FMO DATABASE

FMODB ID: JQ219

Calculation Name: 2C0D-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2C0D

Chain ID: A

ChEMBL ID:

UniProt ID: Q8I5Q6

Base Structure: X-ray

Registration Date: 2023-09-22

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	168
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1783168.831939
FMO2-HF: Nuclear repulsion	1716351.765677
FMO2-HF: Total energy	-66817.066262
FMO2-MP2: Total energy	-67011.933909

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:21:LEU)

Summations of interaction energy for fragment #1(A:21:LEU)

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.
-12.68	-7.674	13.872	-6.302	-12.575	-0.058

Interaction energy analysis for fragmet #1(A:21:LEU)

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 : -0.005

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	23	THR	0	-0.023	-0.001	3.887	1.015	2.114	-0.006	-0.494	-0.599	0.002
4	A	24	LYS	1	0.857	0.924	3.313	-1.692	-1.054	0.036	-0.128	-0.546	0.000
5	A	25	LYS	1	0.857	0.906	5.318	-0.140	-0.096	-0.001	-0.008	-0.035	0.000
6	A	26	ALA	0	0.030	0.016	4.579	-0.491	-0.332	-0.001	-0.012	-0.146	0.000
7	A	27	TYR	0	-0.042	-0.030	4.409	0.063	0.259	-0.001	-0.013	-0.181	0.000
8	A	28	ASN	0	0.052	0.016	6.008	0.014	0.014	0.000	0.000	0.000	0.000
9	A	29	PHE	0	0.006	0.000	8.491	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	30	THR	0	0.009	-0.014	11.366	0.017	0.017	0.000	0.000	0.000	0.000
11	A	31	ALA	0	-0.026	-0.007	14.424	0.006	0.006	0.000	0.000	0.000	0.000
12	A	32	GLN	0	0.019	0.006	16.379	0.011	0.011	0.000	0.000	0.000	0.000
13	A	33	GLY	0	0.045	0.015	17.808	-0.026	-0.026	0.000	0.000	0.000	0.000
14	A	34	LEU	0	-0.066	-0.011	19.524	0.018	0.018	0.000	0.000	0.000	0.000
15	A	35	ASN	0	0.036	0.002	21.640	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	36	LYS	1	0.900	0.939	23.187	0.132	0.132	0.000	0.000	0.000	0.000
17	A	37	ASN	0	-0.064	-0.031	25.577	0.009	0.009	0.000	0.000	0.000	0.000
18	A	38	ASN	0	-0.058	-0.039	26.510	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	39	GLU	-1	-0.800	-0.865	26.742	-0.112	-0.112	0.000	0.000	0.000	0.000
20	A	40	ILE	0	-0.024	-0.021	23.815	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	41	ILE	0	-0.031	-0.010	20.735	0.009	0.009	0.000	0.000	0.000	0.000
22	A	42	ASN	0	0.003	-0.010	18.990	-0.023	-0.023	0.000	0.000	0.000	0.000
23	A	43	VAL	0	-0.001	-0.001	14.904	0.008	0.008	0.000	0.000	0.000	0.000
24	A	44	ASP	-1	-0.766	-0.852	14.984	-0.307	-0.307	0.000	0.000	0.000	0.000
25	A	45	LEU	0	-0.017	0.009	8.282	0.012	0.012	0.000	0.000	0.000	0.000
26	A	46	SER	0	-0.046	-0.055	12.644	0.014	0.014	0.000	0.000	0.000	0.000
