FMO DATABASE

FMODB ID: 4JZ2N

Calculation Name: 4EVM-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4EVM

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

Base Structure: X-ray

Registration Date: 2023-09-23

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	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	137
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1285544.642343
FMO2-HF: Nuclear repulsion	1231387.513867
FMO2-HF: Total energy	-54157.128476
FMO2-MP2: Total energy	-54316.007844

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:51:GLU)

Summations of interaction energy for fragment #1(A:51:GLU)

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.
10.413	17.079	3.657	-4.49	-5.834	0.002

Interaction energy analysis for fragmet #1(A:51:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.980 / q_NPA : -0.992

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	53	ALA	0	0.021	0.008	2.795	4.115	7.675	0.361	-1.880	-2.041	-0.003
4	A	54	ASP	-1	-0.791	-0.890	5.154	27.261	27.381	-0.001	-0.004	-0.115	0.000
5	A	55	PHE	0	-0.052	-0.029	7.335	-2.049	-2.049	0.000	0.000	0.000	0.000
6	A	56	GLU	-1	-0.885	-0.953	10.794	18.562	18.562	0.000	0.000	0.000	0.000
7	A	57	LEU	0	-0.039	-0.013	14.214	-0.789	-0.789	0.000	0.000	0.000	0.000
8	A	58	MET	0	-0.011	0.013	17.058	-0.299	-0.299	0.000	0.000	0.000	0.000
9	A	59	GLY	0	0.040	0.017	20.548	0.057	0.057	0.000	0.000	0.000	0.000
10	A	60	VAL	0	-0.039	-0.029	22.064	-0.448	-0.448	0.000	0.000	0.000	0.000
11	A	61	ASP	-1	-0.843	-0.898	23.695	12.418	12.418	0.000	0.000	0.000	0.000
12	A	62	GLY	0	-0.025	-0.016	25.189	-0.279	-0.279	0.000	0.000	0.000	0.000
13	A	63	LYS	1	0.918	0.964	21.812	-12.223	-12.223	0.000	0.000	0.000	0.000
14	A	64	THR	0	-0.039	-0.027	17.681	0.074	0.074	0.000	0.000	0.000	0.000
15	A	65	TYR	0	-0.087	-0.062	15.690	0.057	0.057	0.000	0.000	0.000	0.000
16	A	66	ARG	1	0.993	0.986	12.478	-17.818	-17.818	0.000	0.000	0.000	0.000
17	A	67	LEU	0	-0.003	0.017	6.378	-0.627	-0.627	0.000	0.000	0.000	0.000
18	A	68	SER	0	-0.072	-0.062	8.218	-0.363	-0.363	0.000	0.000	0.000	0.000
19	A	69	ASP	-1	-0.885	-0.945	9.368	19.880	19.880	0.000	0.000	0.000	0.000
20	A	70	TYR	0	-0.071	-0.045	11.219	-1.551	-1.551	0.000	0.000	0.000	0.000
21	A	71	LYS	1	1.000	1.002	4.933	-45.613	-45.613	0.000	0.000	0.000	0.000
22	A	72	GLY	0	-0.019	-0.002	9.590	-1.967	-1.967	0.000	0.000	0.000	0.000
23	A	73	LYS	1	0.906	0.944	11.577	-18.570	-18.570	0.000	0.000	0.000	0.000
24	A	74	LYS	1	0.883	0.947	10.790	-15.405	-15.405	0.000	0.000	0.000	0.000
25	A	75	VAL	0	0.010	0.004	10.231	-1.185	-1.185	0.000	0.000	0.000	0.000
26	A	76	TYR	0	-0.021	-0.022	11.608	0.280	0.280	0.000	0.000	0.000	0.000
27	A	77	LEU	0	0.011	0.008	10.647	-0.494	-0.494	0.000	0.000	0.000	0.000
