FMO DATABASE

FMODB ID: 987R2

Calculation Name: 1JYO-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1JYO

Chain ID: A

ChEMBL ID:

UniProt ID: P0CL16

Base Structure: X-ray

Registration Date: 2023-09-23

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	130
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1083286.062763
FMO2-HF: Nuclear repulsion	1032640.052787
FMO2-HF: Total energy	-50646.009976
FMO2-MP2: Total energy	-50793.858306

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.
-13.994	-6.643	1.989	-2.945	-6.396	-0.015

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 : 0.035 / 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].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	ALA	0	0.048	0.024	3.532	-2.975	-1.213	-0.002	-0.763	-0.998	0.001
4	A	4	HIS	0	0.007	0.010	2.933	-0.970	0.352	0.137	-0.433	-1.026	-0.001
5	A	5	GLN	0	0.032	0.011	2.531	-1.246	0.078	1.211	-0.602	-1.933	-0.002
6	A	6	ASP	-1	-0.858	-0.922	5.049	0.736	0.818	-0.001	-0.007	-0.074	0.000
7	A	7	ILE	0	0.002	0.008	7.682	0.074	0.074	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.010	-0.003	6.941	0.159	0.159	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.031	0.021	8.974	0.125	0.125	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.085	-0.059	10.870	0.067	0.067	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.008	-0.016	12.328	0.060	0.060	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.033	0.014	12.955	0.043	0.043	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.869	-0.922	14.573	-0.096	-0.096	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.736	0.865	17.003	0.203	0.203	0.000	0.000	0.000	0.000
15	A	15	LEU	0	0.016	0.014	16.126	0.013	0.013	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.034	0.004	19.204	0.010	0.010	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.038	-0.028	15.779	0.015	0.015	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.035	-0.016	13.821	-0.023	-0.023	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.005	0.004	10.899	-0.023	-0.023	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.023	-0.024	6.180	0.126	0.126	0.000	0.000	0.000	0.000
21	A	21	PHE	0	0.003	0.008	3.765	-0.266	-0.002	0.003	-0.029	-0.238	0.000
22	A	22	ASP	-1	-0.781	-0.883	5.049	-1.410	-1.348	-0.001	-0.004	-0.057	0.000
23	A	23	ASP	-1	-0.913	-0.956	4.327	-2.062	-1.890	-0.001	-0.021	-0.151	0.000
24	A	24	ASN	0	-0.159	-0.090	4.874	-0.217	-0.127	-0.001	-0.002	-0.087	0.000
25	A	25	ASN	0	-0.057	-0.028	2.675	-4.138	-1.886	0.645	-1.083	-1.814	-0.013
26	A	26	GLN	0	0.037	0.014	5.372	0.325	0.346	-0.001	-0.001	-0.018	0.000
27	A	27	CYS	0	-0.034	-0.015	7.898	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.033	-0.008	10.129	0.097	0.097	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.006	-0.005	13.701	0.029	0.029	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.058	-0.022	16.633	0.015	0.015	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.002	0.010	19.299	0.009	0.009	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.852	-0.947	22.621	-0.204	-0.204	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.129	-0.064	25.217	0.020	0.020	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.823	-0.900	26.314	-0.201	-0.201	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.012	0.018	22.444	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	36	PHE	0	0.009	0.006	20.762	-0.021	-0.021	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.011	-0.013	16.753	0.015	0.015	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.044	-0.026	13.117	-0.050	-0.050	0.000	0.000	0.000	0.000
39	A	39	ILE	0	0.022	0.026	10.029	0.063	0.063	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.827	-0.924	8.840	-1.143	-1.143	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.015	0.011	4.873	0.168	0.168	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.811	0.884	6.569	0.893	0.893	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.889	-0.945	6.712	-0.645	-0.645	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.962	-0.975	6.298	-0.721	-0.721	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.059	-0.028	8.329	0.126	0.126	0.000	0.000	0.000	0.000
46	A	46	TRP	0	-0.010	-0.023	6.852	-0.138	-0.138	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.001	0.006	10.512	0.194	0.194	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.025	0.000	12.746	-0.092	-0.092	0.000	0.000	0.000	0.000
49	A	49	ASN	0	0.001	-0.014	14.635	0.110	0.110	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.071	0.023	17.640	-0.020	-0.020	0.000	0.000	0.000	0.000
51	A	51	MET	0	-0.043	-0.008	20.608	0.026	0.026	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.006	0.010	23.090	0.009	0.009	0.000	0.000	0.000	0.000
53	A	53	ILE	0	0.006	-0.003	26.742	0.012	0.012	0.000	0.000	0.000	0.000
54	A	54	PRO	0	0.008	0.025	28.531	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.035	-0.001	29.607	0.014	0.014	0.000	0.000	0.000	0.000
56	A	56	SER	0	0.046	0.023	31.960	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	57	PRO	0	0.080	0.042	32.686	0.001	0.001	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.050	-0.039	34.144	0.004	0.004	0.000	0.000	0.000	0.000
59	A	59	CYS	0	-0.048	-0.005	35.080	0.007	0.007	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.066	0.035	38.094	0.006	0.006	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.901	-0.965	38.873	-0.109	-0.109	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.074	-0.058	39.706	0.000	0.000	0.000	0.000	0.000	0.000
