FMO DATABASE

FMODB ID: 899RY

Calculation Name: 5TS9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5TS9

Chain ID: A

ChEMBL ID:

UniProt ID: B2JYH9

Base Structure: X-ray

Registration Date: 2023-09-21

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	OptH
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	163
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1531204.665766
FMO2-HF: Nuclear repulsion	1469012.077653
FMO2-HF: Total energy	-62192.588113
FMO2-MP2: Total energy	-62373.851545

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:18:GLY)

Summations of interaction energy for fragment #1(A:18:GLY)

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.
-4.137	-1.164	1.698	-1.887	-2.784	-0.002

Interaction energy analysis for fragmet #1(A:18:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.037 / q_NPA : 0.010

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	20	GLN	0	0.020	-0.009	3.322	-2.498	-0.911	0.023	-0.671	-0.938	0.002
4	A	21	GLN	0	-0.060	-0.027	2.343	-1.012	-0.079	1.674	-1.115	-1.492	-0.004
5	A	22	ASP	-1	-0.837	-0.919	3.909	-1.789	-1.336	0.001	-0.101	-0.354	0.000
6	A	23	ALA	0	-0.058	-0.021	5.837	0.577	0.577	0.000	0.000	0.000	0.000
7	A	24	PHE	0	0.020	-0.010	8.359	0.191	0.191	0.000	0.000	0.000	0.000
8	A	25	VAL	0	0.011	0.017	8.371	0.114	0.114	0.000	0.000	0.000	0.000
9	A	26	PRO	0	-0.017	-0.014	10.896	0.088	0.088	0.000	0.000	0.000	0.000
10	A	27	LEU	0	0.033	0.026	13.719	0.043	0.043	0.000	0.000	0.000	0.000
11	A	28	VAL	0	0.044	0.033	12.851	0.040	0.040	0.000	0.000	0.000	0.000
12	A	29	ARG	1	0.918	0.964	12.496	0.389	0.389	0.000	0.000	0.000	0.000
13	A	30	SER	0	-0.023	-0.019	16.497	0.034	0.034	0.000	0.000	0.000	0.000
14	A	31	MET	0	0.016	0.003	18.635	0.015	0.015	0.000	0.000	0.000	0.000
15	A	32	ALA	0	0.015	0.014	18.266	0.018	0.018	0.000	0.000	0.000	0.000
16	A	33	ASP	-1	-0.910	-0.958	20.187	-0.154	-0.154	0.000	0.000	0.000	0.000
17	A	34	ARG	1	0.910	0.951	22.594	0.109	0.109	0.000	0.000	0.000	0.000
18	A	35	LEU	0	-0.041	-0.013	22.293	0.014	0.014	0.000	0.000	0.000	0.000
19	A	36	ASN	0	0.060	0.022	22.613	0.013	0.013	0.000	0.000	0.000	0.000
20	A	37	THR	0	-0.089	-0.044	26.032	0.011	0.011	0.000	0.000	0.000	0.000
21	A	38	ALA	0	0.013	0.008	28.454	0.008	0.008	0.000	0.000	0.000	0.000
22	A	39	ASP	-1	-0.810	-0.891	28.748	-0.098	-0.098	0.000	0.000	0.000	0.000
23	A	40	GLN	0	0.018	-0.017	31.306	0.009	0.009	0.000	0.000	0.000	0.000
24	A	41	VAL	0	-0.041	-0.020	33.042	0.006	0.006	0.000	0.000	0.000	0.000
25	A	42	ALA	0	-0.008	0.001	34.038	0.005	0.005	0.000	0.000	0.000	0.000
26	A	43	LEU	0	0.002	0.001	35.283	0.004	0.004	0.000	0.000	0.000	0.000
27	A	44	SER	0	0.007	0.015	37.689	0.004	0.004	0.000	0.000	0.000	0.000
28	A	45	LYS	1	0.802	0.900	36.193	0.061	0.061	0.000	0.000	0.000	0.000
29	A	46	TRP	0	-0.023	-0.007	39.841	0.001	0.001	0.000	0.000	0.000	0.000
30	A	47	ASP	-1	-0.810	-0.876	41.522	-0.046	-0.046	0.000	0.000	0.000	0.000
31	A	48	THR	0	-0.080	-0.051	42.973	0.003	0.003	0.000	0.000	0.000	0.000
32	A	49	GLY	0	0.016	0.014	44.142	0.002	0.002	0.000	0.000	0.000	0.000
33	A	50	GLN	0	-0.064	-0.025	42.354	0.001	0.001	0.000	0.000	0.000	0.000
