FMO DATABASE

FMODB ID: G52K1

Calculation Name: 3BQX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3BQX

Chain ID: A

ChEMBL ID:

UniProt ID: Q0G7J9

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	139
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1125906.792206
FMO2-HF: Nuclear repulsion	1074286.701653
FMO2-HF: Total energy	-51620.090553
FMO2-MP2: Total energy	-51772.545111

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:3:LEU)

Summations of interaction energy for fragment #1(A:3:LEU)

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.
-1.569	0.448	0.004	-0.733	-1.286	0

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.005 / q_NPA : -0.023

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

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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].
3	A	5	GLN	0	-0.013	-0.004	3.505	-0.659	1.299	0.005	-0.721	-1.241
4	A	6	VAL	0	0.049	0.040	4.900	0.053	0.112	-0.001	-0.012	-0.045
5	A	7	ALA	0	0.010	0.002	8.586	0.071	0.071	0.000	0.000	0.000
6	A	8	VAL	0	0.008	-0.013	10.046	0.129	0.129	0.000	0.000	0.000
7	A	9	ILE	0	-0.016	0.022	13.638	-0.023	-0.023	0.000	0.000	0.000
8	A	10	THR	0	0.004	-0.012	15.866	0.032	0.032	0.000	0.000	0.000
9	A	11	LEU	0	-0.037	-0.010	19.009	0.011	0.011	0.000	0.000	0.000
10	A	12	GLY	0	0.020	0.010	22.266	0.002	0.002	0.000	0.000	0.000
11	A	13	ILE	0	-0.043	-0.017	24.989	0.009	0.009	0.000	0.000	0.000
12	A	14	GLY	0	-0.006	-0.014	28.324	0.002	0.002	0.000	0.000	0.000
13	A	15	ASP	-1	-0.851	-0.934	31.925	-0.109	-0.109	0.000	0.000	0.000
14	A	16	LEU	0	0.000	-0.007	29.089	-0.004	-0.004	0.000	0.000	0.000
15	A	17	GLU	-1	-0.996	-0.972	31.324	-0.110	-0.110	0.000	0.000	0.000
16	A	18	ALA	0	0.016	0.000	33.597	-0.001	-0.001	0.000	0.000	0.000
17	A	19	SER	0	0.029	0.009	27.722	-0.006	-0.006	0.000	0.000	0.000
18	A	20	ALA	0	-0.023	-0.030	29.128	-0.007	-0.007	0.000	0.000	0.000
19	A	21	ARG	1	0.930	0.991	30.170	0.099	0.099	0.000	0.000	0.000
20	A	22	PHE	0	0.037	0.020	26.755	0.002	0.002	0.000	0.000	0.000
21	A	23	TYR	0	-0.053	-0.053	24.262	-0.007	-0.007	0.000	0.000	0.000
22	A	24	GLY	0	0.013	0.011	27.687	-0.005	-0.005	0.000	0.000	0.000
23	A	25	GLU	-1	-0.990	-1.005	29.834	-0.105	-0.105	0.000	0.000	0.000
24	A	26	GLY	0	-0.012	-0.004	31.113	0.006	0.006	0.000	0.000	0.000
25	A	27	PHE	0	-0.062	-0.043	25.038	0.003	0.003	0.000	0.000	0.000
26	A	28	GLY	0	-0.045	0.000	27.720	-0.002	-0.002	0.000	0.000	0.000
27	A	29	TRP	0	-0.078	-0.034	22.055	-0.014	-0.014	0.000	0.000	0.000