27	A	47	SER	0	-0.041	-0.027	13.992	0.033	0.033	0.000	0.000	0.000	0.000
28	A	48	PHE	0	0.064	0.023	14.458	0.027	0.027	0.000	0.000	0.000	0.000
29	A	49	ILE	0	-0.022	-0.002	12.083	0.009	0.009	0.000	0.000	0.000	0.000
30	A	50	GLY	0	-0.044	-0.025	15.559	0.020	0.020	0.000	0.000	0.000	0.000
31	A	51	GLN	0	-0.105	-0.046	18.003	0.031	0.031	0.000	0.000	0.000	0.000
32	A	52	LYS	1	0.825	0.906	17.099	0.198	0.198	0.000	0.000	0.000	0.000
33	A	53	TYR	0	-0.029	-0.030	13.628	-0.014	-0.014	0.000	0.000	0.000	0.000
34	A	54	CYS	0	-0.049	-0.022	11.393	0.009	0.009	0.000	0.000	0.000	0.000
35	A	55	CYS	0	0.006	-0.004	11.461	-0.029	-0.029	0.000	0.000	0.000	0.000
36	A	56	LEU	0	-0.013	0.018	6.382	0.036	0.036	0.000	0.000	0.000	0.000
37	A	57	LEU	0	0.016	-0.005	9.958	-0.035	-0.035	0.000	0.000	0.000	0.000
38	A	58	PHE	0	0.051	0.027	6.587	0.025	0.025	0.000	0.000	0.000	0.000
39	A	59	TYR	0	-0.004	-0.002	11.126	0.038	0.038	0.000	0.000	0.000	0.000
40	A	60	PRO	0	0.010	0.028	14.382	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	61	LEU	0	0.041	0.004	16.873	0.018	0.018	0.000	0.000	0.000	0.000
42	A	62	ASN	0	-0.027	-0.011	19.505	0.025	0.025	0.000	0.000	0.000	0.000
43	A	63	TYR	0	0.051	0.014	21.372	0.001	0.001	0.000	0.000	0.000	0.000
44	A	64	THR	0	-0.006	-0.001	22.918	0.006	0.006	0.000	0.000	0.000	0.000
45	A	65	PHE	0	0.030	0.007	19.299	0.004	0.004	0.000	0.000	0.000	0.000
46	A	66	VAL	0	-0.015	0.037	20.245	-0.013	-0.013	0.000	0.000	0.000	0.000
47	A	67	CYS	0	-0.015	-0.014	19.993	0.015	0.015	0.000	0.000	0.000	0.000
48	A	68	PRO	0	0.054	0.020	21.226	-0.011	-0.011	0.000	0.000	0.000	0.000
49	A	69	THR	0	0.033	0.007	23.373	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	70	GLU	-1	-0.716	-0.816	17.088	-0.223	-0.223	0.000	0.000	0.000	0.000
51	A	71	ILE	0	-0.006	0.009	17.533	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	72	ILE	0	0.019	0.014	20.673	0.003	0.003	0.000	0.000	0.000	0.000
53	A	73	GLU	-1	-0.828	-0.910	22.239	-0.086	-0.086	0.000	0.000	0.000	0.000
54	A	74	PHE	0	0.012	-0.004	15.421	0.003	0.003	0.000	0.000	0.000	0.000
55	A	75	ASN	0	0.022	0.011	20.701	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	76	LYS	1	0.797	0.890	23.396	0.089	0.089	0.000	0.000	0.000	0.000
57	A	77	HIS	1	0.833	0.916	22.302	0.111	0.111	0.000	0.000	0.000	0.000
58	A	78	ILE	0	0.015	0.023	21.514	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	79	LYS	1	1.014	0.994	23.155	0.072	0.072	0.000	0.000	0.000	0.000
60	A	80	ASP	-1	-0.889	-0.941	22.569	-0.084	-0.084	0.000	0.000	0.000	0.000
61	A	81	PHE	0	-0.001	-0.020	16.134	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	82	GLU	-1	-0.886	-0.939	20.449	-0.124	-0.124	0.000	0.000	0.000	0.000
