FMO DATABASE

FMODB ID: YZN42

Calculation Name: 4G9M-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4G9M

Chain ID: A

ChEMBL ID:

UniProt ID: L8WGI4

Base Structure: X-ray

Registration Date: 2023-06-22

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

DOI:

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	142
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1285463.321065
FMO2-HF: Nuclear repulsion	1232647.458647
FMO2-HF: Total energy	-52815.862418
FMO2-MP2: Total energy	-52974.234423

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:1:ALA)

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

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.
-0.657	1.38	0.007	-0.976	-1.068	0.004

Interaction energy analysis for fragmet #1(A:1:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.032 / q_NPA : 0.015

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	ILE	0	0.020	0.008	3.650	-0.948	1.089	0.007	-0.976	-1.068	0.004
4	A	4	SER	0	-0.030	-0.014	5.691	0.463	0.463	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.005	0.002	8.739	0.068	0.068	0.000	0.000	0.000	0.000
6	A	6	PRO	0	0.019	0.025	10.535	0.044	0.044	0.000	0.000	0.000	0.000
7	A	7	ALA	0	0.013	0.010	13.367	0.033	0.033	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.043	0.020	16.352	0.007	0.007	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.036	-0.023	17.985	0.000	0.000	0.000	0.000	0.000	0.000
10	A	10	TYR	0	0.024	-0.012	13.844	-0.025	-0.025	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.011	-0.003	18.674	0.028	0.028	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.038	-0.016	18.722	-0.028	-0.028	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.915	0.962	19.489	0.141	0.141	0.000	0.000	0.000	0.000
14	A	14	ASN	0	0.040	0.036	20.434	-0.019	-0.019	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.051	-0.033	18.876	0.015	0.015	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.029	-0.013	21.620	0.018	0.018	0.000	0.000	0.000	0.000
17	A	17	THR	0	0.025	0.033	25.191	0.011	0.011	0.000	0.000	0.000	0.000
18	A	18	GLY	0	-0.039	-0.010	23.011	0.013	0.013	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.087	-0.047	24.077	0.006	0.006	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.041	-0.044	22.764	-0.017	-0.017	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.024	0.019	24.294	0.010	0.010	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.804	-0.891	26.138	-0.086	-0.086	0.000	0.000	0.000	0.000
23	A	23	LEU	0	0.034	0.036	29.158	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	24	TRP	0	0.035	0.004	31.800	0.006	0.006	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.902	0.959	34.848	0.058	0.058	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.045	0.009	33.202	0.003	0.003	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.935	-0.974	34.021	-0.061	-0.061	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.017	-0.008	36.112	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	29	ALA	0	-0.005	0.017	37.102	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.738	-0.823	38.468	-0.097	-0.097	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.010	0.005	38.044	0.004	0.004	0.000	0.000	0.000	0.000
32	A	32	THR	0	-0.074	-0.042	35.858	0.003	0.003	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.032	0.011	35.522	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.004	-0.001	29.243	0.000	0.000	0.000	0.000	0.000	0.000
35	A	35	GLN	0	-0.062	-0.040	31.098	0.003	0.003	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.037	0.020	28.795	-0.008	-0.008	0.000	0.000	0.000	0.000
37	A	37	TYR	0	-0.018	-0.023	28.651	0.014	0.014	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.983	0.988	28.046	0.043	0.043	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.035	-0.018	24.123	0.000	0.000	0.000	0.000	0.000	0.000
40	A	40	HIS	0	-0.014	-0.011	26.457	0.012	0.012	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.029	0.029	25.346	0.007	0.007	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.029	0.020	26.403	0.001	0.001	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.803	-0.916	26.993	-0.089	-0.089	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.086	-0.052	27.773	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.056	-0.037	25.803	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.835	0.942	22.508	0.081	0.081	0.000	0.000	0.000	0.000
47	A	47	TRP	0	-0.029	-0.034	22.476	0.008	0.008	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.858	0.929	21.402	0.108	0.108	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.000	0.015	16.635	0.009	0.009	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.930	0.949	20.057	0.194	0.194	0.000	0.000	0.000	0.000
51	A	51	TRP	0	0.048	0.027	15.904	0.016	0.016	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.041	-0.030	22.274	0.018	0.018	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.023	0.020	24.903	0.016	0.016	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.815	0.917	26.200	0.188	0.188	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.011	-0.001	25.518	-0.008	-0.008	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.010	-0.012	20.591	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	57	GLN	0	0.020	0.016	21.804	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.013	0.000	20.101	0.002	0.002	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.041	-0.014	23.563	0.023	0.023	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.041	0.013	21.226	-0.015	-0.015	0.000	0.000	0.000	0.000
61	A	61	GLN	0	0.010	0.010	24.959	0.010	0.010	0.000	0.000	0.000	0.000
62	A	62	ASN	0	0.019	0.009	25.894	0.003	0.003	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.026	-0.025	24.303	0.005	0.005	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.826	0.936	27.542	0.075	0.075	0.000	0.000	0.000	0.000
