FMO DATABASE

FMODB ID: R5VJ8

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1307075.939657
FMO2-HF: Nuclear repulsion	1244187.457476
FMO2-HF: Total energy	-62888.48218
FMO2-MP2: Total energy	-63074.578365

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.
-21.461	-11.336	7.21	-6.536	-10.798	-0.041

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 : -0.021 / q_NPA : -0.020

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	-0.037	-0.004	3.180	-4.639	-0.981	0.176	-1.919	-1.914	0.011
4	A	6	LEU	0	0.028	0.038	4.647	-0.120	0.085	-0.001	-0.019	-0.185	0.000
5	A	7	ILE	0	-0.013	-0.007	7.439	0.041	0.041	0.000	0.000	0.000	0.000
6	A	8	SER	0	0.036	0.008	9.345	-0.105	-0.105	0.000	0.000	0.000	0.000
7	A	9	PHE	0	0.030	0.003	12.899	0.000	0.000	0.000	0.000	0.000	0.000
8	A	10	ASP	-1	-0.788	-0.889	16.113	0.030	0.030	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.828	0.925	16.866	0.017	0.017	0.000	0.000	0.000	0.000
10	A	12	SER	0	0.032	0.019	20.749	0.000	0.000	0.000	0.000	0.000	0.000
11	A	13	LYS	1	0.938	0.983	21.619	-0.031	-0.031	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.909	0.936	24.855	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	15	HIS	0	0.014	0.017	22.241	0.003	0.003	0.000	0.000	0.000	0.000
14	A	16	PRO	0	0.043	0.015	26.905	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	17	ALA	0	0.071	0.044	27.171	0.000	0.000	0.000	0.000	0.000	0.000
16	A	18	HIS	0	0.052	0.020	26.406	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	19	LEU	0	-0.015	-0.003	23.813	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	20	GLN	0	-0.009	-0.016	22.561	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	21	LEU	0	0.002	0.014	21.542	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	22	ALA	0	0.023	0.002	21.611	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	23	ASN	0	-0.027	-0.030	19.064	-0.008	-0.008	0.000	0.000	0.000	0.000
22	A	24	ASN	0	0.033	-0.006	17.311	0.001	0.001	0.000	0.000	0.000	0.000
23	A	25	LEU	0	0.010	0.012	17.022	-0.015	-0.015	0.000	0.000	0.000	0.000
24	A	26	LYS	1	0.890	0.944	16.658	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	27	ILE	0	-0.002	0.007	11.962	-0.021	-0.021	0.000	0.000	0.000	0.000
26	A	28	ALA	0	0.024	0.010	12.419	-0.047	-0.047	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.003	-0.002	13.579	-0.037	-0.037	0.000	0.000	0.000	0.000
28	A	30	ALA	0	-0.011	-0.006	10.717	-0.035	-0.035	0.000	0.000	0.000	0.000
29	A	31	LEU	0	-0.002	-0.004	7.704	-0.129	-0.129	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.917	-0.947	9.623	-0.330	-0.330	0.000	0.000	0.000	0.000
31	A	33	TYR	0	-0.042	-0.039	11.195	-0.032	-0.032	0.000	0.000	0.000	0.000
32	A	34	ALA	0	-0.006	0.017	6.928	-0.025	-0.025	0.000	0.000	0.000	0.000
33	A	35	SER	0	0.040	0.019	7.751	-0.010	-0.010	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.889	0.937	3.439	-0.665	-0.283	0.007	-0.075	-0.313	0.000
35	A	37	ASN	0	-0.004	-0.017	2.457	-1.864	-0.832	2.015	-1.009	-2.038	-0.009
36	A	38	LEU	0	-0.018	0.002	2.715	-2.313	-1.774	1.415	-0.283	-1.671	-0.009
37	A	39	LYS	1	0.866	0.930	2.970	1.837	2.974	0.063	-0.316	-0.884	0.001
