FMO DATABASE

FMODB ID: NNNKQ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1532020.585456
FMO2-HF: Nuclear repulsion	1469827.571213
FMO2-HF: Total energy	-62193.014243
FMO2-MP2: Total energy	-62374.222064

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.
-2.815	0.087	1.521	-1.743	-2.68	-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 : 0.038 / q_NPA : 0.007

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	0.004	-0.007	3.089	-2.003	-0.410	0.031	-0.653	-0.971	0.001
4	A	21	GLN	0	-0.060	-0.037	2.333	-0.471	0.438	1.489	-1.010	-1.388	-0.003
5	A	22	ASP	-1	-0.815	-0.905	3.910	-1.550	-1.150	0.001	-0.080	-0.321	0.000
6	A	23	ALA	0	-0.054	-0.016	5.838	0.664	0.664	0.000	0.000	0.000	0.000
7	A	24	PHE	0	0.014	-0.012	8.360	0.254	0.254	0.000	0.000	0.000	0.000
8	A	25	VAL	0	-0.002	0.012	8.297	0.153	0.153	0.000	0.000	0.000	0.000
9	A	26	PRO	0	-0.013	-0.009	10.897	0.106	0.106	0.000	0.000	0.000	0.000
10	A	27	LEU	0	0.023	0.018	13.727	0.054	0.054	0.000	0.000	0.000	0.000
11	A	28	VAL	0	0.040	0.017	12.964	0.051	0.051	0.000	0.000	0.000	0.000
12	A	29	ARG	1	0.909	0.948	12.611	0.429	0.429	0.000	0.000	0.000	0.000
13	A	30	SER	0	-0.003	0.007	16.498	0.039	0.039	0.000	0.000	0.000	0.000
14	A	31	MET	0	0.009	0.000	18.623	0.020	0.020	0.000	0.000	0.000	0.000
15	A	32	ALA	0	0.010	0.011	18.235	0.022	0.022	0.000	0.000	0.000	0.000
16	A	33	ASP	-1	-0.902	-0.957	20.188	-0.176	-0.176	0.000	0.000	0.000	0.000
17	A	34	ARG	1	0.905	0.949	22.595	0.134	0.134	0.000	0.000	0.000	0.000
18	A	35	LEU	0	-0.033	-0.005	22.325	0.017	0.017	0.000	0.000	0.000	0.000
19	A	36	ASN	0	0.059	0.022	22.431	0.014	0.014	0.000	0.000	0.000	0.000
20	A	37	THR	0	-0.073	-0.038	26.033	0.013	0.013	0.000	0.000	0.000	0.000
21	A	38	ALA	0	0.010	0.005	28.454	0.010	0.010	0.000	0.000	0.000	0.000
22	A	39	ASP	-1	-0.804	-0.886	28.332	-0.108	-0.108	0.000	0.000	0.000	0.000
23	A	40	GLN	0	0.030	-0.005	31.307	0.010	0.010	0.000	0.000	0.000	0.000
24	A	41	VAL	0	-0.040	-0.021	33.043	0.007	0.007	0.000	0.000	0.000	0.000
25	A	42	ALA	0	-0.007	0.000	34.039	0.005	0.005	0.000	0.000	0.000	0.000
26	A	43	LEU	0	0.013	0.007	35.498	0.004	0.004	0.000	0.000	0.000	0.000
27	A	44	SER	0	0.000	0.016	37.690	0.004	0.004	0.000	0.000	0.000	0.000
28	A	45	LYS	1	0.805	0.907	36.345	0.073	0.073	0.000	0.000	0.000	0.000
29	A	46	TRP	0	-0.023	-0.008	39.834	0.001	0.001	0.000	0.000	0.000	0.000
30	A	47	ASP	-1	-0.814	-0.870	41.523	-0.052	-0.052	0.000	0.000	0.000	0.000
31	A	48	THR	0	-0.075	-0.058	42.936	0.002	0.002	0.000	0.000	0.000	0.000
32	A	49	GLY	0	0.014	0.014	44.147	0.002	0.002	0.000	0.000	0.000	0.000
33	A	50	GLN	0	-0.073	-0.027	42.390	0.001	0.001	0.000	0.000	0.000	0.000
34	A	51	PRO	0	0.023	0.014	41.869	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	52	VAL	0	0.004	-0.013	35.294	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	53	TYR	0	-0.036	-0.006	36.855	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	54	ASP	-1	-0.871	-0.941	38.212	-0.051	-0.051	0.000	0.000	0.000	0.000
38	A	55	GLY	0	0.038	0.021	38.891	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	56	GLN	0	0.023	0.016	39.453	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	57	ARG	1	0.883	0.929	34.966	0.066	0.066	0.000	0.000	0.000	0.000
