FMO DATABASE

FMODB ID: 85V4Y

Calculation Name: 3CAN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CAN

Chain ID: A

ChEMBL ID:

UniProt ID: A6L094

Base Structure: X-ray

Registration Date: 2023-09-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

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	161
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1602569.948505
FMO2-HF: Nuclear repulsion	1538370.752441
FMO2-HF: Total energy	-64199.196064
FMO2-MP2: Total energy	-64383.94319

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:7:GLY)

Summations of interaction energy for fragment #1(A:7:GLY)

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.
0.44	1.368	-0.009	-0.468	-0.451	0.001

Interaction energy analysis for fragmet #1(A:7:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.001 / q_NPA : -0.013

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	9	GLY	0	0.025	0.002	3.844	-0.043	0.885	-0.009	-0.468	-0.451	0.001
4	A	10	VAL	0	-0.033	0.002	6.784	-0.076	-0.076	0.000	0.000	0.000	0.000
5	A	11	THR	0	-0.024	-0.033	10.575	0.176	0.176	0.000	0.000	0.000	0.000
6	A	12	PHE	0	0.013	0.015	13.016	-0.052	-0.052	0.000	0.000	0.000	0.000
7	A	13	CYS	0	-0.011	-0.029	16.847	0.044	0.044	0.000	0.000	0.000	0.000
8	A	14	GLY	0	0.039	0.031	19.309	-0.019	-0.019	0.000	0.000	0.000	0.000
9	A	15	GLY	0	0.040	0.010	23.135	0.003	0.003	0.000	0.000	0.000	0.000
10	A	16	GLU	-1	-0.804	-0.885	24.549	-0.038	-0.038	0.000	0.000	0.000	0.000
11	A	17	PRO	0	-0.025	-0.025	20.628	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	18	LEU	0	-0.025	-0.008	22.061	0.002	0.002	0.000	0.000	0.000	0.000
13	A	19	LEU	0	-0.005	0.014	25.150	0.004	0.004	0.000	0.000	0.000	0.000
14	A	20	HIS	1	0.752	0.854	25.101	0.032	0.032	0.000	0.000	0.000	0.000
15	A	21	PRO	0	0.050	0.034	24.731	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	22	GLU	-1	-0.887	-0.952	24.143	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	23	PHE	0	-0.005	-0.002	22.032	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	24	LEU	0	0.015	0.015	18.534	-0.011	-0.011	0.000	0.000	0.000	0.000
19	A	25	ILE	0	0.018	0.002	19.502	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	26	ASP	-1	-0.818	-0.867	20.228	-0.067	-0.067	0.000	0.000	0.000	0.000
21	A	27	ILE	0	0.006	-0.002	16.442	-0.012	-0.012	0.000	0.000	0.000	0.000
22	A	28	LEU	0	0.012	0.015	14.839	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	29	LYS	1	0.865	0.946	15.633	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	30	ARG	1	0.788	0.859	16.822	0.085	0.085	0.000	0.000	0.000	0.000
25	A	31	CYS	0	-0.039	-0.026	11.939	-0.039	-0.039	0.000	0.000	0.000	0.000
26	A	32	GLY	0	0.050	0.026	11.980	-0.014	-0.014	0.000	0.000	0.000	0.000
27	A	33	GLN	0	-0.070	-0.041	13.499	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	34	GLN	0	-0.070	-0.026	11.723	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	35	GLY	0	-0.006	0.007	9.942	-0.061	-0.061	0.000	0.000	0.000	0.000
30	A	36	ILE	0	-0.075	-0.026	7.298	0.004	0.004	0.000	0.000	0.000	0.000
31	A	37	HIS	0	0.027	0.016	6.268	0.091	0.091	0.000	0.000	0.000	0.000
32	A	38	ARG	1	0.779	0.856	7.982	-0.311	-0.311	0.000	0.000	0.000	0.000
33	A	39	ALA	0	0.027	0.022	11.209	0.090	0.090	0.000	0.000	0.000	0.000
