FMO DATABASE

FMODB ID: LNN99

Calculation Name: 5IX3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5IX3

Chain ID: A

ChEMBL ID:

UniProt ID: U5NVV0

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	166
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1867128.454447
FMO2-HF: Nuclear repulsion	1798049.275988
FMO2-HF: Total energy	-69079.178459
FMO2-MP2: Total energy	-69282.472205

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:0:ALA)

Summations of interaction energy for fragment #1(A:0:ALA)

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.
-11.974	-5.715	0.794	-3.162	-3.891	-0.015

Interaction energy analysis for fragmet #1(A:0:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.007 / 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	2	LYS	1	0.900	0.944	3.672	0.226	2.195	-0.023	-0.985	-0.961	0.004
4	A	3	LEU	0	-0.004	0.008	6.017	0.134	0.134	0.000	0.000	0.000	0.000
5	A	4	ARG	1	0.738	0.819	9.754	0.591	0.591	0.000	0.000	0.000	0.000
6	A	5	ALA	0	0.004	0.011	11.645	0.064	0.064	0.000	0.000	0.000	0.000
7	A	6	LEU	0	-0.008	0.001	15.435	-0.043	-0.043	0.000	0.000	0.000	0.000
8	A	7	GLU	-1	-0.909	-0.963	16.968	-0.331	-0.331	0.000	0.000	0.000	0.000
9	A	8	TYR	0	0.042	0.024	19.459	0.010	0.010	0.000	0.000	0.000	0.000
10	A	9	SER	0	-0.003	-0.015	18.347	0.015	0.015	0.000	0.000	0.000	0.000
11	A	10	ASP	-1	-0.819	-0.876	16.285	-0.463	-0.463	0.000	0.000	0.000	0.000
12	A	11	LEU	0	0.007	0.001	19.096	0.018	0.018	0.000	0.000	0.000	0.000
13	A	12	LEU	0	0.025	0.015	21.151	0.021	0.021	0.000	0.000	0.000	0.000
14	A	13	PHE	0	0.023	0.009	15.103	0.015	0.015	0.000	0.000	0.000	0.000
15	A	14	VAL	0	0.006	-0.003	19.195	0.028	0.028	0.000	0.000	0.000	0.000
16	A	15	HIS	0	0.011	0.003	20.868	0.014	0.014	0.000	0.000	0.000	0.000
17	A	16	GLU	-1	-0.924	-0.958	19.566	-0.059	-0.059	0.000	0.000	0.000	0.000
18	A	17	LEU	0	0.019	0.005	17.165	0.024	0.024	0.000	0.000	0.000	0.000
19	A	18	ASN	0	-0.017	-0.028	20.848	0.038	0.038	0.000	0.000	0.000	0.000
20	A	19	ASN	0	-0.025	-0.006	24.016	0.003	0.003	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.946	-0.968	21.659	0.041	0.041	0.000	0.000	0.000	0.000
22	A	21	TYR	0	-0.102	-0.041	20.642	0.032	0.032	0.000	0.000	0.000	0.000
23	A	22	SER	0	-0.032	-0.026	26.883	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	23	ILE	0	-0.080	-0.030	28.360	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	24	MET	0	0.042	0.020	29.648	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	25	SER	0	0.045	0.022	26.348	0.007	0.007	0.000	0.000	0.000	0.000
