FMO DATABASE

FMODB ID: 94J92

Calculation Name: 2FHQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2FHQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q8A7U5

Base Structure: X-ray

Registration Date: 2023-09-20

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	135
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1169373.736179
FMO2-HF: Nuclear repulsion	1116214.650183
FMO2-HF: Total energy	-53159.085996
FMO2-MP2: Total energy	-53312.973933

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:THR)

Summations of interaction energy for fragment #1(A:3: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.
-1.493	0.324	-0.017	-0.812	-0.989	0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.007 / q_NPA : -0.017

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	5	THR	0	0.020	0.010	3.802	-0.098	1.719	-0.017	-0.812	-0.989	0.002
4	A	6	MET	0	0.047	0.008	5.890	0.359	0.359	0.000	0.000	0.000	0.000
5	A	7	LYS	1	0.918	0.969	8.808	1.031	1.031	0.000	0.000	0.000	0.000
6	A	8	GLU	-1	-0.836	-0.927	5.725	-4.075	-4.075	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.919	0.970	5.908	0.807	0.807	0.000	0.000	0.000	0.000
8	A	10	ALA	0	0.050	0.021	9.196	0.217	0.217	0.000	0.000	0.000	0.000
9	A	11	VAL	0	-0.042	-0.013	12.185	0.113	0.113	0.000	0.000	0.000	0.000
10	A	12	GLU	-1	-0.907	-0.961	8.720	0.058	0.058	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.021	-0.017	12.578	0.077	0.077	0.000	0.000	0.000	0.000
12	A	14	LEU	0	0.004	0.010	14.740	0.049	0.049	0.000	0.000	0.000	0.000
13	A	15	GLN	0	-0.066	-0.041	14.700	0.052	0.052	0.000	0.000	0.000	0.000
14	A	16	LYS	1	0.818	0.920	14.855	0.071	0.071	0.000	0.000	0.000	0.000
15	A	17	CYS	0	-0.046	0.006	18.694	0.007	0.007	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.845	-0.930	21.335	-0.094	-0.094	0.000	0.000	0.000	0.000
17	A	19	VAL	0	-0.050	-0.011	24.546	0.002	0.002	0.000	0.000	0.000	0.000
18	A	20	VAL	0	-0.015	-0.004	23.022	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	21	THR	0	-0.037	-0.016	25.491	0.019	0.019	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.008	0.000	26.745	-0.016	-0.016	0.000	0.000	0.000	0.000
21	A	23	ALA	0	-0.022	-0.025	29.131	0.012	0.012	0.000	0.000	0.000	0.000
22	A	24	SER	0	-0.021	-0.034	30.974	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	25	VAL	0	-0.001	-0.006	33.729	0.001	0.001	0.000	0.000	0.000	0.000
24	A	26	ASN	0	0.050	0.032	36.062	0.000	0.000	0.000	0.000	0.000	0.000
25	A	27	LYS	1	0.988	0.970	39.705	0.061	0.061	0.000	0.000	0.000	0.000
26	A	28	GLU	-1	-0.982	-0.995	42.490	-0.058	-0.058	0.000	0.000	0.000	0.000
27	A	29	GLY	0	-0.019	0.008	39.213	0.001	0.001	0.000	0.000	0.000	0.000
28	A	30	TYR	0	-0.023	-0.007	38.054	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	31	PRO	0	0.007	0.013	33.026	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	32	ARG	1	0.906	0.948	34.508	0.080	0.080	0.000	0.000	0.000	0.000
31	A	33	PRO	0	0.012	0.014	30.809	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.006	-0.014	31.656	0.009	0.009	0.000	0.000	0.000	0.000
33	A	35	PRO	0	0.009	0.014	29.939	-0.010	-0.010	0.000	0.000	0.000	0.000
34	A	36	MET	0	-0.007	-0.009	29.241	0.008	0.008	0.000	0.000	0.000	0.000
35	A	37	SER	0	0.037	0.013	28.449	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	38	LYS	1	0.848	0.926	20.748	0.138	0.138	0.000	0.000	0.000	0.000
37	A	39	ILE	0	-0.013	-0.007	26.526	0.005	0.005	0.000	0.000	0.000	0.000
38	A	40	ALA	0	0.036	0.018	24.854	0.006	0.006	0.000	0.000	0.000	0.000
39	A	41	ALA	0	-0.005	-0.010	20.909	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.894	-0.924	20.494	-0.204	-0.204	0.000	0.000	0.000	0.000