63	A	83	ASN	0	-0.028	-0.012	23.000	0.006	0.006	0.000	0.000	0.000	0.000
64	A	84	LYS	1	0.764	0.874	19.380	0.091	0.091	0.000	0.000	0.000	0.000
65	A	85	ASN	0	-0.013	-0.014	19.554	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	86	VAL	0	-0.004	-0.005	14.955	-0.018	-0.018	0.000	0.000	0.000	0.000
67	A	87	GLU	-1	-0.879	-0.926	15.451	-0.188	-0.188	0.000	0.000	0.000	0.000
68	A	88	LEU	0	-0.051	-0.019	14.839	-0.040	-0.040	0.000	0.000	0.000	0.000
69	A	89	LEU	0	0.016	0.003	12.271	0.016	0.016	0.000	0.000	0.000	0.000
70	A	90	GLY	0	0.024	0.017	13.083	-0.041	-0.041	0.000	0.000	0.000	0.000
71	A	91	ILE	0	-0.036	-0.022	9.501	0.006	0.006	0.000	0.000	0.000	0.000
72	A	92	SER	0	0.014	-0.019	13.341	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	93	VAL	0	-0.007	0.010	13.687	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	94	ASP	-1	-0.854	-0.893	15.903	-0.208	-0.208	0.000	0.000	0.000	0.000
75	A	95	SER	0	0.017	-0.002	19.441	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	96	VAL	0	0.115	0.043	21.460	0.002	0.002	0.000	0.000	0.000	0.000
77	A	97	TYR	0	0.000	0.008	23.118	0.007	0.007	0.000	0.000	0.000	0.000
78	A	98	SER	0	0.016	0.012	22.719	0.008	0.008	0.000	0.000	0.000	0.000
79	A	99	HIS	0	-0.011	-0.013	18.043	0.015	0.015	0.000	0.000	0.000	0.000
80	A	100	LEU	0	0.022	0.011	23.269	0.006	0.006	0.000	0.000	0.000	0.000
81	A	101	ALA	0	-0.010	-0.007	26.654	0.008	0.008	0.000	0.000	0.000	0.000
82	A	102	TRP	0	0.010	-0.019	20.105	0.003	0.003	0.000	0.000	0.000	0.000
83	A	103	LYS	1	0.854	0.932	23.864	0.150	0.150	0.000	0.000	0.000	0.000
84	A	104	ASN	0	-0.045	-0.017	27.200	0.009	0.009	0.000	0.000	0.000	0.000
85	A	105	MET	0	-0.053	0.004	28.847	0.006	0.006	0.000	0.000	0.000	0.000
86	A	106	PRO	0	0.001	-0.005	30.610	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	107	ILE	0	0.044	0.028	28.822	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	108	GLU	-1	-0.836	-0.913	30.844	-0.073	-0.073	0.000	0.000	0.000	0.000
89	A	109	LYS	1	0.808	0.887	32.677	0.071	0.071	0.000	0.000	0.000	0.000
90	A	110	GLY	0	0.018	0.019	28.730	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	111	GLY	0	-0.005	-0.006	27.024	-0.009	-0.009	0.000	0.000	0.000	0.000
92	A	112	ILE	0	-0.048	-0.028	22.416	0.001	0.001	0.000	0.000	0.000	0.000
93	A	113	GLY	0	0.046	0.033	26.152	0.002	0.002	0.000	0.000	0.000	0.000
94	A	114	ASN	0	0.019	0.000	26.840	-0.014	-0.014	0.000	0.000	0.000	0.000
95	A	115	VAL	0	-0.025	-0.009	22.250	0.003	0.003	0.000	0.000	0.000	0.000
96	A	116	GLU	-1	-0.872	-0.946	25.023	-0.109	-0.109	0.000	0.000	0.000	0.000
97	A	117	PHE	0	-0.030	-0.035	17.497	0.000	0.000	0.000	0.000	0.000	0.000