34	A	51	PRO	0	0.020	0.015	41.880	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	52	VAL	0	-0.005	-0.015	35.230	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	53	TYR	0	-0.038	-0.010	36.951	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	54	ASP	-1	-0.882	-0.952	38.246	-0.039	-0.039	0.000	0.000	0.000	0.000
38	A	55	GLY	0	0.037	0.018	38.890	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	56	GLN	0	0.017	0.015	39.452	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	57	ARG	1	0.922	0.968	34.931	0.053	0.053	0.000	0.000	0.000	0.000
41	A	58	GLU	-1	-0.783	-0.922	34.500	-0.060	-0.060	0.000	0.000	0.000	0.000
42	A	59	ALA	0	0.052	0.033	35.005	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	60	GLN	0	-0.025	-0.007	36.575	0.002	0.002	0.000	0.000	0.000	0.000
44	A	61	VAL	0	-0.054	-0.027	31.509	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	62	ILE	0	0.011	0.009	31.048	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	63	ALA	0	0.015	0.008	32.558	0.001	0.001	0.000	0.000	0.000	0.000
47	A	64	ASN	0	-0.005	-0.010	33.748	0.005	0.005	0.000	0.000	0.000	0.000
48	A	65	ALA	0	0.021	0.017	28.779	0.001	0.001	0.000	0.000	0.000	0.000
49	A	66	ALA	0	-0.001	-0.016	30.320	0.002	0.002	0.000	0.000	0.000	0.000
50	A	67	THR	0	-0.077	-0.037	32.106	0.004	0.004	0.000	0.000	0.000	0.000
51	A	68	MET	0	0.007	0.027	29.704	0.000	0.000	0.000	0.000	0.000	0.000
52	A	69	ALA	0	0.004	0.011	28.105	0.001	0.001	0.000	0.000	0.000	0.000
53	A	70	SER	0	-0.024	-0.017	27.912	0.002	0.002	0.000	0.000	0.000	0.000
54	A	71	GLU	-1	-0.918	-0.960	29.426	-0.021	-0.021	0.000	0.000	0.000	0.000
55	A	72	TYR	0	-0.017	-0.015	24.141	0.000	0.000	0.000	0.000	0.000	0.000
56	A	73	GLY	0	-0.044	-0.019	24.183	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	74	LEU	0	-0.031	-0.002	22.203	0.001	0.001	0.000	0.000	0.000	0.000
58	A	75	THR	0	0.012	-0.003	25.726	0.002	0.002	0.000	0.000	0.000	0.000
59	A	76	ALA	0	0.070	0.018	28.002	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	77	GLU	-1	-0.922	-0.959	29.077	-0.041	-0.041	0.000	0.000	0.000	0.000
61	A	78	ASP	-1	-0.828	-0.886	22.920	-0.070	-0.070	0.000	0.000	0.000	0.000
62	A	79	ALA	0	0.044	0.021	25.584	-0.010	-0.010	0.000	0.000	0.000	0.000
63	A	80	ILE	0	0.049	0.022	26.882	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	81	ASN	0	-0.008	0.013	25.736	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	82	ILE	0	0.032	0.029	20.836	-0.008	-0.008	0.000	0.000	0.000	0.000
66	A	83	PHE	0	0.015	-0.012	24.400	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	84	SER	0	-0.031	-0.044	27.041	0.001	0.001	0.000	0.000	0.000	0.000
68	A	85	ASP	-1	-0.790	-0.879	23.820	-0.099	-0.099	0.000	0.000	0.000	0.000
69	A	86	GLN	0	-0.040	-0.028	21.725	-0.011	-0.011	0.000	0.000	0.000	0.000
70	A	87	VAL	0	-0.066	-0.032	25.719	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	88	GLU	-1	-0.879	-0.949	28.040	-0.068	-0.068	0.000	0.000	0.000	0.000
72	A	89	ALA	0	0.038	0.037	24.522	0.000	0.000	0.000	0.000	0.000	0.000
73	A	90	ASN	0	-0.031	-0.020	26.486	0.006	0.006	0.000	0.000	0.000	0.000
74	A	91	LYS	1	0.778	0.880	28.584	0.067	0.067	0.000	0.000	0.000	0.000
75	A	92	GLU	-1	-0.906	-0.942	26.381	-0.111	-0.111	0.000	0.000	0.000	0.000
76	A	93	VAL	0	0.031	0.009	26.505	0.002	0.002	0.000	0.000	0.000	0.000
77	A	94	GLN	0	0.021	0.008	29.534	0.010	0.010	0.000	0.000	0.000	0.000