27	A	26	TYR	0	-0.016	-0.010	28.308	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	27	TRP	0	0.009	-0.012	22.545	-0.007	-0.007	0.000	0.000	0.000	0.000
29	A	28	PHE	0	-0.027	-0.023	26.066	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	29	GLU	-1	-0.925	-0.958	30.006	-0.022	-0.022	0.000	0.000	0.000	0.000
31	A	30	GLU	-1	-0.812	-0.858	32.166	-0.052	-0.052	0.000	0.000	0.000	0.000
32	A	31	PRO	0	-0.043	-0.024	31.957	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	32	TYR	0	-0.044	-0.028	25.477	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	33	GLU	-1	-0.936	-0.984	30.596	-0.026	-0.026	0.000	0.000	0.000	0.000
35	A	34	SER	0	-0.052	-0.001	30.240	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	35	LEU	0	0.020	0.008	25.122	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	36	THR	0	0.009	-0.015	28.308	-0.008	-0.008	0.000	0.000	0.000	0.000
38	A	37	GLU	-1	-0.866	-0.935	31.430	-0.056	-0.056	0.000	0.000	0.000	0.000
39	A	38	LEU	0	0.002	0.016	24.312	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	39	GLN	0	-0.036	-0.023	26.197	0.003	0.003	0.000	0.000	0.000	0.000
41	A	40	HIS	0	0.027	0.019	28.915	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	41	LEU	0	-0.026	-0.013	30.257	0.001	0.001	0.000	0.000	0.000	0.000
43	A	42	PHE	0	-0.029	-0.015	23.090	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	43	ASP	-1	-0.878	-0.951	28.148	-0.135	-0.135	0.000	0.000	0.000	0.000
45	A	44	LYS	1	0.739	0.860	30.395	0.062	0.062	0.000	0.000	0.000	0.000
46	A	45	HIS	1	0.803	0.883	29.301	0.076	0.076	0.000	0.000	0.000	0.000
47	A	46	LEU	0	0.043	0.039	25.439	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	47	LEU	0	-0.086	-0.054	26.728	-0.010	-0.010	0.000	0.000	0.000	0.000
49	A	48	ASP	-1	-0.810	-0.875	28.670	-0.057	-0.057	0.000	0.000	0.000	0.000
50	A	49	GLU	-1	-0.985	-1.000	26.627	-0.081	-0.081	0.000	0.000	0.000	0.000
51	A	50	SER	0	-0.025	-0.034	27.053	0.005	0.005	0.000	0.000	0.000	0.000
52	A	51	GLU	-1	-0.767	-0.873	24.867	-0.049	-0.049	0.000	0.000	0.000	0.000
53	A	52	ARG	1	0.875	0.935	20.399	0.088	0.088	0.000	0.000	0.000	0.000
54	A	53	ARG	1	0.790	0.877	19.054	0.105	0.105	0.000	0.000	0.000	0.000
55	A	54	PHE	0	-0.051	-0.027	13.605	-0.031	-0.031	0.000	0.000	0.000	0.000
56	A	55	ILE	0	0.009	0.019	12.144	0.061	0.061	0.000	0.000	0.000	0.000
57	A	56	VAL	0	-0.034	-0.029	9.246	-0.084	-0.084	0.000	0.000	0.000	0.000
58	A	57	GLU	-1	-0.803	-0.891	7.513	-1.182	-1.182	0.000	0.000	0.000	0.000
59	A	58	ASP	-1	-0.824	-0.903	3.785	-1.097	-0.719	0.000	-0.096	-0.283	0.000
60	A	59	GLU	-1	-0.953	-0.995	2.680	-10.496	-6.711	0.818	-2.070	-2.533	-0.019
61	A	60	ASN	0	-0.053	-0.021	4.696	0.564	0.691	-0.001	-0.011	-0.114	0.000