98	A	118	THR	0	-0.005	0.011	17.950	0.013	0.013	0.000	0.000	0.000	0.000
99	A	119	LEU	0	-0.044	-0.005	17.415	-0.024	-0.024	0.000	0.000	0.000	0.000
100	A	120	VAL	0	0.035	0.007	13.550	0.013	0.013	0.000	0.000	0.000	0.000
101	A	121	SER	0	-0.020	-0.023	15.719	-0.008	-0.008	0.000	0.000	0.000	0.000
102	A	122	ASP	-1	-0.744	-0.841	11.381	-0.485	-0.485	0.000	0.000	0.000	0.000
103	A	123	ILE	0	-0.003	-0.014	14.468	0.003	0.003	0.000	0.000	0.000	0.000
104	A	124	ASN	0	-0.008	-0.012	14.274	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	125	LYS	1	0.847	0.937	12.534	0.272	0.272	0.000	0.000	0.000	0.000
106	A	126	ASP	-1	-0.782	-0.855	10.682	-0.575	-0.575	0.000	0.000	0.000	0.000
107	A	127	ILE	0	0.010	0.011	7.844	-0.121	-0.121	0.000	0.000	0.000	0.000
108	A	128	SER	0	0.001	-0.051	6.648	-0.165	-0.165	0.000	0.000	0.000	0.000
109	A	129	LYS	1	0.809	0.897	6.730	0.426	0.426	0.000	0.000	0.000	0.000
110	A	130	ASN	0	-0.033	-0.007	5.135	-0.208	-0.129	-0.001	-0.011	-0.067	0.000
111	A	131	TYR	0	-0.035	-0.044	2.222	-3.635	-1.831	3.222	-2.136	-2.890	-0.016
112	A	132	ASN	0	-0.092	-0.042	2.203	-0.279	0.464	0.960	0.214	-1.918	-0.009
113	A	133	VAL	0	-0.006	-0.004	4.673	0.103	0.171	-0.001	-0.005	-0.062	0.000
114	A	134	LEU	0	-0.048	-0.006	7.477	0.126	0.126	0.000	0.000	0.000	0.000
115	A	135	TYR	0	-0.033	-0.028	10.178	0.002	0.002	0.000	0.000	0.000	0.000
116	A	136	ASP	-1	-0.826	-0.908	13.456	-0.170	-0.170	0.000	0.000	0.000	0.000
117	A	137	ASN	0	-0.079	-0.048	13.748	-0.016	-0.016	0.000	0.000	0.000	0.000
118	A	138	SER	0	-0.031	0.003	15.105	0.010	0.010	0.000	0.000	0.000	0.000
119	A	139	PHE	0	0.015	-0.025	15.386	0.004	0.004	0.000	0.000	0.000	0.000
120	A	140	ALA	0	0.025	0.021	11.152	-0.024	-0.024	0.000	0.000	0.000	0.000
121	A	141	LEU	0	0.048	0.017	9.809	0.053	0.053	0.000	0.000	0.000	0.000
122	A	142	ARG	1	0.780	0.874	11.446	0.166	0.166	0.000	0.000	0.000	0.000
123	A	143	GLY	0	-0.006	-0.006	7.967	0.006	0.006	0.000	0.000	0.000	0.000
124	A	144	LEU	0	-0.052	-0.035	8.135	0.073	0.073	0.000	0.000	0.000	0.000
125	A	145	PHE	0	0.019	0.005	2.333	-1.041	-0.210	1.435	-0.478	-1.787	-0.001
126	A	146	ILE	0	0.003	0.012	7.364	0.116	0.116	0.000	0.000	0.000	0.000
127	A	147	ILE	0	-0.002	0.001	6.517	-0.119	-0.119	0.000	0.000	0.000	0.000
128	A	148	ASP	-1	-0.734	-0.855	9.133	-0.142	-0.142	0.000	0.000	0.000	0.000
129	A	149	LYS	1	0.921	0.964	11.996	0.071	0.071	0.000	0.000	0.000	0.000
130	A	150	ASN	0	-0.014	-0.003	12.347	0.035	0.035	0.000	0.000	0.000	0.000
131	A	151	GLY	0	0.034	0.028	10.295	0.017	0.017	0.000	0.000	0.000	0.000
132	A	152	CYS	0	-0.068	-0.021	7.524	-0.099	-0.099	0.000	0.000	0.000	0.000
133	A	153	VAL	0	0.040	0.025	2.514	-0.932	0.041	0.471	-0.302	-1.142	0.001