28	A	78	LYS	1	0.917	0.971	14.362	-12.417	-12.417	0.000	0.000	0.000	0.000
29	A	79	PHE	0	0.005	-0.003	12.723	-0.378	-0.378	0.000	0.000	0.000	0.000
30	A	80	TRP	0	-0.048	-0.067	18.145	-0.835	-0.835	0.000	0.000	0.000	0.000
31	A	81	ALA	0	0.055	0.032	21.880	0.228	0.228	0.000	0.000	0.000	0.000
32	A	82	SER	0	-0.069	-0.072	24.941	-0.368	-0.368	0.000	0.000	0.000	0.000
33	A	83	TRP	0	0.006	0.014	25.429	-0.286	-0.286	0.000	0.000	0.000	0.000
34	A	84	CYS	0	-0.083	-0.024	24.362	0.095	0.095	0.000	0.000	0.000	0.000
35	A	85	SER	0	0.049	0.012	28.179	0.178	0.178	0.000	0.000	0.000	0.000
36	A	86	ILE	0	0.028	0.019	26.085	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	88	LEU	0	0.033	0.003	26.113	0.098	0.098	0.000	0.000	0.000	0.000
38	A	89	ALA	0	-0.010	-0.006	29.162	-0.080	-0.080	0.000	0.000	0.000	0.000
39	A	90	SER	0	0.018	0.002	25.428	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	91	LEU	0	-0.055	-0.011	24.363	0.309	0.309	0.000	0.000	0.000	0.000
41	A	92	PRO	0	0.016	0.009	26.726	0.185	0.185	0.000	0.000	0.000	0.000
42	A	93	ASP	-1	-0.865	-0.923	26.186	10.119	10.119	0.000	0.000	0.000	0.000
43	A	94	THR	0	-0.078	-0.044	21.132	0.373	0.373	0.000	0.000	0.000	0.000
44	A	95	ASP	-1	-0.787	-0.911	23.309	11.040	11.040	0.000	0.000	0.000	0.000
45	A	96	GLU	-1	-0.898	-0.948	25.737	10.083	10.083	0.000	0.000	0.000	0.000
46	A	97	ILE	0	-0.028	-0.008	20.425	0.180	0.180	0.000	0.000	0.000	0.000
47	A	98	ALA	0	-0.004	-0.010	21.542	0.369	0.369	0.000	0.000	0.000	0.000
48	A	99	LYS	1	0.908	0.965	22.533	-9.463	-9.463	0.000	0.000	0.000	0.000
49	A	100	GLU	-1	-0.897	-0.956	25.009	10.549	10.549	0.000	0.000	0.000	0.000
50	A	101	ALA	0	-0.040	-0.001	20.068	0.055	0.055	0.000	0.000	0.000	0.000
51	A	102	GLY	0	0.019	0.015	21.583	0.201	0.201	0.000	0.000	0.000	0.000
52	A	103	ASP	-1	-0.971	-0.993	20.605	13.511	13.511	0.000	0.000	0.000	0.000
53	A	104	ASP	-1	-0.965	-0.972	18.956	14.036	14.036	0.000	0.000	0.000	0.000
54	A	105	TYR	0	-0.146	-0.094	15.633	1.160	1.160	0.000	0.000	0.000	0.000
55	A	106	VAL	0	-0.003	0.006	14.337	-0.727	-0.727	0.000	0.000	0.000	0.000
56	A	107	VAL	0	-0.002	0.008	15.368	0.622	0.622	0.000	0.000	0.000	0.000
57	A	108	LEU	0	-0.006	0.001	13.292	-0.184	-0.184	0.000	0.000	0.000	0.000
58	A	109	THR	0	-0.033	-0.028	16.930	-0.075	-0.075	0.000	0.000	0.000	0.000
59	A	110	VAL	0	0.019	0.009	15.213	0.127	0.127	0.000	0.000	0.000	0.000
60	A	111	VAL	0	0.003	0.016	18.630	-0.316	-0.316	0.000	0.000	0.000	0.000
61	A	112	SER	0	0.035	0.001	19.146	0.536	0.536	0.000	0.000	0.000	0.000
62	A	113	PRO	0	-0.011	-0.018	21.680	-0.371	-0.371	0.000	0.000	0.000	0.000
63	A	114	GLY	0	0.018	0.017	24.469	0.284	0.284	0.000	0.000	0.000	0.000
64	A	115	HIS	0	-0.025	0.001	22.120	-0.067	-0.067	0.000	0.000	0.000	0.000