28	A	30	ALA	0	0.031	0.003	25.366	0.011	0.011	0.000	0.000	0.000
29	A	31	PRO	0	-0.036	-0.022	24.362	-0.017	-0.017	0.000	0.000	0.000
30	A	32	VAL	0	-0.034	-0.006	20.109	0.010	0.010	0.000	0.000	0.000
31	A	33	PHE	0	-0.040	-0.030	22.937	0.008	0.008	0.000	0.000	0.000
32	A	34	ARG	1	0.992	0.993	24.639	0.150	0.150	0.000	0.000	0.000
33	A	35	ASN	0	0.005	0.031	26.704	0.011	0.011	0.000	0.000	0.000
34	A	36	PRO	0	-0.017	-0.047	29.463	-0.003	-0.003	0.000	0.000	0.000
35	A	37	GLU	-1	-0.828	-0.897	26.899	-0.174	-0.174	0.000	0.000	0.000
36	A	38	ILE	0	0.012	0.009	21.471	-0.008	-0.008	0.000	0.000	0.000
37	A	39	ILE	0	-0.030	-0.011	24.553	0.011	0.011	0.000	0.000	0.000
38	A	40	PHE	0	0.017	0.008	19.424	-0.021	-0.021	0.000	0.000	0.000
39	A	41	TYR	0	0.073	0.023	20.292	0.030	0.030	0.000	0.000	0.000
40	A	42	GLN	0	-0.027	-0.013	14.270	-0.025	-0.025	0.000	0.000	0.000
41	A	43	MET	0	0.015	0.017	15.517	0.046	0.046	0.000	0.000	0.000
42	A	44	ASN	0	0.003	-0.006	14.391	-0.019	-0.019	0.000	0.000	0.000
43	A	45	GLY	0	-0.026	-0.022	10.682	-0.030	-0.030	0.000	0.000	0.000
44	A	46	PHE	0	-0.049	-0.016	10.072	-0.155	-0.155	0.000	0.000	0.000
45	A	47	VAL	0	0.007	0.010	12.229	0.094	0.094	0.000	0.000	0.000
46	A	48	LEU	0	0.013	0.021	15.500	-0.038	-0.038	0.000	0.000	0.000
47	A	49	ALA	0	0.011	-0.016	18.097	0.024	0.024	0.000	0.000	0.000
48	A	50	THR	0	-0.002	0.011	20.384	0.002	0.002	0.000	0.000	0.000
49	A	51	TRP	0	-0.050	-0.034	20.708	-0.002	-0.002	0.000	0.000	0.000
50	A	52	LEU	0	0.012	0.023	24.952	0.007	0.007	0.000	0.000	0.000
51	A	53	VAL	0	0.015	-0.007	26.656	-0.006	-0.006	0.000	0.000	0.000
52	A	54	GLN	0	-0.025	-0.019	27.189	-0.007	-0.007	0.000	0.000	0.000
53	A	55	ASN	0	0.066	0.032	26.361	0.008	0.008	0.000	0.000	0.000
54	A	56	LEU	0	0.025	0.031	20.483	-0.008	-0.008	0.000	0.000	0.000
55	A	57	GLN	0	-0.019	-0.020	23.302	0.001	0.001	0.000	0.000	0.000
56	A	58	GLU	-1	-0.998	-1.000	25.431	-0.137	-0.137	0.000	0.000	0.000
57	A	59	ASP	-1	-0.950	-0.969	20.044	-0.259	-0.259	0.000	0.000	0.000
58	A	60	VAL	0	-0.058	-0.023	19.823	-0.003	-0.003	0.000	0.000	0.000
59	A	61	GLY	0	-0.002	0.015	21.719	0.012	0.012	0.000	0.000	0.000
60	A	62	VAL	0	-0.079	-0.040	23.023	0.020	0.020	0.000	0.000	0.000
61	A	63	ALA	0	-0.014	-0.020	25.789	-0.010	-0.010	0.000	0.000	0.000
62	A	64	VAL	0	-0.009	-0.005	23.093	0.001	0.001	0.000	0.000	0.000
63	A	65	THR	0	-0.041	-0.025	26.006	0.007	0.007	0.000	0.000	0.000
64	A	66	SER	0	0.046	0.017	26.967	-0.009	-0.009	0.000	0.000	0.000
65	A	67	ARG	1	0.893	0.955	29.319	0.076	0.076	0.000	0.000	0.000
