FMO DATABASE

FMODB ID: 4J39N

Calculation Name: 5HS5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5HS5

Chain ID: A

ChEMBL ID:

UniProt ID: Q2G0D1

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	OptHSide
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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1001255.896928
FMO2-HF: Nuclear repulsion	952906.82651
FMO2-HF: Total energy	-48349.070419
FMO2-MP2: Total energy	-48490.509885

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:8:THR)

Summations of interaction energy for fragment #1(A:8: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.
-6.572	-2.765	0.348	-1.664	-2.49	0.01

Interaction energy analysis for fragmet #1(A:8:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.063 / q_NPA : 0.016

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].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	10	LEU	0	0.031	0.001	3.648	-1.879	0.099	0.027	-0.876	-1.129	0.005
4	A	11	GLY	0	0.004	0.002	2.775	-3.419	-2.196	0.314	-0.658	-0.879	0.004
5	A	12	PHE	0	0.082	0.042	3.521	-0.319	0.199	0.008	-0.126	-0.400	0.001
6	A	13	TYR	0	-0.011	-0.009	5.369	0.479	0.567	-0.001	-0.004	-0.082	0.000
7	A	14	LYS	1	0.917	0.955	7.034	-1.264	-1.264	0.000	0.000	0.000	0.000
8	A	15	GLN	0	-0.034	-0.020	6.167	-0.149	-0.149	0.000	0.000	0.000	0.000
9	A	16	TYR	0	0.025	0.025	9.301	0.026	0.026	0.000	0.000	0.000	0.000
10	A	17	LYS	1	0.883	0.919	11.422	-0.066	-0.066	0.000	0.000	0.000	0.000
11	A	18	ALA	0	-0.003	-0.003	12.391	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	19	LEU	0	0.056	0.020	13.267	-0.005	-0.005	0.000	0.000	0.000	0.000
13	A	20	SER	0	-0.017	-0.012	15.111	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	21	GLU	-1	-0.834	-0.900	16.917	0.079	0.079	0.000	0.000	0.000	0.000
15	A	22	TYR	0	-0.047	-0.014	18.042	0.003	0.003	0.000	0.000	0.000	0.000
16	A	23	ILE	0	0.022	-0.005	17.992	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	24	ASP	-1	-0.875	-0.914	21.179	0.020	0.020	0.000	0.000	0.000	0.000
18	A	25	LYS	1	0.768	0.843	22.206	-0.057	-0.057	0.000	0.000	0.000	0.000
19	A	26	LYS	1	0.782	0.911	23.895	-0.044	-0.044	0.000	0.000	0.000	0.000
20	A	27	TYR	0	-0.071	-0.078	23.794	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	28	LYS	1	0.922	0.970	26.375	-0.028	-0.028	0.000	0.000	0.000	0.000
22	A	29	LEU	0	-0.039	-0.011	24.622	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	30	SER	0	-0.009	-0.037	21.932	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	31	LEU	0	0.094	0.024	15.346	0.004	0.004	0.000	0.000	0.000	0.000
25	A	32	ASN	0	-0.007	-0.004	19.689	-0.024	-0.024	0.000	0.000	0.000	0.000
26	A	33	ASP	-1	-0.742	-0.813	22.035	-0.055	-0.055	0.000	0.000	0.000	0.000
27	A	34	LEU	0	0.034	0.019	20.104	0.004	0.004	0.000	0.000	0.000	0.000
28	A	35	ALA	0	0.036	0.026	20.173	0.001	0.001	0.000	0.000	0.000	0.000
29	A	36	VAL	0	-0.016	-0.011	21.906	0.004	0.004	0.000	0.000	0.000	0.000
30	A	37	LEU	0	-0.004	0.001	25.457	0.005	0.005	0.000	0.000	0.000	0.000
31	A	38	ASP	-1	-0.793	-0.879	22.885	-0.106	-0.106	0.000	0.000	0.000	0.000
32	A	39	LEU	0	0.024	0.026	24.720	0.005	0.005	0.000	0.000	0.000	0.000
