FMO DATABASE

FMODB ID: ZNV2N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1132343.853065
FMO2-HF: Nuclear repulsion	1077895.340909
FMO2-HF: Total energy	-54448.512156
FMO2-MP2: Total energy	-54609.868946

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.
-2.588	-5.909	22.178	-4.049	-14.809	-0.024

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 : -0.053 / q_NPA : -0.027

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	-0.849	-0.927	2.497	-8.572	-7.370	3.753	-1.427	-3.529	-0.022
4	A	5	ARG	1	0.909	0.949	5.238	1.054	1.054	0.000	0.000	0.000	0.000
5	A	6	ASP	-1	-0.802	-0.910	2.083	-0.877	-2.907	7.879	-2.200	-3.649	0.002
6	A	7	LYS	1	0.912	0.977	2.337	3.574	1.263	7.594	-1.598	-3.685	-0.003
7	A	8	ILE	0	-0.025	-0.013	3.146	2.511	0.969	0.056	1.838	-0.352	0.000
8	A	9	ILE	0	-0.024	-0.033	5.345	0.379	0.379	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.054	0.023	2.332	0.172	-0.194	2.070	-0.228	-1.476	0.000
10	A	11	GLU	-1	-0.904	-0.934	5.616	-1.212	-1.212	0.000	0.000	0.000	0.000
11	A	12	ILE	0	-0.036	-0.034	7.796	0.209	0.209	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.000	-0.004	8.781	0.106	0.106	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.948	-0.979	8.990	-0.455	-0.455	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.834	0.943	10.840	0.896	0.896	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.845	-0.936	13.417	-0.258	-0.258	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.025	-0.001	13.305	-0.021	-0.021	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.929	0.965	14.225	0.248	0.248	0.000	0.000	0.000	0.000
18	A	19	THR	0	-0.064	-0.031	14.119	0.008	0.008	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.041	0.037	15.152	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	21	PHE	0	0.044	0.002	12.007	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	22	THR	0	0.034	0.007	14.684	-0.043	-0.043	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.941	-1.007	16.430	-0.332	-0.332	0.000	0.000	0.000	0.000
23	A	24	ILE	0	0.037	0.032	10.090	-0.029	-0.029	0.000	0.000	0.000	0.000
24	A	25	ALA	0	-0.014	-0.007	12.849	-0.047	-0.047	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.942	0.966	14.283	0.257	0.257	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.884	0.952	13.113	0.513	0.513	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.029	-0.010	8.247	-0.042	-0.042	0.000	0.000	0.000	0.000
28	A	29	GLY	0	-0.020	0.012	12.664	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	30	ILE	0	-0.026	0.002	10.106	0.052	0.052	0.000	0.000	0.000	0.000
30	A	31	SER	0	0.035	-0.002	14.513	0.010	0.010	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.745	-0.876	14.407	-0.227	-0.227	0.000	0.000	0.000	0.000
32	A	33	THR	0	0.009	0.001	14.571	-0.029	-0.029	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.005	0.010	12.373	0.030	0.030	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.027	0.034	10.368	-0.021	-0.021	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.842	0.904	10.835	0.145	0.145	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.942	0.966	10.902	-0.101	-0.101	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.749	0.857	5.487	1.053	1.053	0.000	0.000	0.000	0.000
38	A	39	VAL	0	0.067	0.058	7.182	0.007	0.007	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.829	0.916	8.669	0.061	0.061	0.000	0.000	0.000	0.000
40	A	41	ALA	0	-0.013	-0.011	7.293	0.084	0.084	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.002	-0.002	2.560	-0.794	0.054	0.584	-0.258	-1.173	-0.001
42	A	43	GLU	-1	-0.755	-0.875	5.830	-0.044	-0.044	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-1.044	-1.008	9.394	0.343	0.343	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.898	0.950	4.821	-1.085	-1.085	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.082	0.039	8.017	0.045	0.045	0.000	0.000	0.000	0.000
46	A	47	ILE	0	-0.113	-0.053	2.943	-0.930	-0.052	0.242	-0.176	-0.945	0.000
47	A	48	ILE	0	-0.063	-0.022	6.530	-0.166	-0.166	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.868	-0.932	8.498	0.058	0.058	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.032	-0.028	11.840	0.041	0.041	0.000	0.000	0.000	0.000
50	A	51	TYR	0	-0.095	-0.054	11.741	-0.070	-0.070	0.000	0.000	0.000	0.000
51	A	52	THR	0	0.030	0.011	15.254	0.031	0.031	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.006	-0.006	17.561	-0.016	-0.016	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.957	0.994	18.172	0.226	0.226	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.040	0.012	20.077	0.001	0.001	0.000	0.000	0.000	0.000
55	A	56	ASN	0	-0.048	-0.045	23.824	0.008	0.008	0.000	0.000	0.000	0.000
56	A	57	PRO	0	0.086	0.065	25.618	0.007	0.007	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.978	0.993	28.569	0.114	0.114	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.943	0.971	29.150	0.142	0.142	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.021	-0.009	29.341	0.003	0.003	0.000	0.000	0.000	0.000
60	A	61	GLY	0	-0.013	-0.004	32.200	0.007	0.007	0.000	0.000	0.000	0.000
61	A	62	TYR	0	-0.056	-0.040	30.745	0.005	0.005	0.000	0.000	0.000	0.000
62	A	63	SER	0	-0.052	-0.043	31.487	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	64	LEU	0	0.046	0.020	32.862	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	65	VAL	0	0.002	0.018	26.206	0.003	0.003	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.009	-0.023	29.538	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	67	ILE	0	-0.001	-0.006	25.555	0.002	0.002	0.000	0.000	0.000	0.000
67	A	68	THR	0	-0.014	-0.016	28.473	0.004	0.004	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.027	-0.009	29.816	0.001	0.001	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.007	-0.016	31.217	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.872	-0.926	32.479	0.005	0.005	0.000	0.000	0.000	0.000
