FMO DATABASE

FMODB ID: QNV8Y

Calculation Name: 1I1G-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1I1G

Chain ID: A

ChEMBL ID:

UniProt ID: P42180

Base Structure: X-ray

Registration Date: 2023-09-27

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	140
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1130934.959478
FMO2-HF: Nuclear repulsion	1076482.493308
FMO2-HF: Total energy	-54452.46617
FMO2-MP2: Total energy	-54613.369791

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:2:ILE)

Summations of interaction energy for fragment #1(A:2:ILE)

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.
-6.692	0.183	7.309	-3.945	-10.239	-0.004

Interaction energy analysis for fragmet #1(A:2:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.033 / q_NPA : 0.016

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	4	GLU	-1	-0.802	-0.916	3.288	-5.091	-2.384	0.073	-1.423	-1.358	0.002
4	A	5	ARG	1	0.892	0.949	5.337	1.031	1.172	-0.001	-0.006	-0.134	0.000
5	A	6	ASP	-1	-0.791	-0.893	2.218	0.601	1.293	3.118	-1.291	-2.519	-0.003
6	A	7	LYS	1	0.896	0.962	2.795	0.368	2.065	0.856	-0.590	-1.963	-0.003
7	A	8	ILE	0	0.002	-0.002	3.538	0.505	0.420	0.037	0.297	-0.249	0.000
8	A	9	ILE	0	-0.023	-0.019	5.738	0.206	0.206	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.028	0.015	2.421	-0.026	-0.300	1.816	-0.233	-1.309	-0.001
10	A	11	GLU	-1	-0.848	-0.916	6.120	-0.811	-0.811	0.000	0.000	0.000	0.000
11	A	12	ILE	0	-0.054	-0.037	8.241	0.088	0.088	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.014	-0.009	8.633	0.052	0.052	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.952	-0.981	9.152	-0.234	-0.234	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.794	0.913	10.757	0.486	0.486	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.826	-0.905	13.989	-0.048	-0.048	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.044	0.039	13.649	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.837	0.901	14.677	0.068	0.068	0.000	0.000	0.000	0.000
18	A	19	THR	0	-0.051	-0.027	14.275	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.028	0.025	15.396	0.013	0.013	0.000	0.000	0.000	0.000
20	A	21	PHE	0	0.082	0.008	13.118	-0.026	-0.026	0.000	0.000	0.000	0.000
21	A	22	THR	0	0.013	-0.030	15.431	-0.026	-0.026	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.880	-0.928	17.126	-0.155	-0.155	0.000	0.000	0.000	0.000
23	A	24	ILE	0	0.036	0.013	10.327	-0.031	-0.031	0.000	0.000	0.000	0.000
24	A	25	ALA	0	-0.040	-0.008	13.224	-0.046	-0.046	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.867	0.919	15.076	0.096	0.096	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.864	0.928	14.037	0.192	0.192	0.000	0.000	0.000	0.000
27	A	28	LEU	0	0.000	0.007	8.878	-0.058	-0.058	0.000	0.000	0.000	0.000
28	A	29	GLY	0	-0.013	0.017	13.459	-0.022	-0.022	0.000	0.000	0.000	0.000
29	A	30	ILE	0	-0.023	-0.010	11.010	0.019	0.019	0.000	0.000	0.000	0.000
30	A	31	SER	0	0.034	0.012	15.572	0.019	0.019	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.732	-0.841	15.464	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	33	THR	0	-0.013	-0.014	15.645	0.017	0.017	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.006	0.019	12.696	0.044	0.044	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.025	0.020	11.061	0.049	0.049	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.867	0.920	11.249	-0.013	-0.013	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.935	0.968	11.459	-0.269	-0.269	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.781	0.865	5.478	0.279	0.279	0.000	0.000	0.000	0.000
38	A	39	VAL	0	0.053	0.028	7.873	0.158	0.158	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.805	0.890	9.462	-0.318	-0.318	0.000	0.000	0.000	0.000
40	A	41	ALA	0	0.000	-0.001	7.598	0.059	0.059	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.040	-0.034	3.113	-0.419	0.295	0.104	-0.164	-0.653	0.000
