

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	0.839	1.023	3.966	-1.116	-0.691	0.001	-0.154	-0.272	0.000
4	A	4	TYR	0	0.028	-0.095	3.802	-1.206	0.833	-0.011	-0.955	-1.073	0.004
5	A	4	TYR	0	-0.055	0.092	2.433	-2.850	0.035	2.338	-1.581	-3.642	-0.011
6	A	5	GLN	0	0.186	-0.060	5.585	0.303	0.303	0.000	0.000	0.000	0.000
7	A	5	GLN	0	-0.122	0.039	9.622	0.081	0.081	0.000	0.000	0.000	0.000
8	A	6	ALA	0	0.048	-0.090	9.296	-0.076	-0.076	0.000	0.000	0.000	0.000
9	A	6	ALA	0	-0.066	0.087	11.100	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	7	THR	0	0.020	-0.085	11.730	0.073	0.073	0.000	0.000	0.000	0.000
11	A	7	THR	0	-0.119	0.032	14.712	-0.012	-0.012	0.000	0.000	0.000	0.000
12	A	8	LEU	0	0.079	-0.107	15.178	-0.018	-0.018	0.000	0.000	0.000	0.000
13	A	8	LEU	0	-0.095	0.089	15.437	0.006	0.006	0.000	0.000	0.000	0.000
14	A	9	LEU	0	0.065	-0.107	17.634	0.034	0.034	0.000	0.000	0.000	0.000
15	A	9	LEU	0	-0.052	0.138	20.225	0.004	0.004	0.000	0.000	0.000	0.000
16	A	10	ILE	0	0.136	-0.091	21.316	-0.020	-0.020	0.000	0.000	0.000	0.000
17	A	10	ILE	0	-0.154	0.110	21.561	0.002	0.002	0.000	0.000	0.000	0.000
18	A	11	GLU	0	0.086	-0.104	23.994	0.021	0.021	0.000	0.000	0.000	0.000
19	A	11	GLU	-1	-0.852	-0.777	26.048	-0.190	-0.190	0.000	0.000	0.000	0.000
20	A	12	LEU	0	0.090	-0.105	27.227	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	12	LEU	0	-0.048	0.134	30.985	0.002	0.002	0.000	0.000	0.000	0.000
22	A	13	LYS	0	0.079	-0.113	30.766	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	13	LYS	1	0.829	1.053	29.992	0.178	0.178	0.000	0.000	0.000	0.000
24	A	14	LYS	0	0.152	-0.077	31.912	0.008	0.008	0.000	0.000	0.000	0.000
25	A	14	LYS	1	0.767	1.061	29.935	0.178	0.178	0.000	0.000	0.000	0.000
26	A	15	GLY	0	-0.066	-0.141	34.884	0.000	0.000	0.000	0.000	0.000	0.000
27	A	16	ILE	0	0.027	-0.021	35.405	0.009	0.009	0.000	0.000	0.000	0.000
28	A	16	ILE	0	-0.121	0.117	34.221	0.000	0.000	0.000	0.000	0.000	0.000
29	A	17	LEU	0	0.102	-0.111	36.726	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	17	LEU	0	-0.081	0.102	39.453	0.001	0.001	0.000	0.000	0.000	0.000
31	A	18	ASP	0	0.116	-0.128	35.714	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	18	ASP	-1	-0.857	-0.741	33.767	-0.119	-0.119	0.000	0.000	0.000	0.000
33	A	19	PRO	0	-0.008	-0.114	36.658	0.003	0.003	0.000	0.000	0.000	0.000
34	A	20	GLN	0	0.063	0.014	35.116	0.006	0.006	0.000	0.000	0.000	0.000
35	A	20	GLN	0	-0.053	0.087	32.124	0.003	0.003	0.000	0.000	0.000	0.000
36	A	21	GLY	0	0.079	-0.068	35.371	0.003	0.003	0.000	0.000	0.000	0.000
37	A	22	ARG	0	0.101	0.013	36.012	0.001	0.001	0.000	0.000	0.000	0.000
38	A	22	ARG	1	0.686	0.985	36.670	0.104	0.104	0.000	0.000	0.000	0.000
39	A	23	ALA	0	0.138	-0.081	39.378	0.003	0.003	0.000	0.000	0.000	0.000
40	A	23	ALA	0	-0.101	0.087	38.885	0.001	0.001	0.000	0.000	0.000	0.000
