FMO DATABASE

FMODB ID: 8N55Y

Calculation Name: 4M4Z-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4M4Z

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H6Q3

Base Structure: X-ray

Registration Date: 2023-09-26

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	157
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1488846.94927
FMO2-HF: Nuclear repulsion	1427553.277306
FMO2-HF: Total energy	-61293.671963
FMO2-MP2: Total energy	-61474.082201

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:36:THR)

Summations of interaction energy for fragment #1(A:36:THR)

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.
-11.327	-2.866	2.895	-4.614	-6.743	-0.017

Interaction energy analysis for fragmet #1(A:36:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.012 / q_NPA : 0.000

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	38	VAL	0	-0.008	0.009	3.865	0.303	2.535	-0.017	-1.201	-1.014	0.002
4	A	39	ALA	0	0.032	0.029	6.915	-0.158	-0.158	0.000	0.000	0.000	0.000
5	A	40	LEU	0	-0.009	-0.011	10.167	0.200	0.200	0.000	0.000	0.000	0.000
6	A	41	GLY	0	0.009	-0.014	13.218	0.092	0.092	0.000	0.000	0.000	0.000
7	A	42	SER	0	-0.068	-0.017	15.111	-0.025	-0.025	0.000	0.000	0.000	0.000
8	A	43	PHE	0	0.045	0.034	14.697	0.005	0.005	0.000	0.000	0.000	0.000
9	A	44	PRO	0	0.025	0.001	16.429	-0.018	-0.018	0.000	0.000	0.000	0.000
10	A	45	ALA	0	0.026	0.003	18.970	0.019	0.019	0.000	0.000	0.000	0.000
11	A	46	GLY	0	0.038	0.044	20.987	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	47	GLY	0	-0.002	-0.008	22.351	0.019	0.019	0.000	0.000	0.000	0.000
13	A	48	PRO	0	0.010	-0.005	22.664	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	49	ALA	0	-0.035	-0.011	24.236	0.008	0.008	0.000	0.000	0.000	0.000
15	A	50	GLU	-1	-0.807	-0.879	19.052	-0.190	-0.190	0.000	0.000	0.000	0.000
16	A	51	LEU	0	-0.040	-0.016	18.682	-0.023	-0.023	0.000	0.000	0.000	0.000
17	A	52	SER	0	-0.058	-0.027	17.290	-0.016	-0.016	0.000	0.000	0.000	0.000
18	A	53	LEU	0	0.023	0.034	11.219	0.007	0.007	0.000	0.000	0.000	0.000
19	A	54	ARG	1	0.768	0.843	13.497	0.313	0.313	0.000	0.000	0.000	0.000
20	A	55	LEU	0	-0.034	-0.014	12.858	-0.060	-0.060	0.000	0.000	0.000	0.000
21	A	56	GLY	0	0.026	-0.004	10.986	0.051	0.051	0.000	0.000	0.000	0.000
22	A	57	GLU	-1	-0.838	-0.895	9.796	-0.349	-0.349	0.000	0.000	0.000	0.000
23	A	58	PRO	0	0.007	0.015	5.291	-0.097	-0.097	0.000	0.000	0.000	0.000
24	A	59	LEU	0	-0.022	-0.019	4.173	-0.142	0.050	-0.001	-0.024	-0.167	0.000
