FMO DATABASE

FMODB ID: G62Z1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1599398.528819
FMO2-HF: Nuclear repulsion	1535199.467365
FMO2-HF: Total energy	-64199.061454
FMO2-MP2: Total energy	-64383.822986

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.
0.697	1.545	-0.004	-0.383	-0.461	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 : 0.005 / q_NPA : -0.008

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	0.022	0.000	3.798	0.139	0.987	-0.004	-0.383	-0.461	0.001
4	A	10	VAL	0	-0.030	-0.006	6.515	-0.022	-0.022	0.000	0.000	0.000	0.000
5	A	11	THR	0	-0.006	-0.020	10.294	0.177	0.177	0.000	0.000	0.000	0.000
6	A	12	PHE	0	-0.009	0.003	12.799	-0.053	-0.053	0.000	0.000	0.000	0.000
7	A	13	CYS	0	0.022	-0.008	15.909	0.048	0.048	0.000	0.000	0.000	0.000
8	A	14	GLY	0	0.020	0.010	18.692	-0.019	-0.019	0.000	0.000	0.000	0.000
9	A	15	GLY	0	0.047	0.010	22.432	0.004	0.004	0.000	0.000	0.000	0.000
10	A	16	GLU	-1	-0.807	-0.882	24.216	-0.036	-0.036	0.000	0.000	0.000	0.000
11	A	17	PRO	0	-0.009	-0.014	20.245	-0.003	-0.003	0.000	0.000	0.000	0.000
12	A	18	LEU	0	-0.021	-0.009	22.067	0.000	0.000	0.000	0.000	0.000	0.000
13	A	19	LEU	0	-0.020	0.009	24.743	0.005	0.005	0.000	0.000	0.000	0.000
14	A	20	HIS	1	0.751	0.857	24.766	0.035	0.035	0.000	0.000	0.000	0.000
15	A	21	PRO	0	0.045	0.024	24.561	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	22	GLU	-1	-0.888	-0.948	24.200	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	23	PHE	0	-0.019	-0.018	21.559	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	24	LEU	0	0.010	0.015	18.460	-0.010	-0.010	0.000	0.000	0.000	0.000
19	A	25	ILE	0	0.023	0.014	19.420	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	26	ASP	-1	-0.810	-0.863	20.006	-0.072	-0.072	0.000	0.000	0.000	0.000
21	A	27	ILE	0	-0.008	-0.009	16.152	-0.014	-0.014	0.000	0.000	0.000	0.000
22	A	28	LEU	0	0.009	0.011	14.730	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	29	LYS	1	0.870	0.942	15.389	-0.010	-0.010	0.000	0.000	0.000	0.000
24	A	30	ARG	1	0.786	0.866	16.642	0.088	0.088	0.000	0.000	0.000	0.000
25	A	31	CYS	0	-0.042	-0.028	11.721	-0.037	-0.037	0.000	0.000	0.000	0.000
26	A	32	GLY	0	0.042	0.019	11.770	-0.018	-0.018	0.000	0.000	0.000	0.000
27	A	33	GLN	0	-0.071	-0.033	13.084	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	34	GLN	0	-0.056	-0.025	11.667	-0.014	-0.014	0.000	0.000	0.000	0.000
29	A	35	GLY	0	-0.005	0.013	9.695	-0.060	-0.060	0.000	0.000	0.000	0.000
30	A	36	ILE	0	-0.072	-0.026	7.014	-0.032	-0.032	0.000	0.000	0.000	0.000
31	A	37	HIS	0	0.014	0.013	5.995	0.136	0.136	0.000	0.000	0.000	0.000
32	A	38	ARG	1	0.794	0.859	7.631	-0.302	-0.302	0.000	0.000	0.000	0.000
33	A	39	ALA	0	0.005	0.010	10.901	0.096	0.096	0.000	0.000	0.000	0.000
34	A	40	VAL	0	0.006	-0.014	12.846	-0.084	-0.084	0.000	0.000	0.000	0.000
35	A	41	ASP	-1	-0.749	-0.842	16.499	0.102	0.102	0.000	0.000	0.000	0.000
36	A	42	THR	0	0.029	0.004	19.261	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	43	THR	0	-0.003	-0.012	22.277	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	44	LEU	0	0.017	-0.004	24.669	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	45	LEU	0	-0.019	0.009	23.488	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	46	ALA	0	0.033	0.028	27.043	0.005	0.005	0.000	0.000	0.000	0.000
