FMO DATABASE

FMODB ID: KG2N3

Calculation Name: 2F9S-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2F9S

Chain ID: A

ChEMBL ID:

UniProt ID: P35160

Base Structure: X-ray

Registration Date: 2023-09-22

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	138
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1302064.3532
FMO2-HF: Nuclear repulsion	1247215.396887
FMO2-HF: Total energy	-54848.956314
FMO2-MP2: Total energy	-55006.923266

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:38:GLU)

Summations of interaction energy for fragment #1(A:38:GLU)

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.
24.912	28.909	0.949	-1.875	-3.071	0.014

Interaction energy analysis for fragmet #1(A:38:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.971 / q_NPA : -1.000

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	40	SER	0	-0.037	-0.015	3.432	-3.701	-2.405	0.026	-0.569	-0.753	0.004
4	A	41	ASP	-1	-0.853	-0.918	7.028	27.684	27.684	0.000	0.000	0.000	0.000
5	A	42	ALA	0	0.032	0.024	9.201	-1.297	-1.297	0.000	0.000	0.000	0.000
6	A	43	PRO	0	0.001	0.011	11.587	-0.920	-0.920	0.000	0.000	0.000	0.000
7	A	44	ASN	0	-0.020	-0.002	15.275	0.394	0.394	0.000	0.000	0.000	0.000
8	A	45	PHE	0	0.023	0.013	16.904	-0.741	-0.741	0.000	0.000	0.000	0.000
9	A	46	VAL	0	0.015	-0.014	20.542	0.093	0.093	0.000	0.000	0.000	0.000
10	A	47	LEU	0	0.004	0.019	22.915	-0.315	-0.315	0.000	0.000	0.000	0.000
11	A	48	GLU	-1	-0.835	-0.907	25.547	9.735	9.735	0.000	0.000	0.000	0.000
12	A	49	ASP	-1	-0.703	-0.835	27.857	10.617	10.617	0.000	0.000	0.000	0.000
13	A	50	THR	0	-0.027	-0.048	29.036	-0.225	-0.225	0.000	0.000	0.000	0.000
14	A	51	ASN	0	-0.098	-0.054	31.535	-0.564	-0.564	0.000	0.000	0.000	0.000
15	A	52	GLY	0	-0.005	0.014	32.398	-0.273	-0.273	0.000	0.000	0.000	0.000
16	A	53	LYS	1	0.848	0.923	27.185	-11.201	-11.201	0.000	0.000	0.000	0.000
17	A	54	ARG	1	0.945	0.968	26.556	-10.556	-10.556	0.000	0.000	0.000	0.000
18	A	55	ILE	0	-0.006	-0.004	21.731	-0.080	-0.080	0.000	0.000	0.000	0.000
19	A	56	GLU	-1	-0.839	-0.901	19.856	13.854	13.854	0.000	0.000	0.000	0.000
20	A	57	LEU	0	-0.013	0.000	13.973	0.244	0.244	0.000	0.000	0.000	0.000
21	A	58	SER	0	0.008	-0.030	15.801	1.443	1.443	0.000	0.000	0.000	0.000
22	A	59	ASP	-1	-0.874	-0.917	16.859	14.125	14.125	0.000	0.000	0.000	0.000
23	A	60	LEU	0	-0.079	-0.042	16.469	-0.050	-0.050	0.000	0.000	0.000	0.000
24	A	61	LYS	1	0.948	0.978	11.527	-19.731	-19.731	0.000	0.000	0.000	0.000
25	A	62	GLY	0	-0.034	-0.014	12.745	-1.470	-1.470	0.000	0.000	0.000	0.000
26	A	63	LYS	1	0.772	0.870	13.542	-17.877	-17.877	0.000	0.000	0.000	0.000
27	A	64	GLY	0	0.059	0.057	10.767	1.135	1.135	0.000	0.000	0.000	0.000
28	A	65	VAL	0	-0.046	-0.033	11.332	-2.538	-2.538	0.000	0.000	0.000	0.000
