FMO DATABASE

FMODB ID: KR6Y3

Calculation Name: 2HSN-A-Xray311

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2HSN

Chain ID: A

ChEMBL ID:

UniProt ID: P46672

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	160
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1303462.18721
FMO2-HF: Nuclear repulsion	1240576.144849
FMO2-HF: Total energy	-62886.042361
FMO2-MP2: Total energy	-63072.232901

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:MET )

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

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.
-14.762	-5.923	3.17	-4.136	-7.877	-0.009

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

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 : -0.009

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	PHE	0	-0.056	-0.014	3.031	-3.560	0.076	0.455	-1.844	-2.247	0.014
4	A	6	LEU	0	0.058	0.044	4.273	-1.466	-1.240	0.001	-0.037	-0.190	0.000
5	A	7	ILE	0	-0.025	-0.012	7.102	0.211	0.211	0.000	0.000	0.000	0.000
6	A	8	SER	0	0.040	0.005	9.254	-0.137	-0.137	0.000	0.000	0.000	0.000
7	A	9	PHE	0	-0.014	-0.017	12.871	0.033	0.033	0.000	0.000	0.000	0.000
8	A	10	ASP	-1	-0.803	-0.886	16.019	0.024	0.024	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.922	0.955	16.851	0.060	0.060	0.000	0.000	0.000	0.000
10	A	12	SER	0	-0.068	-0.027	21.262	-0.003	-0.003	0.000	0.000	0.000	0.000
11	A	13	LYS	1	1.010	1.042	21.589	-0.036	-0.036	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.904	0.943	24.590	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	15	HIS	0	-0.034	-0.042	22.319	0.008	0.008	0.000	0.000	0.000	0.000
14	A	16	PRO	0	0.028	0.000	27.041	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	17	ALA	0	0.073	0.040	27.195	0.001	0.001	0.000	0.000	0.000	0.000
16	A	18	HIS	0	0.064	0.020	26.592	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	19	LEU	0	-0.030	-0.017	23.529	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	20	GLN	0	0.007	0.013	22.518	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	21	LEU	0	0.012	0.018	21.601	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	22	ALA	0	0.004	0.002	21.868	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	23	ASN	0	-0.051	-0.042	18.914	0.004	0.004	0.000	0.000	0.000	0.000
22	A	24	ASN	0	0.038	0.002	17.478	0.006	0.006	0.000	0.000	0.000	0.000
23	A	25	LEU	0	0.006	0.010	17.398	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	26	LYS	1	0.944	0.970	16.769	-0.027	-0.027	0.000	0.000	0.000	0.000
25	A	27	ILE	0	0.011	0.006	12.185	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	28	ALA	0	0.011	0.000	12.634	-0.041	-0.041	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.003	0.000	14.064	-0.030	-0.030	0.000	0.000	0.000	0.000
28	A	30	ALA	0	-0.007	0.004	10.445	-0.019	-0.019	0.000	0.000	0.000	0.000
29	A	31	LEU	0	-0.001	-0.002	8.317	-0.093	-0.093	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.936	-0.971	10.341	-0.245	-0.245	0.000	0.000	0.000	0.000
31	A	33	TYR	0	-0.052	-0.022	12.647	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	34	ALA	0	-0.015	0.016	7.186	-0.019	-0.019	0.000	0.000	0.000	0.000
33	A	35	SER	0	0.019	-0.009	7.678	0.027	0.027	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.922	0.979	4.879	-0.076	-0.076	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.018	-0.022	2.432	-2.002	-0.703	1.553	-0.983	-1.870	-0.008
36	A	38	LEU	0	-0.022	0.001	2.804	-2.097	-1.405	0.939	-0.156	-1.476	-0.008
37	A	39	LYS	1	0.855	0.928	2.990	1.161	2.028	0.040	-0.216	-0.692	0.000
38	A	40	PRO	0	-0.047	-0.016	2.945	-3.746	-1.831	0.181	-0.867	-1.229	-0.007
39	A	41	GLU	-1	-0.896	-0.933	3.885	-2.198	-1.994	0.001	-0.033	-0.173	0.000
40	A	42	VAL	0	-0.026	-0.026	5.422	0.546	0.546	0.000	0.000	0.000	0.000
41	A	43	ASP	-1	-0.857	-0.931	9.148	-0.166	-0.166	0.000	0.000	0.000	0.000
42	A	44	ASN	0	-0.070	-0.054	11.406	0.060	0.060	0.000	0.000	0.000	0.000
43	A	45	ASP	-1	-0.925	-0.960	15.052	-0.053	-0.053	0.000	0.000	0.000	0.000
44	A	46	ASN	0	0.087	0.064	14.337	0.009	0.009	0.000	0.000	0.000	0.000
45	A	47	ALA	0	-0.034	-0.030	16.710	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	48	ALA	0	-0.041	-0.021	18.296	0.002	0.002	0.000	0.000	0.000	0.000
47	A	49	MET	0	-0.028	0.013	15.205	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	50	GLU	-1	-0.901	-0.955	12.758	0.198	0.198	0.000	0.000	0.000	0.000