41	A	24	VAL	0	0.052	-0.104	36.414	0.006	0.006	0.000	0.000	0.000	0.000
42	A	24	VAL	0	-0.078	0.092	34.677	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	25	GLU	0	0.084	-0.130	37.951	0.002	0.002	0.000	0.000	0.000	0.000
44	A	25	GLU	-1	-0.872	-0.790	37.996	-0.094	-0.094	0.000	0.000	0.000	0.000
45	A	26	GLY	0	-0.035	-0.100	39.685	0.003	0.003	0.000	0.000	0.000	0.000
46	A	27	VAL	0	0.154	0.052	41.210	0.003	0.003	0.000	0.000	0.000	0.000
47	A	27	VAL	0	-0.114	0.079	40.210	0.000	0.000	0.000	0.000	0.000	0.000
48	A	28	LEU	0	0.065	-0.109	39.380	0.005	0.005	0.000	0.000	0.000	0.000
49	A	28	LEU	0	-0.051	0.100	35.954	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	29	LYS	0	0.026	-0.129	40.539	0.002	0.002	0.000	0.000	0.000	0.000
51	A	29	LYS	1	0.797	1.046	41.584	0.076	0.076	0.000	0.000	0.000	0.000
52	A	30	ASP	0	0.102	-0.074	43.833	0.002	0.002	0.000	0.000	0.000	0.000
53	A	30	ASP	-1	-1.013	-0.849	45.158	-0.051	-0.051	0.000	0.000	0.000	0.000
54	A	31	LEU	0	-0.043	-0.126	42.792	0.004	0.004	0.000	0.000	0.000	0.000
55	A	31	LEU	0	-0.116	0.081	40.713	0.000	0.000	0.000	0.000	0.000	0.000
56	A	32	GLY	0	-0.002	-0.119	43.770	0.001	0.001	0.000	0.000	0.000	0.000
57	A	33	HIS	0	0.005	-0.019	40.339	0.001	0.001	0.000	0.000	0.000	0.000
58	A	33	HIS	0	-0.117	0.091	39.443	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	34	PRO	0	0.052	-0.126	40.351	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	35	VAL	0	0.023	-0.004	38.397	0.000	0.000	0.000	0.000	0.000	0.000
61	A	35	VAL	0	-0.020	0.120	36.837	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	36	GLU	0	0.082	-0.130	38.975	0.005	0.005	0.000	0.000	0.000	0.000
63	A	36	GLU	-1	-1.020	-0.855	38.639	-0.098	-0.098	0.000	0.000	0.000	0.000
64	A	37	GLU	0	0.030	-0.128	36.931	0.004	0.004	0.000	0.000	0.000	0.000
65	A	37	GLU	-1	-0.878	-0.808	34.873	-0.130	-0.130	0.000	0.000	0.000	0.000
66	A	38	VAL	0	-0.015	-0.124	34.069	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	38	VAL	0	-0.072	0.104	33.211	0.001	0.001	0.000	0.000	0.000	0.000
68	A	39	ARG	0	0.107	-0.103	31.911	0.007	0.007	0.000	0.000	0.000	0.000
69	A	39	ARG	1	0.688	0.970	29.088	0.159	0.159	0.000	0.000	0.000	0.000
70	A	40	VAL	0	0.024	-0.136	30.317	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	40	VAL	0	-0.103	0.104	30.451	0.002	0.002	0.000	0.000	0.000	0.000
72	A	41	GLY	0	0.004	-0.103	27.155	0.000	0.000	0.000	0.000	0.000	0.000
73	A	42	LYS	0	0.023	-0.016	24.933	0.015	0.015	0.000	0.000	0.000	0.000
74	A	42	LYS	1	0.783	0.989	24.276	0.178	0.178	0.000	0.000	0.000	0.000
75	A	43	VAL	0	0.087	-0.079	21.144	-0.018	-0.018	0.000	0.000	0.000	0.000
76	A	43	VAL	0	-0.046	0.123	19.418	0.001	0.001	0.000	0.000	0.000	0.000
77	A	44	LEU	0	0.035	-0.131	18.739	0.039	0.039	0.000	0.000	0.000	0.000
