FMO DATABASE

FMODB ID: 4JZ9N

Calculation Name: 3G39-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3G39

Chain ID: A

ChEMBL ID:

UniProt ID: D0VX17

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	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	163
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1645168.311046
FMO2-HF: Nuclear repulsion	1580315.586066
FMO2-HF: Total energy	-64852.72498
FMO2-MP2: Total energy	-65038.654497

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.
-2.755	0.559	0.472	-1.72	-2.064	0.005

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 : 0.035 / 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	PRO	0	0.032	0.002	3.556	-0.949	1.285	0.017	-1.131	-1.120	0.003
4	A	4	SER	0	0.008	-0.005	5.663	0.346	0.346	0.000	0.000	0.000	0.000
5	A	5	GLN	0	-0.019	-0.006	7.321	0.213	0.213	0.000	0.000	0.000	0.000
6	A	6	CYS	0	-0.094	-0.023	8.460	-0.026	-0.026	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.001	0.001	9.286	0.120	0.120	0.000	0.000	0.000	0.000
8	A	9	SER	0	0.001	0.006	8.560	0.255	0.255	0.000	0.000	0.000	0.000
9	A	10	GLY	0	0.025	0.015	9.806	0.001	0.001	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.028	-0.024	8.153	-0.228	-0.228	0.000	0.000	0.000	0.000
11	A	12	THR	0	0.013	0.016	9.921	-0.034	-0.034	0.000	0.000	0.000	0.000
12	A	13	VAL	0	-0.004	-0.023	7.117	-0.224	-0.224	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.768	-0.866	9.902	-0.518	-0.518	0.000	0.000	0.000	0.000
14	A	16	SER	0	-0.014	-0.006	13.055	0.098	0.098	0.000	0.000	0.000	0.000
15	A	17	GLY	0	0.082	0.051	16.832	-0.008	-0.008	0.000	0.000	0.000	0.000
16	A	18	LYS	1	0.718	0.852	13.388	0.697	0.697	0.000	0.000	0.000	0.000
17	A	19	SER	0	-0.020	-0.011	16.935	0.021	0.021	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.032	-0.006	13.467	0.011	0.011	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.060	0.019	17.214	0.024	0.024	0.000	0.000	0.000	0.000
20	A	22	SER	0	-0.008	-0.013	14.667	0.052	0.052	0.000	0.000	0.000	0.000
21	A	23	VAL	0	0.008	0.003	12.008	-0.042	-0.042	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.002	0.005	9.057	0.022	0.022	0.000	0.000	0.000	0.000
23	A	25	THR	0	0.036	0.008	7.698	-0.163	-0.163	0.000	0.000	0.000	0.000
24	A	26	GLY	0	-0.013	-0.014	4.854	-0.157	-0.157	0.000	0.000	0.000	0.000
25	A	27	ILE	0	0.006	0.013	3.585	-2.523	-2.297	0.004	-0.150	-0.080	-0.001
26	A	28	PRO	0	-0.001	0.006	2.387	0.107	0.920	0.452	-0.433	-0.831	0.003
27	A	29	THR	0	0.014	0.009	4.861	0.443	0.484	-0.001	-0.006	-0.033	0.000
28	A	30	THR	0	-0.022	-0.011	6.508	-0.014	-0.014	0.000	0.000	0.000	0.000
29	A	31	THR	0	-0.035	-0.033	7.362	-0.052	-0.052	0.000	0.000	0.000	0.000
30	A	32	GLN	0	0.005	0.022	9.259	0.136	0.136	0.000	0.000	0.000	0.000
31	A	33	VAL	0	-0.001	0.016	12.149	0.091	0.091	0.000	0.000	0.000	0.000
32	A	34	LEU	0	-0.004	0.000	10.472	-0.186	-0.186	0.000	0.000	0.000	0.000
33	A	35	TYR	0	0.023	0.014	13.164	0.107	0.107	0.000	0.000	0.000	0.000
34	A	36	LEU	0	-0.007	-0.024	13.073	-0.115	-0.115	0.000	0.000	0.000	0.000
35	A	37	TYR	0	0.021	0.031	16.473	0.043	0.043	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.881	-0.946	19.419	-0.354	-0.354	0.000	0.000	0.000	0.000