66	A	68	PRO	0	0.057	0.053	26.346	-0.007	-0.007	0.000	0.000	0.000
67	A	69	GLY	0	0.023	-0.006	24.306	0.012	0.012	0.000	0.000	0.000
68	A	70	SER	0	-0.053	-0.022	23.285	0.006	0.006	0.000	0.000	0.000
69	A	71	MET	0	-0.031	-0.025	19.410	-0.016	-0.016	0.000	0.000	0.000
70	A	72	ALA	0	-0.003	-0.001	21.114	0.013	0.013	0.000	0.000	0.000
71	A	73	LEU	0	-0.007	0.014	17.840	-0.024	-0.024	0.000	0.000	0.000
72	A	74	ALA	0	0.028	0.024	19.488	0.023	0.023	0.000	0.000	0.000
73	A	75	HIS	0	0.001	0.007	19.757	-0.042	-0.042	0.000	0.000	0.000
74	A	76	ASN	0	-0.004	-0.017	20.820	0.018	0.018	0.000	0.000	0.000
75	A	77	VAL	0	-0.007	-0.004	22.683	-0.009	-0.009	0.000	0.000	0.000
76	A	78	ARG	1	0.855	0.899	20.976	0.167	0.167	0.000	0.000	0.000
77	A	79	ALA	0	0.027	0.007	26.636	0.008	0.008	0.000	0.000	0.000
78	A	80	GLU	-1	-0.908	-0.953	30.104	-0.063	-0.063	0.000	0.000	0.000
79	A	81	THR	0	-0.040	-0.031	31.880	0.000	0.000	0.000	0.000	0.000
80	A	82	GLU	-1	-0.907	-0.955	29.814	-0.096	-0.096	0.000	0.000	0.000
81	A	83	VAL	0	-0.040	-0.014	28.992	-0.005	-0.005	0.000	0.000	0.000
82	A	84	ALA	0	0.040	0.010	31.078	-0.003	-0.003	0.000	0.000	0.000
83	A	85	PRO	0	0.032	0.017	33.849	-0.002	-0.002	0.000	0.000	0.000
84	A	86	LEU	0	-0.013	0.006	26.992	-0.001	-0.001	0.000	0.000	0.000
85	A	87	MET	0	-0.015	-0.002	30.896	-0.002	-0.002	0.000	0.000	0.000
86	A	88	GLU	-1	-0.944	-0.968	32.442	-0.074	-0.074	0.000	0.000	0.000
87	A	89	ARG	1	0.951	0.975	30.843	0.113	0.113	0.000	0.000	0.000
88	A	90	LEU	0	0.006	0.011	28.155	-0.001	-0.001	0.000	0.000	0.000
89	A	91	VAL	0	-0.029	-0.009	32.288	0.000	0.000	0.000	0.000	0.000
90	A	92	ALA	0	-0.036	-0.012	35.331	0.002	0.002	0.000	0.000	0.000
91	A	93	ALA	0	-0.035	-0.007	33.043	0.003	0.003	0.000	0.000	0.000
92	A	94	GLY	0	-0.033	-0.021	34.229	-0.005	-0.005	0.000	0.000	0.000
93	A	95	GLY	0	0.008	0.018	32.638	-0.002	-0.002	0.000	0.000	0.000
94	A	96	GLN	0	-0.035	-0.013	32.845	0.009	0.009	0.000	0.000	0.000
95	A	97	LEU	0	-0.002	-0.013	33.142	-0.004	-0.004	0.000	0.000	0.000
96	A	98	LEU	0	-0.035	-0.016	30.110	0.006	0.006	0.000	0.000	0.000
97	A	99	ARG	1	0.828	0.903	31.807	0.063	0.063	0.000	0.000	0.000
98	A	100	PRO	0	0.021	0.009	33.250	-0.006	-0.006	0.000	0.000	0.000
99	A	101	ALA	0	0.040	0.014	32.907	0.001	0.001	0.000	0.000	0.000
100	A	102	ASP	-1	-0.807	-0.869	33.036	-0.050	-0.050	0.000	0.000	0.000
101	A	103	ALA	0	0.054	0.011	32.448	-0.005	-0.005	0.000	0.000	0.000
102	A	104	PRO	0	-0.045	0.003	28.324	0.005	0.005	0.000	0.000	0.000
103	A	105	PRO	0	0.033	-0.009	29.735	0.003	0.003	0.000	0.000	0.000
