FMO DATABASE

FMODB ID: ZY1QN

Calculation Name: 2HSN-A-Xray372

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: 2023-06-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	160
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1304162.756662
FMO2-HF: Nuclear repulsion	1241274.930056
FMO2-HF: Total energy	-62887.826606
FMO2-MP2: Total energy	-63073.961958

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.
-14.862	-5.447	3.835	-4.396	-8.855	-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 : -0.006 / q_NPA : -0.021

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	-0.049	-0.008	2.958	-4.026	-0.174	0.516	-1.947	-2.421	0.015
4	A	6	LEU	0	0.045	0.041	4.201	-1.232	-0.993	0.000	-0.044	-0.195	0.000
5	A	7	ILE	0	-0.016	-0.011	7.033	0.201	0.201	0.000	0.000	0.000	0.000
6	A	8	SER	0	0.049	0.013	9.394	-0.141	-0.141	0.000	0.000	0.000	0.000
7	A	9	PHE	0	-0.008	-0.018	12.812	0.035	0.035	0.000	0.000	0.000	0.000
8	A	10	ASP	-1	-0.823	-0.888	16.118	0.044	0.044	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.887	0.935	16.735	0.042	0.042	0.000	0.000	0.000	0.000
10	A	12	SER	0	-0.018	-0.003	21.210	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	13	LYS	1	1.005	1.030	21.666	-0.046	-0.046	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.922	0.962	24.577	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	15	HIS	0	-0.034	-0.037	22.406	0.005	0.005	0.000	0.000	0.000	0.000
14	A	16	PRO	0	0.035	0.007	27.217	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	17	ALA	0	0.063	0.036	27.358	0.002	0.002	0.000	0.000	0.000	0.000
16	A	18	HIS	0	0.063	0.018	26.742	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	19	LEU	0	-0.027	-0.014	23.942	0.001	0.001	0.000	0.000	0.000	0.000
18	A	20	GLN	0	0.013	0.008	22.675	0.001	0.001	0.000	0.000	0.000	0.000
19	A	21	LEU	0	0.014	0.018	21.750	0.000	0.000	0.000	0.000	0.000	0.000
20	A	22	ALA	0	0.014	0.008	21.996	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	23	ASN	0	-0.033	-0.043	19.153	0.006	0.006	0.000	0.000	0.000	0.000
22	A	24	ASN	0	0.040	0.004	17.626	0.013	0.013	0.000	0.000	0.000	0.000
23	A	25	LEU	0	-0.001	0.008	17.520	-0.010	-0.010	0.000	0.000	0.000	0.000
24	A	26	LYS	1	0.895	0.947	16.852	-0.056	-0.056	0.000	0.000	0.000	0.000
25	A	27	ILE	0	-0.004	-0.004	12.327	0.001	0.001	0.000	0.000	0.000	0.000
26	A	28	ALA	0	0.017	0.003	12.742	-0.024	-0.024	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.011	0.005	14.132	-0.021	-0.021	0.000	0.000	0.000	0.000
28	A	30	ALA	0	-0.012	0.000	10.599	-0.012	-0.012	0.000	0.000	0.000	0.000
29	A	31	LEU	0	0.001	-0.001	8.283	-0.066	-0.066	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.920	-0.958	10.153	-0.140	-0.140	0.000	0.000	0.000	0.000
31	A	33	TYR	0	-0.055	-0.028	12.552	0.004	0.004	0.000	0.000	0.000	0.000
32	A	34	ALA	0	-0.012	0.018	7.125	-0.016	-0.016	0.000	0.000	0.000	0.000
33	A	35	SER	0	0.019	-0.008	7.636	0.041	0.041	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.895	0.955	4.340	-0.282	-0.082	-0.001	-0.030	-0.168	0.000
35	A	37	ASN	0	0.024	-0.012	2.465	-1.354	-0.177	1.702	-0.934	-1.946	-0.007
36	A	38	LEU	0	-0.016	0.006	2.708	-2.104	-1.479	1.222	-0.189	-1.659	-0.009
