FMO DATABASE

FMODB ID: 1677Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1487092.16739
FMO2-HF: Nuclear repulsion	1425799.313429
FMO2-HF: Total energy	-61292.85396
FMO2-MP2: Total energy	-61473.191377

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.
-4.115	4.386	1.932	-4.274	-6.16	-0.019

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 : 0.026 / q_NPA : 0.006

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	-0.004	0.022	3.786	-0.477	1.931	-0.018	-1.296	-1.094	0.002
4	A	39	ALA	0	0.042	0.034	6.658	-0.123	-0.123	0.000	0.000	0.000	0.000
5	A	40	LEU	0	0.035	0.004	10.007	-0.008	-0.008	0.000	0.000	0.000	0.000
6	A	41	GLY	0	-0.008	-0.011	12.943	-0.002	-0.002	0.000	0.000	0.000	0.000
7	A	42	SER	0	-0.025	0.005	15.231	0.006	0.006	0.000	0.000	0.000	0.000
8	A	43	PHE	0	-0.019	0.040	15.020	-0.005	-0.005	0.000	0.000	0.000	0.000
9	A	44	PRO	0	0.051	0.004	16.704	0.005	0.005	0.000	0.000	0.000	0.000
10	A	45	ALA	0	0.033	-0.013	19.304	0.000	0.000	0.000	0.000	0.000	0.000
11	A	46	GLY	0	0.025	0.038	21.225	0.002	0.002	0.000	0.000	0.000	0.000
12	A	47	GLY	0	0.005	-0.004	22.498	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	48	PRO	0	-0.001	-0.006	22.907	0.002	0.002	0.000	0.000	0.000	0.000
14	A	49	ALA	0	-0.042	-0.018	24.550	0.000	0.000	0.000	0.000	0.000	0.000
15	A	50	GLU	-1	-0.842	-0.925	19.553	0.020	0.020	0.000	0.000	0.000	0.000
16	A	51	LEU	0	0.004	-0.003	19.128	0.004	0.004	0.000	0.000	0.000	0.000
17	A	52	SER	0	-0.104	-0.054	17.293	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	53	LEU	0	0.023	0.032	11.133	0.005	0.005	0.000	0.000	0.000	0.000
19	A	54	ARG	1	0.864	0.921	13.731	-0.056	-0.056	0.000	0.000	0.000	0.000
20	A	55	LEU	0	-0.051	-0.021	12.491	0.021	0.021	0.000	0.000	0.000	0.000
21	A	56	GLY	0	0.010	-0.009	10.076	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	57	GLU	-1	-0.849	-0.893	9.121	0.131	0.131	0.000	0.000	0.000	0.000
23	A	58	PRO	0	0.021	0.015	5.645	-0.044	-0.044	0.000	0.000	0.000	0.000
24	A	59	LEU	0	-0.040	-0.036	4.707	-0.708	-0.515	-0.001	-0.030	-0.162	0.000
25	A	60	THR	0	0.010	-0.004	2.719	-0.744	1.293	0.615	-1.234	-1.418	-0.013
26	A	61	ILE	0	-0.047	-0.031	2.595	-0.979	-0.089	0.548	-0.231	-1.207	0.001
27	A	62	VAL	0	-0.026	-0.008	4.684	-0.324	-0.251	-0.001	-0.004	-0.069	0.000
28	A	63	SER	0	-0.033	-0.026	7.798	0.000	0.000	0.000	0.000	0.000	0.000
29	A	64	GLU	-1	-0.825	-0.910	6.871	-0.152	-0.152	0.000	0.000	0.000	0.000
30	A	65	ASP	-1	-0.950	-0.961	10.482	-0.068	-0.068	0.000	0.000	0.000	0.000
31	A	66	GLY	0	0.023	0.016	14.231	0.014	0.014	0.000	0.000	0.000	0.000
32	A	67	ASP	-1	-0.959	-0.986	13.518	-0.025	-0.025	0.000	0.000	0.000	0.000
33	A	68	TRP	0	-0.035	-0.019	14.018	0.009	0.009	0.000	0.000	0.000	0.000
34	A	69	TRP	0	0.010	0.000	6.480	-0.032	-0.032	0.000	0.000	0.000	0.000
35	A	70	THR	0	0.010	0.006	10.117	0.045	0.045	0.000	0.000	0.000	0.000
36	A	71	VAL	0	-0.021	-0.012	6.574	-0.089	-0.089	0.000	0.000	0.000	0.000
37	A	72	LEU	0	0.038	0.015	6.970	0.015	0.015	0.000	0.000	0.000	0.000