63	A	63	ILE	0	0.032	0.043	35.346	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	64	TRP	0	0.021	0.010	30.917	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.907	0.960	35.031	0.100	0.100	0.000	0.000	0.000	0.000
66	A	66	GLN	0	0.033	0.037	36.267	0.003	0.003	0.000	0.000	0.000	0.000
67	A	67	ILE	0	0.051	0.020	30.533	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	68	MET	0	-0.017	-0.003	30.785	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.070	-0.036	33.396	0.001	0.001	0.000	0.000	0.000	0.000
70	A	70	ILE	0	0.062	0.037	30.653	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	71	ASN	0	0.000	-0.016	28.023	-0.017	-0.017	0.000	0.000	0.000	0.000
72	A	72	GLY	0	-0.036	-0.005	29.702	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.936	-0.978	31.800	-0.139	-0.139	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.005	0.007	26.784	0.000	0.000	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.017	0.008	26.973	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.090	-0.045	28.057	0.001	0.001	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.069	-0.036	28.584	0.016	0.016	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.056	-0.023	21.095	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.824	-0.903	23.326	-0.251	-0.251	0.000	0.000	0.000	0.000
80	A	80	GLY	0	-0.003	0.009	22.207	-0.024	-0.024	0.000	0.000	0.000	0.000
81	A	81	THR	0	-0.102	-0.056	23.046	0.028	0.028	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.020	0.021	23.722	-0.023	-0.023	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.001	0.001	23.096	0.015	0.015	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.019	-0.040	25.254	0.002	0.002	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.007	0.002	20.780	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.887	-0.953	24.439	-0.177	-0.177	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.003	-0.007	24.165	0.008	0.008	0.000	0.000	0.000	0.000
88	A	88	ALA	0	-0.033	-0.012	23.920	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.892	-0.914	26.065	-0.158	-0.158	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.036	-0.025	24.659	0.009	0.009	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.023	0.002	25.873	-0.012	-0.012	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.016	-0.017	19.915	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	93	LEU	0	0.028	0.025	22.356	0.016	0.016	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.012	-0.010	17.826	-0.032	-0.032	0.000	0.000	0.000	0.000
95	A	95	HIS	0	0.050	0.020	18.253	0.023	0.023	0.000	0.000	0.000	0.000
96	A	96	ALA	0	-0.020	-0.011	15.164	-0.072	-0.072	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.015	0.026	13.430	0.060	0.060	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.013	-0.023	13.076	-0.080	-0.080	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.827	-0.874	14.309	-0.221	-0.221	0.000	0.000	0.000	0.000
100	A	100	LEU	0	0.025	0.005	8.639	-0.021	-0.021	0.000	0.000	0.000	0.000
101	A	101	THR	0	-0.091	-0.069	11.921	0.038	0.038	0.000	0.000	0.000	0.000
102	A	102	ASN	0	-0.008	-0.009	14.086	0.039	0.039	0.000	0.000	0.000	0.000
103	A	103	THR	0	0.056	0.025	14.548	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	104	TYR	0	0.037	0.004	16.241	-0.020	-0.020	0.000	0.000	0.000	0.000
105	A	105	HIS	0	-0.080	-0.026	18.332	0.002	0.002	0.000	0.000	0.000	0.000
106	A	106	ILE	0	0.045	0.031	12.437	0.001	0.001	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.010	-0.004	16.590	-0.014	-0.014	0.000	0.000	0.000	0.000
108	A	108	SER	0	0.011	0.016	18.417	0.003	0.003	0.000	0.000	0.000	0.000
109	A	109	GLN	0	0.032	0.008	17.523	-0.028	-0.028	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.021	-0.014	14.022	-0.010	-0.010	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.943	-0.966	18.247	-0.210	-0.210	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.007	-0.013	21.736	0.020	0.020	0.000	0.000	0.000	0.000
113	A	113	PHE	0	0.009	0.002	19.266	0.008	0.008	0.000	0.000	0.000	0.000
114	A	114	VAL	0	0.009	0.003	19.879	0.007	0.007	0.000	0.000	0.000	0.000
115	A	115	ASN	0	-0.014	-0.011	22.474	0.016	0.016	0.000	0.000	0.000	0.000
116	A	116	GLN	0	-0.043	-0.040	24.669	0.024	0.024	0.000	0.000	0.000	0.000
117	A	117	GLN	0	-0.032	-0.024	21.471	-0.011	-0.011	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.918	-0.963	25.143	-0.180	-0.180	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.013	0.003	27.849	0.015	0.015	0.000	0.000	0.000	0.000
120	A	120	LEU	0	0.000	-0.012	26.723	0.013	0.013	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.776	0.886	27.130	0.217	0.217	0.000	0.000	0.000	0.000
122	A	122	ASN	0	-0.057	-0.042	29.950	0.018	0.018	0.000	0.000	0.000	0.000
123	A	123	ILE	0	-0.059	-0.025	32.878	0.010	0.010	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.005	-0.001	30.852	0.008	0.008	0.000	0.000	0.000	0.000
125	A	125	GLN	0	0.007	0.015	31.743	-0.007	-0.007	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.970	-0.994	34.321	-0.116	-0.116	0.000	0.000	0.000	0.000
127	A	127	TYR	0	-0.059	-0.048	35.052	0.006	0.006	0.000	0.000	0.000	0.000
128	A	128	ALA	0	-0.014	0.006	33.154	-0.005	-0.005	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.795	0.868	30.743	0.186	0.186	0.000	0.000	0.000	0.000
130	A	130	VAL	0	-0.032	0.002	34.955	-0.001	-0.001	0.000	0.000	0.000	0.000

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