62	A	61	GLN	0	-0.063	-0.050	7.536	0.410	0.410	0.000	0.000	0.000	0.000
63	A	62	VAL	0	0.010	0.025	8.632	-0.129	-0.129	0.000	0.000	0.000	0.000
64	A	63	VAL	0	-0.031	-0.020	8.887	0.118	0.118	0.000	0.000	0.000	0.000
65	A	64	GLY	0	0.013	-0.020	11.676	0.133	0.133	0.000	0.000	0.000	0.000
66	A	65	ILE	0	-0.024	0.017	14.181	-0.096	-0.096	0.000	0.000	0.000	0.000
67	A	66	VAL	0	0.002	-0.004	14.346	0.060	0.060	0.000	0.000	0.000	0.000
68	A	67	GLU	-1	-0.818	-0.894	16.987	-0.098	-0.098	0.000	0.000	0.000	0.000
69	A	68	LEU	0	-0.041	-0.029	19.696	0.026	0.026	0.000	0.000	0.000	0.000
70	A	69	VAL	0	0.090	0.033	22.288	-0.018	-0.018	0.000	0.000	0.000	0.000
71	A	70	GLU	-1	-0.838	-0.916	25.922	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	71	ILE	0	-0.110	-0.047	23.650	0.007	0.007	0.000	0.000	0.000	0.000
73	A	72	ASN	0	0.077	0.039	27.859	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	73	TYR	0	-0.025	-0.033	25.962	0.005	0.005	0.000	0.000	0.000	0.000
75	A	74	ILE	0	-0.037	-0.015	30.875	0.000	0.000	0.000	0.000	0.000	0.000
76	A	75	HIS	0	-0.010	-0.025	33.446	0.005	0.005	0.000	0.000	0.000	0.000
77	A	76	ARG	1	0.775	0.882	27.034	0.018	0.018	0.000	0.000	0.000	0.000
78	A	77	ASN	0	0.022	0.000	27.776	0.006	0.006	0.000	0.000	0.000	0.000
79	A	78	CYS	0	-0.004	0.013	24.176	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	79	GLU	-1	-0.798	-0.900	25.897	0.031	0.031	0.000	0.000	0.000	0.000
81	A	80	ILE	0	-0.065	-0.036	18.119	-0.011	-0.011	0.000	0.000	0.000	0.000
82	A	81	GLN	0	-0.005	0.001	21.474	0.021	0.021	0.000	0.000	0.000	0.000
83	A	82	ILE	0	-0.019	-0.023	15.374	-0.016	-0.016	0.000	0.000	0.000	0.000
84	A	83	ILE	0	0.012	0.024	17.884	0.028	0.028	0.000	0.000	0.000	0.000
85	A	84	ILE	0	-0.069	-0.038	12.898	-0.010	-0.010	0.000	0.000	0.000	0.000
86	A	85	LYS	1	0.912	0.964	14.702	0.051	0.051	0.000	0.000	0.000	0.000
87	A	86	PRO	0	0.027	0.022	16.082	0.072	0.072	0.000	0.000	0.000	0.000
88	A	87	GLU	-1	-0.853	-0.934	15.819	0.102	0.102	0.000	0.000	0.000	0.000
89	A	88	PHE	0	-0.045	-0.026	10.806	0.071	0.071	0.000	0.000	0.000	0.000
90	A	89	SER	0	-0.056	-0.033	13.496	0.127	0.127	0.000	0.000	0.000	0.000
91	A	90	GLY	0	-0.043	-0.035	15.796	0.018	0.018	0.000	0.000	0.000	0.000
92	A	91	LYS	1	0.940	0.974	10.410	-0.614	-0.614	0.000	0.000	0.000	0.000
93	A	92	GLY	0	0.014	0.016	10.093	0.273	0.273	0.000	0.000	0.000	0.000
94	A	93	TYR	0	0.037	-0.011	6.645	0.224	0.224	0.000	0.000	0.000	0.000
95	A	94	ALA	0	0.021	0.018	10.389	-0.131	-0.131	0.000	0.000	0.000	0.000
96	A	95	LYS	1	0.859	0.915	11.708	-0.815	-0.815	0.000	0.000	0.000	0.000
97	A	96	PHE	0	0.045	0.029	6.425	-0.065	-0.065	0.000	0.000	0.000	0.000