78	A	95	TYR	0	0.003	-0.015	33.005	0.006	0.006	0.000	0.000	0.000	0.000
79	A	96	ALA	0	-0.001	0.011	31.224	0.004	0.004	0.000	0.000	0.000	0.000
80	A	97	LEU	0	-0.009	-0.001	30.797	0.003	0.003	0.000	0.000	0.000	0.000
81	A	98	LEU	0	0.019	0.018	33.997	0.004	0.004	0.000	0.000	0.000	0.000
82	A	99	ASN	0	-0.007	-0.011	36.866	0.006	0.006	0.000	0.000	0.000	0.000
83	A	100	ASN	0	-0.010	-0.001	32.622	0.005	0.005	0.000	0.000	0.000	0.000
84	A	101	TRP	0	0.028	0.011	34.362	0.002	0.002	0.000	0.000	0.000	0.000
85	A	102	ARG	1	0.913	0.949	39.274	0.053	0.053	0.000	0.000	0.000	0.000
86	A	103	ARG	1	0.864	0.932	36.217	0.064	0.064	0.000	0.000	0.000	0.000
87	A	104	GLN	0	-0.040	-0.016	37.591	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	105	GLY	0	-0.013	0.005	42.281	0.002	0.002	0.000	0.000	0.000	0.000
89	A	106	ASP	-1	-0.887	-0.946	42.552	-0.045	-0.045	0.000	0.000	0.000	0.000
90	A	107	ALA	0	-0.068	-0.021	38.853	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	108	PRO	0	0.000	0.000	35.174	0.002	0.002	0.000	0.000	0.000	0.000
92	A	109	ALA	0	0.043	0.022	38.201	0.001	0.001	0.000	0.000	0.000	0.000
93	A	110	THR	0	-0.021	-0.011	34.053	0.002	0.002	0.000	0.000	0.000	0.000
94	A	111	PRO	0	0.027	0.024	36.914	0.002	0.002	0.000	0.000	0.000	0.000
95	A	112	ARG	1	0.808	0.883	37.035	0.049	0.049	0.000	0.000	0.000	0.000
96	A	113	GLN	0	0.000	-0.004	32.147	0.001	0.001	0.000	0.000	0.000	0.000
97	A	114	SER	0	0.032	0.022	37.293	0.000	0.000	0.000	0.000	0.000	0.000
98	A	115	LEU	0	0.080	0.031	36.335	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	116	ALA	0	-0.020	-0.010	37.015	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	117	GLY	0	-0.005	-0.007	38.583	0.001	0.001	0.000	0.000	0.000	0.000
101	A	118	VAL	0	0.001	-0.008	33.782	0.000	0.000	0.000	0.000	0.000	0.000
102	A	119	ILE	0	0.022	0.008	31.960	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	120	ARG	1	0.976	0.993	32.371	0.040	0.040	0.000	0.000	0.000	0.000
104	A	121	PRO	0	0.034	0.014	33.044	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	122	ILE	0	-0.036	-0.018	27.783	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	123	LEU	0	-0.023	-0.021	28.341	-0.005	-0.005	0.000	0.000	0.000	0.000
107	A	124	ASP	-1	-0.888	-0.935	28.887	-0.054	-0.054	0.000	0.000	0.000	0.000
108	A	125	LYS	1	0.891	0.945	27.464	0.068	0.068	0.000	0.000	0.000	0.000
109	A	126	LEU	0	0.004	-0.001	23.005	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	127	GLN	0	-0.032	-0.011	24.391	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	128	ALA	0	0.053	0.025	25.380	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	129	SER	0	-0.017	-0.008	21.786	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	130	ILE	0	0.026	0.015	20.450	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	131	MET	0	-0.030	0.002	20.536	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	132	GLN	0	0.020	0.020	20.276	0.009	0.009	0.000	0.000	0.000	0.000
116	A	133	ASN	0	-0.046	-0.033	16.645	0.013	0.013	0.000	0.000	0.000	0.000
117	A	134	LEU	0	-0.021	-0.021	16.801	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	135	GLN	0	0.014	0.010	18.097	0.003	0.003	0.000	0.000	0.000	0.000
119	A	136	SER	0	-0.072	-0.039	15.782	0.024	0.024	0.000	0.000	0.000	0.000
120	A	137	VAL	0	-0.011	0.001	11.903	0.026	0.026	0.000	0.000	0.000	0.000
