FMO DATABASE

FMODB ID: VQ2Q1

Calculation Name: 3H8K-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3H8K

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UKV5

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	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	164
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1638956.869022
FMO2-HF: Nuclear repulsion	1572750.536414
FMO2-HF: Total energy	-66206.332608
FMO2-MP2: Total energy	-66393.942593

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:2:ALA)

Summations of interaction energy for fragment #1(A:2: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.
-13.809	-11.119	6.204	-3.376	-5.518	0.009

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.060 / q_NPA : 0.018

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	4	THR	0	0.010	-0.012	3.399	-0.806	0.745	0.029	-0.849	-0.731	-0.001
4	A	5	ALA	0	0.075	0.066	6.177	0.232	0.232	0.000	0.000	0.000	0.000
5	A	6	LEU	0	0.020	0.015	2.248	-0.467	-0.566	2.278	-0.562	-1.617	-0.003
6	A	7	LYS	1	0.877	0.924	1.995	-11.288	-10.236	3.899	-1.932	-3.019	0.013
7	A	8	ARG	1	0.806	0.894	4.682	-0.037	0.033	-0.001	-0.014	-0.055	0.000
8	A	9	LEU	0	0.030	0.018	7.450	0.059	0.059	0.000	0.000	0.000	0.000
9	A	10	MET	0	-0.017	-0.005	5.251	-0.050	0.066	-0.001	-0.019	-0.096	0.000
10	A	11	ALA	0	-0.073	-0.032	8.256	0.044	0.044	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.742	-0.852	10.331	-0.030	-0.030	0.000	0.000	0.000	0.000
12	A	13	TYR	0	0.002	-0.003	11.485	0.003	0.003	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.947	0.982	11.536	-0.368	-0.368	0.000	0.000	0.000	0.000
14	A	15	GLN	0	-0.010	-0.010	13.863	0.001	0.001	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.026	0.004	15.854	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	17	THR	0	-0.031	-0.020	15.930	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.099	-0.036	17.901	0.003	0.003	0.000	0.000	0.000	0.000
18	A	19	ASN	0	-0.067	-0.047	19.635	0.000	0.000	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.014	0.012	21.986	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	21	PRO	0	-0.027	0.002	21.633	0.002	0.002	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.854	-0.932	24.636	0.004	0.004	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.025	-0.010	27.773	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	24	ILE	0	-0.046	-0.024	22.429	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	25	VAL	0	0.017	0.013	22.019	0.006	0.006	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.014	-0.017	18.519	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.012	0.000	15.391	0.018	0.018	0.000	0.000	0.000	0.000
27	A	28	PRO	0	-0.040	-0.012	11.620	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	29	MET	0	-0.013	0.003	14.185	0.016	0.016	0.000	0.000	0.000	0.000
29	A	30	ASN	0	-0.010	-0.028	14.876	0.031	0.031	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.859	-0.912	10.855	-0.106	-0.106	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.956	-0.958	9.569	-0.318	-0.318	0.000	0.000	0.000	0.000
32	A	33	ASN	0	-0.034	-0.035	9.815	-0.161	-0.161	0.000	0.000	0.000	0.000
33	A	34	PHE	0	0.055	0.016	7.257	0.039	0.039	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.047	-0.014	6.592	-0.045	-0.045	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.838	-0.894	10.991	-0.205	-0.205	0.000	0.000	0.000	0.000
36	A	37	TRP	0	-0.046	-0.019	11.306	0.032	0.032	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.924	-0.958	16.146	-0.097	-0.097	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.014	-0.021	19.153	0.005	0.005	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.005	-0.001	21.632	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	41	ILE	0	0.001	0.005	24.931	0.005	0.005	0.000	0.000	0.000	0.000
41	A	42	MET	0	-0.016	0.007	27.269	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	43	GLY	0	0.003	0.006	30.914	0.001	0.001	0.000	0.000	0.000	0.000
43	A	44	PRO	0	-0.011	-0.014	32.479	0.002	0.002	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.885	-0.941	34.960	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	46	ASP	-1	-0.915	-0.940	38.363	0.001	0.001	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.046	-0.040	37.257	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	48	CYS	0	-0.076	-0.037	39.478	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	49	PHE	0	0.004	-0.018	35.584	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.849	-0.898	36.284	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	51	PHE	0	-0.022	-0.034	35.724	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.003	0.013	35.171	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	53	VAL	0	-0.017	-0.015	29.878	0.001	0.001	0.000	0.000	0.000	0.000