104	A	106	HIS	0	-0.068	-0.023	25.828	0.003	0.003	0.000	0.000	0.000
105	A	107	GLY	0	0.014	0.013	27.755	-0.002	-0.002	0.000	0.000	0.000
106	A	108	GLY	0	0.002	0.003	28.665	-0.007	-0.007	0.000	0.000	0.000
107	A	109	LEU	0	-0.031	-0.008	29.146	0.005	0.005	0.000	0.000	0.000
108	A	110	ARG	1	0.852	0.907	27.460	0.062	0.062	0.000	0.000	0.000
109	A	111	GLY	0	0.039	0.017	29.138	0.010	0.010	0.000	0.000	0.000
110	A	112	TYR	0	-0.050	-0.023	25.274	-0.002	-0.002	0.000	0.000	0.000
111	A	113	VAL	0	0.003	-0.008	28.771	0.011	0.011	0.000	0.000	0.000
112	A	114	ALA	0	-0.014	0.004	28.433	-0.011	-0.011	0.000	0.000	0.000
113	A	115	ASP	-1	-0.749	-0.852	26.626	-0.165	-0.165	0.000	0.000	0.000
114	A	116	PRO	0	0.006	-0.016	29.354	0.007	0.007	0.000	0.000	0.000
115	A	117	ASP	-1	-0.846	-0.909	28.521	-0.137	-0.137	0.000	0.000	0.000
116	A	118	GLY	0	-0.045	-0.026	29.892	0.003	0.003	0.000	0.000	0.000
117	A	119	HIS	0	-0.067	-0.043	24.334	0.000	0.000	0.000	0.000	0.000
118	A	120	ILE	0	-0.009	-0.004	25.504	0.004	0.004	0.000	0.000	0.000
119	A	121	TRP	0	0.039	0.010	20.556	-0.023	-0.023	0.000	0.000	0.000
120	A	122	GLU	-1	-0.912	-0.974	23.487	-0.107	-0.107	0.000	0.000	0.000
121	A	123	ILE	0	-0.038	-0.006	24.326	-0.016	-0.016	0.000	0.000	0.000
122	A	124	ALA	0	0.042	-0.005	24.237	0.015	0.015	0.000	0.000	0.000
123	A	125	PHE	0	0.015	0.024	25.395	-0.010	-0.010	0.000	0.000	0.000
124	A	126	ASN	0	0.015	-0.013	22.980	0.017	0.017	0.000	0.000	0.000
125	A	127	PRO	0	-0.001	-0.007	23.659	-0.008	-0.008	0.000	0.000	0.000
126	A	128	VAL	0	-0.011	0.008	22.455	0.003	0.003	0.000	0.000	0.000
127	A	129	TRP	0	-0.016	-0.004	17.428	-0.002	-0.002	0.000	0.000	0.000
128	A	130	PRO	0	-0.018	-0.003	18.213	-0.010	-0.010	0.000	0.000	0.000
129	A	131	ILE	0	0.022	0.021	18.084	-0.024	-0.024	0.000	0.000	0.000
130	A	132	GLY	0	0.001	0.000	16.992	0.024	0.024	0.000	0.000	0.000
131	A	133	ALA	0	-0.028	-0.023	18.014	0.001	0.001	0.000	0.000	0.000
132	A	134	ASP	-1	-0.890	-0.937	16.520	-0.240	-0.240	0.000	0.000	0.000
133	A	135	GLY	0	-0.002	0.001	16.312	-0.042	-0.042	0.000	0.000	0.000
134	A	136	SER	0	-0.034	-0.051	13.030	0.027	0.027	0.000	0.000	0.000
135	A	137	VAL	0	0.068	0.060	14.321	0.048	0.048	0.000	0.000	0.000
136	A	138	THR	0	-0.034	-0.012	12.609	-0.045	-0.045	0.000	0.000	0.000
137	A	139	PHE	0	0.013	0.001	14.379	0.031	0.031	0.000	0.000	0.000
138	A	140	ALA	0	0.005	0.001	16.350	0.016	0.016	0.000	0.000	0.000
139	A	141	ALA	0	-0.009	0.000	19.236	-0.005	-0.005	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)