65	A	65	SER	0	0.024	0.018	30.944	0.003	0.003	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.008	0.012	30.712	0.004	0.004	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.061	-0.022	31.694	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	68	TYR	0	-0.009	-0.031	28.012	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.007	0.005	26.554	0.008	0.008	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.075	0.035	29.684	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.044	-0.040	32.880	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.007	0.016	35.423	0.005	0.005	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.008	-0.003	38.405	0.005	0.005	0.000	0.000	0.000	0.000
74	A	74	ASN	0	0.010	0.022	38.413	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	75	ILE	0	0.002	0.010	32.377	0.002	0.002	0.000	0.000	0.000	0.000
76	A	76	GLN	0	-0.012	-0.006	36.216	0.004	0.004	0.000	0.000	0.000	0.000
77	A	77	ASN	0	0.056	0.006	35.354	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.047	-0.034	35.609	0.007	0.007	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.032	0.020	36.463	0.006	0.006	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.014	-0.002	35.133	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.006	0.011	29.616	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.044	-0.022	33.090	0.006	0.006	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.019	0.015	33.013	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.018	-0.034	33.679	0.006	0.006	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.012	-0.043	34.040	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	86	THR	0	-0.070	-0.030	34.900	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.041	-0.014	29.716	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	88	VAL	0	0.000	0.002	29.697	0.004	0.004	0.000	0.000	0.000	0.000
89	A	89	PRO	0	-0.028	0.001	27.945	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.018	-0.027	24.280	0.004	0.004	0.000	0.000	0.000	0.000
91	A	91	ASP	-1	-0.750	-0.874	22.393	-0.304	-0.304	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.036	-0.012	17.142	0.018	0.018	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.019	0.014	18.191	-0.056	-0.056	0.000	0.000	0.000	0.000
94	A	94	ALA	0	-0.027	-0.012	14.191	0.016	0.016	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.014	0.003	16.049	0.045	0.045	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.853	-0.911	15.678	-0.345	-0.345	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.841	0.904	16.057	0.200	0.200	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.019	-0.010	15.083	0.027	0.027	0.000	0.000	0.000	0.000
99	A	99	PHE	0	0.021	0.006	11.842	-0.057	-0.057	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.056	0.037	17.521	0.050	0.050	0.000	0.000	0.000	0.000
101	A	101	ILE	0	-0.023	-0.013	20.629	-0.028	-0.028	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.870	-0.949	22.856	-0.254	-0.254	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.024	0.002	25.489	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.026	-0.013	26.862	0.001	0.001	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.822	-0.916	28.077	-0.176	-0.176	0.000	0.000	0.000	0.000
106	A	106	HIS	0	-0.084	-0.047	30.953	0.014	0.014	0.000	0.000	0.000	0.000
107	A	107	ARG	1	0.899	0.943	26.063	0.247	0.247	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.011	0.012	28.458	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	109	PHE	0	-0.052	-0.028	30.328	0.002	0.002	0.000	0.000	0.000	0.000
110	A	110	VAL	0	0.032	0.021	25.344	-0.013	-0.013	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.015	-0.009	25.343	0.017	0.017	0.000	0.000	0.000	0.000
112	A	112	ASP	-1	-0.832	-0.915	26.491	-0.152	-0.152	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.026	-0.003	27.618	0.009	0.009	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.989	0.999	29.558	0.093	0.093	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.895	-0.961	33.138	-0.077	-0.077	0.000	0.000	0.000	0.000
116	A	116	SER	0	-0.018	-0.007	29.499	0.001	0.001	0.000	0.000	0.000	0.000
117	A	117	ASN	0	-0.016	-0.003	30.699	0.007	0.007	0.000	0.000	0.000	0.000
118	A	118	PRO	0	0.011	-0.013	29.851	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.042	-0.004	31.117	0.004	0.004	0.000	0.000	0.000	0.000
120	A	120	ASN	0	0.013	-0.009	32.570	-0.009	-0.009	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.891	-0.942	33.512	-0.058	-0.058	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.014	0.013	32.405	0.002	0.002	0.000	0.000	0.000	0.000
123	A	123	PRO	0	0.016	0.004	32.787	-0.007	-0.007	0.000	0.000	0.000	0.000
124	A	124	VAL	0	-0.006	0.001	28.414	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	125	ILE	0	-0.029	-0.016	31.434	0.007	0.007	0.000	0.000	0.000	0.000
126	A	126	TYR	0	0.018	-0.005	29.954	-0.015	-0.015	0.000	0.000	0.000	0.000
127	A	127	TYR	0	-0.008	-0.020	31.093	0.015	0.015	0.000	0.000	0.000	0.000
128	A	128	ASN	0	-0.003	0.009	30.752	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	129	ASN	0	0.018	0.005	24.507	0.007	0.007	0.000	0.000	0.000	0.000
130	A	130	ASN	0	-0.026	-0.017	28.614	0.005	0.005	0.000	0.000	0.000	0.000
131	A	131	ALA	0	0.016	0.016	23.440	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	132	THR	0	0.027	0.006	24.948	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	133	ASP	-1	-0.765	-0.886	22.902	-0.206	-0.206	0.000	0.000	0.000	0.000
134	A	134	ASN	0	-0.045	-0.013	23.865	-0.014	-0.014	0.000	0.000	0.000	0.000
135	A	135	GLN	0	-0.070	-0.027	25.334	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	136	LYS	1	0.768	0.889	19.927	0.230	0.230	0.000	0.000	0.000	0.000
137	A	137	TRP	0	-0.017	-0.022	19.755	0.034	0.034	0.000	0.000	0.000	0.000
138	A	138	LYS	1	0.941	0.955	15.265	0.168	0.168	0.000	0.000	0.000	0.000
139	A	139	PHE	0	0.034	0.010	14.387	0.039	0.039	0.000	0.000	0.000	0.000
140	A	140	ILE	0	-0.058	-0.033	13.739	-0.042	-0.042	0.000	0.000	0.000	0.000
141	A	141	ASP	-1	-0.879	-0.935	12.849	-0.301	-0.301	0.000	0.000	0.000	0.000
142	A	142	GLU	-1	-0.882	-0.916	14.849	-0.089	-0.089	0.000	0.000	0.000	0.000

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