53	A	54	PHE	0	0.028	-0.010	29.343	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	55	PRO	0	-0.002	0.005	26.011	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.016	-0.005	23.672	0.000	0.000	0.000	0.000	0.000	0.000
56	A	57	ILE	0	0.009	0.014	19.610	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	58	LEU	0	-0.010	-0.017	17.291	0.010	0.010	0.000	0.000	0.000	0.000
58	A	59	SER	0	-0.045	-0.040	15.804	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	60	PHE	0	-0.027	-0.019	11.915	0.016	0.016	0.000	0.000	0.000	0.000
60	A	61	PRO	0	-0.015	0.010	13.055	-0.050	-0.050	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.003	-0.021	8.227	-0.039	-0.039	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.842	-0.910	9.312	-0.428	-0.428	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.015	0.004	9.997	0.072	0.072	0.000	0.000	0.000	0.000
64	A	65	PRO	0	-0.046	-0.041	9.760	-0.061	-0.061	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.043	-0.032	13.032	0.045	0.045	0.000	0.000	0.000	0.000
66	A	67	SER	0	-0.008	-0.021	14.973	0.037	0.037	0.000	0.000	0.000	0.000
67	A	68	PRO	0	-0.006	0.003	15.501	-0.017	-0.017	0.000	0.000	0.000	0.000
68	A	69	PRO	0	-0.023	-0.012	15.465	-0.025	-0.025	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.935	0.962	17.040	0.219	0.219	0.000	0.000	0.000	0.000
70	A	71	MET	0	0.044	0.028	19.376	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	72	ARG	1	0.854	0.923	22.011	0.103	0.103	0.000	0.000	0.000	0.000
72	A	73	PHE	0	0.051	0.025	24.618	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	74	THR	0	-0.056	-0.044	25.397	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	75	CYS	0	-0.023	0.022	28.208	0.002	0.002	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.805	-0.891	31.506	-0.039	-0.039	0.000	0.000	0.000	0.000
76	A	77	MET	0	0.006	0.001	30.795	0.003	0.003	0.000	0.000	0.000	0.000
77	A	78	PHE	0	-0.014	-0.013	34.596	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	79	HIS	0	0.050	0.004	33.926	0.000	0.000	0.000	0.000	0.000	0.000
79	A	80	PRO	0	-0.027	-0.005	35.321	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	81	ASN	0	0.051	0.013	31.280	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.031	-0.015	29.877	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	83	TYR	0	0.048	0.016	30.223	0.002	0.002	0.000	0.000	0.000	0.000
83	A	84	PRO	0	-0.009	-0.014	32.281	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.830	-0.885	29.878	-0.078	-0.078	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.044	0.021	28.958	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.737	0.865	25.760	0.078	0.078	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.054	0.033	25.400	0.006	0.006	0.000	0.000	0.000	0.000
88	A	89	CYS	0	-0.110	-0.051	26.241	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	90	ILE	0	0.075	0.044	25.705	0.005	0.005	0.000	0.000	0.000	0.000
90	A	91	SER	0	0.031	-0.004	26.709	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.014	0.006	22.352	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.046	-0.040	21.159	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	94	HIS	0	-0.028	-0.007	23.025	-0.018	-0.018	0.000	0.000	0.000	0.000
94	A	95	ALA	0	0.015	-0.002	21.843	0.004	0.004	0.000	0.000	0.000	0.000
95	A	96	PRO	0	-0.025	-0.022	21.834	0.006	0.006	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.018	0.007	24.542	-0.009	-0.009	0.000	0.000	0.000	0.000
97	A	98	ASP	-1	-0.973	-0.977	27.315	-0.039	-0.039	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.859	-0.927	29.980	-0.056	-0.056	0.000	0.000	0.000	0.000
99	A	100	PRO	0	-0.033	-0.032	30.524	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	101	MET	0	-0.041	-0.020	28.981	0.000	0.000	0.000	0.000	0.000	0.000
101	A	102	GLY	0	-0.036	-0.011	32.289	0.000	0.000	0.000	0.000	0.000	0.000
102	A	103	TYR	0	-0.032	0.006	27.756	0.002	0.002	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.859	-0.948	33.559	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	105	SER	0	-0.070	-0.042	35.069	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.065	-0.036	33.493	0.002	0.002	0.000	0.000	0.000	0.000
106	A	107	ALA	0	0.001	0.028	30.755	0.002	0.002	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.819	-0.897	25.361	-0.020	-0.020	0.000	0.000	0.000	0.000