25	A	60	THR	0	-0.002	-0.021	2.296	-4.316	-2.696	1.722	-1.638	-1.704	-0.010
26	A	61	ILE	0	-0.056	-0.027	2.547	-0.557	0.108	0.770	0.006	-1.441	0.000
27	A	62	VAL	0	-0.022	-0.008	4.378	0.255	0.385	-0.001	-0.010	-0.120	0.000
28	A	63	SER	0	-0.023	-0.014	7.561	0.135	0.135	0.000	0.000	0.000	0.000
29	A	64	GLU	-1	-0.789	-0.896	6.796	-0.413	-0.413	0.000	0.000	0.000	0.000
30	A	65	ASP	-1	-0.937	-0.948	10.613	-0.065	-0.065	0.000	0.000	0.000	0.000
31	A	66	GLY	0	0.012	0.007	14.354	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	67	ASP	-1	-0.952	-0.989	13.756	-0.284	-0.284	0.000	0.000	0.000	0.000
33	A	68	TRP	0	-0.035	-0.011	14.116	-0.065	-0.065	0.000	0.000	0.000	0.000
34	A	69	TRP	0	0.011	0.011	7.522	-0.055	-0.055	0.000	0.000	0.000	0.000
35	A	70	THR	0	0.022	0.003	9.616	0.016	0.016	0.000	0.000	0.000	0.000
36	A	71	VAL	0	-0.025	-0.011	6.197	-0.066	-0.066	0.000	0.000	0.000	0.000
37	A	72	LEU	0	0.055	0.020	6.844	0.227	0.227	0.000	0.000	0.000	0.000
38	A	73	SER	0	-0.031	-0.031	6.890	-0.362	-0.362	0.000	0.000	0.000	0.000
39	A	74	GLU	-1	-0.860	-0.914	3.458	-5.375	-4.218	0.020	-0.552	-0.625	-0.004
40	A	75	VAL	0	-0.052	-0.029	7.906	0.195	0.195	0.000	0.000	0.000	0.000
41	A	76	SER	0	-0.061	-0.044	11.297	0.073	0.073	0.000	0.000	0.000	0.000
42	A	77	GLY	0	0.000	0.006	11.653	0.054	0.054	0.000	0.000	0.000	0.000
43	A	78	ARG	1	0.820	0.903	12.586	0.350	0.350	0.000	0.000	0.000	0.000
44	A	79	GLU	-1	-0.904	-0.947	11.611	-0.464	-0.464	0.000	0.000	0.000	0.000
45	A	80	TYR	0	-0.027	-0.016	11.260	0.114	0.114	0.000	0.000	0.000	0.000
46	A	81	ASN	0	-0.005	-0.002	11.533	-0.050	-0.050	0.000	0.000	0.000	0.000
47	A	82	ILE	0	-0.022	-0.022	10.307	0.043	0.043	0.000	0.000	0.000	0.000
48	A	83	PRO	0	0.017	0.020	12.698	-0.023	-0.023	0.000	0.000	0.000	0.000
49	A	84	SER	0	0.034	0.018	10.885	-0.054	-0.054	0.000	0.000	0.000	0.000
50	A	85	VAL	0	-0.019	-0.017	11.291	-0.109	-0.109	0.000	0.000	0.000	0.000
51	A	86	HIS	0	-0.046	-0.015	12.938	0.032	0.032	0.000	0.000	0.000	0.000
52	A	87	VAL	0	-0.006	-0.012	6.384	-0.023	-0.023	0.000	0.000	0.000	0.000
53	A	88	ALA	0	0.005	0.027	8.413	0.053	0.053	0.000	0.000	0.000	0.000
54	A	89	LYS	1	0.861	0.920	3.863	-0.087	0.106	-0.001	-0.049	-0.143	0.000
55	A	90	VAL	0	-0.029	-0.022	3.506	1.162	2.225	0.014	-0.452	-0.625	0.002
56	A	91	SER	0	0.029	0.014	2.836	-1.277	-0.068	0.389	-0.694	-0.904	-0.007
57	A	92	HIS	0	0.005	-0.026	5.441	-0.051	-0.051	0.000	0.000	0.000	0.000
58	A	93	GLY	0	0.022	0.027	6.807	-0.092	-0.092	0.000	0.000	0.000	0.000