38	A	73	SER	0	-0.035	-0.040	7.050	0.157	0.157	0.000	0.000	0.000	0.000
39	A	74	GLU	-1	-0.880	-0.929	4.694	1.324	1.498	-0.001	-0.006	-0.166	0.000
40	A	75	VAL	0	-0.036	-0.017	9.193	-0.073	-0.073	0.000	0.000	0.000	0.000
41	A	76	SER	0	-0.056	-0.034	12.599	-0.042	-0.042	0.000	0.000	0.000	0.000
42	A	77	GLY	0	-0.003	0.009	11.992	-0.024	-0.024	0.000	0.000	0.000	0.000
43	A	78	ARG	1	0.854	0.924	12.943	-0.038	-0.038	0.000	0.000	0.000	0.000
44	A	79	GLU	-1	-0.895	-0.947	12.043	-0.103	-0.103	0.000	0.000	0.000	0.000
45	A	80	TYR	0	-0.058	-0.036	11.488	0.017	0.017	0.000	0.000	0.000	0.000
46	A	81	ASN	0	0.005	0.006	11.988	-0.014	-0.014	0.000	0.000	0.000	0.000
47	A	82	ILE	0	-0.007	-0.006	10.422	0.018	0.018	0.000	0.000	0.000	0.000
48	A	83	PRO	0	0.032	0.024	12.821	-0.013	-0.013	0.000	0.000	0.000	0.000
49	A	84	SER	0	0.039	0.019	10.717	0.004	0.004	0.000	0.000	0.000	0.000
50	A	85	VAL	0	-0.007	-0.011	11.069	0.005	0.005	0.000	0.000	0.000	0.000
51	A	86	HIS	0	-0.059	-0.025	12.893	0.007	0.007	0.000	0.000	0.000	0.000
52	A	87	VAL	0	-0.005	-0.005	6.368	0.008	0.008	0.000	0.000	0.000	0.000
53	A	88	ALA	0	-0.010	0.008	8.203	0.022	0.022	0.000	0.000	0.000	0.000
54	A	89	LYS	1	0.884	0.937	4.128	-0.743	-0.566	-0.001	-0.041	-0.136	0.000
55	A	90	VAL	0	-0.013	-0.014	3.312	-0.781	0.386	0.040	-0.486	-0.721	0.001
56	A	91	SER	0	0.026	0.010	2.678	0.004	1.375	0.752	-0.945	-1.178	-0.010
57	A	92	HIS	0	0.014	-0.023	5.194	-0.501	-0.490	-0.001	-0.001	-0.009	0.000
58	A	93	GLY	0	0.010	0.017	6.271	-0.138	-0.138	0.000	0.000	0.000	0.000
59	A	94	TRP	0	0.044	0.008	7.454	-0.077	-0.077	0.000	0.000	0.000	0.000
60	A	95	LEU	0	-0.053	-0.012	8.112	-0.061	-0.061	0.000	0.000	0.000	0.000
61	A	96	TYR	0	0.021	0.011	7.170	0.082	0.082	0.000	0.000	0.000	0.000
62	A	97	GLU	-1	-0.933	-0.970	8.192	0.726	0.726	0.000	0.000	0.000	0.000
63	A	98	GLY	0	-0.001	-0.006	9.726	-0.073	-0.073	0.000	0.000	0.000	0.000
64	A	99	LEU	0	0.013	0.019	11.227	-0.025	-0.025	0.000	0.000	0.000	0.000
65	A	100	SER	0	0.011	0.005	13.296	0.012	0.012	0.000	0.000	0.000	0.000
66	A	101	ARG	1	0.961	0.965	16.613	-0.039	-0.039	0.000	0.000	0.000	0.000
67	A	102	GLU	-1	-0.873	-0.953	19.013	0.032	0.032	0.000	0.000	0.000	0.000
68	A	103	LYS	1	0.881	0.924	14.682	-0.021	-0.021	0.000	0.000	0.000	0.000
69	A	104	ALA	0	0.011	0.011	14.446	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	105	GLU	-1	-0.886	-0.926	15.508	0.023	0.023	0.000	0.000	0.000	0.000
71	A	106	GLU	-1	-0.895	-0.960	16.809	0.016	0.016	0.000	0.000	0.000	0.000
72	A	107	LEU	0	0.020	0.008	10.264	0.001	0.001	0.000	0.000	0.000	0.000
73	A	108	LEU	0	0.008	0.005	14.237	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	109	LEU	0	-0.079	-0.054	16.029	0.000	0.000	0.000	0.000	0.000	0.000
75	A	110	LEU	0	0.000	0.021	13.434	0.001	0.001	0.000	0.000	0.000	0.000
76	A	111	PRO	0	-0.026	-0.026	17.329	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	112	GLY	0	0.031	0.017	17.138	0.000	0.000	0.000	0.000	0.000	0.000
78	A	113	ASN	0	0.015	0.016	14.468	-0.009	-0.009	0.000	0.000	0.000	0.000