71	A	72	THR	0	0.022	0.016	33.413	0.000	0.000	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.938	0.989	36.044	-0.017	-0.017	0.000	0.000	0.000	0.000
73	A	74	PRO	0	0.065	0.002	35.054	0.001	0.001	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.905	-0.963	34.783	0.034	0.034	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.878	0.943	35.676	-0.024	-0.024	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.002	-0.005	28.846	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	78	PHE	0	0.033	-0.003	25.712	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.866	-0.935	30.649	0.039	0.039	0.000	0.000	0.000	0.000
79	A	80	VAL	0	-0.032	-0.022	33.019	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	81	ALA	0	-0.015	-0.008	27.918	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.924	-0.964	28.905	0.041	0.041	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.928	0.971	30.165	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.039	-0.030	30.232	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.960	0.972	24.226	-0.039	-0.039	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.963	-0.973	28.581	0.005	0.005	0.000	0.000	0.000	0.000
86	A	87	TYR	0	-0.059	-0.018	31.099	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.840	-0.925	29.757	-0.046	-0.046	0.000	0.000	0.000	0.000
88	A	89	PHE	0	-0.045	-0.032	30.249	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	90	VAL	0	-0.007	-0.008	26.709	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.873	0.939	24.455	0.087	0.087	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.872	-0.929	20.207	-0.157	-0.157	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.018	-0.006	22.850	0.001	0.001	0.000	0.000	0.000	0.000
93	A	94	TYR	0	-0.074	-0.050	18.579	0.005	0.005	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.006	0.009	22.801	0.001	0.001	0.000	0.000	0.000	0.000
95	A	96	SER	0	-0.006	-0.012	22.960	0.000	0.000	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.000	-0.009	24.268	0.010	0.010	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.041	-0.011	25.897	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.900	-0.961	27.423	-0.020	-0.020	0.000	0.000	0.000	0.000
99	A	100	HIS	1	0.771	0.872	29.892	0.020	0.020	0.000	0.000	0.000	0.000
100	A	101	MET	0	0.035	0.031	28.205	0.000	0.000	0.000	0.000	0.000	0.000
101	A	102	ILE	0	0.003	0.012	27.240	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	103	MET	0	-0.001	-0.007	22.792	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.034	0.032	25.445	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.014	0.024	22.762	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.013	-0.014	26.073	0.000	0.000	0.000	0.000	0.000	0.000
106	A	107	TRP	0	-0.106	-0.050	24.509	-0.009	-0.009	0.000	0.000	0.000	0.000
107	A	108	ALA	0	0.074	0.048	30.407	0.004	0.004	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.893	0.919	33.666	0.053	0.053	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.811	-0.903	36.054	-0.053	-0.053	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.069	0.049	38.479	0.002	0.002	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.886	-0.935	40.090	-0.040	-0.040	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.839	-0.896	36.731	-0.047	-0.047	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.076	-0.066	35.076	0.003	0.003	0.000	0.000	0.000	0.000
114	A	115	ALA	0	0.008	0.000	37.558	0.003	0.003	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.930	-0.959	40.845	-0.029	-0.029	0.000	0.000	0.000	0.000
116	A	117	ILE	0	-0.021	-0.010	34.650	0.004	0.004	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.016	-0.013	36.719	0.004	0.004	0.000	0.000	0.000	0.000
118	A	119	SER	0	0.022	0.010	38.340	0.005	0.005	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.063	-0.037	41.281	0.005	0.005	0.000	0.000	0.000	0.000
120	A	121	LYS	1	0.887	0.948	37.310	0.023	0.023	0.000	0.000	0.000	0.000
121	A	122	ILE	0	0.018	0.003	33.408	0.003	0.003	0.000	0.000	0.000	0.000
122	A	123	GLY	0	-0.027	-0.014	36.999	0.003	0.003	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.870	0.940	40.102	0.012	0.012	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.032	0.012	35.153	0.002	0.002	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.860	-0.916	39.098	0.016	0.016	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.027	0.001	38.385	0.002	0.002	0.000	0.000	0.000	0.000
127	A	128	VAL	0	-0.016	-0.006	36.078	0.001	0.001	0.000	0.000	0.000	0.000
128	A	129	THR	0	-0.012	-0.008	37.857	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.928	0.946	37.327	0.008	0.008	0.000	0.000	0.000	0.000
130	A	131	VAL	0	0.032	0.064	34.928	0.000	0.000	0.000	0.000	0.000	0.000
131	A	132	CYS	0	-0.086	-0.061	33.829	0.002	0.002	0.000	0.000	0.000	0.000
132	A	133	PRO	0	0.037	0.044	32.983	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	134	ALA	0	0.049	0.031	30.432	0.002	0.002	0.000	0.000	0.000	0.000
134	A	135	ILE	0	-0.030	-0.018	30.747	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	136	ILE	0	-0.028	-0.002	25.162	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	137	LEU	0	-0.003	0.018	29.482	0.001	0.001	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.895	-0.972	27.954	-0.140	-0.140	0.000	0.000	0.000	0.000
138	A	139	LYS	1	0.862	0.946	19.886	0.233	0.233	0.000	0.000	0.000	0.000
139	A	140	LEU	0	0.063	0.017	23.173	-0.005	-0.005	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.971	0.993	14.281	0.486	0.486	0.000	0.000	0.000	0.000

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