59	A	94	TRP	0	0.030	0.008	8.205	-0.066	-0.066	0.000	0.000	0.000	0.000
60	A	95	LEU	0	-0.037	-0.009	8.484	-0.112	-0.112	0.000	0.000	0.000	0.000
61	A	96	TYR	0	0.008	-0.012	7.531	-0.116	-0.116	0.000	0.000	0.000	0.000
62	A	97	GLU	-1	-0.900	-0.959	6.461	-0.525	-0.525	0.000	0.000	0.000	0.000
63	A	98	GLY	0	-0.009	-0.020	9.354	-0.160	-0.160	0.000	0.000	0.000	0.000
64	A	99	LEU	0	-0.015	0.013	11.490	0.017	0.017	0.000	0.000	0.000	0.000
65	A	100	SER	0	0.005	-0.027	13.128	0.069	0.069	0.000	0.000	0.000	0.000
66	A	101	ARG	1	0.828	0.900	16.863	0.083	0.083	0.000	0.000	0.000	0.000
67	A	102	GLU	-1	-0.837	-0.913	19.412	-0.131	-0.131	0.000	0.000	0.000	0.000
68	A	103	LYS	1	0.852	0.897	15.068	0.286	0.286	0.000	0.000	0.000	0.000
69	A	104	ALA	0	0.029	0.015	15.166	0.005	0.005	0.000	0.000	0.000	0.000
70	A	105	GLU	-1	-0.819	-0.887	16.172	-0.028	-0.028	0.000	0.000	0.000	0.000
71	A	106	GLU	-1	-0.845	-0.915	17.521	-0.196	-0.196	0.000	0.000	0.000	0.000
72	A	107	LEU	0	0.043	0.020	11.292	0.017	0.017	0.000	0.000	0.000	0.000
73	A	108	LEU	0	0.025	0.013	15.150	0.039	0.039	0.000	0.000	0.000	0.000
74	A	109	LEU	0	-0.087	-0.037	17.353	0.018	0.018	0.000	0.000	0.000	0.000
75	A	110	LEU	0	0.014	0.028	14.222	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	111	PRO	0	-0.010	-0.026	18.251	0.022	0.022	0.000	0.000	0.000	0.000
77	A	112	GLY	0	0.013	0.017	17.750	0.008	0.008	0.000	0.000	0.000	0.000
78	A	113	ASN	0	0.020	0.010	15.734	0.050	0.050	0.000	0.000	0.000	0.000
79	A	114	PRO	0	0.001	0.012	18.501	-0.023	-0.023	0.000	0.000	0.000	0.000
80	A	115	GLY	0	-0.032	-0.028	21.266	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	116	GLY	0	0.036	0.004	22.064	0.005	0.005	0.000	0.000	0.000	0.000
82	A	117	ALA	0	-0.019	0.005	17.309	0.015	0.015	0.000	0.000	0.000	0.000
83	A	118	PHE	0	0.009	-0.004	14.894	-0.030	-0.030	0.000	0.000	0.000	0.000
84	A	119	LEU	0	0.008	0.008	12.179	0.042	0.042	0.000	0.000	0.000	0.000
85	A	120	ILE	0	-0.002	-0.007	12.633	-0.028	-0.028	0.000	0.000	0.000	0.000
86	A	121	ARG	1	0.904	0.968	12.055	0.081	0.081	0.000	0.000	0.000	0.000
87	A	122	GLU	-1	-0.804	-0.897	12.920	-0.027	-0.027	0.000	0.000	0.000	0.000
88	A	123	SER	0	-0.076	-0.023	14.701	-0.030	-0.030	0.000	0.000	0.000	0.000
89	A	124	GLN	0	0.084	0.021	16.023	-0.032	-0.032	0.000	0.000	0.000	0.000
90	A	125	THR	0	-0.025	-0.016	17.807	0.009	0.009	0.000	0.000	0.000	0.000
91	A	126	ARG	1	0.852	0.926	19.739	0.059	0.059	0.000	0.000	0.000	0.000
92	A	127	ARG	1	0.959	0.977	17.388	0.078	0.078	0.000	0.000	0.000	0.000