79	A	114	PRO	0	0.002	0.008	17.453	0.004	0.004	0.000	0.000	0.000	0.000
80	A	115	GLY	0	-0.022	-0.027	19.830	0.001	0.001	0.000	0.000	0.000	0.000
81	A	116	GLY	0	0.032	0.006	20.767	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	117	ALA	0	-0.018	0.007	15.824	0.004	0.004	0.000	0.000	0.000	0.000
83	A	118	PHE	0	0.020	0.006	14.365	0.004	0.004	0.000	0.000	0.000	0.000
84	A	119	LEU	0	0.013	0.011	11.760	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	120	ILE	0	-0.003	-0.007	12.263	0.002	0.002	0.000	0.000	0.000	0.000
86	A	121	ARG	1	0.888	0.957	11.787	-0.048	-0.048	0.000	0.000	0.000	0.000
87	A	122	GLU	-1	-0.860	-0.939	12.789	0.239	0.239	0.000	0.000	0.000	0.000
88	A	123	SER	0	-0.089	-0.043	14.648	-0.030	-0.030	0.000	0.000	0.000	0.000
89	A	124	GLN	0	0.075	0.024	16.078	0.004	0.004	0.000	0.000	0.000	0.000
90	A	125	THR	0	-0.027	-0.014	18.295	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	126	ARG	1	0.840	0.903	20.735	-0.085	-0.085	0.000	0.000	0.000	0.000
92	A	127	ARG	1	0.985	0.988	18.925	-0.101	-0.101	0.000	0.000	0.000	0.000
93	A	128	GLY	0	0.130	0.104	17.523	0.011	0.011	0.000	0.000	0.000	0.000
94	A	129	SER	0	-0.084	-0.043	18.483	-0.017	-0.017	0.000	0.000	0.000	0.000
95	A	130	TYR	0	0.120	0.053	13.346	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	131	SER	0	-0.106	-0.056	16.880	-0.022	-0.022	0.000	0.000	0.000	0.000
97	A	132	LEU	0	0.049	0.040	16.681	0.010	0.010	0.000	0.000	0.000	0.000
98	A	133	SER	0	-0.030	-0.026	16.564	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	134	VAL	0	0.051	0.026	17.135	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	135	ARG	1	0.839	0.932	19.058	-0.013	-0.013	0.000	0.000	0.000	0.000
101	A	136	LEU	0	0.024	0.005	20.752	0.000	0.000	0.000	0.000	0.000	0.000
102	A	137	SER	0	-0.003	-0.018	24.498	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	138	ARG	1	0.880	0.940	26.348	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	139	PRO	0	0.026	0.051	25.653	0.000	0.000	0.000	0.000	0.000	0.000
105	A	140	ALA	0	0.059	0.017	28.895	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	141	SER	0	0.002	-0.028	28.654	0.001	0.001	0.000	0.000	0.000	0.000
107	A	142	TRP	0	-0.017	-0.017	28.326	0.000	0.000	0.000	0.000	0.000	0.000
108	A	143	ASP	-1	-0.820	-0.877	27.224	0.027	0.027	0.000	0.000	0.000	0.000
109	A	144	ARG	1	0.942	0.979	23.909	-0.015	-0.015	0.000	0.000	0.000	0.000
110	A	145	ILE	0	0.018	0.021	19.523	0.000	0.000	0.000	0.000	0.000	0.000
111	A	146	ARG	1	0.844	0.917	22.418	-0.031	-0.031	0.000	0.000	0.000	0.000
112	A	147	HIS	0	-0.046	-0.040	19.593	0.009	0.009	0.000	0.000	0.000	0.000
113	A	148	TYR	0	0.046	0.029	21.586	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	149	ARG	1	0.876	0.927	21.322	-0.059	-0.059	0.000	0.000	0.000	0.000
115	A	150	ILE	0	0.023	0.018	17.688	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	151	HIS	0	-0.057	-0.027	21.665	0.008	0.008	0.000	0.000	0.000	0.000
117	A	152	CYS	0	0.031	0.019	21.636	0.007	0.007	0.000	0.000	0.000	0.000