37	A	39	LYS	1	0.850	0.922	2.860	0.837	1.854	0.070	-0.259	-0.828	0.000
38	A	40	PRO	0	-0.038	-0.009	3.023	-4.080	-2.002	0.327	-0.957	-1.448	-0.008
39	A	41	GLU	-1	-0.886	-0.928	4.023	-2.395	-2.169	0.000	-0.036	-0.190	0.000
40	A	42	VAL	0	-0.022	-0.024	5.399	0.548	0.549	-0.001	0.000	0.000	0.000
41	A	43	ASP	-1	-0.866	-0.937	9.116	-0.175	-0.175	0.000	0.000	0.000	0.000
42	A	44	ASN	0	-0.067	-0.058	11.367	0.076	0.076	0.000	0.000	0.000	0.000
43	A	45	ASP	-1	-0.892	-0.941	15.019	-0.061	-0.061	0.000	0.000	0.000	0.000
44	A	46	ASN	0	0.052	0.050	14.637	0.003	0.003	0.000	0.000	0.000	0.000
45	A	47	ALA	0	-0.024	-0.017	16.656	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	48	ALA	0	-0.053	-0.030	18.238	0.003	0.003	0.000	0.000	0.000	0.000
47	A	49	MET	0	-0.026	0.012	15.437	0.001	0.001	0.000	0.000	0.000	0.000
48	A	50	GLU	-1	-0.867	-0.926	12.644	0.167	0.167	0.000	0.000	0.000	0.000
49	A	51	LEU	0	-0.012	-0.012	6.753	0.005	0.005	0.000	0.000	0.000	0.000
50	A	52	ARG	1	0.888	0.940	9.153	-0.145	-0.145	0.000	0.000	0.000	0.000
51	A	53	ASN	0	0.021	-0.005	7.189	0.459	0.459	0.000	0.000	0.000	0.000
52	A	54	THR	0	-0.033	-0.041	6.248	-0.553	-0.553	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.864	0.925	6.058	-0.331	-0.331	0.000	0.000	0.000	0.000
54	A	56	GLU	-1	-0.876	-0.928	9.684	-0.094	-0.094	0.000	0.000	0.000	0.000
55	A	57	PRO	0	-0.038	-0.010	13.261	0.041	0.041	0.000	0.000	0.000	0.000
56	A	58	PHE	0	-0.023	-0.018	16.050	-0.023	-0.023	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.011	-0.004	18.261	0.002	0.002	0.000	0.000	0.000	0.000
58	A	60	LEU	0	0.000	0.006	20.959	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	61	PHE	0	0.029	0.003	21.481	0.001	0.001	0.000	0.000	0.000	0.000
60	A	62	ASP	-1	-0.832	-0.916	25.137	-0.022	-0.022	0.000	0.000	0.000	0.000
61	A	63	ALA	0	0.025	0.005	28.106	0.003	0.003	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.040	-0.037	31.314	0.004	0.004	0.000	0.000	0.000	0.000
63	A	65	ALA	0	0.018	-0.003	27.492	0.003	0.003	0.000	0.000	0.000	0.000
64	A	66	ILE	0	-0.017	-0.003	27.273	0.003	0.003	0.000	0.000	0.000	0.000
65	A	67	LEU	0	-0.021	-0.018	29.601	0.003	0.003	0.000	0.000	0.000	0.000
66	A	68	ARG	1	0.839	0.890	31.423	0.009	0.009	0.000	0.000	0.000	0.000
67	A	69	TYR	0	-0.013	0.003	24.610	0.002	0.002	0.000	0.000	0.000	0.000
68	A	70	VAL	0	-0.063	-0.032	29.913	0.003	0.003	0.000	0.000	0.000	0.000
69	A	71	MET	0	-0.080	-0.031	31.930	0.001	0.001	0.000	0.000	0.000	0.000
70	A	72	ASP	-1	-0.933	-0.955	31.545	0.008	0.008	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.813	-0.890	33.029	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	74	PHE	0	-0.006	-0.019	28.754	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.853	-0.911	33.806	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	76	GLY	0	-0.001	0.001	37.308	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	77	GLN	0	-0.020	-0.016	31.065	0.000	0.000	0.000	0.000	0.000	0.000
76	A	78	THR	0	0.012	-0.002	36.430	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	79	SER	0	-0.082	-0.053	38.349	0.000	0.000	0.000	0.000	0.000	0.000
78	A	80	ASP	-1	-0.856	-0.919	40.865	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.878	0.928	43.002	0.004	0.004	0.000	0.000	0.000	0.000