93	A	128	GLY	0	0.107	0.074	17.533	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	129	SER	0	-0.082	-0.043	18.630	0.006	0.006	0.000	0.000	0.000	0.000
95	A	130	TYR	0	0.046	0.004	13.411	0.001	0.001	0.000	0.000	0.000	0.000
96	A	131	SER	0	-0.122	-0.073	17.093	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	132	LEU	0	0.060	0.056	16.868	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	133	SER	0	-0.035	-0.034	16.856	-0.026	-0.026	0.000	0.000	0.000	0.000
99	A	134	VAL	0	0.054	0.017	17.636	0.018	0.018	0.000	0.000	0.000	0.000
100	A	135	ARG	1	0.806	0.915	20.001	-0.027	-0.027	0.000	0.000	0.000	0.000
101	A	136	LEU	0	0.029	0.017	21.944	0.011	0.011	0.000	0.000	0.000	0.000
102	A	137	SER	0	0.013	-0.010	25.675	0.000	0.000	0.000	0.000	0.000	0.000
103	A	138	ARG	1	0.877	0.932	27.743	-0.022	-0.022	0.000	0.000	0.000	0.000
104	A	139	PRO	0	0.031	0.046	26.760	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	140	ALA	0	0.050	0.022	30.069	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	141	SER	0	0.007	-0.021	30.207	0.000	0.000	0.000	0.000	0.000	0.000
107	A	142	TRP	0	-0.015	-0.016	29.715	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	143	ASP	-1	-0.804	-0.849	28.443	-0.018	-0.018	0.000	0.000	0.000	0.000
109	A	144	ARG	1	0.954	0.981	25.084	0.044	0.044	0.000	0.000	0.000	0.000
110	A	145	ILE	0	0.021	0.021	20.307	0.008	0.008	0.000	0.000	0.000	0.000
111	A	146	ARG	1	0.783	0.869	23.450	0.000	0.000	0.000	0.000	0.000	0.000
112	A	147	HIS	0	0.023	0.002	20.155	0.003	0.003	0.000	0.000	0.000	0.000
113	A	148	TYR	0	0.030	0.012	21.752	0.001	0.001	0.000	0.000	0.000	0.000
114	A	149	ARG	1	0.849	0.913	21.555	0.004	0.004	0.000	0.000	0.000	0.000
115	A	150	ILE	0	0.017	0.018	17.842	0.006	0.006	0.000	0.000	0.000	0.000
116	A	151	HIS	0	-0.015	0.011	21.812	-0.015	-0.015	0.000	0.000	0.000	0.000
117	A	152	CYS	0	0.006	0.008	22.050	0.013	0.013	0.000	0.000	0.000	0.000
118	A	153	LEU	0	-0.062	-0.008	24.180	-0.009	-0.009	0.000	0.000	0.000	0.000
119	A	154	ASP	-1	-0.848	-0.925	25.900	0.047	0.047	0.000	0.000	0.000	0.000
120	A	155	ASN	0	-0.031	-0.032	27.225	0.008	0.008	0.000	0.000	0.000	0.000
121	A	156	GLY	0	-0.004	-0.008	23.526	0.008	0.008	0.000	0.000	0.000	0.000
122	A	157	TRP	0	-0.009	0.009	22.797	0.013	0.013	0.000	0.000	0.000	0.000
123	A	158	LEU	0	0.003	-0.013	19.499	-0.013	-0.013	0.000	0.000	0.000	0.000
124	A	159	TYR	0	0.029	0.006	22.955	0.003	0.003	0.000	0.000	0.000	0.000