29	A	66	PHE	0	0.056	0.005	12.406	1.495	1.495	0.000	0.000	0.000	0.000
30	A	67	LEU	0	0.001	0.014	13.923	-1.713	-1.713	0.000	0.000	0.000	0.000
31	A	68	ASN	0	-0.042	-0.041	15.538	-0.117	-0.117	0.000	0.000	0.000	0.000
32	A	69	PHE	0	0.043	0.030	16.475	-0.745	-0.745	0.000	0.000	0.000	0.000
33	A	70	TRP	0	-0.041	-0.051	20.819	-0.384	-0.384	0.000	0.000	0.000	0.000
34	A	71	GLY	0	0.078	0.024	24.318	-0.167	-0.167	0.000	0.000	0.000	0.000
35	A	72	THR	0	-0.118	-0.098	28.148	-0.062	-0.062	0.000	0.000	0.000	0.000
36	A	73	TRP	0	0.031	0.008	28.044	-0.121	-0.121	0.000	0.000	0.000	0.000
37	A	74	CYS	0	-0.032	0.002	26.072	-0.137	-0.137	0.000	0.000	0.000	0.000
38	A	75	GLU	-1	-0.785	-0.891	28.812	9.813	9.813	0.000	0.000	0.000	0.000
39	A	76	PRO	0	-0.022	-0.019	25.021	0.131	0.131	0.000	0.000	0.000	0.000
40	A	77	CYS	0	0.016	0.036	23.797	0.491	0.491	0.000	0.000	0.000	0.000
41	A	78	LYS	1	0.811	0.908	25.776	-9.400	-9.400	0.000	0.000	0.000	0.000
42	A	79	LYS	1	0.882	0.954	26.494	-11.719	-11.719	0.000	0.000	0.000	0.000
43	A	80	GLU	-1	-0.794	-0.905	21.239	15.189	15.189	0.000	0.000	0.000	0.000
44	A	81	PHE	0	0.050	0.013	23.553	0.250	0.250	0.000	0.000	0.000	0.000
45	A	82	PRO	0	0.011	0.005	25.397	0.125	0.125	0.000	0.000	0.000	0.000
46	A	83	TYR	0	-0.012	0.002	22.783	-0.032	-0.032	0.000	0.000	0.000	0.000
47	A	84	MET	0	-0.013	0.005	20.004	0.391	0.391	0.000	0.000	0.000	0.000
48	A	85	ALA	0	0.044	0.028	21.982	0.273	0.273	0.000	0.000	0.000	0.000
49	A	86	ASN	0	-0.064	-0.040	24.775	-0.574	-0.574	0.000	0.000	0.000	0.000
50	A	87	GLN	0	0.029	-0.003	19.371	0.496	0.496	0.000	0.000	0.000	0.000
51	A	88	TYR	0	-0.010	-0.028	19.967	0.083	0.083	0.000	0.000	0.000	0.000
52	A	89	LYS	1	0.814	0.902	21.409	-11.421	-11.421	0.000	0.000	0.000	0.000
53	A	90	HIS	0	-0.042	-0.005	18.370	-0.556	-0.556	0.000	0.000	0.000	0.000
54	A	91	PHE	0	0.039	0.025	15.230	0.200	0.200	0.000	0.000	0.000	0.000
55	A	92	LYS	1	0.880	0.942	17.786	-13.319	-13.319	0.000	0.000	0.000	0.000
56	A	93	SER	0	-0.051	-0.032	19.855	0.320	0.320	0.000	0.000	0.000	0.000
57	A	94	GLN	0	-0.042	-0.022	16.094	0.894	0.894	0.000	0.000	0.000	0.000
58	A	95	GLY	0	0.049	0.027	15.371	1.255	1.255	0.000	0.000	0.000	0.000
59	A	96	VAL	0	-0.013	-0.008	13.103	1.420	1.420	0.000	0.000	0.000	0.000
60	A	97	GLU	-1	-0.775	-0.861	15.337	13.378	13.378	0.000	0.000	0.000	0.000
61	A	98	ILE	0	-0.017	-0.006	16.155	1.102	1.102	0.000	0.000	0.000	0.000
62	A	99	VAL	0	-0.018	-0.015	18.059	-0.735	-0.735	0.000	0.000	0.000	0.000
63	A	100	ALA	0	0.039	0.025	19.233	0.426	0.426	0.000	0.000	0.000	0.000
64	A	101	VAL	0	0.031	0.014	19.820	-0.826	-0.826	0.000	0.000	0.000	0.000
65	A	102	ASN	0	-0.049	-0.036	22.467	-0.169	-0.169	0.000	0.000	0.000	0.000