41	A	47	ARG	1	0.818	0.886	29.754	-0.021	-0.021	0.000	0.000	0.000	0.000
42	A	48	LYS	1	1.046	1.005	28.673	-0.045	-0.045	0.000	0.000	0.000	0.000
43	A	49	GLU	-1	-0.831	-0.894	28.146	0.033	0.033	0.000	0.000	0.000	0.000
44	A	50	THR	0	-0.010	-0.011	25.060	0.000	0.000	0.000	0.000	0.000	0.000
45	A	51	VAL	0	0.054	0.030	23.687	0.001	0.001	0.000	0.000	0.000	0.000
46	A	52	ASP	-1	-0.807	-0.871	23.159	0.087	0.087	0.000	0.000	0.000	0.000
47	A	53	GLU	-1	-0.780	-0.883	23.300	0.048	0.048	0.000	0.000	0.000	0.000
48	A	54	VAL	0	0.029	0.002	18.969	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	55	MET	0	-0.011	0.023	18.808	0.011	0.011	0.000	0.000	0.000	0.000
50	A	56	ARG	1	0.837	0.920	18.803	-0.051	-0.051	0.000	0.000	0.000	0.000
51	A	57	ASN	0	-0.129	-0.077	17.392	-0.011	-0.011	0.000	0.000	0.000	0.000
52	A	58	CYS	0	-0.062	-0.038	14.011	-0.022	-0.022	0.000	0.000	0.000	0.000
53	A	59	GLU	-1	-0.722	-0.829	9.911	0.229	0.229	0.000	0.000	0.000	0.000
54	A	60	LEU	0	-0.050	-0.005	11.844	0.053	0.053	0.000	0.000	0.000	0.000
55	A	61	LEU	0	-0.008	0.001	14.272	-0.055	-0.055	0.000	0.000	0.000	0.000
56	A	62	LEU	0	-0.037	-0.023	13.818	0.035	0.035	0.000	0.000	0.000	0.000
57	A	63	ILE	0	0.001	-0.006	17.942	-0.034	-0.034	0.000	0.000	0.000	0.000
58	A	64	ASP	-1	-0.829	-0.889	21.564	0.105	0.105	0.000	0.000	0.000	0.000
59	A	65	LEU	0	-0.018	-0.027	23.378	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	66	LYS	1	0.735	0.788	25.988	-0.043	-0.043	0.000	0.000	0.000	0.000
61	A	67	SER	0	0.042	0.021	28.175	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	68	MET	0	0.034	0.039	31.485	0.002	0.002	0.000	0.000	0.000	0.000
63	A	69	ASP	-1	-0.892	-0.943	33.560	0.036	0.036	0.000	0.000	0.000	0.000
64	A	70	SER	0	0.016	-0.025	35.593	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	71	THR	0	0.010	0.011	36.773	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	72	VAL	0	-0.036	-0.002	33.876	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	73	HIS	0	0.002	-0.018	30.025	0.005	0.005	0.000	0.000	0.000	0.000
68	A	74	GLN	0	-0.032	-0.002	33.612	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	75	THR	0	-0.082	-0.054	36.257	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	76	PHE	0	-0.044	-0.035	31.807	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	77	CYM	-1	-0.732	-0.776	30.365	0.038	0.038	0.000	0.000	0.000	0.000
72	A	78	ASP	-1	-0.936	-0.956	31.902	0.007	0.007	0.000	0.000	0.000	0.000
73	A	79	VAL	0	-0.078	-0.045	31.099	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	80	PRO	0	0.012	0.024	34.166	0.003	0.003	0.000	0.000	0.000	0.000
75	A	81	ASN	0	-0.023	-0.031	31.945	0.000	0.000	0.000	0.000	0.000	0.000
76	A	82	GLU	-1	-0.786	-0.890	32.434	0.048	0.048	0.000	0.000	0.000	0.000
77	A	83	LEU	0	-0.117	-0.056	30.147	0.004	0.004	0.000	0.000	0.000	0.000
78	A	84	ILE	0	0.051	0.036	27.084	0.005	0.005	0.000	0.000	0.000	0.000
79	A	85	LEU	0	0.027	0.013	28.308	0.010	0.010	0.000	0.000	0.000	0.000