134	A	154	ARG	1	0.765	0.839	5.608	0.255	0.255	0.000	0.000	0.000	0.000
135	A	155	HIS	0	0.023	0.006	7.084	0.253	0.253	0.000	0.000	0.000	0.000
136	A	156	GLN	0	0.049	0.021	1.936	-5.458	-7.086	7.759	-2.929	-3.202	-0.035
137	A	157	THR	0	-0.033	-0.008	5.955	0.364	0.364	0.000	0.000	0.000	0.000
138	A	158	VAL	0	0.002	-0.008	7.444	-0.174	-0.174	0.000	0.000	0.000	0.000
139	A	159	ASN	0	-0.073	-0.035	9.915	0.081	0.081	0.000	0.000	0.000	0.000
140	A	160	ASP	-1	-0.823	-0.925	13.654	-0.142	-0.142	0.000	0.000	0.000	0.000
141	A	161	LEU	0	0.009	0.022	15.056	-0.008	-0.008	0.000	0.000	0.000	0.000
142	A	162	PRO	0	0.001	-0.009	17.016	-0.004	-0.004	0.000	0.000	0.000	0.000
143	A	163	ILE	0	-0.033	0.001	18.571	0.008	0.008	0.000	0.000	0.000	0.000
144	A	164	GLY	0	0.018	0.024	17.769	-0.022	-0.022	0.000	0.000	0.000	0.000
145	A	165	ARG	1	0.749	0.829	11.975	0.341	0.341	0.000	0.000	0.000	0.000
146	A	166	ASN	0	0.033	0.014	17.485	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	167	VAL	0	0.028	0.018	18.470	0.000	0.000	0.000	0.000	0.000	0.000
148	A	168	GLN	0	-0.009	-0.017	19.229	-0.003	-0.003	0.000	0.000	0.000	0.000
149	A	169	GLU	-1	-0.779	-0.865	17.108	-0.032	-0.032	0.000	0.000	0.000	0.000
150	A	170	VAL	0	-0.006	0.023	13.834	0.003	0.003	0.000	0.000	0.000	0.000
151	A	171	LEU	0	-0.003	0.001	15.919	-0.003	-0.003	0.000	0.000	0.000	0.000
152	A	172	ARG	1	0.900	0.920	18.604	0.039	0.039	0.000	0.000	0.000	0.000
153	A	173	THR	0	-0.022	-0.011	12.361	0.024	0.024	0.000	0.000	0.000	0.000
154	A	174	ILE	0	-0.021	-0.014	14.429	0.006	0.006	0.000	0.000	0.000	0.000
155	A	175	ASP	-1	-0.788	-0.882	15.808	-0.062	-0.062	0.000	0.000	0.000	0.000
156	A	176	SER	0	-0.020	-0.013	16.308	0.020	0.020	0.000	0.000	0.000	0.000
157	A	177	ILE	0	-0.046	-0.021	11.402	0.015	0.015	0.000	0.000	0.000	0.000
158	A	178	ILE	0	-0.005	-0.004	15.390	0.009	0.009	0.000	0.000	0.000	0.000
159	A	179	HIS	0	-0.015	-0.003	18.512	-0.002	-0.002	0.000	0.000	0.000	0.000
160	A	180	VAL	0	-0.004	0.010	15.683	0.009	0.009	0.000	0.000	0.000	0.000
161	A	181	ASP	-1	-0.784	-0.860	15.771	-0.066	-0.066	0.000	0.000	0.000	0.000
162	A	182	THR	0	-0.097	-0.058	18.469	-0.001	-0.001	0.000	0.000	0.000	0.000
163	A	183	SER	0	-0.016	-0.004	21.720	0.007	0.007	0.000	0.000	0.000	0.000
164	A	184	GLY	0	-0.027	-0.008	19.699	0.007	0.007	0.000	0.000	0.000	0.000
165	A	185	GLU	-1	-0.883	-0.942	20.597	0.082	0.082	0.000	0.000	0.000	0.000
166	A	186	VAL	0	-0.019	-0.017	17.813	0.012	0.012	0.000	0.000	0.000	0.000
167	A	187	CYS	0	-0.075	-0.041	18.568	-0.002	-0.002	0.000	0.000	0.000	0.000
168	A	188	PRO	0	0.010	0.029	19.737	-0.010	-0.010	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:21:LEU)