66	A	103	VAL	0	0.016	-0.003	23.901	-0.037	-0.037	0.000	0.000	0.000	0.000
67	A	104	GLY	0	0.040	0.030	26.525	-0.309	-0.309	0.000	0.000	0.000	0.000
68	A	105	GLU	-1	-0.789	-0.835	29.821	9.714	9.714	0.000	0.000	0.000	0.000
69	A	106	SER	0	0.006	-0.007	32.245	0.073	0.073	0.000	0.000	0.000	0.000
70	A	107	LYS	1	0.868	0.921	32.508	-9.346	-9.346	0.000	0.000	0.000	0.000
71	A	108	ILE	0	0.004	0.008	34.609	0.102	0.102	0.000	0.000	0.000	0.000
72	A	109	ALA	0	0.018	0.017	34.828	-0.020	-0.020	0.000	0.000	0.000	0.000
73	A	110	VAL	0	0.061	0.027	29.604	0.084	0.084	0.000	0.000	0.000	0.000
74	A	111	HIS	0	-0.003	-0.012	32.227	0.171	0.171	0.000	0.000	0.000	0.000
75	A	112	ASN	0	0.009	-0.003	34.266	0.056	0.056	0.000	0.000	0.000	0.000
76	A	113	PHE	0	0.038	0.036	28.459	-0.114	-0.114	0.000	0.000	0.000	0.000
77	A	114	MET	0	0.026	0.000	28.188	0.075	0.075	0.000	0.000	0.000	0.000
78	A	115	LYS	1	0.872	0.949	31.502	-8.982	-8.982	0.000	0.000	0.000	0.000
79	A	116	SER	0	-0.045	-0.033	34.365	-0.099	-0.099	0.000	0.000	0.000	0.000
80	A	117	TYR	0	-0.015	-0.005	29.524	-0.079	-0.079	0.000	0.000	0.000	0.000
81	A	118	GLY	0	-0.037	-0.006	29.780	0.326	0.326	0.000	0.000	0.000	0.000
82	A	119	VAL	0	-0.039	-0.014	26.305	0.254	0.254	0.000	0.000	0.000	0.000
83	A	120	ASN	0	-0.054	-0.034	25.668	-0.037	-0.037	0.000	0.000	0.000	0.000
84	A	121	PHE	0	0.010	0.010	22.376	0.176	0.176	0.000	0.000	0.000	0.000
85	A	122	PRO	0	-0.032	-0.017	21.759	-0.552	-0.552	0.000	0.000	0.000	0.000
86	A	123	VAL	0	0.021	0.011	23.092	0.434	0.434	0.000	0.000	0.000	0.000
87	A	124	VAL	0	-0.035	-0.022	22.484	-0.308	-0.308	0.000	0.000	0.000	0.000
88	A	125	LEU	0	-0.027	-0.017	25.524	0.063	0.063	0.000	0.000	0.000	0.000
89	A	126	ASP	-1	-0.729	-0.856	24.089	12.364	12.364	0.000	0.000	0.000	0.000
90	A	127	THR	0	-0.094	-0.051	26.338	-0.149	-0.149	0.000	0.000	0.000	0.000
91	A	128	ASP	-1	-0.880	-0.948	28.897	10.200	10.200	0.000	0.000	0.000	0.000
92	A	129	ARG	1	0.770	0.862	25.949	-11.378	-11.378	0.000	0.000	0.000	0.000
93	A	130	GLN	0	0.007	0.011	24.520	0.505	0.505	0.000	0.000	0.000	0.000
94	A	131	VAL	0	-0.032	-0.027	19.464	0.508	0.508	0.000	0.000	0.000	0.000
95	A	132	LEU	0	-0.027	-0.031	19.890	0.711	0.711	0.000	0.000	0.000	0.000
96	A	133	ASP	-1	-0.791	-0.871	20.440	12.433	12.433	0.000	0.000	0.000	0.000
97	A	134	ALA	0	-0.047	-0.013	19.223	0.244	0.244	0.000	0.000	0.000	0.000
98	A	135	TYR	0	-0.090	-0.077	13.216	1.545	1.545	0.000	0.000	0.000	0.000
99	A	136	ASP	-1	-0.941	-0.959	16.632	15.928	15.928	0.000	0.000	0.000	0.000
100	A	137	VAL	0	-0.037	-0.012	17.692	0.107	0.107	0.000	0.000	0.000	0.000
101	A	138	SER	0	0.019	0.011	19.862	-0.899	-0.899	0.000	0.000	0.000	0.000
102	A	139	PRO	0	-0.054	-0.023	20.307	-0.548	-0.548	0.000	0.000	0.000	0.000