42	A	43	GLU	-1	-0.785	-0.864	6.298	0.338	0.338	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.881	-0.931	9.724	0.512	0.512	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.795	0.905	2.711	-4.232	-3.545	0.112	-0.228	-0.572	0.003
45	A	46	GLY	0	0.033	0.023	7.686	0.130	0.130	0.000	0.000	0.000	0.000
46	A	47	ILE	0	-0.060	-0.031	2.408	-0.720	-0.124	1.194	-0.307	-1.482	-0.002
47	A	48	ILE	0	-0.066	-0.032	6.322	-0.228	-0.228	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.902	-0.949	8.809	0.348	0.348	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.001	-0.001	11.864	-0.014	-0.014	0.000	0.000	0.000	0.000
50	A	51	TYR	0	-0.105	-0.060	13.017	-0.047	-0.047	0.000	0.000	0.000	0.000
51	A	52	THR	0	0.022	0.004	15.208	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.002	0.002	17.613	-0.020	-0.020	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.945	0.970	17.818	0.013	0.013	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.043	0.024	20.372	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	56	ASN	0	-0.017	-0.015	24.025	0.000	0.000	0.000	0.000	0.000	0.000
56	A	57	PRO	0	0.064	0.039	25.433	0.002	0.002	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.883	0.946	28.425	0.030	0.030	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.926	0.951	29.448	0.038	0.038	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.020	0.003	29.106	0.002	0.002	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.036	0.023	32.463	0.004	0.004	0.000	0.000	0.000	0.000
61	A	62	TYR	0	0.014	0.003	30.726	0.001	0.001	0.000	0.000	0.000	0.000
62	A	63	SER	0	-0.039	-0.054	31.356	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	64	LEU	0	-0.020	0.009	32.791	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	65	VAL	0	0.026	0.020	25.978	0.005	0.005	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.033	-0.023	29.119	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	67	ILE	0	0.015	0.016	24.630	0.007	0.007	0.000	0.000	0.000	0.000
67	A	68	THR	0	0.000	-0.014	27.659	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.006	0.014	29.240	0.007	0.007	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.010	-0.021	30.425	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.797	-0.860	31.660	0.035	0.035	0.000	0.000	0.000	0.000
71	A	72	THR	0	0.050	0.004	32.649	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.844	0.921	35.729	-0.049	-0.049	0.000	0.000	0.000	0.000
73	A	74	PRO	0	0.008	-0.008	34.654	0.004	0.004	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.861	-0.926	34.358	0.062	0.062	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.829	0.908	35.341	-0.055	-0.055	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.036	-0.017	28.697	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	78	PHE	0	0.068	0.020	25.425	0.000	0.000	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.799	-0.907	30.320	0.086	0.086	0.000	0.000	0.000	0.000
79	A	80	VAL	0	-0.056	-0.026	32.031	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	81	ALA	0	0.017	0.010	27.070	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.876	-0.931	28.541	0.127	0.127	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.864	0.929	29.820	-0.069	-0.069	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.045	-0.024	29.277	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.773	0.870	25.169	-0.118	-0.118	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.818	-0.895	27.719	0.103	0.103	0.000	0.000	0.000	0.000
86	A	87	TYR	0	-0.054	-0.025	30.469	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.814	-0.899	28.604	0.053	0.053	0.000	0.000	0.000	0.000
88	A	89	PHE	0	0.016	0.000	29.417	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	90	VAL	0	-0.026	-0.021	25.758	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.775	0.879	24.131	-0.045	-0.045	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.897	-0.923	19.420	0.033	0.033	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.038	-0.014	21.724	-0.013	-0.013	0.000	0.000	0.000	0.000