118	A	153	LEU	0	-0.071	-0.019	23.749	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	154	ASP	-1	-0.922	-0.961	25.881	0.069	0.069	0.000	0.000	0.000	0.000
120	A	155	ASN	0	0.059	0.013	27.610	0.007	0.007	0.000	0.000	0.000	0.000
121	A	156	GLY	0	-0.007	-0.005	23.501	0.002	0.002	0.000	0.000	0.000	0.000
122	A	157	TRP	0	-0.023	-0.002	22.621	0.012	0.012	0.000	0.000	0.000	0.000
123	A	158	LEU	0	-0.015	-0.026	19.202	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	159	TYR	0	0.023	0.012	22.733	-0.006	-0.006	0.000	0.000	0.000	0.000
125	A	160	ILE	0	0.032	0.034	21.343	0.002	0.002	0.000	0.000	0.000	0.000
126	A	161	SER	0	-0.020	-0.066	25.090	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	162	PRO	0	-0.012	-0.014	28.640	0.002	0.002	0.000	0.000	0.000	0.000
128	A	163	ARG	1	0.896	0.960	30.368	-0.042	-0.042	0.000	0.000	0.000	0.000
129	A	164	LEU	0	-0.006	0.005	27.382	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	165	THR	0	-0.013	0.001	26.097	0.007	0.007	0.000	0.000	0.000	0.000
131	A	166	PHE	0	0.057	0.009	21.897	0.000	0.000	0.000	0.000	0.000	0.000
132	A	167	PRO	0	-0.008	0.021	21.765	0.003	0.003	0.000	0.000	0.000	0.000
133	A	168	SER	0	0.028	0.001	17.156	0.011	0.011	0.000	0.000	0.000	0.000
134	A	169	LEU	0	0.049	0.015	13.682	-0.019	-0.019	0.000	0.000	0.000	0.000
135	A	170	GLN	0	0.021	0.006	12.458	-0.049	-0.049	0.000	0.000	0.000	0.000
136	A	171	ALA	0	0.022	0.018	15.985	-0.021	-0.021	0.000	0.000	0.000	0.000
137	A	172	LEU	0	-0.023	0.008	18.582	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	173	VAL	0	0.002	-0.022	14.678	-0.015	-0.015	0.000	0.000	0.000	0.000
139	A	174	ASP	-1	-0.961	-0.956	18.010	0.070	0.070	0.000	0.000	0.000	0.000
140	A	175	HIS	0	0.090	0.038	19.932	-0.014	-0.014	0.000	0.000	0.000	0.000
141	A	176	TYR	0	-0.094	-0.069	21.135	-0.006	-0.006	0.000	0.000	0.000	0.000
142	A	177	SER	0	-0.045	-0.023	19.126	-0.008	-0.008	0.000	0.000	0.000	0.000
143	A	178	GLU	-1	-0.992	-0.981	21.489	0.036	0.036	0.000	0.000	0.000	0.000
144	A	179	LEU	0	-0.033	-0.029	25.087	-0.005	-0.005	0.000	0.000	0.000	0.000
145	A	180	ALA	0	-0.001	-0.024	25.082	0.005	0.005	0.000	0.000	0.000	0.000
146	A	181	ASP	-1	-0.889	-0.927	27.143	0.030	0.030	0.000	0.000	0.000	0.000
147	A	182	ASP	-1	-0.931	-0.911	28.003	0.050	0.050	0.000	0.000	0.000	0.000
148	A	183	ILE	0	-0.084	-0.038	23.729	0.001	0.001	0.000	0.000	0.000	0.000
149	A	184	CYS	0	-0.110	-0.061	23.226	-0.005	-0.005	0.000	0.000	0.000	0.000
150	A	186	LEU	0	0.069	0.046	23.760	0.003	0.003	0.000	0.000	0.000	0.000
151	A	187	LEU	0	-0.078	-0.040	17.929	-0.004	-0.004	0.000	0.000	0.000	0.000
152	A	188	LYS	1	0.928	0.975	19.247	-0.012	-0.012	0.000	0.000	0.000	0.000
153	A	189	GLU	-1	-0.924	-0.973	15.002	0.000	0.000	0.000	0.000	0.000	0.000
154	A	190	PRO	0	0.002	-0.003	10.678	0.008	0.008	0.000	0.000	0.000	0.000
155	A	191	CYS	0	-0.040	-0.009	10.941	-0.001	-0.001	0.000	0.000	0.000	0.000
156	A	192	VAL	0	-0.032	-0.015	10.032	-0.037	-0.037	0.000	0.000	0.000	0.000
157	A	193	LEU	0	0.001	0.007	5.766	-0.115	-0.115	0.000	0.000	0.000	0.000

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