49	A	51	LEU	0	-0.011	-0.011	6.570	-0.013	-0.013	0.000	0.000	0.000	0.000
50	A	52	ARG	1	0.927	0.968	9.106	-0.185	-0.185	0.000	0.000	0.000	0.000
51	A	53	ASN	0	0.014	-0.008	7.189	0.446	0.446	0.000	0.000	0.000	0.000
52	A	54	THR	0	-0.042	-0.040	6.175	-0.580	-0.580	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.895	0.949	6.278	-0.742	-0.742	0.000	0.000	0.000	0.000
54	A	56	GLU	-1	-0.875	-0.927	9.684	-0.028	-0.028	0.000	0.000	0.000	0.000
55	A	57	PRO	0	-0.035	-0.007	13.261	0.049	0.049	0.000	0.000	0.000	0.000
56	A	58	PHE	0	-0.021	-0.019	16.050	-0.024	-0.024	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.006	-0.004	18.578	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	60	LEU	0	-0.004	0.005	20.959	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	61	PHE	0	0.030	0.003	21.286	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	62	ASP	-1	-0.870	-0.927	24.958	0.005	0.005	0.000	0.000	0.000	0.000
61	A	63	ALA	0	0.045	0.007	27.918	0.003	0.003	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.001	-0.008	31.170	0.002	0.002	0.000	0.000	0.000	0.000
63	A	65	ALA	0	-0.002	-0.012	27.329	0.002	0.002	0.000	0.000	0.000	0.000
64	A	66	ILE	0	-0.015	0.000	27.418	0.003	0.003	0.000	0.000	0.000	0.000
65	A	67	LEU	0	-0.022	-0.009	29.601	0.002	0.002	0.000	0.000	0.000	0.000
66	A	68	ARG	1	0.845	0.899	31.444	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	69	TYR	0	-0.015	0.009	25.042	0.002	0.002	0.000	0.000	0.000	0.000
68	A	70	VAL	0	-0.070	-0.039	30.102	0.002	0.002	0.000	0.000	0.000	0.000
69	A	71	MET	0	-0.093	-0.041	32.123	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	72	ASP	-1	-0.944	-0.961	32.205	0.029	0.029	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.830	-0.902	33.216	0.015	0.015	0.000	0.000	0.000	0.000
72	A	74	PHE	0	0.016	-0.014	28.962	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.869	-0.917	33.777	0.016	0.016	0.000	0.000	0.000	0.000
74	A	76	GLY	0	-0.026	-0.024	37.224	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	77	GLN	0	-0.025	-0.036	30.985	0.000	0.000	0.000	0.000	0.000	0.000
76	A	78	THR	0	0.026	0.010	36.256	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	79	SER	0	-0.072	-0.032	38.178	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	80	ASP	-1	-0.847	-0.915	40.696	0.007	0.007	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.882	0.923	43.037	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	82	TYR	0	0.024	0.010	33.122	0.000	0.000	0.000	0.000	0.000	0.000
81	A	83	GLN	0	0.069	0.029	35.538	0.000	0.000	0.000	0.000	0.000	0.000
82	A	84	PHE	0	-0.017	-0.001	39.279	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	85	ALA	0	0.029	0.004	39.305	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	86	LEU	0	-0.026	-0.015	33.908	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	87	ALA	0	-0.013	-0.013	36.964	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	88	SER	0	-0.079	-0.030	38.442	0.000	0.000	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.016	0.000	40.922	0.000	0.000	0.000	0.000	0.000	0.000
88	A	90	GLN	0	0.072	0.038	33.032	0.000	0.000	0.000	0.000	0.000	0.000
89	A	91	ASN	0	0.026	0.005	36.316	0.000	0.000	0.000	0.000	0.000	0.000
90	A	92	LEU	0	0.004	-0.006	37.373	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.018	-0.004	37.079	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	94	TYR	0	-0.036	-0.003	31.117	0.000	0.000	0.000	0.000	0.000	0.000
93	A	95	HIS	0	-0.075	-0.024	36.178	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.938	0.956	36.376	0.010	0.010	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.926	-0.950	39.822	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.012	0.003	42.124	0.000	0.000	0.000	0.000	0.000	0.000
97	A	99	PRO	0	-0.002	0.009	44.058	0.000	0.000	0.000	0.000	0.000	0.000
98	A	100	GLN	0	0.045	-0.001	47.198	0.001	0.001	0.000	0.000	0.000	0.000
99	A	101	GLN	0	0.036	0.022	49.819	0.000	0.000	0.000	0.000	0.000	0.000
100	A	102	HIS	0	0.006	-0.009	47.457	0.000	0.000	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.023	0.022	45.499	0.000	0.000	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.854	-0.890	47.859	0.002	0.002	0.000	0.000	0.000	0.000
103	A	105	VAL	0	-0.005	-0.004	51.380	0.000	0.000	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.051	-0.020	45.028	0.000	0.000	0.000	0.000	0.000	0.000
105	A	107	THR	0	0.018	-0.024	46.691	0.000	0.000	0.000	0.000	0.000	0.000
