FMO DATABASE

FMODB ID: R5GR8

Calculation Name: 1S7I-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1S7I

Chain ID: A

ChEMBL ID:

UniProt ID: Q9I3Z5

Base Structure: X-ray

Registration Date: 2023-06-20

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	124
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-915917.158026
FMO2-HF: Nuclear repulsion	867583.258287
FMO2-HF: Total energy	-48333.89974
FMO2-MP2: Total energy	-48472.664717

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:1:LEU)

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

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.
-3.726	0.537	0.765	-2.175	-2.85	0

Interaction energy analysis for fragmet #1(A:1:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.017 / q_NPA : 0.008

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].
3	A	3	PHE	0	0.023	0.025	2.766	-2.790	0.801	0.722	-2.008	-2.304
4	A	4	GLN	0	-0.108	-0.088	3.173	0.002	0.553	0.043	-0.152	-0.441
5	A	5	GLY	0	0.020	-0.003	6.287	0.091	0.091	0.000	0.000	0.000
6	A	6	ASN	0	0.039	0.040	9.878	-0.061	-0.061	0.000	0.000	0.000
7	A	7	MET	0	-0.041	-0.002	13.267	-0.036	-0.036	0.000	0.000	0.000
8	A	8	LYS	1	0.897	0.937	15.423	0.343	0.343	0.000	0.000	0.000
9	A	9	TYR	0	-0.018	-0.027	17.355	-0.016	-0.016	0.000	0.000	0.000
10	A	10	LEU	0	0.006	0.009	22.281	0.013	0.013	0.000	0.000	0.000
11	A	11	CYS	0	-0.056	-0.021	25.774	0.000	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.000	-0.012	28.447	0.008	0.008	0.000	0.000	0.000
13	A	13	ILE	0	0.008	0.013	31.731	0.002	0.002	0.000	0.000	0.000
14	A	14	TYR	0	-0.008	-0.011	33.544	0.002	0.002	0.000	0.000	0.000
15	A	15	PHE	0	0.091	0.034	37.826	0.002	0.002	0.000	0.000	0.000
16	A	16	ASP	-1	-0.791	-0.860	41.449	-0.061	-0.061	0.000	0.000	0.000
17	A	17	GLU	-1	-0.692	-0.821	44.259	-0.064	-0.064	0.000	0.000	0.000
18	A	18	ALA	0	-0.060	-0.020	46.252	0.003	0.003	0.000	0.000	0.000
19	A	19	LYS	1	0.809	0.876	46.872	0.062	0.062	0.000	0.000	0.000
20	A	20	LEU	0	0.025	0.017	44.257	0.001	0.001	0.000	0.000	0.000
21	A	21	ALA	0	-0.033	-0.009	48.363	0.002	0.002	0.000	0.000	0.000
22	A	22	ALA	0	-0.043	-0.027	51.092	0.002	0.002	0.000	0.000	0.000
23	A	23	VAL	0	-0.015	0.008	46.564	0.001	0.001	0.000	0.000	0.000
24	A	24	PRO	0	0.026	0.022	49.886	0.001	0.001	0.000	0.000	0.000
25	A	25	ALA	0	0.047	-0.003	49.641	-0.001	-0.001	0.000	0.000	0.000
26	A	26	GLU	-1	-0.951	-0.974	49.124	-0.032	-0.032	0.000	0.000	0.000
27	A	27	GLU	-1	-0.918	-0.958	45.923	-0.044	-0.044	0.000	0.000	0.000
28	A	28	LEU	0	-0.028	-0.023	44.741	-0.002	-0.002	0.000	0.000	0.000
29	A	29	ALA	0	0.008	0.003	44.231	-0.003	-0.003	0.000	0.000	0.000
30	A	30	ALA	0	0.045	0.030	43.771	-0.001	-0.001	0.000	0.000	0.000
31	A	31	ILE	0	-0.002	0.003	39.547	-0.002	-0.002	0.000	0.000	0.000
32	A	32	VAL	0	0.006	-0.006	39.278	-0.004	-0.004	0.000	0.000	0.000
33	A	33	ASP	-1	-0.869	-0.935	39.228	-0.044	-0.044	0.000	0.000	0.000
34	A	34	GLU	-1	-0.887	-0.938	37.554	-0.053	-0.053	0.000	0.000	0.000
35	A	35	CYS	0	-0.035	-0.021	34.383	-0.005	-0.005	0.000	0.000	0.000