65	A	116	LYS	1	0.879	0.935	20.303	-12.986	-12.986	0.000	0.000	0.000	0.000
66	A	117	GLY	0	0.038	0.007	24.665	-0.149	-0.149	0.000	0.000	0.000	0.000
67	A	118	GLU	-1	-0.806	-0.831	25.308	10.702	10.702	0.000	0.000	0.000	0.000
68	A	119	GLN	0	-0.011	-0.024	27.426	-0.281	-0.281	0.000	0.000	0.000	0.000
69	A	120	SER	0	0.048	0.016	28.142	0.462	0.462	0.000	0.000	0.000	0.000
70	A	121	GLU	-1	-0.826	-0.933	25.450	12.034	12.034	0.000	0.000	0.000	0.000
71	A	122	ALA	0	-0.029	-0.020	27.836	-0.045	-0.045	0.000	0.000	0.000	0.000
72	A	123	ASP	-1	-0.882	-0.937	31.210	8.797	8.797	0.000	0.000	0.000	0.000
73	A	124	PHE	0	-0.022	-0.006	26.156	-0.125	-0.125	0.000	0.000	0.000	0.000
74	A	125	LYS	1	0.929	0.956	26.454	-11.411	-11.411	0.000	0.000	0.000	0.000
75	A	126	ASN	0	-0.048	-0.023	30.107	-0.103	-0.103	0.000	0.000	0.000	0.000
76	A	127	TRP	0	0.021	0.015	28.774	-0.023	-0.023	0.000	0.000	0.000	0.000
77	A	128	TYR	0	0.039	0.008	27.296	-0.070	-0.070	0.000	0.000	0.000	0.000
78	A	129	LYS	1	0.921	0.960	31.178	-9.260	-9.260	0.000	0.000	0.000	0.000
79	A	130	GLY	0	-0.024	0.006	33.903	-0.204	-0.204	0.000	0.000	0.000	0.000
80	A	131	LEU	0	-0.087	-0.044	29.443	-0.113	-0.113	0.000	0.000	0.000	0.000
81	A	132	ASP	-1	-0.852	-0.907	32.462	8.829	8.829	0.000	0.000	0.000	0.000
82	A	133	TYR	0	-0.001	-0.010	27.507	-0.036	-0.036	0.000	0.000	0.000	0.000
83	A	134	LYS	1	0.828	0.890	28.368	-8.651	-8.651	0.000	0.000	0.000	0.000
84	A	135	ASN	0	-0.066	-0.038	25.510	0.094	0.094	0.000	0.000	0.000	0.000
85	A	136	LEU	0	0.007	0.014	22.178	0.563	0.563	0.000	0.000	0.000	0.000
86	A	137	PRO	0	-0.008	0.022	19.642	-0.229	-0.229	0.000	0.000	0.000	0.000
87	A	138	VAL	0	-0.006	0.007	21.055	0.244	0.244	0.000	0.000	0.000	0.000
88	A	139	LEU	0	-0.024	-0.008	15.579	-0.348	-0.348	0.000	0.000	0.000	0.000
89	A	140	VAL	0	0.004	-0.007	19.642	-0.235	-0.235	0.000	0.000	0.000	0.000
90	A	141	ASP	-1	-0.748	-0.865	16.521	17.704	17.704	0.000	0.000	0.000	0.000
91	A	142	PRO	0	-0.022	-0.021	19.261	-0.083	-0.083	0.000	0.000	0.000	0.000
92	A	143	SER	0	-0.102	-0.066	17.622	-0.098	-0.098	0.000	0.000	0.000	0.000
93	A	144	GLY	0	0.025	0.008	19.008	-0.085	-0.085	0.000	0.000	0.000	0.000
94	A	145	LYS	1	0.977	0.983	14.117	-18.190	-18.190	0.000	0.000	0.000	0.000
95	A	146	LEU	0	0.048	0.032	11.905	0.897	0.897	0.000	0.000	0.000	0.000
96	A	147	LEU	0	-0.051	-0.020	12.769	0.317	0.317	0.000	0.000	0.000	0.000
97	A	148	GLU	-1	-0.969	-0.978	13.384	20.332	20.332	0.000	0.000	0.000	0.000
98	A	149	THR	0	0.014	0.002	8.998	0.164	0.164	0.000	0.000	0.000	0.000
99	A	150	TYR	0	-0.024	-0.017	7.521	1.266	1.266	0.000	0.000	0.000	0.000
100	A	151	GLY	0	0.005	0.014	10.342	-0.756	-0.756	0.000	0.000	0.000	0.000
101	A	152	VAL	0	-0.014	-0.002	12.833	-1.096	-1.096	0.000	0.000	0.000	0.000