41	A	58	GLU	-1	-0.771	-0.899	34.494	-0.076	-0.076	0.000	0.000	0.000	0.000
42	A	59	ALA	0	0.036	0.027	35.006	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	60	GLN	0	-0.030	-0.017	36.576	0.002	0.002	0.000	0.000	0.000	0.000
44	A	61	VAL	0	-0.043	-0.025	31.482	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	62	ILE	0	0.008	0.009	31.145	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	63	ALA	0	0.018	0.010	32.559	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	64	ASN	0	0.001	0.002	33.763	0.005	0.005	0.000	0.000	0.000	0.000
48	A	65	ALA	0	0.019	0.015	28.756	0.001	0.001	0.000	0.000	0.000	0.000
49	A	66	ALA	0	0.000	-0.012	30.321	0.000	0.000	0.000	0.000	0.000	0.000
50	A	67	THR	0	-0.084	-0.046	32.107	0.004	0.004	0.000	0.000	0.000	0.000
51	A	68	MET	0	0.020	0.045	29.149	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	69	ALA	0	-0.004	0.010	28.048	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	70	SER	0	-0.018	-0.015	27.721	0.000	0.000	0.000	0.000	0.000	0.000
54	A	71	GLU	-1	-0.909	-0.959	29.217	-0.049	-0.049	0.000	0.000	0.000	0.000
55	A	72	TYR	0	-0.015	-0.018	24.071	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	73	GLY	0	-0.050	-0.023	23.978	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	74	LEU	0	-0.025	0.003	21.984	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	75	THR	0	0.014	-0.004	25.543	0.005	0.005	0.000	0.000	0.000	0.000
59	A	76	ALA	0	0.072	0.020	27.844	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	77	GLU	-1	-0.865	-0.926	28.655	-0.072	-0.072	0.000	0.000	0.000	0.000
61	A	78	ASP	-1	-0.818	-0.868	22.977	-0.125	-0.125	0.000	0.000	0.000	0.000
62	A	79	ALA	0	0.049	0.023	25.556	-0.010	-0.010	0.000	0.000	0.000	0.000
63	A	80	ILE	0	0.040	0.018	26.882	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	81	ASN	0	-0.060	-0.021	25.860	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	82	ILE	0	0.040	0.035	20.785	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	83	PHE	0	0.016	-0.010	24.401	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	84	SER	0	-0.030	-0.034	27.042	0.004	0.004	0.000	0.000	0.000	0.000
68	A	85	ASP	-1	-0.781	-0.860	23.863	-0.131	-0.131	0.000	0.000	0.000	0.000
69	A	86	GLN	0	-0.030	-0.024	21.822	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	87	VAL	0	-0.060	-0.031	25.719	0.001	0.001	0.000	0.000	0.000	0.000
71	A	88	GLU	-1	-0.841	-0.912	28.002	-0.084	-0.084	0.000	0.000	0.000	0.000
72	A	89	ALA	0	0.034	0.032	24.541	0.002	0.002	0.000	0.000	0.000	0.000
73	A	90	ASN	0	-0.032	-0.013	26.487	0.009	0.009	0.000	0.000	0.000	0.000
74	A	91	LYS	1	0.764	0.852	28.585	0.086	0.086	0.000	0.000	0.000	0.000
75	A	92	GLU	-1	-0.907	-0.947	26.315	-0.128	-0.128	0.000	0.000	0.000	0.000
76	A	93	VAL	0	0.043	0.015	26.498	0.004	0.004	0.000	0.000	0.000	0.000
77	A	94	GLN	0	0.017	0.004	29.534	0.012	0.012	0.000	0.000	0.000	0.000
78	A	95	TYR	0	0.003	-0.017	33.006	0.007	0.007	0.000	0.000	0.000	0.000
79	A	96	ALA	0	-0.008	0.009	31.218	0.005	0.005	0.000	0.000	0.000	0.000
80	A	97	LEU	0	-0.005	0.000	30.703	0.004	0.004	0.000	0.000	0.000	0.000
81	A	98	LEU	0	0.013	0.015	33.998	0.005	0.005	0.000	0.000	0.000	0.000
