FMO DATABASE

FMODB ID: RY818

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1132972.668245
FMO2-HF: Nuclear repulsion	1078522.005652
FMO2-HF: Total energy	-54450.662593
FMO2-MP2: Total energy	-54611.844812

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.
-8.866	-3.44	11.751	-4.135	-13.044	-0.005

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 : -0.042 / q_NPA : -0.002

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	-0.838	-0.929	2.666	-8.239	-5.316	1.079	-0.912	-3.091	0.002
4	A	5	ARG	1	0.929	0.973	5.807	0.801	0.801	0.000	0.000	0.000	0.000
5	A	6	ASP	-1	-0.814	-0.915	2.147	-0.196	0.558	3.606	-1.664	-2.696	0.000
6	A	7	LYS	1	0.904	0.988	2.716	0.903	2.167	1.294	-0.642	-1.916	-0.006
7	A	8	ILE	0	-0.015	-0.019	3.514	0.869	0.926	0.010	0.166	-0.234	0.000
8	A	9	ILE	0	-0.035	-0.028	5.391	0.310	0.310	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.054	0.025	2.184	0.748	-0.497	3.202	-0.359	-1.598	-0.001
10	A	11	GLU	-1	-0.869	-0.919	5.963	-1.047	-1.047	0.000	0.000	0.000	0.000
11	A	12	ILE	0	-0.028	-0.027	8.257	0.167	0.167	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.006	0.006	8.412	0.087	0.087	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.980	-0.995	9.064	-0.324	-0.324	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.802	0.912	10.966	0.713	0.713	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.824	-0.910	13.728	-0.098	-0.098	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.006	0.009	13.449	-0.010	-0.010	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.889	0.934	14.397	0.129	0.129	0.000	0.000	0.000	0.000
18	A	19	THR	0	-0.072	-0.038	13.992	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.046	0.033	15.115	0.012	0.012	0.000	0.000	0.000	0.000
20	A	21	PHE	0	0.072	0.015	12.407	-0.031	-0.031	0.000	0.000	0.000	0.000
21	A	22	THR	0	0.036	-0.016	14.910	-0.039	-0.039	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.885	-0.946	16.563	-0.220	-0.220	0.000	0.000	0.000	0.000
23	A	24	ILE	0	0.049	0.014	9.984	-0.037	-0.037	0.000	0.000	0.000	0.000
24	A	25	ALA	0	-0.012	0.008	13.259	-0.048	-0.048	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.880	0.933	14.690	0.137	0.137	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.834	0.915	13.589	0.295	0.295	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.033	-0.018	8.759	-0.046	-0.046	0.000	0.000	0.000	0.000
28	A	29	GLY	0	-0.006	0.023	13.234	-0.011	-0.011	0.000	0.000	0.000	0.000
29	A	30	ILE	0	-0.032	-0.009	10.494	0.046	0.046	0.000	0.000	0.000	0.000
30	A	31	SER	0	0.039	0.001	15.075	0.011	0.011	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.748	-0.841	14.785	-0.023	-0.023	0.000	0.000	0.000	0.000
32	A	33	THR	0	0.035	0.017	14.826	0.005	0.005	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.008	0.013	12.180	0.055	0.055	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.031	0.024	10.633	0.047	0.047	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.825	0.896	10.953	-0.026	-0.026	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.952	0.967	10.989	-0.355	-0.355	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.729	0.831	5.375	0.163	0.163	0.000	0.000	0.000	0.000
38	A	39	VAL	0	0.064	0.055	7.362	0.156	0.156	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.830	0.923	8.771	-0.323	-0.323	0.000	0.000	0.000	0.000
40	A	41	ALA	0	0.005	0.006	7.274	0.079	0.079	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.034	-0.026	2.640	-0.623	0.114	0.853	-0.253	-1.337	-0.001
42	A	43	GLU	-1	-0.789	-0.896	5.865	0.359	0.359	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.949	-0.970	9.403	0.534	0.534	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.856	0.940	3.176	-3.793	-3.301	0.022	-0.159	-0.355	0.002
45	A	46	GLY	0	0.078	0.036	7.833	-0.035	-0.035	0.000	0.000	0.000	0.000
46	A	47	ILE	0	-0.108	-0.056	2.310	-0.690	-0.246	1.685	-0.312	-1.817	-0.001
47	A	48	ILE	0	-0.052	-0.019	5.979	-0.260	-0.260	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.884	-0.934	8.188	0.353	0.353	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.018	-0.022	11.403	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	51	TYR	0	-0.102	-0.058	12.179	-0.066	-0.066	0.000	0.000	0.000	0.000
51	A	52	THR	0	0.026	0.009	15.159	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.011	0.000	17.436	-0.020	-0.020	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.955	0.983	17.661	0.087	0.087	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.047	0.018	19.927	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	56	ASN	0	-0.037	-0.035	23.649	0.003	0.003	0.000	0.000	0.000	0.000
56	A	57	PRO	0	0.090	0.062	25.430	0.003	0.003	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.936	0.972	28.341	0.065	0.065	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.943	0.974	29.528	0.076	0.076	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.024	-0.008	28.545	0.003	0.003	0.000	0.000	0.000	0.000
60	A	61	GLY	0	-0.007	0.000	31.997	0.005	0.005	0.000	0.000	0.000	0.000
61	A	62	TYR	0	-0.032	-0.037	30.436	0.002	0.002	0.000	0.000	0.000	0.000
62	A	63	SER	0	-0.047	-0.044	31.212	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	64	LEU	0	0.040	0.031	32.603	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	65	VAL	0	0.007	0.015	25.772	0.005	0.005	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.029	-0.034	29.178	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	67	ILE	0	0.007	0.006	24.882	0.006	0.006	0.000	0.000	0.000	0.000
67	A	68	THR	0	-0.023	-0.023	27.977	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.030	-0.008	29.204	0.005	0.005	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.003	-0.020	30.723	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.784	-0.857	32.104	0.017	0.017	0.000	0.000	0.000	0.000