41	A	43	GLY	0	-0.016	-0.029	16.421	-0.037	-0.037	0.000	0.000	0.000	0.000
42	A	44	ILE	0	0.005	-0.014	14.833	0.008	0.008	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.089	-0.041	17.973	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	46	THR	0	0.048	0.027	19.819	0.016	0.016	0.000	0.000	0.000	0.000
45	A	47	ILE	0	-0.033	-0.012	21.002	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	48	TRP	0	0.048	0.020	24.600	0.013	0.013	0.000	0.000	0.000	0.000
47	A	49	MET	0	-0.012	-0.002	27.508	0.002	0.002	0.000	0.000	0.000	0.000
48	A	50	SER	0	0.023	0.021	30.368	0.000	0.000	0.000	0.000	0.000	0.000
49	A	51	THR	0	-0.034	-0.025	34.107	0.001	0.001	0.000	0.000	0.000	0.000
50	A	52	GLY	0	0.080	0.047	37.079	0.002	0.002	0.000	0.000	0.000	0.000
51	A	53	ALA	0	-0.033	-0.034	40.713	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.895	-0.950	42.632	-0.056	-0.056	0.000	0.000	0.000	0.000
53	A	55	SER	0	-0.051	0.005	39.515	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	56	LEU	0	0.045	-0.011	40.175	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.813	0.925	33.166	0.096	0.096	0.000	0.000	0.000	0.000
56	A	58	THR	0	0.024	0.010	37.564	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	59	ILE	0	0.023	0.013	39.187	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	60	ASP	-1	-0.820	-0.896	37.569	-0.085	-0.085	0.000	0.000	0.000	0.000
59	A	61	PHE	0	0.001	-0.024	32.037	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.039	-0.003	37.051	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	63	SER	0	-0.090	-0.028	40.054	0.002	0.002	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.018	-0.023	35.610	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	65	PRO	0	0.094	0.053	32.984	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	66	LYS	1	0.925	0.972	31.042	0.122	0.122	0.000	0.000	0.000	0.000
65	A	67	ALA	0	0.032	0.014	28.864	0.009	0.009	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.034	-0.013	26.184	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	69	LEU	0	0.016	0.022	22.467	0.015	0.015	0.000	0.000	0.000	0.000
68	A	70	CYS	0	-0.045	-0.018	22.017	-0.019	-0.019	0.000	0.000	0.000	0.000
69	A	71	PHE	0	0.042	0.013	16.702	0.015	0.015	0.000	0.000	0.000	0.000
70	A	72	GLN	0	-0.001	-0.012	19.584	-0.027	-0.027	0.000	0.000	0.000	0.000
71	A	73	GLU	-1	-0.768	-0.895	17.737	-0.058	-0.058	0.000	0.000	0.000	0.000
72	A	74	LYS	1	0.914	0.955	17.030	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	75	GLY	0	-0.008	0.002	17.822	0.004	0.004	0.000	0.000	0.000	0.000
74	A	76	ASP	-1	-0.797	-0.882	13.485	-0.258	-0.258	0.000	0.000	0.000	0.000
75	A	77	SER	0	-0.036	-0.036	16.434	0.012	0.012	0.000	0.000	0.000	0.000
76	A	78	VAL	0	-0.005	-0.005	15.021	-0.057	-0.057	0.000	0.000	0.000	0.000
77	A	79	ALA	0	-0.008	-0.005	17.732	0.038	0.038	0.000	0.000	0.000	0.000
78	A	80	LEU	0	0.004	-0.010	17.937	-0.036	-0.036	0.000	0.000	0.000	0.000
79	A	81	MET	0	-0.022	-0.024	21.407	0.032	0.032	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.024	0.004	23.560	-0.029	-0.029	0.000	0.000	0.000	0.000
81	A	83	GLU	-1	-0.873	-0.909	25.998	-0.168	-0.168	0.000	0.000	0.000	0.000
82	A	84	VAL	0	-0.036	-0.015	28.485	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	85	GLU	-1	-0.924	-0.948	30.795	-0.143	-0.143	0.000	0.000	0.000	0.000
84	A	86	VAL	0	0.005	-0.011	33.294	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	87	VAL	0	-0.032	-0.018	32.903	0.002	0.002	0.000	0.000	0.000	0.000
86	A	88	THR	0	0.008	-0.016	36.259	0.002	0.002	0.000	0.000	0.000	0.000
87	A	89	ASP	-1	-0.863	-0.928	36.152	-0.081	-0.081	0.000	0.000	0.000	0.000
88	A	90	GLU	-1	-0.895	-0.959	37.881	-0.056	-0.056	0.000	0.000	0.000	0.000