37	A	39	ASN	0	-0.085	-0.045	16.650	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	40	GLN	0	0.047	0.016	20.317	0.054	0.054	0.000	0.000	0.000	0.000
39	A	41	ILE	0	-0.001	0.011	16.539	0.014	0.014	0.000	0.000	0.000	0.000
40	A	42	THR	0	0.005	0.002	20.453	0.029	0.029	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.906	0.941	21.554	0.238	0.238	0.000	0.000	0.000	0.000
42	A	44	LEU	0	0.014	0.013	17.469	-0.038	-0.038	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.870	-0.937	15.835	-0.306	-0.306	0.000	0.000	0.000	0.000
44	A	46	PRO	0	-0.017	-0.031	17.992	-0.019	-0.019	0.000	0.000	0.000	0.000
45	A	47	GLY	0	0.035	0.031	17.474	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	48	VAL	0	-0.051	-0.018	13.169	-0.035	-0.035	0.000	0.000	0.000	0.000
47	A	49	PHE	0	0.055	0.012	12.560	-0.127	-0.127	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.847	-0.938	14.097	-0.308	-0.308	0.000	0.000	0.000	0.000
49	A	51	ARG	1	0.900	0.939	7.123	0.703	0.703	0.000	0.000	0.000	0.000
50	A	52	LEU	0	-0.006	0.007	8.997	-0.010	-0.010	0.000	0.000	0.000	0.000
51	A	53	THR	0	0.027	0.008	12.174	0.023	0.023	0.000	0.000	0.000	0.000
52	A	54	GLN	0	-0.021	-0.005	12.171	0.087	0.087	0.000	0.000	0.000	0.000
53	A	55	LEU	0	-0.011	0.001	12.462	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	56	THR	0	-0.023	-0.012	14.621	0.054	0.054	0.000	0.000	0.000	0.000
55	A	57	ARG	1	0.810	0.866	16.350	0.400	0.400	0.000	0.000	0.000	0.000
56	A	58	LEU	0	-0.008	0.005	15.209	-0.088	-0.088	0.000	0.000	0.000	0.000
57	A	59	ASP	-1	-0.808	-0.879	17.146	-0.375	-0.375	0.000	0.000	0.000	0.000
58	A	60	LEU	0	0.013	-0.011	17.002	-0.056	-0.056	0.000	0.000	0.000	0.000
59	A	61	ASP	-1	-0.802	-0.857	20.284	-0.308	-0.308	0.000	0.000	0.000	0.000
60	A	62	ASN	0	-0.036	-0.037	22.743	-0.015	-0.015	0.000	0.000	0.000	0.000
61	A	63	ASN	0	-0.039	-0.017	20.053	-0.032	-0.032	0.000	0.000	0.000	0.000
62	A	64	GLN	0	0.023	0.004	23.651	0.037	0.037	0.000	0.000	0.000	0.000
63	A	65	LEU	0	-0.021	-0.008	20.787	0.014	0.014	0.000	0.000	0.000	0.000
64	A	66	THR	0	-0.021	-0.004	24.914	0.020	0.020	0.000	0.000	0.000	0.000
65	A	67	VAL	0	-0.050	-0.036	26.050	0.016	0.016	0.000	0.000	0.000	0.000
66	A	68	LEU	0	0.021	0.015	22.340	-0.024	-0.024	0.000	0.000	0.000	0.000
67	A	69	PRO	0	0.001	-0.002	20.518	0.028	0.028	0.000	0.000	0.000	0.000
68	A	70	ALA	0	0.021	-0.004	23.636	-0.005	-0.005	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.038	0.020	23.334	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	72	VAL	0	-0.059	-0.015	18.589	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	73	PHE	0	0.063	0.013	18.717	-0.045	-0.045	0.000	0.000	0.000	0.000
72	A	74	ASP	-1	-0.839	-0.894	20.502	-0.192	-0.192	0.000	0.000	0.000	0.000
73	A	75	LYS	1	0.840	0.915	17.371	0.240	0.240	0.000	0.000	0.000	0.000
74	A	76	LEU	0	-0.012	0.019	15.610	0.004	0.004	0.000	0.000	0.000	0.000
75	A	77	THR	0	-0.008	-0.003	18.608	0.014	0.014	0.000	0.000	0.000	0.000
76	A	78	GLN	0	-0.044	-0.028	16.894	0.045	0.045	0.000	0.000	0.000	0.000
77	A	79	LEU	0	-0.034	-0.001	18.127	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	80	THR	0	-0.015	-0.005	20.176	0.032	0.032	0.000	0.000	0.000	0.000
79	A	81	GLN	0	-0.043	-0.022	21.176	0.002	0.002	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.043	0.021	20.448	-0.037	-0.037	0.000	0.000	0.000	0.000