125	A	160	ILE	0	0.023	0.014	21.440	-0.009	-0.009	0.000	0.000	0.000	0.000
126	A	161	SER	0	0.016	-0.024	25.564	-0.010	-0.010	0.000	0.000	0.000	0.000
127	A	162	PRO	0	-0.015	-0.018	28.965	0.005	0.005	0.000	0.000	0.000	0.000
128	A	163	ARG	1	0.866	0.931	30.769	-0.032	-0.032	0.000	0.000	0.000	0.000
129	A	164	LEU	0	-0.004	0.012	27.615	0.001	0.001	0.000	0.000	0.000	0.000
130	A	165	THR	0	-0.004	-0.002	26.129	0.001	0.001	0.000	0.000	0.000	0.000
131	A	166	PHE	0	0.053	0.019	22.277	0.004	0.004	0.000	0.000	0.000	0.000
132	A	167	PRO	0	-0.006	0.013	22.393	-0.004	-0.004	0.000	0.000	0.000	0.000
133	A	168	SER	0	0.020	-0.002	17.445	0.008	0.008	0.000	0.000	0.000	0.000
134	A	169	LEU	0	0.029	0.009	14.280	-0.011	-0.011	0.000	0.000	0.000	0.000
135	A	170	GLN	0	0.011	-0.003	12.296	-0.049	-0.049	0.000	0.000	0.000	0.000
136	A	171	ALA	0	0.029	0.020	16.391	-0.007	-0.007	0.000	0.000	0.000	0.000
137	A	172	LEU	0	-0.033	0.003	19.179	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	173	VAL	0	0.003	-0.022	15.119	-0.014	-0.014	0.000	0.000	0.000	0.000
139	A	174	ASP	-1	-0.946	-0.952	18.375	0.151	0.151	0.000	0.000	0.000	0.000
140	A	175	HIS	0	0.070	0.036	20.332	-0.014	-0.014	0.000	0.000	0.000	0.000
141	A	176	TYR	0	-0.089	-0.066	21.520	-0.008	-0.008	0.000	0.000	0.000	0.000
142	A	177	SER	0	-0.033	-0.031	19.756	-0.001	-0.001	0.000	0.000	0.000	0.000
143	A	178	GLU	-1	-1.009	-0.991	22.019	0.089	0.089	0.000	0.000	0.000	0.000
144	A	179	LEU	0	-0.009	-0.010	25.745	-0.010	-0.010	0.000	0.000	0.000	0.000
145	A	180	ALA	0	0.000	-0.022	25.643	0.003	0.003	0.000	0.000	0.000	0.000
146	A	181	ASP	-1	-0.899	-0.941	27.567	0.044	0.044	0.000	0.000	0.000	0.000
147	A	182	ASP	-1	-0.874	-0.896	28.831	0.043	0.043	0.000	0.000	0.000	0.000
148	A	183	ILE	0	-0.097	-0.040	24.189	-0.005	-0.005	0.000	0.000	0.000	0.000
149	A	184	CYS	0	-0.113	-0.064	23.999	-0.006	-0.006	0.000	0.000	0.000	0.000
150	A	186	LEU	0	0.070	0.056	24.361	0.001	0.001	0.000	0.000	0.000	0.000
151	A	187	LEU	0	-0.064	-0.037	18.251	-0.007	-0.007	0.000	0.000	0.000	0.000
152	A	188	LYS	1	0.800	0.896	20.046	-0.088	-0.088	0.000	0.000	0.000	0.000
153	A	189	GLU	-1	-0.785	-0.889	16.456	0.132	0.132	0.000	0.000	0.000	0.000
154	A	190	PRO	0	-0.008	-0.003	11.726	-0.033	-0.033	0.000	0.000	0.000	0.000
155	A	191	CYS	0	-0.047	-0.007	12.073	-0.048	-0.048	0.000	0.000	0.000	0.000
156	A	192	VAL	0	-0.009	-0.001	11.513	0.105	0.105	0.000	0.000	0.000	0.000
157	A	193	LEU	0	-0.007	0.009	7.250	0.192	0.192	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:36:THR)