80	A	86	LYS	1	0.888	0.941	30.133	-0.049	-0.049	0.000	0.000	0.000	0.000
81	A	87	ASN	0	-0.029	-0.030	26.046	0.003	0.003	0.000	0.000	0.000	0.000
82	A	88	ILE	0	0.025	0.020	24.799	0.009	0.009	0.000	0.000	0.000	0.000
83	A	89	ARG	1	0.885	0.949	26.210	-0.081	-0.081	0.000	0.000	0.000	0.000
84	A	90	ARG	1	0.785	0.859	27.006	-0.077	-0.077	0.000	0.000	0.000	0.000
85	A	91	VAL	0	0.003	-0.010	21.162	0.001	0.001	0.000	0.000	0.000	0.000
86	A	92	ALA	0	0.013	0.012	23.875	0.011	0.011	0.000	0.000	0.000	0.000
87	A	93	GLU	-1	-0.903	-0.964	25.427	0.095	0.095	0.000	0.000	0.000	0.000
88	A	94	ALA	0	-0.088	-0.034	24.166	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	95	ASP	-1	-0.883	-0.921	23.530	0.206	0.206	0.000	0.000	0.000	0.000
90	A	96	PHE	0	-0.003	-0.002	16.424	0.018	0.018	0.000	0.000	0.000	0.000
91	A	97	PRO	0	0.020	0.007	15.498	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	98	TYR	0	0.003	-0.032	17.377	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	99	TYR	0	0.002	0.005	11.542	0.056	0.056	0.000	0.000	0.000	0.000
94	A	100	ILE	0	-0.001	0.002	17.681	-0.033	-0.033	0.000	0.000	0.000	0.000
95	A	101	ARG	1	0.806	0.883	16.666	-0.117	-0.117	0.000	0.000	0.000	0.000
96	A	102	ILE	0	0.030	0.011	20.771	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	103	PRO	0	0.004	0.004	23.151	0.001	0.001	0.000	0.000	0.000	0.000
98	A	104	LEU	0	-0.014	0.019	24.535	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	105	ILE	0	0.029	-0.007	26.949	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	106	GLU	-1	-0.804	-0.881	30.050	0.040	0.040	0.000	0.000	0.000	0.000
101	A	107	GLY	0	-0.028	-0.041	33.107	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	108	VAL	0	-0.062	-0.020	32.351	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	109	ASN	0	-0.039	-0.043	28.288	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	110	ALA	0	0.039	0.028	30.817	0.007	0.007	0.000	0.000	0.000	0.000
105	A	111	ASP	-1	-0.848	-0.915	31.897	0.054	0.054	0.000	0.000	0.000	0.000
106	A	112	GLU	-1	-0.778	-0.905	34.095	0.064	0.064	0.000	0.000	0.000	0.000
107	A	113	LYS	1	0.964	0.990	35.090	-0.042	-0.042	0.000	0.000	0.000	0.000
108	A	114	ASN	0	0.013	0.002	30.769	0.003	0.003	0.000	0.000	0.000	0.000
109	A	115	ILE	0	0.017	0.017	28.578	0.006	0.006	0.000	0.000	0.000	0.000
110	A	116	LYS	1	0.901	0.941	31.123	-0.057	-0.057	0.000	0.000	0.000	0.000
111	A	117	LEU	0	-0.020	-0.004	33.457	0.003	0.003	0.000	0.000	0.000	0.000
112	A	118	SER	0	-0.018	-0.038	28.722	0.003	0.003	0.000	0.000	0.000	0.000
113	A	119	ALA	0	-0.012	-0.004	28.954	0.009	0.009	0.000	0.000	0.000	0.000
114	A	120	GLU	-1	-0.858	-0.901	30.026	0.079	0.079	0.000	0.000	0.000	0.000
115	A	121	PHE	0	-0.054	-0.024	28.275	0.001	0.001	0.000	0.000	0.000	0.000
116	A	122	LEU	0	0.018	0.004	24.917	0.004	0.004	0.000	0.000	0.000	0.000
117	A	123	ALA	0	0.026	0.018	27.930	0.008	0.008	0.000	0.000	0.000	0.000
118	A	124	SER	0	-0.114	-0.052	29.512	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	125	LEU	0	-0.063	-0.022	26.819	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	126	PRO	0	-0.029	-0.016	28.337	0.004	0.004	0.000	0.000	0.000	0.000