82	A	99	ASN	0	-0.007	-0.008	36.871	0.006	0.006	0.000	0.000	0.000	0.000
83	A	100	ASN	0	-0.001	0.007	32.761	0.006	0.006	0.000	0.000	0.000	0.000
84	A	101	TRP	0	0.035	0.013	34.175	0.003	0.003	0.000	0.000	0.000	0.000
85	A	102	ARG	1	0.914	0.950	39.275	0.061	0.061	0.000	0.000	0.000	0.000
86	A	103	ARG	1	0.857	0.921	36.170	0.070	0.070	0.000	0.000	0.000	0.000
87	A	104	GLN	0	-0.051	-0.017	37.485	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	105	GLY	0	-0.012	0.001	42.282	0.002	0.002	0.000	0.000	0.000	0.000
89	A	106	ASP	-1	-0.887	-0.943	42.555	-0.049	-0.049	0.000	0.000	0.000	0.000
90	A	107	ALA	0	-0.066	-0.021	38.926	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	108	PRO	0	0.002	0.006	35.135	0.002	0.002	0.000	0.000	0.000	0.000
92	A	109	ALA	0	0.051	0.024	38.202	0.001	0.001	0.000	0.000	0.000	0.000
93	A	110	THR	0	-0.024	-0.009	34.025	0.002	0.002	0.000	0.000	0.000	0.000
94	A	111	PRO	0	0.021	0.021	36.671	0.002	0.002	0.000	0.000	0.000	0.000
95	A	112	ARG	1	0.806	0.863	37.036	0.054	0.054	0.000	0.000	0.000	0.000
96	A	113	GLN	0	-0.011	-0.007	32.223	0.001	0.001	0.000	0.000	0.000	0.000
97	A	114	SER	0	0.031	0.014	37.294	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	115	LEU	0	0.088	0.038	36.251	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	116	ALA	0	-0.024	-0.012	37.016	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	117	GLY	0	-0.006	-0.005	38.584	0.000	0.000	0.000	0.000	0.000	0.000
101	A	118	VAL	0	-0.007	-0.012	33.670	0.000	0.000	0.000	0.000	0.000	0.000
102	A	119	ILE	0	0.017	0.002	31.917	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	120	ARG	1	0.974	0.994	32.373	0.050	0.050	0.000	0.000	0.000	0.000
104	A	121	PRO	0	0.040	0.018	33.045	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	122	ILE	0	-0.045	-0.018	27.792	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	123	LEU	0	-0.018	-0.014	28.342	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	124	ASP	-1	-0.884	-0.942	28.888	-0.073	-0.073	0.000	0.000	0.000	0.000
108	A	125	LYS	1	0.904	0.948	27.533	0.081	0.081	0.000	0.000	0.000	0.000
109	A	126	LEU	0	0.000	0.002	22.967	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	127	GLN	0	-0.063	-0.037	24.392	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	128	ALA	0	0.069	0.034	25.382	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	129	SER	0	-0.014	-0.008	21.716	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	130	ILE	0	0.017	0.011	20.448	-0.014	-0.014	0.000	0.000	0.000	0.000
114	A	131	MET	0	-0.017	0.007	20.537	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	132	GLN	0	0.003	0.001	20.604	0.009	0.009	0.000	0.000	0.000	0.000
116	A	133	ASN	0	-0.037	-0.018	16.703	0.000	0.000	0.000	0.000	0.000	0.000
117	A	134	LEU	0	-0.022	-0.015	16.802	-0.021	-0.021	0.000	0.000	0.000	0.000
118	A	135	GLN	0	0.005	0.010	17.910	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	136	SER	0	-0.063	-0.043	15.906	0.020	0.020	0.000	0.000	0.000	0.000
120	A	137	VAL	0	-0.015	-0.003	11.655	0.010	0.010	0.000	0.000	0.000	0.000
121	A	138	ALA	0	0.010	0.001	14.039	-0.010	-0.010	0.000	0.000	0.000	0.000