34	A	40	VAL	0	-0.009	-0.028	12.924	-0.086	-0.086	0.000	0.000	0.000	0.000
35	A	41	ASP	-1	-0.758	-0.832	16.668	0.097	0.097	0.000	0.000	0.000	0.000
36	A	42	THR	0	0.028	0.001	19.545	-0.015	-0.015	0.000	0.000	0.000	0.000
37	A	43	THR	0	-0.012	-0.030	22.604	0.001	0.001	0.000	0.000	0.000	0.000
38	A	44	LEU	0	0.013	0.004	25.116	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	45	LEU	0	-0.013	0.006	23.556	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	46	ALA	0	0.032	0.026	27.433	0.005	0.005	0.000	0.000	0.000	0.000
41	A	47	ARG	1	0.831	0.898	29.650	-0.027	-0.027	0.000	0.000	0.000	0.000
42	A	48	LYS	1	0.969	0.975	28.891	-0.043	-0.043	0.000	0.000	0.000	0.000
43	A	49	GLU	-1	-0.778	-0.870	28.083	0.040	0.040	0.000	0.000	0.000	0.000
44	A	50	THR	0	-0.013	-0.008	25.519	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	51	VAL	0	0.065	0.030	23.766	0.000	0.000	0.000	0.000	0.000	0.000
46	A	52	ASP	-1	-0.805	-0.880	23.255	0.090	0.090	0.000	0.000	0.000	0.000
47	A	53	GLU	-1	-0.789	-0.882	23.346	0.050	0.050	0.000	0.000	0.000	0.000
48	A	54	VAL	0	0.030	0.005	18.923	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	55	MET	0	-0.023	0.017	18.970	0.014	0.014	0.000	0.000	0.000	0.000
50	A	56	ARG	1	0.823	0.916	19.459	-0.054	-0.054	0.000	0.000	0.000	0.000
51	A	57	ASN	0	-0.118	-0.071	17.757	-0.014	-0.014	0.000	0.000	0.000	0.000
52	A	58	CYS	0	-0.065	-0.038	14.294	-0.021	-0.021	0.000	0.000	0.000	0.000
53	A	59	GLU	-1	-0.731	-0.835	10.141	0.244	0.244	0.000	0.000	0.000	0.000
54	A	60	LEU	0	-0.049	-0.009	11.959	0.064	0.064	0.000	0.000	0.000	0.000
55	A	61	LEU	0	0.002	0.005	14.280	-0.062	-0.062	0.000	0.000	0.000	0.000
56	A	62	LEU	0	-0.018	-0.011	14.318	0.034	0.034	0.000	0.000	0.000	0.000
57	A	63	ILE	0	-0.021	-0.010	18.488	-0.032	-0.032	0.000	0.000	0.000	0.000
58	A	64	ASP	-1	-0.806	-0.878	22.124	0.095	0.095	0.000	0.000	0.000	0.000
59	A	65	LEU	0	-0.011	-0.021	24.018	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	66	LYS	1	0.766	0.810	26.383	-0.044	-0.044	0.000	0.000	0.000	0.000
61	A	67	SER	0	0.030	0.020	28.470	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	68	MET	0	0.040	0.043	31.814	0.002	0.002	0.000	0.000	0.000	0.000
63	A	69	ASP	-1	-0.845	-0.906	33.771	0.037	0.037	0.000	0.000	0.000	0.000
64	A	70	SER	0	0.007	-0.033	35.913	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	71	THR	0	-0.011	-0.015	36.964	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	72	VAL	0	-0.022	0.009	34.220	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	73	HIS	0	0.008	-0.014	30.339	0.005	0.005	0.000	0.000	0.000	0.000
68	A	74	GLN	0	-0.058	-0.025	34.162	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	75	THR	0	-0.069	-0.047	36.741	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	76	PHE	0	-0.042	-0.035	32.153	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	77	CYM	-1	-0.778	-0.812	30.507	0.040	0.040	0.000	0.000	0.000	0.000
72	A	78	ASP	-1	-0.927	-0.953	31.856	0.008	0.008	0.000	0.000	0.000	0.000
73	A	79	VAL	0	-0.059	-0.023	31.259	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	80	PRO	0	0.034	0.033	34.373	0.003	0.003	0.000	0.000	0.000	0.000
75	A	81	ASN	0	-0.024	-0.032	32.260	0.001	0.001	0.000	0.000	0.000	0.000