71	A	72	THR	0	0.015	-0.011	32.620	0.001	0.001	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.837	0.930	35.758	-0.041	-0.041	0.000	0.000	0.000	0.000
73	A	74	PRO	0	0.082	0.011	34.860	0.004	0.004	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.850	-0.936	34.720	0.052	0.052	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.831	0.935	35.698	-0.048	-0.048	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.052	-0.018	28.976	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	78	PHE	0	0.075	0.017	25.615	0.000	0.000	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.818	-0.911	30.667	0.075	0.075	0.000	0.000	0.000	0.000
79	A	80	VAL	0	-0.083	-0.050	32.391	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	81	ALA	0	0.006	0.000	27.754	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.925	-0.960	28.707	0.110	0.110	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.897	0.963	29.981	-0.058	-0.058	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.041	-0.038	29.462	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.854	0.920	25.001	-0.106	-0.106	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.874	-0.933	27.990	0.087	0.087	0.000	0.000	0.000	0.000
86	A	87	TYR	0	-0.060	-0.009	30.591	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.757	-0.881	29.094	0.032	0.032	0.000	0.000	0.000	0.000
88	A	89	PHE	0	-0.039	-0.032	29.739	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	90	VAL	0	0.001	-0.006	26.060	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.786	0.893	23.920	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.867	-0.908	19.541	-0.025	-0.025	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.040	-0.021	22.179	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	94	TYR	0	-0.078	-0.062	17.548	0.019	0.019	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.005	0.012	22.533	-0.007	-0.007	0.000	0.000	0.000	0.000
95	A	96	SER	0	-0.017	-0.013	22.680	0.000	0.000	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.005	-0.008	24.032	0.008	0.008	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.024	-0.007	25.665	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.927	-0.968	27.203	-0.015	-0.015	0.000	0.000	0.000	0.000
99	A	100	HIS	1	0.807	0.878	29.682	0.002	0.002	0.000	0.000	0.000	0.000
100	A	101	MET	0	0.027	0.033	27.924	0.003	0.003	0.000	0.000	0.000	0.000
101	A	102	ILE	0	0.013	0.013	26.981	0.003	0.003	0.000	0.000	0.000	0.000
102	A	103	MET	0	-0.010	-0.011	21.948	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.051	0.037	24.791	0.005	0.005	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.018	0.020	22.333	-0.012	-0.012	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.015	-0.013	25.543	0.006	0.006	0.000	0.000	0.000	0.000
106	A	107	TRP	0	-0.084	-0.040	24.122	-0.010	-0.010	0.000	0.000	0.000	0.000
107	A	108	ALA	0	0.050	0.043	29.980	0.005	0.005	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.860	0.904	33.302	0.006	0.006	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.810	-0.902	35.708	-0.020	-0.020	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.050	0.031	38.130	0.002	0.002	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.899	-0.944	39.703	-0.014	-0.014	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.831	-0.896	36.327	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.061	-0.051	34.576	0.003	0.003	0.000	0.000	0.000	0.000
114	A	115	ALA	0	0.022	0.004	37.089	0.004	0.004	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.837	-0.891	40.345	0.008	0.008	0.000	0.000	0.000	0.000
116	A	117	ILE	0	-0.020	-0.009	34.165	0.004	0.004	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.028	-0.012	35.899	0.004	0.004	0.000	0.000	0.000	0.000
118	A	119	SER	0	0.088	0.030	37.760	0.003	0.003	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.130	-0.074	40.743	0.004	0.004	0.000	0.000	0.000	0.000
120	A	121	LYS	1	0.907	0.959	36.733	-0.018	-0.018	0.000	0.000	0.000	0.000
121	A	122	ILE	0	0.019	0.002	33.018	0.004	0.004	0.000	0.000	0.000	0.000
122	A	123	GLY	0	-0.027	-0.016	36.344	0.002	0.002	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.801	0.901	39.440	-0.015	-0.015	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.031	0.013	34.419	0.003	0.003	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.728	-0.864	38.533	0.039	0.039	0.000	0.000	0.000	0.000
126	A	127	GLY	0	-0.022	-0.019	38.233	0.004	0.004	0.000	0.000	0.000	0.000
127	A	128	VAL	0	0.004	0.002	35.283	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	129	THR	0	-0.026	-0.012	37.469	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.860	0.906	36.742	-0.011	-0.011	0.000	0.000	0.000	0.000
130	A	131	VAL	0	0.019	0.052	34.372	0.002	0.002	0.000	0.000	0.000	0.000
131	A	132	CYS	0	-0.086	-0.059	33.405	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	133	PRO	0	0.042	0.049	32.453	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	134	ALA	0	0.056	0.024	30.058	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	135	ILE	0	-0.028	-0.016	30.323	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	136	ILE	0	-0.028	-0.007	24.978	-0.006	-0.006	0.000	0.000	0.000	0.000
136	A	137	LEU	0	0.006	0.027	29.180	0.002	0.002	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.933	-0.992	27.886	-0.106	-0.106	0.000	0.000	0.000	0.000
138	A	139	LYS	1	0.911	0.967	19.458	0.154	0.154	0.000	0.000	0.000	0.000
139	A	140	LEU	0	0.064	0.029	23.076	-0.005	-0.005	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.958	0.980	14.624	0.425	0.425	0.000	0.000	0.000	0.000

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