33	A	40	THR	0	-0.113	-0.073	26.672	0.008	0.008	0.000	0.000	0.000	0.000
34	A	41	MET	0	0.005	0.000	27.301	0.006	0.006	0.000	0.000	0.000	0.000
35	A	42	LYS	1	0.798	0.897	22.458	0.118	0.118	0.000	0.000	0.000	0.000
36	A	43	HIS	0	-0.053	-0.037	28.227	0.011	0.011	0.000	0.000	0.000	0.000
37	A	44	CYS	0	-0.073	-0.040	32.059	0.002	0.002	0.000	0.000	0.000	0.000
38	A	45	LYS	1	0.927	0.958	32.915	0.032	0.032	0.000	0.000	0.000	0.000
39	A	46	ASP	-1	-0.892	-0.933	34.578	-0.024	-0.024	0.000	0.000	0.000	0.000
40	A	47	GLU	-1	-0.838	-0.887	37.601	-0.030	-0.030	0.000	0.000	0.000	0.000
41	A	48	LYS	1	0.792	0.883	37.909	0.027	0.027	0.000	0.000	0.000	0.000
42	A	49	VAL	0	0.053	0.030	35.370	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	50	LEU	0	-0.037	-0.013	38.299	0.001	0.001	0.000	0.000	0.000	0.000
44	A	51	MET	0	0.024	0.015	34.379	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	52	GLN	0	0.019	0.001	35.865	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	53	SER	0	0.047	0.034	36.293	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	54	PHE	0	0.012	0.011	28.928	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	55	LEU	0	-0.002	-0.018	31.770	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	56	LYS	1	0.808	0.909	31.398	0.088	0.088	0.000	0.000	0.000	0.000
50	A	57	THR	0	0.034	0.016	29.280	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	58	ALA	0	0.024	0.004	27.554	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	59	MET	0	-0.100	-0.054	26.530	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	60	ASP	-1	-0.828	-0.893	26.742	-0.115	-0.115	0.000	0.000	0.000	0.000
54	A	61	GLU	-1	-0.895	-0.955	24.454	-0.127	-0.127	0.000	0.000	0.000	0.000
55	A	62	LEU	0	-0.044	-0.024	21.342	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	63	ASP	-1	-0.915	-0.935	21.770	-0.200	-0.200	0.000	0.000	0.000	0.000
57	A	64	LEU	0	-0.035	-0.008	22.208	0.004	0.004	0.000	0.000	0.000	0.000
58	A	65	SER	0	0.019	-0.006	25.303	0.009	0.009	0.000	0.000	0.000	0.000
59	A	66	ARG	1	1.001	0.965	28.726	0.059	0.059	0.000	0.000	0.000	0.000
60	A	67	THR	0	-0.042	-0.029	31.337	0.002	0.002	0.000	0.000	0.000	0.000
61	A	68	LYS	1	0.986	0.988	23.187	0.123	0.123	0.000	0.000	0.000	0.000
62	A	69	LEU	0	0.066	0.053	26.662	0.004	0.004	0.000	0.000	0.000	0.000
63	A	70	LEU	0	-0.008	-0.009	29.202	0.006	0.006	0.000	0.000	0.000	0.000
64	A	71	VAL	0	-0.060	-0.016	29.281	0.006	0.006	0.000	0.000	0.000	0.000
65	A	72	SER	0	0.029	-0.018	26.514	0.002	0.002	0.000	0.000	0.000	0.000
66	A	73	ILE	0	-0.010	0.004	28.885	0.005	0.005	0.000	0.000	0.000	0.000
67	A	74	ARG	1	0.887	0.945	31.790	0.037	0.037	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.914	0.946	27.465	0.045	0.045	0.000	0.000	0.000	0.000
69	A	76	LEU	0	0.018	0.017	27.544	0.005	0.005	0.000	0.000	0.000	0.000
70	A	77	ILE	0	-0.049	-0.023	31.470	0.004	0.004	0.000	0.000	0.000	0.000
71	A	78	GLU	-1	-0.888	-0.924	34.060	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	79	LYS	1	0.767	0.870	30.905	0.012	0.012	0.000	0.000	0.000	0.000
73	A	80	GLU	-1	-0.917	-0.954	33.616	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	81	ARG	1	0.946	0.969	28.915	0.012	0.012	0.000	0.000	0.000	0.000