36	A	36	MET	0	0.003	0.022	34.186	-0.005	-0.005	0.000	0.000	0.000
37	A	37	THR	0	0.009	0.004	34.035	0.000	0.000	0.000	0.000	0.000
38	A	38	TYR	0	-0.048	-0.041	28.641	-0.001	-0.001	0.000	0.000	0.000
39	A	39	SER	0	0.002	-0.010	29.838	-0.008	-0.008	0.000	0.000	0.000
40	A	40	ASP	-1	-0.876	-0.915	28.926	-0.060	-0.060	0.000	0.000	0.000
41	A	41	GLN	0	-0.106	-0.059	28.790	-0.002	-0.002	0.000	0.000	0.000
42	A	42	LEU	0	-0.011	-0.009	25.288	-0.002	-0.002	0.000	0.000	0.000
43	A	43	GLY	0	0.017	-0.001	24.468	-0.008	-0.008	0.000	0.000	0.000
44	A	44	LYS	1	0.880	0.932	24.080	0.029	0.029	0.000	0.000	0.000
45	A	45	ALA	0	-0.051	-0.017	22.984	0.007	0.007	0.000	0.000	0.000
46	A	46	GLY	0	0.001	0.013	19.918	-0.002	-0.002	0.000	0.000	0.000
47	A	47	HIS	0	-0.083	-0.047	19.406	-0.003	-0.003	0.000	0.000	0.000
48	A	48	TYR	0	-0.024	-0.026	21.665	-0.016	-0.016	0.000	0.000	0.000
49	A	49	ILE	0	-0.014	0.011	19.543	-0.004	-0.004	0.000	0.000	0.000
50	A	50	ALA	0	-0.009	-0.020	23.838	0.008	0.008	0.000	0.000	0.000
51	A	51	SER	0	-0.010	0.020	27.379	-0.006	-0.006	0.000	0.000	0.000
52	A	52	HIS	0	-0.004	0.014	30.496	0.008	0.008	0.000	0.000	0.000
53	A	53	ALA	0	0.022	0.025	34.026	-0.004	-0.004	0.000	0.000	0.000
54	A	54	LEU	0	-0.051	-0.037	35.486	-0.001	-0.001	0.000	0.000	0.000
55	A	55	GLN	0	-0.016	-0.009	38.887	0.006	0.006	0.000	0.000	0.000
56	A	56	SER	0	0.016	-0.025	42.102	-0.002	-0.002	0.000	0.000	0.000
57	A	57	VAL	0	0.017	0.005	42.091	-0.001	-0.001	0.000	0.000	0.000
58	A	58	GLN	0	-0.031	-0.026	44.296	0.001	0.001	0.000	0.000	0.000
59	A	59	THR	0	-0.085	-0.050	44.197	0.001	0.001	0.000	0.000	0.000
60	A	60	ALA	0	-0.032	0.000	42.326	-0.002	-0.002	0.000	0.000	0.000
61	A	61	THR	0	0.007	-0.006	42.831	0.004	0.004	0.000	0.000	0.000
62	A	62	THR	0	-0.054	-0.021	41.310	-0.007	-0.007	0.000	0.000	0.000
63	A	63	LEU	0	-0.022	-0.013	40.593	0.004	0.004	0.000	0.000	0.000
64	A	64	ARG	1	0.967	0.977	40.895	0.086	0.086	0.000	0.000	0.000
65	A	65	HIS	0	0.027	0.014	38.611	0.004	0.004	0.000	0.000	0.000
66	A	66	GLN	0	0.010	-0.003	42.496	-0.002	-0.002	0.000	0.000	0.000
67	A	67	GLY	0	-0.011	-0.003	44.200	-0.002	-0.002	0.000	0.000	0.000
68	A	68	GLY	0	0.046	0.022	44.191	-0.003	-0.003	0.000	0.000	0.000
69	A	69	ARG	1	0.875	0.934	45.272	0.064	0.064	0.000	0.000	0.000
70	A	70	LEU	0	0.031	0.024	42.092	-0.003	-0.003	0.000	0.000	0.000
71	A	71	ALA	0	-0.038	-0.017	45.492	0.004	0.004	0.000	0.000	0.000
72	A	72	MET	0	0.019	0.001	45.589	-0.003	-0.003	0.000	0.000	0.000
73	A	73	THR	0	-0.034	-0.022	46.309	0.002	0.002	0.000	0.000	0.000
74	A	74	ASP	-1	-0.889	-0.936	46.525	-0.063	-0.063	0.000	0.000	0.000
75	A	75	GLY	0	0.069	0.053	46.563	0.000	0.000	0.000	0.000	0.000
76	A	76	PRO	0	-0.012	-0.005	42.410	-0.004	-0.004	0.000	0.000	0.000
77	A	77	PHE	0	-0.035	-0.026	39.120	0.000	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.047	-0.033	41.736	0.000	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.905	-0.929	43.784	-0.068	-0.068	0.000	0.000	0.000
80	A	80	THR	0	-0.048	-0.056	40.917	-0.001	-0.001	0.000	0.000	0.000