121	A	138	ALA	0	0.013	0.003	14.227	0.003	0.003	0.000	0.000	0.000	0.000
122	A	139	PRO	0	-0.031	-0.019	13.357	0.002	0.002	0.000	0.000	0.000	0.000
123	A	140	LEU	0	0.009	0.003	8.792	0.014	0.014	0.000	0.000	0.000	0.000
124	A	141	ARG	1	0.765	0.848	12.273	0.034	0.034	0.000	0.000	0.000	0.000
125	A	142	SER	0	-0.008	0.001	15.056	-0.011	-0.011	0.000	0.000	0.000	0.000
126	A	143	ILE	0	-0.027	0.007	8.903	0.023	0.023	0.000	0.000	0.000	0.000
127	A	144	ALA	0	0.027	0.002	12.613	-0.042	-0.042	0.000	0.000	0.000	0.000
128	A	145	ASP	-1	-0.915	-0.957	7.659	-0.220	-0.220	0.000	0.000	0.000	0.000
129	A	146	CYS	0	-0.029	0.018	9.969	-0.106	-0.106	0.000	0.000	0.000	0.000
130	A	147	HIS	0	0.046	0.004	11.815	-0.071	-0.071	0.000	0.000	0.000	0.000
131	A	148	ALA	0	-0.003	0.007	9.862	-0.022	-0.022	0.000	0.000	0.000	0.000
132	A	149	LEU	0	-0.018	-0.003	5.556	-0.140	-0.140	0.000	0.000	0.000	0.000
133	A	150	VAL	0	0.045	0.020	8.529	-0.078	-0.078	0.000	0.000	0.000	0.000
134	A	151	ALA	0	0.035	0.017	11.532	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	152	SER	0	-0.025	-0.016	7.436	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	153	ALA	0	-0.019	-0.003	9.210	-0.007	-0.007	0.000	0.000	0.000	0.000
137	A	154	VAL	0	0.005	0.001	9.936	0.050	0.050	0.000	0.000	0.000	0.000
138	A	155	GLY	0	-0.008	0.003	12.311	0.042	0.042	0.000	0.000	0.000	0.000
139	A	156	GLN	0	-0.022	-0.014	6.907	0.174	0.174	0.000	0.000	0.000	0.000
140	A	157	VAL	0	-0.012	-0.006	11.313	0.053	0.053	0.000	0.000	0.000	0.000
141	A	158	ALA	0	-0.019	-0.020	14.107	0.046	0.046	0.000	0.000	0.000	0.000
142	A	159	GLU	-1	-0.919	-0.947	13.866	-0.221	-0.221	0.000	0.000	0.000	0.000
143	A	160	GLN	0	-0.018	-0.025	11.781	0.064	0.064	0.000	0.000	0.000	0.000
144	A	161	ALA	0	-0.057	-0.025	16.048	0.029	0.029	0.000	0.000	0.000	0.000
145	A	162	SER	0	-0.029	-0.008	18.868	0.028	0.028	0.000	0.000	0.000	0.000
146	A	163	LEU	0	-0.054	-0.011	18.681	0.020	0.020	0.000	0.000	0.000	0.000
147	A	164	ASP	-1	-0.801	-0.878	21.271	-0.130	-0.130	0.000	0.000	0.000	0.000
148	A	165	VAL	0	-0.001	-0.023	22.597	-0.010	-0.010	0.000	0.000	0.000	0.000
149	A	166	LEU	0	-0.015	0.003	23.646	-0.003	-0.003	0.000	0.000	0.000	0.000
150	A	167	HIS	1	0.829	0.866	22.948	0.124	0.124	0.000	0.000	0.000	0.000
151	A	168	ARG	1	1.002	1.009	16.938	0.201	0.201	0.000	0.000	0.000	0.000
152	A	169	ALA	0	0.000	0.012	20.104	-0.009	-0.009	0.000	0.000	0.000	0.000
153	A	170	ALA	0	0.047	0.023	22.428	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	171	LEU	0	-0.037	-0.027	16.630	0.004	0.004	0.000	0.000	0.000	0.000
155	A	172	ASP	-1	-0.887	-0.960	17.229	-0.243	-0.243	0.000	0.000	0.000	0.000
156	A	173	ARG	1	0.814	0.919	19.356	0.110	0.110	0.000	0.000	0.000	0.000
157	A	174	ALA	0	-0.010	-0.012	20.732	0.009	0.009	0.000	0.000	0.000	0.000
158	A	175	VAL	0	-0.008	-0.014	15.988	0.007	0.007	0.000	0.000	0.000	0.000
159	A	176	ALA	0	-0.037	0.002	18.126	-0.004	-0.004	0.000	0.000	0.000	0.000
160	A	177	ARG	1	0.823	0.903	20.213	0.085	0.085	0.000	0.000	0.000	0.000
161	A	178	ILE	0	0.043	0.026	14.743	0.015	0.015	0.000	0.000	0.000	0.000
162	A	180	VAL	0	-0.015	-0.002	16.915	0.009	0.009	0.000	0.000	0.000	0.000
163	A	181	LYS	1	0.990	0.991	18.600	0.056	0.056	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:18:GLY)