89	A	91	LYS	1	0.928	0.966	34.018	0.087	0.087	0.000	0.000	0.000	0.000
90	A	92	LEU	0	0.001	0.008	31.551	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	93	LYS	1	0.830	0.923	34.588	0.062	0.062	0.000	0.000	0.000	0.000
92	A	94	GLN	0	0.003	0.006	36.890	0.004	0.004	0.000	0.000	0.000	0.000
93	A	95	GLU	-1	-0.934	-0.965	32.309	-0.083	-0.083	0.000	0.000	0.000	0.000
94	A	96	LEU	0	-0.031	-0.020	29.337	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	97	TRP	0	0.002	0.028	32.656	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	98	GLN	0	-0.024	-0.021	30.930	0.006	0.006	0.000	0.000	0.000	0.000
97	A	99	ASP	-1	-0.856	-0.931	34.593	-0.031	-0.031	0.000	0.000	0.000	0.000
98	A	100	TRP	0	-0.038	-0.027	31.845	0.002	0.002	0.000	0.000	0.000	0.000
99	A	101	PHE	0	-0.005	-0.017	33.177	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	102	ILE	0	-0.003	0.008	38.235	0.000	0.000	0.000	0.000	0.000	0.000
101	A	103	GLU	-1	-0.979	-0.994	40.588	-0.032	-0.032	0.000	0.000	0.000	0.000
102	A	104	HIS	0	-0.058	-0.011	37.870	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	105	PHE	0	-0.048	-0.028	37.566	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	106	PRO	0	0.050	0.017	43.027	0.001	0.001	0.000	0.000	0.000	0.000
105	A	107	GLY	0	-0.043	-0.016	45.871	0.002	0.002	0.000	0.000	0.000	0.000
106	A	108	GLY	0	0.000	0.002	43.025	0.001	0.001	0.000	0.000	0.000	0.000
107	A	109	PRO	0	0.015	-0.004	39.602	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	110	THR	0	0.008	-0.008	41.185	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	111	ASP	-1	-0.836	-0.895	43.398	-0.046	-0.046	0.000	0.000	0.000	0.000
110	A	112	PRO	0	0.002	-0.003	43.657	-0.004	-0.004	0.000	0.000	0.000	0.000
111	A	113	GLY	0	-0.014	-0.006	44.517	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	114	TYR	0	-0.081	-0.055	36.022	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.006	-0.002	37.286	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	116	LEU	0	0.009	0.004	32.620	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.055	-0.026	31.951	0.000	0.000	0.000	0.000	0.000	0.000
116	A	118	LYS	1	0.951	0.999	27.452	0.163	0.163	0.000	0.000	0.000	0.000
117	A	119	PHE	0	-0.005	-0.008	22.921	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	120	THR	0	0.043	0.014	24.180	-0.018	-0.018	0.000	0.000	0.000	0.000
119	A	121	ALA	0	-0.034	-0.007	20.495	0.007	0.007	0.000	0.000	0.000	0.000
120	A	122	ASN	0	-0.021	-0.030	22.053	-0.025	-0.025	0.000	0.000	0.000	0.000
121	A	123	HIS	0	-0.044	-0.021	19.814	-0.030	-0.030	0.000	0.000	0.000	0.000
122	A	124	ALA	0	-0.017	-0.005	16.088	0.012	0.012	0.000	0.000	0.000	0.000
123	A	125	THR	0	0.006	0.005	17.374	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	126	TYR	0	0.015	-0.007	12.996	-0.057	-0.057	0.000	0.000	0.000	0.000
125	A	127	TRP	0	-0.002	0.018	14.966	0.020	0.020	0.000	0.000	0.000	0.000
126	A	128	ILE	0	0.041	0.014	9.939	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.912	-0.959	8.452	-0.343	-0.343	0.000	0.000	0.000	0.000
128	A	130	GLY	0	-0.027	0.007	11.931	0.017	0.017	0.000	0.000	0.000	0.000
129	A	131	THR	0	-0.049	-0.033	11.568	0.033	0.033	0.000	0.000	0.000	0.000
130	A	132	PHE	0	-0.014	-0.018	13.659	-0.044	-0.044	0.000	0.000	0.000	0.000
131	A	133	ILE	0	-0.034	-0.011	10.550	-0.017	-0.017	0.000	0.000	0.000	0.000
132	A	134	HIS	0	0.041	0.016	14.527	-0.025	-0.025	0.000	0.000	0.000	0.000
133	A	135	LYS	1	0.846	0.938	11.442	0.822	0.822	0.000	0.000	0.000	0.000
134	A	136	LYS	1	1.018	1.025	16.573	0.348	0.348	0.000	0.000	0.000	0.000
135	A	137	LEU	0	-0.074	-0.058	15.577	-0.073	-0.073	0.000	0.000	0.000	0.000

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