38	A	40	PRO	0	-0.038	-0.003	2.169	-11.222	-8.208	3.535	-2.973	-3.577	-0.035
39	A	41	GLU	-1	-0.876	-0.931	3.550	-2.117	-1.959	0.000	0.058	-0.216	0.000
40	A	42	VAL	0	-0.009	-0.022	5.509	0.495	0.495	0.000	0.000	0.000	0.000
41	A	43	ASP	-1	-0.830	-0.913	9.352	0.006	0.006	0.000	0.000	0.000	0.000
42	A	44	ASN	0	-0.052	-0.048	11.488	0.015	0.015	0.000	0.000	0.000	0.000
43	A	45	ASP	-1	-0.912	-0.941	14.801	-0.024	-0.024	0.000	0.000	0.000	0.000
44	A	46	ASN	0	0.008	0.009	15.179	-0.015	-0.015	0.000	0.000	0.000	0.000
45	A	47	ALA	0	-0.014	-0.019	16.980	-0.013	-0.013	0.000	0.000	0.000	0.000
46	A	48	ALA	0	-0.057	-0.034	18.376	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	49	MET	0	-0.050	0.012	15.454	0.007	0.007	0.000	0.000	0.000	0.000
48	A	50	GLU	-1	-0.838	-0.908	12.643	0.193	0.193	0.000	0.000	0.000	0.000
49	A	51	LEU	0	-0.010	-0.017	7.280	0.000	0.000	0.000	0.000	0.000	0.000
50	A	52	ARG	1	0.861	0.934	9.409	-0.278	-0.278	0.000	0.000	0.000	0.000
51	A	53	ASN	0	0.026	-0.001	7.460	0.506	0.506	0.000	0.000	0.000	0.000
52	A	54	THR	0	-0.044	-0.044	6.437	-0.390	-0.390	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.882	0.933	6.572	-0.089	-0.089	0.000	0.000	0.000	0.000
54	A	56	GLU	-1	-0.869	-0.927	9.893	0.000	0.000	0.000	0.000	0.000	0.000
55	A	57	PRO	0	-0.046	-0.015	13.542	0.014	0.014	0.000	0.000	0.000	0.000
56	A	58	PHE	0	-0.027	-0.016	16.289	-0.018	-0.018	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.003	0.006	18.503	0.005	0.005	0.000	0.000	0.000	0.000
58	A	60	LEU	0	-0.015	-0.009	21.370	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	61	PHE	0	0.011	-0.007	21.645	0.001	0.001	0.000	0.000	0.000	0.000
60	A	62	ASP	-1	-0.785	-0.877	25.816	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	63	ALA	0	0.029	0.009	28.548	0.001	0.001	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.070	-0.058	31.752	0.002	0.002	0.000	0.000	0.000	0.000
63	A	65	ALA	0	0.025	0.001	27.707	0.001	0.001	0.000	0.000	0.000	0.000
64	A	66	ILE	0	-0.026	-0.008	27.610	0.001	0.001	0.000	0.000	0.000	0.000
65	A	67	LEU	0	-0.016	-0.016	29.968	0.001	0.001	0.000	0.000	0.000	0.000
66	A	68	ARG	1	0.820	0.888	31.626	0.006	0.006	0.000	0.000	0.000	0.000
67	A	69	TYR	0	0.018	0.009	25.297	0.001	0.001	0.000	0.000	0.000	0.000
68	A	70	VAL	0	-0.082	-0.043	30.399	0.001	0.001	0.000	0.000	0.000	0.000
69	A	71	MET	0	-0.078	-0.038	32.547	0.000	0.000	0.000	0.000	0.000	0.000
70	A	72	ASP	-1	-0.930	-0.951	31.940	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.811	-0.887	33.600	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	74	PHE	0	-0.003	-0.016	29.303	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.834	-0.891	34.191	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	76	GLY	0	-0.017	-0.027	37.783	0.000	0.000	0.000	0.000	0.000	0.000
75	A	77	GLN	0	-0.011	-0.015	31.314	0.000	0.000	0.000	0.000	0.000	0.000
76	A	78	THR	0	-0.019	-0.010	36.682	0.000	0.000	0.000	0.000	0.000	0.000
77	A	79	SER	0	-0.049	-0.024	38.650	0.000	0.000	0.000	0.000	0.000	0.000
78	A	80	ASP	-1	-0.888	-0.943	41.246	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.863	0.927	43.094	0.002	0.002	0.000	0.000	0.000	0.000