78	A	44	LEU	0	-0.093	0.090	18.277	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	45	GLU	0	0.121	-0.089	15.179	-0.063	-0.063	0.000	0.000	0.000	0.000
80	A	45	GLU	-1	-0.906	-0.773	14.962	-0.371	-0.371	0.000	0.000	0.000	0.000
81	A	46	ILE	0	-0.007	-0.156	13.367	0.092	0.092	0.000	0.000	0.000	0.000
82	A	46	ILE	0	-0.044	0.125	11.841	0.001	0.001	0.000	0.000	0.000	0.000
83	A	47	VAL	0	0.155	-0.069	9.710	-0.215	-0.215	0.000	0.000	0.000	0.000
84	A	47	VAL	0	-0.116	0.085	8.504	0.042	0.042	0.000	0.000	0.000	0.000
85	A	48	PHE	0	-0.033	-0.126	8.019	0.352	0.352	0.000	0.000	0.000	0.000
86	A	48	PHE	0	-0.074	0.098	7.492	-0.074	-0.074	0.000	0.000	0.000	0.000
87	A	49	PRO	0	-0.016	-0.104	4.043	-0.648	-0.489	-0.001	-0.087	-0.071	0.000
88	A	50	ALA	0	0.077	0.004	2.436	1.248	2.202	0.141	-0.414	-0.682	0.001
89	A	50	ALA	0	-0.066	0.089	4.180	0.129	0.204	-0.001	-0.030	-0.044	0.000
90	A	51	GLU	0	0.150	-0.083	1.971	-9.106	-9.511	7.492	-3.865	-3.222	-0.047
91	A	51	GLU	-1	-1.048	-0.867	5.701	0.142	0.142	0.000	0.000	0.000	0.000
92	A	52	ASN	0	0.040	-0.062	3.228	-1.904	-0.682	0.188	-0.490	-0.920	-0.004
93	A	52	ASN	0	-0.061	0.063	5.169	0.332	0.332	0.000	0.000	0.000	0.000
94	A	53	LEU	0	0.174	-0.082	4.128	0.050	0.073	-0.001	0.002	-0.023	0.000
95	A	53	LEU	0	-0.089	0.108	6.416	0.035	0.035	0.000	0.000	0.000	0.000
96	A	54	LEU	0	0.050	-0.100	6.449	0.237	0.237	0.000	0.000	0.000	0.000
97	A	54	LEU	0	-0.039	0.095	9.238	0.034	0.034	0.000	0.000	0.000	0.000
98	A	55	GLU	0	0.159	-0.085	7.596	0.298	0.298	0.000	0.000	0.000	0.000
99	A	55	GLU	-1	-0.879	-0.780	6.705	-1.827	-1.827	0.000	0.000	0.000	0.000
100	A	56	ALA	0	0.114	-0.092	6.964	0.397	0.397	0.000	0.000	0.000	0.000
101	A	56	ALA	0	-0.072	0.099	5.901	-0.084	-0.084	0.000	0.000	0.000	0.000
102	A	57	GLU	0	0.111	-0.111	7.864	0.278	0.278	0.000	0.000	0.000	0.000
103	A	57	GLU	-1	-0.957	-0.811	11.039	-0.826	-0.826	0.000	0.000	0.000	0.000
104	A	58	GLU	0	0.049	-0.135	11.119	0.184	0.184	0.000	0.000	0.000	0.000
105	A	58	GLU	-1	-1.017	-0.839	11.469	-0.920	-0.920	0.000	0.000	0.000	0.000
106	A	59	LYS	0	0.040	-0.133	10.470	0.217	0.217	0.000	0.000	0.000	0.000
107	A	59	LYS	1	0.778	1.008	7.132	1.290	1.290	0.000	0.000	0.000	0.000
108	A	60	ALA	0	0.086	-0.070	11.419	0.177	0.177	0.000	0.000	0.000	0.000
109	A	60	ALA	0	-0.071	0.096	11.345	-0.009	-0.009	0.000	0.000	0.000	0.000
110	A	61	LYS	0	0.060	-0.125	12.896	0.116	0.116	0.000	0.000	0.000	0.000
111	A	61	LYS	1	0.807	1.021	15.331	0.670	0.670	0.000	0.000	0.000	0.000
112	A	62	ALA	0	0.085	-0.081	15.151	0.091	0.091	0.000	0.000	0.000	0.000
113	A	62	ALA	0	-0.095	0.105	14.975	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	63	MET	0	0.054	-0.127	15.262	0.087	0.087	0.000	0.000	0.000	0.000
115	A	63	MET	0	-0.109	0.099	11.554	0.036	0.036	0.000	0.000	0.000	0.000
116	A	64	GLY	0	0.013	-0.099	16.646	0.058	0.058	0.000	0.000	0.000	0.000
117	A	65	ALA	0	0.098	-0.006	18.974	0.049	0.049	0.000	0.000	0.000	0.000