108	A	109	ARG	1	0.860	0.930	24.538	0.037	0.037	0.000	0.000	0.000	0.000
109	A	110	TRP	0	-0.008	0.004	15.394	0.009	0.009	0.000	0.000	0.000	0.000
110	A	111	SER	0	0.020	-0.008	19.789	0.005	0.005	0.000	0.000	0.000	0.000
111	A	112	PRO	0	0.014	0.000	15.479	0.005	0.005	0.000	0.000	0.000	0.000
112	A	113	VAL	0	-0.023	0.003	16.719	0.024	0.024	0.000	0.000	0.000	0.000
113	A	114	GLN	0	-0.006	0.010	18.904	0.020	0.020	0.000	0.000	0.000	0.000
114	A	115	SER	0	-0.004	-0.015	16.072	0.004	0.004	0.000	0.000	0.000	0.000
115	A	116	VAL	0	0.062	0.020	14.524	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.934	-0.963	17.341	0.048	0.048	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.885	0.942	19.856	-0.046	-0.046	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.005	0.009	18.168	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	120	LEU	0	0.019	0.006	20.086	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.020	0.010	23.322	0.002	0.002	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.018	0.004	25.064	0.001	0.001	0.000	0.000	0.000	0.000
122	A	123	VAL	0	0.009	-0.012	25.199	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	124	VAL	0	0.010	0.001	27.309	0.000	0.000	0.000	0.000	0.000	0.000
124	A	125	SER	0	-0.002	-0.025	29.380	0.002	0.002	0.000	0.000	0.000	0.000
125	A	126	MET	0	-0.028	0.001	30.086	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	127	LEU	0	-0.053	-0.023	30.527	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	128	ALA	0	0.002	0.002	33.440	0.000	0.000	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.941	-0.942	34.453	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	130	PRO	0	-0.039	-0.031	35.547	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	131	ASN	0	-0.049	-0.031	33.650	0.002	0.002	0.000	0.000	0.000	0.000
131	A	132	ASP	-1	-0.864	-0.927	35.115	-0.030	-0.030	0.000	0.000	0.000	0.000
132	A	133	GLU	-1	-0.835	-0.900	30.791	-0.027	-0.027	0.000	0.000	0.000	0.000
133	A	134	SER	0	0.008	-0.030	31.801	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	135	GLY	0	-0.012	0.010	34.240	-0.002	-0.002	0.000	0.000	0.000	0.000
135	A	136	ALA	0	-0.010	-0.001	32.461	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	137	ASN	0	-0.008	0.000	34.394	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	138	VAL	0	0.087	0.028	37.069	0.003	0.003	0.000	0.000	0.000	0.000
138	A	139	ASP	-1	-0.868	-0.909	40.334	-0.029	-0.029	0.000	0.000	0.000	0.000
139	A	140	ALA	0	-0.002	0.011	38.428	0.002	0.002	0.000	0.000	0.000	0.000
140	A	141	SER	0	-0.024	-0.045	38.801	0.001	0.001	0.000	0.000	0.000	0.000
141	A	142	LYS	1	0.772	0.871	40.976	0.032	0.032	0.000	0.000	0.000	0.000
142	A	143	MET	0	0.005	0.025	43.802	0.002	0.002	0.000	0.000	0.000	0.000
143	A	144	TRP	0	0.030	0.018	40.742	0.002	0.002	0.000	0.000	0.000	0.000
144	A	145	ARG	1	0.792	0.864	43.485	0.021	0.021	0.000	0.000	0.000	0.000
145	A	146	ASP	-1	-0.844	-0.890	46.058	-0.018	-0.018	0.000	0.000	0.000	0.000
146	A	147	ASP	-1	-0.874	-0.930	47.769	-0.016	-0.016	0.000	0.000	0.000	0.000
147	A	148	ARG	1	0.901	0.958	44.356	0.013	0.013	0.000	0.000	0.000	0.000
148	A	149	GLU	-1	-0.793	-0.902	46.331	-0.011	-0.011	0.000	0.000	0.000	0.000
149	A	150	GLN	0	-0.066	-0.038	47.356	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	151	PHE	0	0.023	0.002	38.606	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	152	TYR	0	0.010	-0.009	43.091	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	153	LYS	1	0.762	0.879	44.119	0.014	0.014	0.000	0.000	0.000	0.000
153	A	154	ILE	0	0.016	0.008	41.096	0.000	0.000	0.000	0.000	0.000	0.000
154	A	155	ALA	0	0.026	0.019	39.627	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	156	LYS	1	0.905	0.939	39.697	0.011	0.011	0.000	0.000	0.000	0.000
156	A	157	GLN	0	-0.028	-0.019	41.701	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	158	ILE	0	-0.036	-0.009	35.919	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	159	VAL	0	0.025	0.028	37.097	-0.002	-0.002	0.000	0.000	0.000	0.000
159	A	160	GLN	0	-0.022	-0.006	37.812	-0.001	-0.001	0.000	0.000	0.000	0.000
160	A	161	LYS	1	0.788	0.874	37.682	0.033	0.033	0.000	0.000	0.000	0.000
161	A	162	SER	0	-0.080	-0.037	33.420	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	163	LEU	0	0.006	0.011	34.133	-0.001	-0.001	0.000	0.000	0.000	0.000
163	A	164	GLY	0	-0.035	-0.009	36.685	0.001	0.001	0.000	0.000	0.000	0.000
164	A	165	LEU	0	-0.087	-0.040	38.449	0.002	0.002	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)