81	A	83	SER	0	-0.034	-0.045	21.727	0.024	0.024	0.000	0.000	0.000	0.000
82	A	84	LEU	0	0.018	-0.004	22.550	-0.026	-0.026	0.000	0.000	0.000	0.000
83	A	85	ASN	0	-0.026	-0.016	25.055	0.005	0.005	0.000	0.000	0.000	0.000
84	A	86	ASP	-1	-0.744	-0.833	26.646	-0.226	-0.226	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.036	-0.006	23.910	-0.025	-0.025	0.000	0.000	0.000	0.000
86	A	88	GLN	0	0.007	-0.004	27.856	0.029	0.029	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.024	0.000	25.749	0.010	0.010	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.916	0.953	29.781	0.134	0.134	0.000	0.000	0.000	0.000
89	A	91	SER	0	-0.041	-0.020	31.400	0.007	0.007	0.000	0.000	0.000	0.000
90	A	92	ILE	0	0.034	0.014	27.117	-0.014	-0.014	0.000	0.000	0.000	0.000
91	A	93	PRO	0	-0.004	0.007	26.253	0.016	0.016	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.948	0.957	29.359	0.102	0.102	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.049	0.034	29.685	0.001	0.001	0.000	0.000	0.000	0.000
94	A	96	ALA	0	-0.046	-0.013	25.415	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	97	PHE	0	0.048	-0.004	24.986	-0.021	-0.021	0.000	0.000	0.000	0.000
96	A	98	ASP	-1	-0.848	-0.897	27.050	-0.133	-0.133	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.018	-0.020	23.830	0.019	0.019	0.000	0.000	0.000	0.000
98	A	100	LEU	0	-0.025	0.014	22.148	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	101	LYS	1	0.895	0.936	23.506	0.150	0.150	0.000	0.000	0.000	0.000
100	A	102	SER	0	-0.038	-0.046	23.150	0.021	0.021	0.000	0.000	0.000	0.000
101	A	103	LEU	0	-0.040	0.007	24.040	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	104	THR	0	-0.021	-0.045	25.743	0.015	0.015	0.000	0.000	0.000	0.000
103	A	105	HIS	0	-0.010	0.021	25.856	0.001	0.001	0.000	0.000	0.000	0.000
104	A	106	ILE	0	0.005	0.009	25.531	-0.021	-0.021	0.000	0.000	0.000	0.000
105	A	107	TRP	0	-0.013	0.003	24.629	0.010	0.010	0.000	0.000	0.000	0.000
106	A	108	LEU	0	0.026	-0.005	27.529	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	109	LEU	0	0.014	0.019	30.188	0.006	0.006	0.000	0.000	0.000	0.000
108	A	110	ASN	0	-0.039	-0.030	31.036	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	111	ASN	0	0.031	0.015	28.433	-0.018	-0.018	0.000	0.000	0.000	0.000
110	A	112	PRO	0	-0.011	0.021	31.832	0.013	0.013	0.000	0.000	0.000	0.000
111	A	113	TRP	0	-0.047	-0.037	29.289	0.006	0.006	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.783	-0.892	35.569	-0.103	-0.103	0.000	0.000	0.000	0.000
113	A	115	CYS	0	-0.079	-0.031	37.498	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	116	ALA	0	0.009	0.025	40.578	0.006	0.006	0.000	0.000	0.000	0.000
115	A	167	CYS	0	-0.016	0.040	38.026	0.001	0.001	0.000	0.000	0.000	0.000
116	A	118	SER	0	0.037	-0.008	39.530	0.001	0.001	0.000	0.000	0.000	0.000
117	A	119	ASP	-1	-0.897	-0.976	34.474	-0.122	-0.122	0.000	0.000	0.000	0.000
118	A	120	ILE	0	-0.031	-0.006	35.323	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	121	LEU	0	-0.009	-0.002	36.881	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	122	TYR	0	-0.076	-0.058	29.814	0.001	0.001	0.000	0.000	0.000	0.000
121	A	123	LEU	0	0.043	0.027	31.218	0.000	0.000	0.000	0.000	0.000	0.000