122	A	139	PRO	0	-0.024	-0.013	13.157	0.003	0.003	0.000	0.000	0.000	0.000
123	A	140	LEU	0	0.005	0.001	8.344	0.009	0.009	0.000	0.000	0.000	0.000
124	A	141	ARG	1	0.773	0.849	12.104	0.107	0.107	0.000	0.000	0.000	0.000
125	A	142	SER	0	0.019	0.010	14.921	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	143	ILE	0	-0.055	-0.010	8.925	0.039	0.039	0.000	0.000	0.000	0.000
127	A	144	ALA	0	0.023	0.001	12.583	-0.034	-0.034	0.000	0.000	0.000	0.000
128	A	145	ASP	-1	-0.890	-0.952	7.214	-0.533	-0.533	0.000	0.000	0.000	0.000
129	A	146	CYS	0	-0.032	0.018	9.976	-0.121	-0.121	0.000	0.000	0.000	0.000
130	A	147	HIS	0	0.046	0.004	11.776	-0.069	-0.069	0.000	0.000	0.000	0.000
131	A	148	ALA	0	0.007	0.010	9.992	-0.014	-0.014	0.000	0.000	0.000	0.000
132	A	149	LEU	0	-0.018	0.014	5.391	-0.121	-0.121	0.000	0.000	0.000	0.000
133	A	150	VAL	0	0.045	0.019	8.529	-0.062	-0.062	0.000	0.000	0.000	0.000
134	A	151	ALA	0	0.032	0.015	11.533	0.008	0.008	0.000	0.000	0.000	0.000
135	A	152	SER	0	-0.032	-0.024	7.479	0.013	0.013	0.000	0.000	0.000	0.000
136	A	153	ALA	0	-0.014	-0.003	9.107	0.011	0.011	0.000	0.000	0.000	0.000
137	A	154	VAL	0	0.009	0.004	9.937	0.063	0.063	0.000	0.000	0.000	0.000
138	A	155	GLY	0	-0.013	0.000	12.305	0.051	0.051	0.000	0.000	0.000	0.000
139	A	156	GLN	0	-0.033	-0.026	6.923	0.206	0.206	0.000	0.000	0.000	0.000
140	A	157	VAL	0	-0.001	-0.002	11.314	0.060	0.060	0.000	0.000	0.000	0.000
141	A	158	ALA	0	-0.016	-0.017	14.108	0.051	0.051	0.000	0.000	0.000	0.000
142	A	159	GLU	-1	-0.921	-0.953	13.900	-0.203	-0.203	0.000	0.000	0.000	0.000
143	A	160	GLN	0	-0.037	-0.015	11.295	0.061	0.061	0.000	0.000	0.000	0.000
144	A	161	ALA	0	-0.050	-0.027	16.049	0.030	0.030	0.000	0.000	0.000	0.000
145	A	162	SER	0	-0.035	-0.010	18.871	0.028	0.028	0.000	0.000	0.000	0.000
146	A	163	LEU	0	-0.046	-0.006	18.808	0.018	0.018	0.000	0.000	0.000	0.000
147	A	164	ASP	-1	-0.807	-0.876	21.272	-0.138	-0.138	0.000	0.000	0.000	0.000
148	A	165	VAL	0	0.012	-0.021	22.598	-0.011	-0.011	0.000	0.000	0.000	0.000
149	A	166	LEU	0	-0.023	0.002	23.646	-0.005	-0.005	0.000	0.000	0.000	0.000
150	A	167	HIS	1	0.818	0.854	22.948	0.133	0.133	0.000	0.000	0.000	0.000
151	A	168	ARG	1	0.982	0.999	16.630	0.215	0.215	0.000	0.000	0.000	0.000
152	A	169	ALA	0	-0.009	0.009	20.105	-0.012	-0.012	0.000	0.000	0.000	0.000
153	A	170	ALA	0	0.051	0.023	22.429	-0.003	-0.003	0.000	0.000	0.000	0.000
154	A	171	LEU	0	-0.038	-0.024	16.771	0.001	0.001	0.000	0.000	0.000	0.000
155	A	172	ASP	-1	-0.885	-0.963	17.177	-0.279	-0.279	0.000	0.000	0.000	0.000
156	A	173	ARG	1	0.788	0.907	19.356	0.135	0.135	0.000	0.000	0.000	0.000
157	A	174	ALA	0	-0.006	-0.006	20.686	0.008	0.008	0.000	0.000	0.000	0.000
158	A	175	VAL	0	-0.007	-0.012	15.892	0.004	0.004	0.000	0.000	0.000	0.000
159	A	176	ALA	0	-0.033	0.001	18.126	-0.010	-0.010	0.000	0.000	0.000	0.000
160	A	177	ARG	1	0.799	0.869	20.213	0.119	0.119	0.000	0.000	0.000	0.000
161	A	178	ILE	0	0.034	0.022	14.793	0.013	0.013	0.000	0.000	0.000	0.000
162	A	180	VAL	0	-0.008	0.000	16.841	0.021	0.021	0.000	0.000	0.000	0.000
163	A	181	LYS	1	0.987	0.992	18.509	0.090	0.090	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

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