98	A	97	ALA	0	0.021	0.004	9.964	-0.118	-0.118	0.000	0.000	0.000	0.000
99	A	98	PHE	0	0.020	0.006	12.005	-0.072	-0.072	0.000	0.000	0.000	0.000
100	A	99	GLU	-1	-0.797	-0.870	10.924	0.680	0.680	0.000	0.000	0.000	0.000
101	A	100	LYS	1	0.884	0.931	8.080	-0.362	-0.362	0.000	0.000	0.000	0.000
102	A	101	ALA	0	0.045	0.032	12.655	-0.051	-0.051	0.000	0.000	0.000	0.000
103	A	102	ILE	0	0.021	0.026	15.804	-0.025	-0.025	0.000	0.000	0.000	0.000
104	A	103	ILE	0	-0.028	-0.003	13.299	-0.018	-0.018	0.000	0.000	0.000	0.000
105	A	104	TYR	0	0.004	-0.003	15.379	-0.018	-0.018	0.000	0.000	0.000	0.000
106	A	105	ALA	0	0.046	0.024	17.080	-0.011	-0.011	0.000	0.000	0.000	0.000
107	A	106	PHE	0	0.004	-0.005	20.208	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	107	ASN	0	-0.049	-0.038	17.903	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	108	ILE	0	-0.063	-0.016	15.737	-0.012	-0.012	0.000	0.000	0.000	0.000
110	A	109	LEU	0	-0.011	-0.002	20.164	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	110	ASN	0	-0.011	0.011	22.816	0.011	0.011	0.000	0.000	0.000	0.000
112	A	111	MET	0	-0.030	0.020	24.076	0.002	0.002	0.000	0.000	0.000	0.000
113	A	112	HIS	0	-0.051	-0.037	25.861	0.007	0.007	0.000	0.000	0.000	0.000
114	A	113	LYS	1	0.809	0.873	27.123	-0.043	-0.043	0.000	0.000	0.000	0.000
115	A	114	ILE	0	-0.007	0.010	22.127	-0.011	-0.011	0.000	0.000	0.000	0.000
116	A	115	TYR	0	-0.001	-0.009	25.372	0.014	0.014	0.000	0.000	0.000	0.000
117	A	116	LEU	0	0.027	0.030	22.785	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	117	TYR	0	0.020	0.008	26.304	0.004	0.004	0.000	0.000	0.000	0.000
119	A	118	VAL	0	-0.023	-0.004	25.792	0.004	0.004	0.000	0.000	0.000	0.000
120	A	119	ASP	-1	-0.790	-0.868	27.950	0.067	0.067	0.000	0.000	0.000	0.000
121	A	120	ALA	0	0.039	0.009	29.639	0.011	0.011	0.000	0.000	0.000	0.000
122	A	121	ASP	-1	-0.873	-0.931	31.646	0.084	0.084	0.000	0.000	0.000	0.000
123	A	122	ASN	0	-0.078	-0.042	24.728	0.022	0.022	0.000	0.000	0.000	0.000
124	A	123	LYS	1	0.999	0.977	26.329	-0.110	-0.110	0.000	0.000	0.000	0.000
125	A	124	LYS	1	0.980	0.992	19.018	-0.238	-0.238	0.000	0.000	0.000	0.000
126	A	125	ALA	0	-0.010	0.000	21.568	0.025	0.025	0.000	0.000	0.000	0.000
127	A	126	ILE	0	0.050	0.025	22.241	0.011	0.011	0.000	0.000	0.000	0.000
128	A	127	HIS	0	-0.050	-0.017	22.609	0.003	0.003	0.000	0.000	0.000	0.000
129	A	128	ILE	0	-0.033	0.004	17.036	0.023	0.023	0.000	0.000	0.000	0.000
130	A	129	TYR	0	0.041	0.012	19.493	0.005	0.005	0.000	0.000	0.000	0.000
131	A	130	GLU	-1	-0.866	-0.938	21.619	0.172	0.172	0.000	0.000	0.000	0.000
132	A	131	SER	0	-0.148	-0.079	18.597	0.018	0.018	0.000	0.000	0.000	0.000