93	A	94	TYR	0	-0.048	-0.045	17.330	0.020	0.020	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.017	0.007	22.164	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	96	SER	0	-0.038	-0.024	22.397	0.001	0.001	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.014	0.001	24.064	0.005	0.005	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.004	0.006	25.828	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.939	-0.977	27.531	0.009	0.009	0.000	0.000	0.000	0.000
99	A	100	HIS	1	0.816	0.879	29.460	-0.022	-0.022	0.000	0.000	0.000	0.000
100	A	101	MET	0	0.034	0.029	28.205	0.005	0.005	0.000	0.000	0.000	0.000
101	A	102	ILE	0	-0.003	0.014	26.978	0.010	0.010	0.000	0.000	0.000	0.000
102	A	103	MET	0	-0.022	-0.005	21.983	-0.012	-0.012	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.069	0.035	24.846	0.010	0.010	0.000	0.000	0.000	0.000
104	A	105	VAL	0	-0.002	0.002	22.412	-0.011	-0.011	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.005	0.001	25.561	0.006	0.006	0.000	0.000	0.000	0.000
106	A	107	TRP	0	-0.043	-0.028	24.319	-0.009	-0.009	0.000	0.000	0.000	0.000
107	A	108	ALA	0	0.042	0.035	30.091	0.004	0.004	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.788	0.875	33.401	-0.017	-0.017	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.821	-0.886	35.845	0.001	0.001	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.066	0.018	38.142	0.002	0.002	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.888	-0.942	39.974	0.003	0.003	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.790	-0.883	36.612	0.017	0.017	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.015	-0.015	34.668	0.003	0.003	0.000	0.000	0.000	0.000
114	A	115	ALA	0	0.022	0.012	37.350	0.003	0.003	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.826	-0.897	40.460	0.024	0.024	0.000	0.000	0.000	0.000
116	A	117	ILE	0	-0.004	-0.002	33.968	0.003	0.003	0.000	0.000	0.000	0.000
117	A	118	ILE	0	0.011	0.001	35.754	0.004	0.004	0.000	0.000	0.000	0.000
118	A	119	SER	0	-0.043	-0.030	37.941	0.003	0.003	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.059	-0.054	40.932	0.003	0.003	0.000	0.000	0.000	0.000
120	A	121	LYS	1	0.820	0.944	36.776	-0.028	-0.028	0.000	0.000	0.000	0.000
121	A	122	ILE	0	0.048	0.019	33.227	0.004	0.004	0.000	0.000	0.000	0.000
122	A	123	GLY	0	-0.008	-0.010	36.438	0.003	0.003	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.838	0.911	39.410	-0.030	-0.030	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.036	0.006	34.047	0.002	0.002	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.758	-0.867	38.185	0.049	0.049	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.013	0.000	37.217	0.006	0.006	0.000	0.000	0.000	0.000
127	A	128	VAL	0	-0.004	0.005	35.167	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	129	THR	0	-0.056	-0.034	37.339	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.841	0.907	36.729	-0.028	-0.028	0.000	0.000	0.000	0.000
130	A	131	VAL	0	0.033	0.031	34.252	0.004	0.004	0.000	0.000	0.000	0.000
131	A	132	CYS	0	-0.064	-0.037	33.199	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	133	PRO	0	0.027	0.027	32.305	0.000	0.000	0.000	0.000	0.000	0.000
133	A	134	ALA	0	0.025	0.011	29.804	-0.003	-0.003	0.000	0.000	0.000	0.000
134	A	135	ILE	0	-0.004	-0.001	29.954	0.000	0.000	0.000	0.000	0.000	0.000
135	A	136	ILE	0	-0.023	-0.011	24.741	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	137	LEU	0	-0.003	0.002	28.900	0.001	0.001	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.936	-0.977	27.545	-0.069	-0.069	0.000	0.000	0.000	0.000
138	A	139	LYS	1	0.897	0.936	20.185	0.083	0.083	0.000	0.000	0.000	0.000
139	A	140	LEU	0	0.047	0.027	23.094	-0.007	-0.007	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.988	1.007	14.129	0.282	0.282	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ILE)