121	A	127	ARG	1	0.824	0.906	18.567	-0.274	-0.274	0.000	0.000	0.000	0.000
122	A	128	HIS	0	-0.012	0.000	23.587	0.005	0.005	0.000	0.000	0.000	0.000
123	A	129	PRO	0	-0.007	0.006	20.244	0.017	0.017	0.000	0.000	0.000	0.000
124	A	130	GLU	-1	-0.909	-0.962	15.483	0.391	0.391	0.000	0.000	0.000	0.000
125	A	131	ILE	0	-0.079	-0.041	14.926	0.011	0.011	0.000	0.000	0.000	0.000
126	A	132	ILE	0	0.034	0.016	18.089	-0.012	-0.012	0.000	0.000	0.000	0.000
127	A	133	ASN	0	-0.057	-0.042	15.100	0.013	0.013	0.000	0.000	0.000	0.000
128	A	134	LEU	0	0.047	0.026	19.113	-0.023	-0.023	0.000	0.000	0.000	0.000
129	A	135	LEU	0	-0.026	-0.013	17.758	0.004	0.004	0.000	0.000	0.000	0.000
130	A	136	PRO	0	0.038	0.021	21.672	-0.012	-0.012	0.000	0.000	0.000	0.000
131	A	137	TYR	0	0.018	0.019	24.088	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	138	HIS	0	-0.040	-0.022	24.208	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	139	ASP	-1	-0.941	-0.952	26.823	-0.016	-0.016	0.000	0.000	0.000	0.000
134	A	158	LYS	1	0.806	0.900	36.863	-0.029	-0.029	0.000	0.000	0.000	0.000
135	A	159	MET	0	0.005	-0.005	31.078	0.002	0.002	0.000	0.000	0.000	0.000
136	A	160	GLN	0	-0.008	0.000	32.959	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	161	THR	0	0.025	-0.008	27.700	0.002	0.002	0.000	0.000	0.000	0.000
138	A	162	PRO	0	-0.034	-0.002	27.905	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	163	SER	0	0.043	0.020	29.549	0.002	0.002	0.000	0.000	0.000	0.000
140	A	164	GLU	-1	-0.874	-0.947	27.757	0.064	0.064	0.000	0.000	0.000	0.000
141	A	165	GLU	-1	-0.932	-0.962	29.530	0.053	0.053	0.000	0.000	0.000	0.000
142	A	166	VAL	0	0.055	0.025	30.870	0.005	0.005	0.000	0.000	0.000	0.000
143	A	167	GLN	0	-0.040	-0.033	25.226	0.014	0.014	0.000	0.000	0.000	0.000
144	A	168	GLN	0	0.043	0.010	24.987	0.017	0.017	0.000	0.000	0.000	0.000
145	A	169	GLN	0	-0.033	-0.011	28.438	0.005	0.005	0.000	0.000	0.000	0.000
146	A	170	CYS	0	-0.063	-0.029	27.780	0.001	0.001	0.000	0.000	0.000	0.000
147	A	171	ILE	0	0.016	0.006	22.867	0.008	0.008	0.000	0.000	0.000	0.000
148	A	172	GLN	0	-0.080	-0.035	26.492	0.010	0.010	0.000	0.000	0.000	0.000
149	A	173	ILE	0	0.033	0.022	29.450	0.002	0.002	0.000	0.000	0.000	0.000
150	A	174	LEU	0	-0.019	-0.020	24.801	0.002	0.002	0.000	0.000	0.000	0.000
151	A	175	THR	0	-0.023	-0.023	26.193	0.011	0.011	0.000	0.000	0.000	0.000
152	A	176	ASP	-1	-0.887	-0.931	27.516	0.096	0.096	0.000	0.000	0.000	0.000
153	A	177	TYR	0	-0.168	-0.110	30.083	-0.005	-0.005	0.000	0.000	0.000	0.000
154	A	178	GLY	0	-0.035	-0.013	28.148	0.002	0.002	0.000	0.000	0.000	0.000
155	A	179	LEU	0	-0.065	-0.018	24.604	0.015	0.015	0.000	0.000	0.000	0.000
156	A	180	LYS	1	0.937	0.978	18.178	-0.340	-0.340	0.000	0.000	0.000	0.000
157	A	181	ALA	0	0.035	0.010	20.954	0.010	0.010	0.000	0.000	0.000	0.000
158	A	182	THR	0	0.002	-0.001	16.413	0.001	0.001	0.000	0.000	0.000	0.000
159	A	183	ILE	0	0.011	0.020	19.865	-0.009	-0.009	0.000	0.000	0.000	0.000
160	A	184	GLY	0	-0.008	-0.007	17.451	0.008	0.008	0.000	0.000	0.000	0.000
161	A	185	GLY	0	0.003	-0.003	12.796	0.062	0.062	0.000	0.000	0.000	0.000

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