76	A	82	GLU	-1	-0.786	-0.880	32.586	0.049	0.049	0.000	0.000	0.000	0.000
77	A	83	LEU	0	-0.114	-0.040	30.210	0.002	0.002	0.000	0.000	0.000	0.000
78	A	84	ILE	0	0.059	0.034	27.389	0.005	0.005	0.000	0.000	0.000	0.000
79	A	85	LEU	0	0.021	0.011	28.522	0.010	0.010	0.000	0.000	0.000	0.000
80	A	86	LYS	1	0.869	0.928	30.324	-0.050	-0.050	0.000	0.000	0.000	0.000
81	A	87	ASN	0	-0.046	-0.034	26.289	0.002	0.002	0.000	0.000	0.000	0.000
82	A	88	ILE	0	0.028	0.012	24.965	0.009	0.009	0.000	0.000	0.000	0.000
83	A	89	ARG	1	0.827	0.919	26.298	-0.085	-0.085	0.000	0.000	0.000	0.000
84	A	90	ARG	1	0.818	0.872	27.388	-0.079	-0.079	0.000	0.000	0.000	0.000
85	A	91	VAL	0	-0.012	-0.016	21.553	0.002	0.002	0.000	0.000	0.000	0.000
86	A	92	ALA	0	0.023	0.018	23.884	0.013	0.013	0.000	0.000	0.000	0.000
87	A	93	GLU	-1	-0.898	-0.957	25.413	0.097	0.097	0.000	0.000	0.000	0.000
88	A	94	ALA	0	-0.090	-0.038	24.503	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	95	ASP	-1	-0.883	-0.926	23.630	0.216	0.216	0.000	0.000	0.000	0.000
90	A	96	PHE	0	0.007	0.003	16.391	0.022	0.022	0.000	0.000	0.000	0.000
91	A	97	PRO	0	0.009	-0.001	15.685	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	98	TYR	0	-0.012	-0.037	17.350	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	99	TYR	0	0.004	0.005	11.109	0.033	0.033	0.000	0.000	0.000	0.000
94	A	100	ILE	0	-0.005	-0.005	18.027	-0.033	-0.033	0.000	0.000	0.000	0.000
95	A	101	ARG	1	0.798	0.869	17.689	-0.103	-0.103	0.000	0.000	0.000	0.000
96	A	102	ILE	0	0.035	0.008	21.221	-0.014	-0.014	0.000	0.000	0.000	0.000
97	A	103	PRO	0	0.013	0.002	23.485	0.001	0.001	0.000	0.000	0.000	0.000
98	A	104	LEU	0	-0.006	0.031	25.086	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	105	ILE	0	0.026	-0.005	27.337	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	106	GLU	-1	-0.785	-0.887	30.489	0.038	0.038	0.000	0.000	0.000	0.000
101	A	107	GLY	0	-0.041	-0.046	33.520	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	108	VAL	0	-0.062	-0.016	33.063	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	109	ASN	0	-0.023	-0.031	28.852	0.000	0.000	0.000	0.000	0.000	0.000
104	A	110	ALA	0	0.013	0.022	31.393	0.007	0.007	0.000	0.000	0.000	0.000
105	A	111	ASP	-1	-0.834	-0.912	32.321	0.054	0.054	0.000	0.000	0.000	0.000
106	A	112	GLU	-1	-0.789	-0.906	34.531	0.066	0.066	0.000	0.000	0.000	0.000
107	A	113	LYS	1	0.900	0.952	35.549	-0.042	-0.042	0.000	0.000	0.000	0.000
108	A	114	ASN	0	0.011	-0.001	30.902	0.004	0.004	0.000	0.000	0.000	0.000
109	A	115	ILE	0	0.016	0.014	29.034	0.007	0.007	0.000	0.000	0.000	0.000
110	A	116	LYS	1	0.889	0.939	31.332	-0.058	-0.058	0.000	0.000	0.000	0.000
111	A	117	LEU	0	-0.007	0.005	33.512	0.004	0.004	0.000	0.000	0.000	0.000
112	A	118	SER	0	-0.026	-0.038	28.780	0.003	0.003	0.000	0.000	0.000	0.000
113	A	119	ALA	0	0.006	0.005	29.256	0.010	0.010	0.000	0.000	0.000	0.000
114	A	120	GLU	-1	-0.860	-0.914	30.322	0.080	0.080	0.000	0.000	0.000	0.000
115	A	121	PHE	0	-0.050	-0.027	28.428	0.002	0.002	0.000	0.000	0.000	0.000
116	A	122	LEU	0	0.014	0.007	25.125	0.004	0.004	0.000	0.000	0.000	0.000
117	A	123	ALA	0	0.049	0.032	27.939	0.010	0.010	0.000	0.000	0.000	0.000
118	A	124	SER	0	-0.123	-0.065	29.925	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	125	LEU	0	-0.027	-0.006	26.899	-0.008	-0.008	0.000	0.000	0.000	0.000