118	A	65	ALA	0	-0.095	0.089	20.256	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	66	LEU	0	0.030	-0.111	19.974	0.035	0.035	0.000	0.000	0.000	0.000
120	A	66	LEU	0	-0.141	0.078	19.071	0.000	0.000	0.000	0.000	0.000	0.000
121	A	67	LEU	0	0.018	-0.096	20.905	0.035	0.035	0.000	0.000	0.000	0.000
122	A	67	LEU	0	-0.083	0.069	18.720	0.001	0.001	0.000	0.000	0.000	0.000
123	A	68	ALA	0	0.152	-0.092	22.451	0.027	0.027	0.000	0.000	0.000	0.000
124	A	68	ALA	0	-0.101	0.115	23.904	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	69	ASN	0	0.096	-0.076	24.928	0.001	0.001	0.000	0.000	0.000	0.000
126	A	69	ASN	0	-0.118	0.069	29.290	0.002	0.002	0.000	0.000	0.000	0.000
127	A	70	PRO	0	0.049	-0.082	27.859	0.002	0.002	0.000	0.000	0.000	0.000
128	A	71	VAL	0	0.055	-0.021	29.527	-0.006	-0.006	0.000	0.000	0.000	0.000
129	A	71	VAL	0	-0.078	0.100	33.392	0.001	0.001	0.000	0.000	0.000	0.000
130	A	72	MET	0	0.157	-0.058	31.891	0.002	0.002	0.000	0.000	0.000	0.000
131	A	72	MET	0	-0.136	0.083	31.105	0.005	0.005	0.000	0.000	0.000	0.000
132	A	73	GLU	0	-0.012	-0.156	28.195	0.008	0.008	0.000	0.000	0.000	0.000
133	A	73	GLU	-1	-0.842	-0.790	27.310	-0.178	-0.178	0.000	0.000	0.000	0.000
134	A	74	VAL	0	0.062	-0.085	26.182	0.002	0.002	0.000	0.000	0.000	0.000
135	A	74	VAL	0	-0.051	0.100	25.923	0.000	0.000	0.000	0.000	0.000	0.000
136	A	75	TYR	0	0.048	-0.073	21.719	0.019	0.019	0.000	0.000	0.000	0.000
137	A	75	TYR	0	-0.036	0.082	18.349	-0.019	-0.019	0.000	0.000	0.000	0.000
138	A	76	ALA	0	0.090	-0.129	20.524	-0.003	-0.003	0.000	0.000	0.000	0.000
139	A	76	ALA	0	-0.055	0.128	21.161	0.007	0.007	0.000	0.000	0.000	0.000
140	A	77	LEU	0	0.109	-0.084	15.909	0.032	0.032	0.000	0.000	0.000	0.000
141	A	77	LEU	0	-0.149	0.097	12.614	-0.018	-0.018	0.000	0.000	0.000	0.000
142	A	78	GLU	0	0.109	-0.098	16.843	-0.031	-0.031	0.000	0.000	0.000	0.000
143	A	78	GLU	-1	-1.023	-0.868	17.846	-0.319	-0.319	0.000	0.000	0.000	0.000
144	A	79	ALA	0	0.082	-0.113	14.371	0.010	0.010	0.000	0.000	0.000	0.000
145	A	79	ALA	0	-0.078	0.098	13.991	0.011	0.011	0.000	0.000	0.000	0.000
146	A	80	LEU	0	0.064	-0.130	10.508	0.038	0.038	0.000	0.000	0.000	0.000
147	A	80	LEU	0	-0.097	0.134	8.255	-0.009	-0.009	0.000	0.000	0.000	0.000
148	A	81	LYS	0	0.013	-0.082	8.204	-0.052	-0.052	0.000	0.000	0.000	0.000
149	A	81	LYS	1	0.824	1.031	8.778	0.473	0.473	0.000	0.000	0.000	0.000
150	A	82	GLU	0	0.159	-0.104	4.392	-0.170	-0.110	-0.001	-0.023	-0.035	0.000
151	A	82	GLU	-1	-0.939	-0.781	2.380	-7.031	-4.490	2.822	-2.235	-3.128	-0.021
152	A	83	LEU	0	0.009	-0.157	4.586	0.156	0.253	-0.001	-0.007	-0.088	0.000
153	A	83	LEU	0	-0.113	0.093	6.038	0.076	0.076	0.000	0.000	0.000	0.000
154	A	84	PRO	0	0.014	-0.071	4.515	0.237	0.363	-0.001	-0.006	-0.120	0.000

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