102	A	153	ARG	1	0.902	0.939	15.591	-14.463	-14.463	0.000	0.000	0.000	0.000
103	A	154	SER	0	-0.079	-0.037	18.874	-0.728	-0.728	0.000	0.000	0.000	0.000
104	A	155	TYR	0	0.023	0.038	19.294	0.418	0.418	0.000	0.000	0.000	0.000
105	A	156	PRO	0	0.048	-0.002	20.781	-0.507	-0.507	0.000	0.000	0.000	0.000
106	A	157	THR	0	-0.026	-0.017	14.750	-0.119	-0.119	0.000	0.000	0.000	0.000
107	A	158	GLN	0	-0.018	0.022	16.064	0.580	0.580	0.000	0.000	0.000	0.000
108	A	159	ALA	0	0.036	0.011	10.748	0.311	0.311	0.000	0.000	0.000	0.000
109	A	160	PHE	0	-0.006	-0.001	10.809	-0.599	-0.599	0.000	0.000	0.000	0.000
110	A	161	ILE	0	0.018	0.007	5.606	1.232	1.232	0.000	0.000	0.000	0.000
111	A	162	ASP	-1	-0.749	-0.865	5.832	34.297	34.297	0.000	0.000	0.000	0.000
112	A	163	LYS	1	0.902	0.963	7.519	-17.932	-17.932	0.000	0.000	0.000	0.000
113	A	164	GLU	-1	-0.971	-0.987	6.074	31.346	31.346	0.000	0.000	0.000	0.000
114	A	165	GLY	0	-0.023	-0.002	4.434	5.478	5.810	0.000	-0.054	-0.278	0.000
115	A	166	LYS	1	0.920	0.945	2.161	-53.625	-50.403	3.252	-3.408	-3.066	0.005
116	A	167	LEU	0	-0.035	-0.010	3.102	-6.023	-6.591	0.045	0.856	-0.334	0.000
117	A	168	VAL	0	-0.019	0.001	5.209	0.761	0.761	0.000	0.000	0.000	0.000
118	A	169	LYS	1	0.951	0.967	7.863	-17.178	-17.178	0.000	0.000	0.000	0.000
119	A	170	THR	0	-0.003	0.001	10.129	0.233	0.233	0.000	0.000	0.000	0.000
120	A	171	HIS	0	-0.027	-0.015	12.536	-0.123	-0.123	0.000	0.000	0.000	0.000
121	A	172	PRO	0	-0.015	0.010	16.279	-0.039	-0.039	0.000	0.000	0.000	0.000
122	A	173	GLY	0	0.046	0.003	18.696	-0.474	-0.474	0.000	0.000	0.000	0.000
123	A	174	PHE	0	0.001	-0.018	21.110	0.445	0.445	0.000	0.000	0.000	0.000
124	A	175	MET	0	-0.031	-0.012	18.583	0.367	0.367	0.000	0.000	0.000	0.000
125	A	176	GLU	-1	-0.851	-0.917	22.561	10.419	10.419	0.000	0.000	0.000	0.000
126	A	177	LYS	1	0.946	0.966	23.518	-9.923	-9.923	0.000	0.000	0.000	0.000
127	A	178	ASP	-1	-0.856	-0.929	23.459	10.786	10.786	0.000	0.000	0.000	0.000
128	A	179	ALA	0	-0.040	-0.017	21.978	0.366	0.366	0.000	0.000	0.000	0.000
129	A	180	ILE	0	-0.022	-0.004	18.230	0.764	0.764	0.000	0.000	0.000	0.000
130	A	181	LEU	0	0.034	0.017	18.699	0.790	0.790	0.000	0.000	0.000	0.000
131	A	182	GLN	0	-0.065	-0.037	19.974	0.036	0.036	0.000	0.000	0.000	0.000
132	A	183	THR	0	-0.051	-0.042	14.939	0.442	0.442	0.000	0.000	0.000	0.000
133	A	184	LEU	0	0.003	-0.004	14.249	0.998	0.998	0.000	0.000	0.000	0.000
134	A	185	LYS	1	0.892	0.947	15.886	-11.282	-11.282	0.000	0.000	0.000	0.000
135	A	186	GLU	-1	-0.890	-0.926	16.674	14.009	14.009	0.000	0.000	0.000	0.000
136	A	187	LEU	0	-0.068	-0.016	10.547	0.996	0.996	0.000	0.000	0.000	0.000
137	A	188	ALA	0	0.019	0.003	12.142	-1.264	-1.264	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:51:GLU)