81	A	81	LYS	1	0.845	0.907	44.217	0.064	0.064	0.000	0.000	0.000
82	A	82	GLU	-1	-0.865	-0.941	40.507	-0.077	-0.077	0.000	0.000	0.000
83	A	83	GLN	0	0.012	0.036	41.149	-0.003	-0.003	0.000	0.000	0.000
84	A	84	LEU	0	-0.023	-0.011	33.764	-0.001	-0.001	0.000	0.000	0.000
85	A	85	GLY	0	0.070	0.032	37.806	0.002	0.002	0.000	0.000	0.000
86	A	86	GLY	0	0.010	0.002	35.423	0.005	0.005	0.000	0.000	0.000
87	A	87	PHE	0	-0.049	-0.023	28.724	-0.006	-0.006	0.000	0.000	0.000
88	A	88	TYR	0	0.039	-0.007	27.795	0.007	0.007	0.000	0.000	0.000
89	A	89	LEU	0	-0.056	-0.020	22.437	-0.009	-0.009	0.000	0.000	0.000
90	A	90	ILE	0	0.008	-0.006	22.632	0.009	0.009	0.000	0.000	0.000
91	A	91	GLU	-1	-0.822	-0.920	15.682	-0.302	-0.302	0.000	0.000	0.000
92	A	92	ALA	0	-0.034	-0.011	17.991	0.033	0.033	0.000	0.000	0.000
93	A	93	ARG	1	0.871	0.912	14.791	0.133	0.133	0.000	0.000	0.000
94	A	94	ASP	-1	-0.811	-0.897	14.969	-0.282	-0.282	0.000	0.000	0.000
95	A	95	LEU	0	0.074	0.032	17.618	0.028	0.028	0.000	0.000	0.000
96	A	96	ASN	0	0.006	0.004	20.884	0.027	0.027	0.000	0.000	0.000
97	A	97	GLN	0	0.022	0.016	18.944	0.001	0.001	0.000	0.000	0.000
98	A	98	ALA	0	0.023	0.011	21.473	0.017	0.017	0.000	0.000	0.000
99	A	99	LEU	0	0.009	-0.002	23.029	0.015	0.015	0.000	0.000	0.000
100	A	100	GLN	0	-0.047	-0.023	23.787	0.005	0.005	0.000	0.000	0.000
101	A	101	ILE	0	-0.002	0.014	22.621	0.011	0.011	0.000	0.000	0.000
102	A	102	ALA	0	0.059	0.016	26.810	0.009	0.009	0.000	0.000	0.000
103	A	103	ALA	0	-0.047	-0.013	28.936	0.007	0.007	0.000	0.000	0.000
104	A	104	LYS	1	0.891	0.938	30.427	0.069	0.069	0.000	0.000	0.000
105	A	105	ILE	0	-0.007	0.021	29.059	0.004	0.004	0.000	0.000	0.000
106	A	106	PRO	0	0.010	0.011	32.838	0.000	0.000	0.000	0.000	0.000
107	A	107	PRO	0	0.042	0.002	35.409	0.001	0.001	0.000	0.000	0.000
108	A	108	GLY	0	0.017	0.006	35.617	0.000	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.807	0.899	36.535	0.056	0.056	0.000	0.000	0.000
110	A	110	LEU	0	-0.042	-0.012	39.550	0.003	0.003	0.000	0.000	0.000
111	A	111	GLY	0	-0.008	-0.009	39.815	0.002	0.002	0.000	0.000	0.000
112	A	112	CYS	0	-0.108	-0.028	36.331	-0.002	-0.002	0.000	0.000	0.000
113	A	113	VAL	0	0.049	0.015	30.744	-0.001	-0.001	0.000	0.000	0.000
114	A	114	GLU	-1	-0.845	-0.885	30.396	-0.153	-0.153	0.000	0.000	0.000
115	A	115	VAL	0	-0.003	-0.005	24.916	-0.003	-0.003	0.000	0.000	0.000
116	A	116	ARG	1	0.820	0.889	25.495	0.168	0.168	0.000	0.000	0.000
117	A	117	PRO	0	0.008	0.002	20.324	0.001	0.001	0.000	0.000	0.000
118	A	118	VAL	0	-0.015	0.005	19.281	0.014	0.014	0.000	0.000	0.000
119	A	119	LYS	1	0.914	0.952	19.657	0.241	0.241	0.000	0.000	0.000
120	A	120	GLU	-1	-0.921	-0.966	17.518	-0.347	-0.347	0.000	0.000	0.000
121	A	121	TRP	0	-0.035	-0.016	9.692	-0.058	-0.058	0.000	0.000	0.000
122	A	122	GLU	-1	-0.846	-0.908	12.771	-0.377	-0.377	0.000	0.000	0.000
123	A	123	GLY	0	0.095	0.037	9.327	0.013	0.013	0.000	0.000	0.000
124	A	124	SER	0	-0.068	-0.014	3.947	-0.311	-0.190	0.000	-0.015	-0.105

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