122	A	124	SER	0	-0.017	-0.024	34.167	0.002	0.002	0.000	0.000	0.000	0.000
123	A	125	ARG	1	0.838	0.877	37.607	0.088	0.088	0.000	0.000	0.000	0.000
124	A	126	TRP	0	0.017	0.026	29.166	0.004	0.004	0.000	0.000	0.000	0.000
125	A	127	ILE	0	0.024	-0.002	33.559	0.001	0.001	0.000	0.000	0.000	0.000
126	A	128	SER	0	-0.070	-0.045	35.486	0.005	0.005	0.000	0.000	0.000	0.000
127	A	129	GLN	0	-0.044	-0.020	36.526	0.007	0.007	0.000	0.000	0.000	0.000
128	A	130	HIS	1	0.857	0.933	32.816	0.127	0.127	0.000	0.000	0.000	0.000
129	A	131	PRO	0	0.054	0.029	34.173	-0.008	-0.008	0.000	0.000	0.000	0.000
130	A	132	GLY	0	0.005	-0.006	35.547	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	133	LEU	0	-0.010	0.003	29.900	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	134	VAL	0	-0.009	0.001	30.222	-0.013	-0.013	0.000	0.000	0.000	0.000
133	A	135	PHE	0	-0.023	-0.007	29.862	0.011	0.011	0.000	0.000	0.000	0.000
134	A	136	GLY	0	0.069	0.028	31.366	-0.008	-0.008	0.000	0.000	0.000	0.000
135	A	137	TYR	0	-0.071	-0.088	29.754	0.003	0.003	0.000	0.000	0.000	0.000
136	A	138	LEU	0	-0.013	0.004	31.807	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	139	ASN	0	0.022	0.010	33.801	0.000	0.000	0.000	0.000	0.000	0.000
138	A	140	LEU	0	-0.020	-0.005	33.718	-0.006	-0.006	0.000	0.000	0.000	0.000
139	A	141	ASP	-1	-0.797	-0.918	34.985	-0.115	-0.115	0.000	0.000	0.000	0.000
140	A	142	PRO	0	-0.009	0.017	35.642	-0.007	-0.007	0.000	0.000	0.000	0.000
141	A	143	ASP	-1	-0.806	-0.870	36.692	-0.101	-0.101	0.000	0.000	0.000	0.000
142	A	144	SER	0	-0.046	-0.027	34.583	-0.001	-0.001	0.000	0.000	0.000	0.000
143	A	145	ALA	0	-0.001	0.008	33.857	-0.005	-0.005	0.000	0.000	0.000	0.000
144	A	146	ARG	1	0.848	0.921	35.419	0.126	0.126	0.000	0.000	0.000	0.000
145	A	148	SER	0	0.058	0.023	38.075	0.003	0.003	0.000	0.000	0.000	0.000
146	A	149	GLY	0	-0.016	0.000	39.842	0.004	0.004	0.000	0.000	0.000	0.000
147	A	150	THR	0	-0.006	-0.027	43.441	0.002	0.002	0.000	0.000	0.000	0.000
148	A	151	ASN	0	-0.082	-0.035	41.024	0.005	0.005	0.000	0.000	0.000	0.000
149	A	152	THR	0	0.050	0.025	42.518	0.000	0.000	0.000	0.000	0.000	0.000
150	A	153	PRO	0	0.040	0.018	40.230	-0.005	-0.005	0.000	0.000	0.000	0.000
151	A	154	VAL	0	0.048	0.015	35.827	0.005	0.005	0.000	0.000	0.000	0.000
152	A	155	ARG	1	0.785	0.863	38.482	0.104	0.104	0.000	0.000	0.000	0.000
153	A	156	ALA	0	-0.022	-0.006	40.028	0.004	0.004	0.000	0.000	0.000	0.000
154	A	157	VAL	0	0.003	0.009	40.654	0.004	0.004	0.000	0.000	0.000	0.000
155	A	158	THR	0	0.009	0.003	43.559	0.000	0.000	0.000	0.000	0.000	0.000
156	A	159	GLU	-1	-0.767	-0.847	42.733	-0.079	-0.079	0.000	0.000	0.000	0.000
157	A	160	ALA	0	-0.015	-0.002	45.369	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	161	SER	0	0.005	0.015	44.707	0.002	0.002	0.000	0.000	0.000	0.000
159	A	162	THR	0	-0.037	-0.017	42.067	-0.001	-0.001	0.000	0.000	0.000	0.000
160	A	163	SER	0	0.031	0.012	43.460	0.005	0.005	0.000	0.000	0.000	0.000
161	A	164	PRO	0	0.049	0.024	41.550	-0.003	-0.003	0.000	0.000	0.000	0.000
162	A	165	SER	0	-0.056	-0.046	42.253	-0.002	-0.002	0.000	0.000	0.000	0.000
163	A	166	LYS	1	0.832	0.912	43.361	0.078	0.078	0.000	0.000	0.000	0.000

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