133	A	132	GLU	-1	-0.917	-0.975	15.954	0.388	0.388	0.000	0.000	0.000	0.000
134	A	133	GLY	0	-0.005	-0.001	19.515	-0.019	-0.019	0.000	0.000	0.000	0.000
135	A	134	PHE	0	-0.061	-0.026	20.494	-0.022	-0.022	0.000	0.000	0.000	0.000
136	A	135	LYS	1	0.943	0.971	24.860	-0.095	-0.095	0.000	0.000	0.000	0.000
137	A	136	THR	0	0.002	-0.003	28.551	-0.005	-0.005	0.000	0.000	0.000	0.000
138	A	137	GLU	-1	-0.839	-0.902	31.068	0.059	0.059	0.000	0.000	0.000	0.000
139	A	138	GLY	0	-0.006	-0.004	33.548	-0.006	-0.006	0.000	0.000	0.000	0.000
140	A	139	LEU	0	-0.028	-0.011	34.040	0.005	0.005	0.000	0.000	0.000	0.000
141	A	140	LEU	0	-0.048	-0.015	34.442	-0.004	-0.004	0.000	0.000	0.000	0.000
142	A	141	LYS	1	0.935	0.948	37.127	-0.049	-0.049	0.000	0.000	0.000	0.000
143	A	142	GLU	-1	-0.956	-0.995	39.345	0.029	0.029	0.000	0.000	0.000	0.000
144	A	143	GLN	0	0.015	0.025	35.567	-0.002	-0.002	0.000	0.000	0.000	0.000
145	A	144	PHE	0	0.021	0.010	32.163	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	145	TYR	0	0.007	0.022	36.062	0.003	0.003	0.000	0.000	0.000	0.000
147	A	146	THR	0	-0.001	-0.012	33.002	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	147	LYS	1	0.950	0.956	31.640	-0.051	-0.051	0.000	0.000	0.000	0.000
149	A	148	GLY	0	0.015	0.012	36.493	0.002	0.002	0.000	0.000	0.000	0.000
150	A	149	LYS	1	0.907	0.955	38.560	-0.041	-0.041	0.000	0.000	0.000	0.000
151	A	150	TYR	0	0.074	0.048	38.412	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	151	LYS	1	0.701	0.829	33.035	-0.062	-0.062	0.000	0.000	0.000	0.000
153	A	152	ASP	-1	-0.776	-0.878	36.312	0.048	0.048	0.000	0.000	0.000	0.000
154	A	153	ALA	0	-0.025	-0.016	31.772	0.005	0.005	0.000	0.000	0.000	0.000
155	A	154	TYR	0	-0.052	-0.025	30.091	-0.004	-0.004	0.000	0.000	0.000	0.000
156	A	155	PHE	0	0.015	0.037	30.482	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	156	MET	0	-0.008	-0.019	26.279	0.005	0.005	0.000	0.000	0.000	0.000
158	A	157	SER	0	-0.034	-0.026	26.897	-0.005	-0.005	0.000	0.000	0.000	0.000
159	A	158	LEU	0	0.051	0.039	21.557	0.009	0.009	0.000	0.000	0.000	0.000
160	A	159	LEU	0	-0.019	-0.012	25.764	-0.014	-0.014	0.000	0.000	0.000	0.000
161	A	160	LYS	1	0.918	0.981	24.113	-0.021	-0.021	0.000	0.000	0.000	0.000
162	A	161	SER	0	0.001	-0.024	25.489	0.006	0.006	0.000	0.000	0.000	0.000
163	A	162	GLU	-1	-0.870	-0.943	26.457	0.102	0.102	0.000	0.000	0.000	0.000
164	A	163	TYR	0	0.002	-0.001	16.803	0.000	0.000	0.000	0.000	0.000	0.000
165	A	164	ILE	0	-0.062	-0.028	22.359	0.014	0.014	0.000	0.000	0.000	0.000
166	A	165	LEU	0	-0.057	-0.007	24.075	0.004	0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ALA)