75	A	82	LEU	0	0.007	0.013	31.585	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	83	SER	0	0.009	0.005	34.076	0.004	0.004	0.000	0.000	0.000	0.000
77	A	84	LYS	1	0.925	0.951	37.569	0.020	0.020	0.000	0.000	0.000	0.000
78	A	85	VAL	0	-0.029	-0.017	39.874	0.003	0.003	0.000	0.000	0.000	0.000
79	A	86	ARG	1	0.862	0.912	43.385	0.021	0.021	0.000	0.000	0.000	0.000
80	A	87	SER	0	-0.013	0.039	45.801	0.001	0.001	0.000	0.000	0.000	0.000
81	A	88	SER	0	0.020	-0.013	48.040	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	89	LYS	1	0.900	0.929	51.130	0.026	0.026	0.000	0.000	0.000	0.000
83	A	90	ASP	-1	-0.765	-0.863	49.248	-0.026	-0.026	0.000	0.000	0.000	0.000
84	A	91	GLU	-1	-0.741	-0.875	48.675	-0.023	-0.023	0.000	0.000	0.000	0.000
85	A	92	ARG	1	0.902	0.956	46.192	0.028	0.028	0.000	0.000	0.000	0.000
86	A	93	LYS	1	0.834	0.914	44.368	0.029	0.029	0.000	0.000	0.000	0.000
87	A	94	ILE	0	-0.020	-0.004	40.356	0.002	0.002	0.000	0.000	0.000	0.000
88	A	95	TYR	0	0.014	-0.007	40.170	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	96	ILE	0	-0.021	-0.021	33.523	0.003	0.003	0.000	0.000	0.000	0.000
90	A	97	TYR	0	0.018	-0.009	36.381	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	98	LEU	0	0.027	0.036	30.929	0.002	0.002	0.000	0.000	0.000	0.000
92	A	99	ASN	0	0.004	0.014	35.491	0.002	0.002	0.000	0.000	0.000	0.000
93	A	100	ASN	0	0.076	0.017	36.359	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	101	ASP	-1	-0.851	-0.930	36.552	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	102	ASP	-1	-0.782	-0.888	33.741	-0.022	-0.022	0.000	0.000	0.000	0.000
96	A	103	ILE	0	-0.006	-0.001	32.259	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	104	SER	0	-0.007	0.004	31.530	0.000	0.000	0.000	0.000	0.000	0.000
98	A	105	LYS	1	0.817	0.902	31.166	0.011	0.011	0.000	0.000	0.000	0.000
99	A	106	PHE	0	-0.019	-0.003	24.823	0.001	0.001	0.000	0.000	0.000	0.000
100	A	107	ASN	0	0.009	-0.020	26.937	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	108	ALA	0	0.023	0.027	26.909	0.003	0.003	0.000	0.000	0.000	0.000
102	A	109	LEU	0	-0.049	-0.027	23.386	0.004	0.004	0.000	0.000	0.000	0.000
103	A	110	PHE	0	0.000	-0.015	20.868	0.001	0.001	0.000	0.000	0.000	0.000
104	A	111	GLU	-1	-0.892	-0.905	21.541	0.017	0.017	0.000	0.000	0.000	0.000
105	A	112	ASP	-1	-0.755	-0.831	22.050	0.048	0.048	0.000	0.000	0.000	0.000
106	A	113	VAL	0	-0.051	-0.051	18.406	0.009	0.009	0.000	0.000	0.000	0.000
107	A	114	GLU	-1	-0.919	-0.967	17.415	-0.046	-0.046	0.000	0.000	0.000	0.000
108	A	115	GLN	0	-0.012	0.002	16.979	0.021	0.021	0.000	0.000	0.000	0.000
109	A	116	PHE	0	-0.047	-0.029	15.933	0.034	0.034	0.000	0.000	0.000	0.000
110	A	117	LEU	0	0.002	-0.009	10.972	0.034	0.034	0.000	0.000	0.000	0.000
111	A	118	ASN	0	0.036	0.029	12.570	0.029	0.029	0.000	0.000	0.000	0.000
112	A	119	ILE	0	-0.035	-0.013	13.419	0.057	0.057	0.000	0.000	0.000	0.000
113	A	120	LEU	0	-0.055	-0.040	10.749	0.073	0.073	0.000	0.000	0.000	0.000
114	A	121	GLU	-1	-0.901	-0.935	8.185	0.035	0.035	0.000	0.000	0.000	0.000
115	A	122	HIS	0	-0.092	-0.025	9.182	0.092	0.092	0.000	0.000	0.000	0.000
116	A	123	HIS	1	0.920	0.966	9.485	-0.293	-0.293	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:THR)