106	A	108	ASN	0	0.032	0.005	48.775	0.000	0.000	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.939	0.972	48.944	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	110	ALA	0	-0.015	0.002	46.705	0.000	0.000	0.000	0.000	0.000	0.000
109	A	111	ILE	0	-0.066	-0.035	48.535	0.001	0.001	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.948	-0.938	51.221	0.004	0.004	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.048	-0.044	49.885	0.000	0.000	0.000	0.000	0.000	0.000
112	A	114	TYR	0	-0.049	-0.024	46.389	0.000	0.000	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.022	-0.019	46.758	0.001	0.001	0.000	0.000	0.000	0.000
114	A	116	VAL	0	0.087	0.038	49.328	0.000	0.000	0.000	0.000	0.000	0.000
115	A	117	GLU	-1	-0.876	-0.917	50.151	0.007	0.007	0.000	0.000	0.000	0.000
116	A	118	LEU	0	-0.016	-0.016	47.589	0.000	0.000	0.000	0.000	0.000	0.000
117	A	119	LYS	1	0.829	0.897	49.911	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.969	-0.917	47.486	0.011	0.011	0.000	0.000	0.000	0.000
119	A	121	PRO	0	0.044	-0.067	45.385	0.000	0.000	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.037	0.008	44.214	0.000	0.000	0.000	0.000	0.000	0.000
121	A	123	THR	0	0.043	0.040	40.967	0.001	0.001	0.000	0.000	0.000	0.000
122	A	124	THR	0	0.052	0.010	36.163	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.022	-0.010	38.546	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	126	ASP	-1	-0.860	-0.912	39.712	0.009	0.009	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.025	-0.015	39.882	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	128	ILE	0	-0.001	0.009	35.217	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	129	LEU	0	-0.026	-0.006	39.118	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	130	PHE	0	0.015	-0.010	42.168	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	131	ALA	0	-0.018	-0.004	39.643	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	132	ASN	0	-0.006	-0.009	37.718	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	133	VAL	0	0.008	0.000	41.261	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	134	TYR	0	-0.018	-0.010	44.246	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	135	ALA	0	-0.034	-0.025	41.393	0.000	0.000	0.000	0.000	0.000	0.000
134	A	136	LEU	0	-0.048	-0.014	42.239	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	137	ASN	0	-0.038	-0.039	45.198	0.000	0.000	0.000	0.000	0.000	0.000
136	A	138	SER	0	0.057	0.029	47.955	0.000	0.000	0.000	0.000	0.000	0.000
137	A	139	SER	0	-0.021	0.005	49.574	0.000	0.000	0.000	0.000	0.000	0.000
138	A	140	LEU	0	0.071	0.042	51.103	0.000	0.000	0.000	0.000	0.000	0.000
139	A	141	VAL	0	-0.004	-0.010	48.301	0.000	0.000	0.000	0.000	0.000	0.000
140	A	142	HIS	0	-0.064	-0.021	51.787	0.000	0.000	0.000	0.000	0.000	0.000
141	A	143	SER	0	-0.017	-0.011	54.308	0.000	0.000	0.000	0.000	0.000	0.000
142	A	144	LYS	1	0.838	0.957	53.043	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	145	PHE	0	-0.045	-0.069	50.380	0.000	0.000	0.000	0.000	0.000	0.000
144	A	146	PRO	0	0.031	0.028	54.025	0.000	0.000	0.000	0.000	0.000	0.000
145	A	147	GLU	-1	-0.948	-0.964	55.548	0.005	0.005	0.000	0.000	0.000	0.000
146	A	148	LEU	0	-0.055	-0.026	49.075	0.000	0.000	0.000	0.000	0.000	0.000
147	A	149	PRO	0	0.086	0.040	48.504	0.000	0.000	0.000	0.000	0.000	0.000
148	A	150	SER	0	0.047	0.017	49.198	0.000	0.000	0.000	0.000	0.000	0.000
149	A	151	LYS	1	0.966	0.983	43.348	-0.014	-0.014	0.000	0.000	0.000	0.000
150	A	152	VAL	0	0.064	0.032	44.758	0.000	0.000	0.000	0.000	0.000	0.000
151	A	153	HIS	0	-0.015	0.001	45.826	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	154	ASN	0	-0.018	-0.030	45.230	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	155	ALA	0	-0.005	0.007	41.647	0.000	0.000	0.000	0.000	0.000	0.000
154	A	156	VAL	0	0.023	0.015	42.915	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	157	ALA	0	-0.031	-0.012	45.168	-0.001	-0.001	0.000	0.000	0.000	0.000
156	A	158	LEU	0	-0.073	-0.040	39.305	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	159	ALA	0	0.024	-0.007	40.800	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	160	LYS	1	0.916	0.973	41.756	-0.004	-0.004	0.000	0.000	0.000	0.000
159	A	161	LYS	1	0.866	0.945	43.967	-0.004	-0.004	0.000	0.000	0.000	0.000
160	A	162	HIS	-1	-0.915	-0.942	41.128	-0.001	-0.001	0.000	0.000	0.000	0.000

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