80	A	82	TYR	0	0.034	0.025	33.383	0.000	0.000	0.000	0.000	0.000	0.000
81	A	83	GLN	0	0.050	0.016	36.280	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	84	PHE	0	0.002	-0.002	39.509	0.000	0.000	0.000	0.000	0.000	0.000
83	A	85	ALA	0	0.009	0.003	39.524	0.000	0.000	0.000	0.000	0.000	0.000
84	A	86	LEU	0	0.003	0.009	33.933	0.000	0.000	0.000	0.000	0.000	0.000
85	A	87	ALA	0	-0.019	-0.023	37.315	0.000	0.000	0.000	0.000	0.000	0.000
86	A	88	SER	0	-0.101	-0.051	38.653	0.001	0.001	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.003	0.010	40.711	0.000	0.000	0.000	0.000	0.000	0.000
88	A	90	GLN	0	0.079	0.049	32.935	0.000	0.000	0.000	0.000	0.000	0.000
89	A	91	ASN	0	-0.010	-0.017	36.687	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	92	LEU	0	-0.002	-0.003	37.725	0.000	0.000	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.010	-0.006	37.887	0.000	0.000	0.000	0.000	0.000	0.000
92	A	94	TYR	0	-0.025	0.008	31.833	0.000	0.000	0.000	0.000	0.000	0.000
93	A	95	HIS	0	-0.067	-0.020	36.573	0.000	0.000	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.925	0.947	35.769	0.005	0.005	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.918	-0.952	40.408	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.026	0.022	42.281	0.000	0.000	0.000	0.000	0.000	0.000
97	A	99	PRO	0	0.020	0.021	44.175	0.000	0.000	0.000	0.000	0.000	0.000
98	A	100	GLN	0	0.023	-0.013	47.241	0.000	0.000	0.000	0.000	0.000	0.000
99	A	101	GLN	0	0.020	0.016	49.999	0.000	0.000	0.000	0.000	0.000	0.000
100	A	102	HIS	0	0.010	-0.003	47.890	0.000	0.000	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.025	0.015	45.640	0.000	0.000	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.831	-0.890	48.174	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	105	VAL	0	-0.006	0.008	51.566	0.000	0.000	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.034	-0.013	45.376	0.000	0.000	0.000	0.000	0.000	0.000
105	A	107	THR	0	-0.002	-0.030	46.908	0.000	0.000	0.000	0.000	0.000	0.000
106	A	108	ASN	0	-0.024	-0.031	49.011	0.000	0.000	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.958	0.988	49.029	0.000	0.000	0.000	0.000	0.000	0.000
108	A	110	ALA	0	0.006	0.006	46.890	0.000	0.000	0.000	0.000	0.000	0.000
109	A	111	ILE	0	-0.028	-0.018	48.680	0.000	0.000	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.943	-0.958	51.527	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.097	-0.051	50.373	0.000	0.000	0.000	0.000	0.000	0.000
112	A	114	TYR	0	-0.003	-0.011	46.635	0.000	0.000	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.053	-0.031	46.855	0.000	0.000	0.000	0.000	0.000	0.000
114	A	116	VAL	0	0.114	0.052	49.643	0.000	0.000	0.000	0.000	0.000	0.000
115	A	117	GLU	-1	-0.859	-0.910	51.444	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	118	LEU	0	-0.033	-0.018	47.816	0.000	0.000	0.000	0.000	0.000	0.000
117	A	119	LYS	1	0.863	0.917	50.391	0.001	0.001	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.799	-0.876	47.271	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	121	PRO	0	-0.002	-0.019	45.763	0.000	0.000	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.056	-0.008	44.563	0.000	0.000	0.000	0.000	0.000	0.000