103	A	140	LEU	0	0.027	0.023	21.643	0.466	0.466	0.000	0.000	0.000	0.000
104	A	141	PRO	0	-0.006	-0.024	20.641	-0.617	-0.617	0.000	0.000	0.000	0.000
105	A	142	THR	0	-0.008	-0.016	16.363	0.294	0.294	0.000	0.000	0.000	0.000
106	A	143	THR	0	-0.020	-0.006	14.037	-0.757	-0.757	0.000	0.000	0.000	0.000
107	A	144	PHE	0	0.004	0.001	11.252	1.181	1.181	0.000	0.000	0.000	0.000
108	A	145	LEU	0	-0.038	-0.012	9.043	-1.303	-1.303	0.000	0.000	0.000	0.000
109	A	146	ILE	0	0.004	0.003	7.791	4.206	4.206	0.000	0.000	0.000	0.000
110	A	147	ASN	0	0.054	0.013	4.345	-7.529	-7.297	-0.001	-0.025	-0.206	0.000
111	A	148	PRO	0	0.033	0.020	7.338	-2.947	-2.947	0.000	0.000	0.000	0.000
112	A	149	GLU	-1	-0.862	-0.928	5.780	35.876	35.876	0.000	0.000	0.000	0.000
113	A	150	GLY	0	-0.037	-0.015	8.728	-2.458	-2.458	0.000	0.000	0.000	0.000
114	A	151	LYS	1	0.823	0.906	3.825	-34.777	-34.486	0.000	-0.067	-0.224	0.000
115	A	152	VAL	0	-0.007	-0.006	6.490	2.141	2.141	0.000	0.000	0.000	0.000
116	A	153	VAL	0	0.025	0.008	2.419	-2.501	-0.466	0.925	-1.210	-1.750	0.010
117	A	154	LYS	1	0.870	0.949	4.275	-26.940	-26.797	-0.001	-0.004	-0.138	0.000
118	A	155	VAL	0	0.022	0.019	7.572	-1.778	-1.778	0.000	0.000	0.000	0.000
119	A	156	VAL	0	-0.042	-0.024	11.082	0.339	0.339	0.000	0.000	0.000	0.000
120	A	157	THR	0	0.033	0.020	14.478	-0.452	-0.452	0.000	0.000	0.000	0.000
121	A	158	GLY	0	0.002	0.004	18.051	-0.227	-0.227	0.000	0.000	0.000	0.000
122	A	159	THR	0	-0.071	-0.040	20.091	0.432	0.432	0.000	0.000	0.000	0.000
123	A	160	MET	0	-0.021	-0.002	17.211	0.852	0.852	0.000	0.000	0.000	0.000
124	A	161	THR	0	0.023	-0.029	20.636	-0.606	-0.606	0.000	0.000	0.000	0.000
125	A	162	GLU	-1	-0.771	-0.877	20.287	13.666	13.666	0.000	0.000	0.000	0.000
126	A	163	SER	0	0.000	0.002	20.000	0.316	0.316	0.000	0.000	0.000	0.000
127	A	164	MET	0	0.009	0.043	16.745	0.424	0.424	0.000	0.000	0.000	0.000
128	A	165	ILE	0	0.027	0.007	15.533	1.350	1.350	0.000	0.000	0.000	0.000
129	A	166	HIS	0	-0.037	-0.025	15.829	1.304	1.304	0.000	0.000	0.000	0.000
130	A	167	ASP	-1	-0.875	-0.947	13.465	21.279	21.279	0.000	0.000	0.000	0.000
131	A	168	TYR	0	-0.036	-0.037	11.367	2.846	2.846	0.000	0.000	0.000	0.000
132	A	169	MET	0	0.000	0.008	11.093	1.390	1.390	0.000	0.000	0.000	0.000
133	A	170	ASN	0	-0.009	-0.013	11.989	0.535	0.535	0.000	0.000	0.000	0.000
134	A	171	LEU	0	-0.062	-0.017	5.870	0.225	0.225	0.000	0.000	0.000	0.000
135	A	172	ILE	0	-0.030	-0.010	6.675	5.324	5.324	0.000	0.000	0.000	0.000
136	A	173	LYS	1	0.851	0.935	8.457	-23.067	-23.067	0.000	0.000	0.000	0.000
137	A	174	PRO	0	-0.028	-0.004	10.302	2.083	2.083	0.000	0.000	0.000	0.000
138	A	175	GLY	0	-0.029	-0.004	10.419	-2.194	-2.194	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:38:GLU)