80	A	82	TYR	0	0.019	0.016	33.363	0.000	0.000	0.000	0.000	0.000	0.000
81	A	83	GLN	0	0.078	0.034	35.758	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	84	PHE	0	-0.012	0.002	39.443	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	85	ALA	0	0.011	-0.007	39.571	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	86	LEU	0	-0.018	-0.004	33.999	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	87	ALA	0	-0.013	-0.011	37.159	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	88	SER	0	-0.094	-0.039	38.639	0.000	0.000	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.004	0.000	41.107	0.000	0.000	0.000	0.000	0.000	0.000
88	A	90	GLN	0	0.061	0.047	33.095	0.001	0.001	0.000	0.000	0.000	0.000
89	A	91	ASN	0	0.011	0.001	36.500	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	92	LEU	0	0.009	-0.006	37.558	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.023	-0.008	37.402	0.000	0.000	0.000	0.000	0.000	0.000
92	A	94	TYR	0	-0.036	-0.003	31.458	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	95	HIS	0	-0.072	-0.021	36.347	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.939	0.954	35.961	0.026	0.026	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.934	-0.955	39.973	-0.014	-0.014	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.019	0.009	42.135	0.000	0.000	0.000	0.000	0.000	0.000
97	A	99	PRO	0	0.001	0.006	44.293	0.001	0.001	0.000	0.000	0.000	0.000
98	A	100	GLN	0	0.037	-0.002	47.366	0.001	0.001	0.000	0.000	0.000	0.000
99	A	101	GLN	0	0.025	0.018	49.991	0.000	0.000	0.000	0.000	0.000	0.000
100	A	102	HIS	0	0.017	-0.003	47.638	0.000	0.000	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.030	0.021	45.582	0.000	0.000	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.847	-0.892	48.041	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.002	0.010	51.561	0.000	0.000	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.039	-0.011	45.313	0.000	0.000	0.000	0.000	0.000	0.000
105	A	107	THR	0	0.016	-0.023	46.787	0.000	0.000	0.000	0.000	0.000	0.000
106	A	108	ASN	0	-0.012	-0.023	48.965	0.001	0.001	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.962	0.988	49.082	0.007	0.007	0.000	0.000	0.000	0.000
108	A	110	ALA	0	-0.015	0.002	46.966	0.000	0.000	0.000	0.000	0.000	0.000
109	A	111	ILE	0	-0.052	-0.036	48.706	0.000	0.000	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.931	-0.933	51.387	-0.004	-0.004	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.085	-0.056	50.150	0.000	0.000	0.000	0.000	0.000	0.000
112	A	114	TYR	0	-0.017	-0.012	46.564	0.000	0.000	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.031	-0.022	46.627	0.000	0.000	0.000	0.000	0.000	0.000
114	A	116	VAL	0	0.086	0.032	49.498	0.000	0.000	0.000	0.000	0.000	0.000
115	A	117	GLU	-1	-0.875	-0.914	50.417	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	118	LEU	0	-0.022	-0.014	47.598	0.000	0.000	0.000	0.000	0.000	0.000
117	A	119	LYS	1	0.841	0.894	50.001	0.002	0.002	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.849	-0.857	46.763	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	121	PRO	0	0.056	-0.038	45.183	0.000	0.000	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.059	-0.002	44.223	0.000	0.000	0.000	0.000	0.000	0.000
121	A	123	THR	0	0.025	0.007	40.918	0.000	0.000	0.000	0.000	0.000	0.000
122	A	124	THR	0	0.044	-0.008	36.032	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.027	-0.004	38.611	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	126	ASP	-1	-0.855	-0.892	39.887	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.019	-0.009	40.122	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	128	ILE	0	0.027	0.021	35.259	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	129	LEU	0	-0.012	0.005	39.287	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	130	PHE	0	0.016	-0.008	42.336	0.000	0.000	0.000	0.000	0.000	0.000
129	A	131	ALA	0	-0.022	-0.008	39.854	0.000	0.000	0.000	0.000	0.000	0.000
130	A	132	ASN	0	-0.012	-0.023	37.841	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	133	VAL	0	0.019	0.006	41.448	0.000	0.000	0.000	0.000	0.000	0.000
132	A	134	TYR	0	-0.025	-0.014	44.373	0.000	0.000	0.000	0.000	0.000	0.000
133	A	135	ALA	0	-0.042	-0.028	41.569	0.000	0.000	0.000	0.000	0.000	0.000
134	A	136	LEU	0	-0.033	-0.010	42.365	0.000	0.000	0.000	0.000	0.000	0.000
135	A	137	ASN	0	-0.026	-0.032	45.376	0.000	0.000	0.000	0.000	0.000	0.000
136	A	138	SER	0	0.058	0.029	48.095	0.001	0.001	0.000	0.000	0.000	0.000
137	A	139	SER	0	-0.042	-0.001	49.751	0.001	0.001	0.000	0.000	0.000	0.000
138	A	140	LEU	0	0.059	0.038	51.233	0.000	0.000	0.000	0.000	0.000	0.000
139	A	141	VAL	0	-0.010	-0.010	48.486	0.000	0.000	0.000	0.000	0.000	0.000
140	A	142	HIS	0	-0.054	-0.018	51.972	0.000	0.000	0.000	0.000	0.000	0.000
141	A	143	SER	0	-0.008	-0.014	54.478	0.000	0.000	0.000	0.000	0.000	0.000
142	A	144	LYS	1	0.841	0.950	53.258	0.005	0.005	0.000	0.000	0.000	0.000
143	A	145	PHE	0	-0.052	-0.066	50.723	0.000	0.000	0.000	0.000	0.000	0.000
144	A	146	PRO	0	0.020	0.023	54.062	0.000	0.000	0.000	0.000	0.000	0.000
145	A	147	GLU	-1	-0.943	-0.959	55.569	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	148	LEU	0	-0.045	-0.022	49.084	0.000	0.000	0.000	0.000	0.000	0.000
147	A	149	PRO	0	0.077	0.031	48.533	0.000	0.000	0.000	0.000	0.000	0.000
148	A	150	SER	0	0.049	0.017	49.198	0.000	0.000	0.000	0.000	0.000	0.000
149	A	151	LYS	1	0.834	0.904	44.314	0.000	0.000	0.000	0.000	0.000	0.000
150	A	152	VAL	0	0.055	0.023	44.759	0.000	0.000	0.000	0.000	0.000	0.000
151	A	153	HIS	0	-0.019	-0.002	45.826	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	154	ASN	0	-0.016	-0.026	45.531	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	155	ALA	0	0.015	0.017	41.628	0.000	0.000	0.000	0.000	0.000	0.000
154	A	156	VAL	0	0.030	0.018	42.915	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	157	ALA	0	0.001	0.003	45.168	-0.001	-0.001	0.000	0.000	0.000	0.000
156	A	158	LEU	0	-0.052	-0.018	39.395	0.000	0.000	0.000	0.000	0.000	0.000
157	A	159	ALA	0	0.034	0.002	40.819	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	160	LYS	1	0.916	0.975	41.756	0.007	0.007	0.000	0.000	0.000	0.000
159	A	161	LYS	1	0.836	0.924	44.000	0.008	0.008	0.000	0.000	0.000	0.000
160	A	162	HIS	0	0.026	0.021	41.128	0.000	0.000	0.000	0.000	0.000	0.000

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