121	A	123	THR	0	0.017	-0.005	41.128	0.000	0.000	0.000	0.000	0.000	0.000
122	A	124	THR	0	0.048	-0.002	36.277	0.000	0.000	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.024	-0.003	39.130	0.000	0.000	0.000	0.000	0.000	0.000
124	A	126	ASP	-1	-0.843	-0.885	40.150	-0.002	-0.002	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.018	-0.006	40.401	0.000	0.000	0.000	0.000	0.000	0.000
126	A	128	ILE	0	0.039	0.030	35.614	0.000	0.000	0.000	0.000	0.000	0.000
127	A	129	LEU	0	-0.017	0.007	39.512	0.000	0.000	0.000	0.000	0.000	0.000
128	A	130	PHE	0	0.011	-0.008	42.518	0.000	0.000	0.000	0.000	0.000	0.000
129	A	131	ALA	0	-0.015	-0.005	39.998	0.000	0.000	0.000	0.000	0.000	0.000
130	A	132	ASN	0	-0.023	-0.027	38.005	0.000	0.000	0.000	0.000	0.000	0.000
131	A	133	VAL	0	0.030	0.006	41.682	0.000	0.000	0.000	0.000	0.000	0.000
132	A	134	TYR	0	-0.005	-0.013	44.630	0.000	0.000	0.000	0.000	0.000	0.000
133	A	135	ALA	0	-0.035	-0.026	41.583	0.000	0.000	0.000	0.000	0.000	0.000
134	A	136	LEU	0	-0.037	-0.007	42.506	0.000	0.000	0.000	0.000	0.000	0.000
135	A	137	ASN	0	-0.001	-0.013	45.535	0.000	0.000	0.000	0.000	0.000	0.000
136	A	138	SER	0	0.024	0.014	48.242	0.000	0.000	0.000	0.000	0.000	0.000
137	A	139	SER	0	-0.048	-0.011	49.809	0.000	0.000	0.000	0.000	0.000	0.000
138	A	140	LEU	0	0.055	0.047	51.640	0.000	0.000	0.000	0.000	0.000	0.000
139	A	141	VAL	0	-0.016	-0.009	48.400	0.000	0.000	0.000	0.000	0.000	0.000
140	A	142	HIS	0	-0.037	-0.017	51.867	0.000	0.000	0.000	0.000	0.000	0.000
141	A	143	SER	0	-0.014	-0.025	54.450	0.000	0.000	0.000	0.000	0.000	0.000
142	A	144	LYS	1	0.844	0.940	53.799	0.001	0.001	0.000	0.000	0.000	0.000
143	A	145	PHE	0	-0.072	-0.051	51.166	0.000	0.000	0.000	0.000	0.000	0.000
144	A	146	PRO	0	0.019	0.025	54.164	0.000	0.000	0.000	0.000	0.000	0.000
145	A	147	GLU	-1	-0.934	-0.966	55.613	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	148	LEU	0	-0.039	-0.017	49.374	0.000	0.000	0.000	0.000	0.000	0.000
147	A	149	PRO	0	0.065	0.028	49.228	0.000	0.000	0.000	0.000	0.000	0.000
148	A	150	SER	0	0.025	0.008	49.389	0.000	0.000	0.000	0.000	0.000	0.000
149	A	151	LYS	1	0.819	0.885	44.833	0.001	0.001	0.000	0.000	0.000	0.000
150	A	152	VAL	0	0.049	0.028	45.108	0.000	0.000	0.000	0.000	0.000	0.000
151	A	153	HIS	0	-0.006	-0.005	46.336	0.000	0.000	0.000	0.000	0.000	0.000
152	A	154	ASN	0	0.008	-0.002	45.969	0.000	0.000	0.000	0.000	0.000	0.000
153	A	155	ALA	0	0.022	0.022	41.982	0.000	0.000	0.000	0.000	0.000	0.000
154	A	156	VAL	0	0.022	0.011	43.139	0.000	0.000	0.000	0.000	0.000	0.000
155	A	157	ALA	0	-0.016	-0.009	45.486	0.000	0.000	0.000	0.000	0.000	0.000
156	A	158	LEU	0	-0.038	-0.013	39.650	0.000	0.000	0.000	0.000	0.000	0.000
157	A	159	ALA	0	0.069	0.025	40.947	0.000	0.000	0.000	0.000	0.000	0.000
158	A	160	LYS	1	0.877	0.961	42.041	0.001	0.001	0.000	0.000	0.000	0.000
159	A	161	LYS	1	0.815	0.894	43.628	0.002	0.002	0.000	0.000	0.000	0.000
160	A	162	HIS	0	0.018	0.027	40.999	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)