120	A	126	PRO	0	-0.038	-0.018	28.373	0.004	0.004	0.000	0.000	0.000	0.000
121	A	127	ARG	1	0.820	0.907	18.834	-0.278	-0.278	0.000	0.000	0.000	0.000
122	A	128	HIS	0	0.001	0.012	24.049	0.004	0.004	0.000	0.000	0.000	0.000
123	A	129	PRO	0	-0.007	0.010	20.538	0.018	0.018	0.000	0.000	0.000	0.000
124	A	130	GLU	-1	-0.851	-0.935	16.026	0.378	0.378	0.000	0.000	0.000	0.000
125	A	131	ILE	0	-0.075	-0.036	15.257	0.023	0.023	0.000	0.000	0.000	0.000
126	A	132	ILE	0	0.050	0.026	18.216	-0.015	-0.015	0.000	0.000	0.000	0.000
127	A	133	ASN	0	-0.039	-0.031	15.249	0.007	0.007	0.000	0.000	0.000	0.000
128	A	134	LEU	0	0.056	0.032	19.291	-0.026	-0.026	0.000	0.000	0.000	0.000
129	A	135	LEU	0	-0.040	-0.031	18.153	0.004	0.004	0.000	0.000	0.000	0.000
130	A	136	PRO	0	0.029	0.013	22.126	-0.012	-0.012	0.000	0.000	0.000	0.000
131	A	137	TYR	0	0.021	0.023	24.653	-0.006	-0.006	0.000	0.000	0.000	0.000
132	A	138	HIS	0	-0.043	-0.032	24.667	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	139	ASP	-1	-0.959	-0.957	27.097	-0.014	-0.014	0.000	0.000	0.000	0.000
134	A	158	LYS	1	0.812	0.900	37.263	-0.028	-0.028	0.000	0.000	0.000	0.000
135	A	159	MET	0	-0.011	-0.012	31.367	0.001	0.001	0.000	0.000	0.000	0.000
136	A	160	GLN	0	0.010	0.010	33.441	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	161	THR	0	0.024	0.000	28.230	0.002	0.002	0.000	0.000	0.000	0.000
138	A	162	PRO	0	-0.031	0.001	28.313	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	163	SER	0	0.049	0.020	29.868	0.002	0.002	0.000	0.000	0.000	0.000
140	A	164	GLU	-1	-0.834	-0.923	27.589	0.069	0.069	0.000	0.000	0.000	0.000
141	A	165	GLU	-1	-0.934	-0.960	29.776	0.053	0.053	0.000	0.000	0.000	0.000
142	A	166	VAL	0	0.061	0.031	31.167	0.005	0.005	0.000	0.000	0.000	0.000
143	A	167	GLN	0	-0.051	-0.035	25.499	0.013	0.013	0.000	0.000	0.000	0.000
144	A	168	GLN	0	-0.004	-0.018	25.467	0.018	0.018	0.000	0.000	0.000	0.000
145	A	169	GLN	0	-0.043	-0.021	28.449	0.006	0.006	0.000	0.000	0.000	0.000
146	A	170	CYS	0	-0.050	-0.020	27.858	0.002	0.002	0.000	0.000	0.000	0.000
147	A	171	ILE	0	0.006	0.007	22.835	0.008	0.008	0.000	0.000	0.000	0.000
148	A	172	GLN	0	-0.082	-0.033	26.421	0.010	0.010	0.000	0.000	0.000	0.000
149	A	173	ILE	0	0.038	0.014	29.460	0.003	0.003	0.000	0.000	0.000	0.000
150	A	174	LEU	0	-0.039	-0.027	24.797	0.002	0.002	0.000	0.000	0.000	0.000
151	A	175	THR	0	-0.012	-0.014	26.416	0.011	0.011	0.000	0.000	0.000	0.000
152	A	176	ASP	-1	-0.895	-0.934	27.810	0.097	0.097	0.000	0.000	0.000	0.000
153	A	177	TYR	0	-0.140	-0.097	30.541	-0.006	-0.006	0.000	0.000	0.000	0.000
154	A	178	GLY	0	-0.028	-0.011	28.389	0.002	0.002	0.000	0.000	0.000	0.000
155	A	179	LEU	0	-0.066	-0.022	24.843	0.017	0.017	0.000	0.000	0.000	0.000
156	A	180	LYS	1	0.896	0.954	18.223	-0.352	-0.352	0.000	0.000	0.000	0.000
157	A	181	ALA	0	0.017	0.001	21.093	0.003	0.003	0.000	0.000	0.000	0.000
158	A	182	THR	0	-0.018	-0.019	16.478	0.011	0.011	0.000	0.000	0.000	0.000
159	A	183	ILE	0	0.019	0.026	19.897	-0.013	-0.013	0.000	0.000	0.000	0.000
160	A	184	GLY	0	0.005	0.010	17.530	0.016	0.016	0.000	0.000	0.000	0.000
161	A	185	GLY	0	0.001	-0.001	13.179	0.053	0.053	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLY)