FMO DATABASE

FMODB ID: YY462

Calculation Name: 2J4B-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2J4B

Chain ID: A

ChEMBL ID:

UniProt ID: Q8SQS4

Base Structure: X-ray

Registration Date: 2023-06-19

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	131
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1312323.173026
FMO2-HF: Nuclear repulsion	1257430.122176
FMO2-HF: Total energy	-54893.05085
FMO2-MP2: Total energy	-55056.735886

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:18:GLN)

Summations of interaction energy for fragment #1(A:18:GLN)

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.
-0.218	4.878	0.304	-2.205	-3.194	-0.003

Interaction energy analysis for fragmet #1(A:18:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.052 / q_NPA : 0.021

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	20	GLU	-1	-0.728	-0.840	3.543	-1.109	1.392	-0.013	-1.150	-1.339	0.004
4	A	21	THR	0	0.020	-0.002	2.906	-1.669	0.132	0.312	-0.768	-1.345	-0.007
5	A	22	SER	0	-0.019	-0.021	3.274	0.241	0.947	0.006	-0.280	-0.431	0.000
6	A	23	TYR	0	-0.018	0.004	5.673	0.665	0.665	0.000	0.000	0.000	0.000
7	A	24	VAL	0	0.047	0.032	8.102	0.151	0.151	0.000	0.000	0.000	0.000
8	A	25	SER	0	-0.002	0.011	8.150	0.112	0.112	0.000	0.000	0.000	0.000
9	A	26	LEU	0	-0.002	-0.004	9.683	0.159	0.159	0.000	0.000	0.000	0.000
10	A	27	LYS	1	0.817	0.909	11.596	0.297	0.297	0.000	0.000	0.000	0.000
11	A	28	THR	0	-0.023	-0.033	12.713	0.098	0.098	0.000	0.000	0.000	0.000
12	A	29	TRP	0	0.004	0.022	14.032	0.050	0.050	0.000	0.000	0.000	0.000
13	A	30	ILE	0	0.001	-0.011	15.660	0.074	0.074	0.000	0.000	0.000	0.000
14	A	31	GLU	-1	-0.923	-0.962	17.447	-0.215	-0.215	0.000	0.000	0.000	0.000
15	A	32	ASP	-1	-0.885	-0.938	18.862	-0.361	-0.361	0.000	0.000	0.000	0.000
16	A	33	SER	0	-0.132	-0.065	20.290	0.029	0.029	0.000	0.000	0.000	0.000
17	A	34	LEU	0	0.028	-0.009	21.883	0.030	0.030	0.000	0.000	0.000	0.000
18	A	35	ASP	-1	-0.815	-0.906	25.172	-0.201	-0.201	0.000	0.000	0.000	0.000
19	A	36	LEU	0	-0.081	-0.033	27.056	0.007	0.007	0.000	0.000	0.000	0.000
20	A	37	PHE	0	0.006	-0.020	23.398	0.006	0.006	0.000	0.000	0.000	0.000
21	A	38	LYS	1	0.866	0.941	21.826	0.241	0.241	0.000	0.000	0.000	0.000
22	A	39	ASN	0	-0.028	-0.015	22.836	0.011	0.011	0.000	0.000	0.000	0.000
23	A	40	ASP	-1	-0.816	-0.909	23.856	-0.184	-0.184	0.000	0.000	0.000	0.000
24	A	41	LEU	0	-0.031	-0.012	18.412	-0.014	-0.014	0.000	0.000	0.000	0.000
25	A	42	LEU	0	0.028	0.016	18.814	-0.026	-0.026	0.000	0.000	0.000	0.000
26	A	43	PRO	0	-0.038	-0.018	19.338	0.005	0.005	0.000	0.000	0.000	0.000
27	A	44	LEU	0	0.017	0.009	14.653	0.027	0.027	0.000	0.000	0.000	0.000
28	A	45	LEU	0	0.020	-0.001	13.669	-0.025	-0.025	0.000	0.000	0.000	0.000
29	A	46	TYR	0	0.017	0.011	15.022	0.046	0.046	0.000	0.000	0.000	0.000
30	A	47	PRO	0	0.015	0.008	16.482	0.052	0.052	0.000	0.000	0.000	0.000
31	A	48	LEU	0	0.009	0.010	9.488	0.023	0.023	0.000	0.000	0.000	0.000
32	A	49	PHE	0	-0.009	0.002	11.699	0.021	0.021	0.000	0.000	0.000	0.000
33	A	50	ILE	0	-0.001	0.016	12.644	0.130	0.130	0.000	0.000	0.000	0.000
34	A	51	HIS	0	0.001	-0.003	11.960	0.134	0.134	0.000	0.000	0.000	0.000
35	A	52	ILE	0	-0.013	0.000	7.333	0.057	0.057	0.000	0.000	0.000	0.000
36	A	53	TYR	0	-0.035	-0.025	9.675	0.361	0.361	0.000	0.000	0.000	0.000
37	A	54	PHE	0	0.014	-0.018	12.062	0.118	0.118	0.000	0.000	0.000	0.000
38	A	55	ASP	-1	-0.811	-0.897	8.556	0.436	0.436	0.000	0.000	0.000	0.000
39	A	56	LEU	0	-0.051	-0.019	6.164	0.238	0.238	0.000	0.000	0.000	0.000
40	A	57	ILE	0	0.006	0.018	9.970	0.082	0.082	0.000	0.000	0.000	0.000
41	A	58	GLN	0	-0.057	-0.017	12.453	-0.094	-0.094	0.000	0.000	0.000	0.000
42	A	59	GLN	0	-0.076	-0.048	6.658	0.510	0.510	0.000	0.000	0.000	0.000
43	A	60	ASN	0	-0.057	-0.026	11.923	0.009	0.009	0.000	0.000	0.000	0.000
44	A	61	LYS	1	0.808	0.902	6.379	-4.651	-4.651	0.000	0.000	0.000	0.000
45	A	62	THR	0	0.040	0.005	11.765	0.058	0.058	0.000	0.000	0.000	0.000
46	A	63	ASP	-1	-0.846	-0.922	13.193	0.929	0.929	0.000	0.000	0.000	0.000
47	A	64	GLU	-1	-0.783	-0.881	6.659	4.720	4.720	0.000	0.000	0.000	0.000
48	A	65	ALA	0	-0.017	-0.006	10.332	-0.089	-0.089	0.000	0.000	0.000	0.000
49	A	66	LYS	1	0.872	0.925	11.722	-0.998	-0.998	0.000	0.000	0.000	0.000
50	A	67	GLU	-1	-0.927	-0.957	11.647	1.204	1.204	0.000	0.000	0.000	0.000
51	A	68	PHE	0	-0.074	-0.033	8.309	-0.189	-0.189	0.000	0.000	0.000	0.000
52	A	69	PHE	0	-0.017	-0.019	11.174	-0.234	-0.234	0.000	0.000	0.000	0.000
53	A	70	GLU	-1	-0.809	-0.920	14.294	0.273	0.273	0.000	0.000	0.000	0.000
54	A	71	LYS	1	0.820	0.934	9.852	-1.295	-1.295	0.000	0.000	0.000	0.000
55	A	72	TYR	0	-0.038	-0.048	9.592	-0.217	-0.217	0.000	0.000	0.000	0.000
56	A	73	ARG	1	0.771	0.867	15.099	-0.363	-0.363	0.000	0.000	0.000	0.000
57	A	74	GLY	0	-0.025	-0.013	17.905	-0.030	-0.030	0.000	0.000	0.000	0.000
58	A	75	ASP	-1	-0.790	-0.885	15.662	-0.073	-0.073	0.000	0.000	0.000	0.000
59	A	76	HIS	1	0.806	0.885	15.592	-0.037	-0.037	0.000	0.000	0.000	0.000
60	A	77	TYR	0	0.070	0.034	20.950	0.035	0.035	0.000	0.000	0.000	0.000
61	A	78	ASN	0	0.049	0.040	23.672	0.010	0.010	0.000	0.000	0.000	0.000
62	A	79	LYS	1	0.828	0.889	22.682	-0.016	-0.016	0.000	0.000	0.000	0.000
63	A	80	SER	0	0.009	0.004	24.192	0.018	0.018	0.000	0.000	0.000	0.000
64	A	81	GLU	-1	-0.931	-0.956	25.242	0.107	0.107	0.000	0.000	0.000	0.000
65	A	82	GLU	-1	-0.815	-0.900	23.761	0.066	0.066	0.000	0.000	0.000	0.000
66	A	83	ILE	0	-0.049	-0.017	19.062	0.026	0.026	0.000	0.000	0.000	0.000
67	A	84	LYS	1	0.903	0.929	21.791	-0.173	-0.173	0.000	0.000	0.000	0.000
68	A	85	GLN	0	-0.029	-0.008	24.375	0.004	0.004	0.000	0.000	0.000	0.000
69	A	86	PHE	0	0.008	-0.022	19.156	0.020	0.020	0.000	0.000	0.000	0.000
70	A	87	GLU	-1	-0.771	-0.839	20.167	0.303	0.303	0.000	0.000	0.000	0.000
71	A	88	SER	0	-0.032	-0.008	20.974	0.034	0.034	0.000	0.000	0.000	0.000
72	A	89	ILE	0	-0.079	-0.032	19.199	0.000	0.000	0.000	0.000	0.000	0.000
73	A	90	TYR	0	0.015	0.015	17.996	0.043	0.043	0.000	0.000	0.000	0.000
74	A	91	THR	0	0.015	-0.015	17.431	0.079	0.079	0.000	0.000	0.000	0.000
75	A	92	VAL	0	0.091	0.023	17.079	-0.042	-0.042	0.000	0.000	0.000	0.000
76	A	93	GLN	0	-0.031	-0.018	19.504	-0.039	-0.039	0.000	0.000	0.000	0.000
77	A	94	HIS	0	0.023	0.029	21.482	0.002	0.002	0.000	0.000	0.000	0.000
78	A	95	ILE	0	0.025	0.016	16.889	-0.035	-0.035	0.000	0.000	0.000	0.000
79	A	96	HIS	0	-0.080	-0.053	20.530	-0.056	-0.056	0.000	0.000	0.000	0.000
80	A	97	GLU	-1	-0.882	-0.914	24.057	0.259	0.259	0.000	0.000	0.000	0.000
81	A	98	ASN	0	-0.029	-0.004	24.470	-0.037	-0.037	0.000	0.000	0.000	0.000
82	A	99	ASN	0	0.053	0.006	24.730	0.007	0.007	0.000	0.000	0.000	0.000
83	A	100	PHE	0	0.015	0.023	23.103	-0.016	-0.016	0.000	0.000	0.000	0.000
84	A	101	ALA	0	0.026	0.011	20.811	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	102	TYR	0	0.012	0.006	20.694	0.003	0.003	0.000	0.000	0.000	0.000
86	A	103	THR	0	-0.030	-0.040	22.080	-0.013	-0.013	0.000	0.000	0.000	0.000
87	A	104	PHE	0	-0.007	0.002	17.191	-0.022	-0.022	0.000	0.000	0.000	0.000
88	A	105	LYS	1	0.890	0.958	16.563	-0.297	-0.297	0.000	0.000	0.000	0.000
89	A	106	ASN	0	-0.058	-0.028	18.223	0.004	0.004	0.000	0.000	0.000	0.000
90	A	107	SER	0	-0.017	-0.002	20.945	-0.015	-0.015	0.000	0.000	0.000	0.000
91	A	108	LYS	1	0.829	0.917	19.456	0.130	0.130	0.000	0.000	0.000	0.000
92	A	109	TYR	0	0.021	0.019	19.732	0.018	0.018	0.000	0.000	0.000	0.000
93	A	110	HIS	0	-0.015	-0.003	21.242	-0.026	-0.026	0.000	0.000	0.000	0.000
94	A	111	LEU	0	-0.038	-0.014	18.798	0.001	0.001	0.000	0.000	0.000	0.000
95	A	112	SER	0	-0.028	-0.014	23.307	0.009	0.009	0.000	0.000	0.000	0.000
96	A	113	MET	0	-0.012	0.002	18.693	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	114	GLY	0	0.032	0.027	24.900	0.014	0.014	0.000	0.000	0.000	0.000
98	A	115	ARG	1	0.927	0.946	25.173	0.177	0.177	0.000	0.000	0.000	0.000
99	A	116	TYR	0	0.017	0.004	25.056	-0.013	-0.013	0.000	0.000	0.000	0.000
100	A	117	ALA	0	0.062	0.044	22.574	-0.023	-0.023	0.000	0.000	0.000	0.000
101	A	118	PHE	0	0.035	0.010	19.997	-0.042	-0.042	0.000	0.000	0.000	0.000
102	A	119	ASP	-1	-0.891	-0.950	19.918	-0.364	-0.364	0.000	0.000	0.000	0.000
103	A	120	LEU	0	-0.013	-0.006	20.028	-0.037	-0.037	0.000	0.000	0.000	0.000
104	A	121	LEU	0	0.001	-0.001	14.810	-0.057	-0.057	0.000	0.000	0.000	0.000
105	A	122	ILE	0	-0.029	-0.018	15.376	-0.100	-0.100	0.000	0.000	0.000	0.000
106	A	123	ASN	0	0.012	0.006	15.532	-0.065	-0.065	0.000	0.000	0.000	0.000
107	A	124	PHE	0	0.000	0.008	11.369	-0.103	-0.103	0.000	0.000	0.000	0.000
108	A	125	LEU	0	-0.045	-0.037	10.147	-0.160	-0.160	0.000	0.000	0.000	0.000
109	A	126	GLU	-1	-0.949	-0.983	10.917	-0.694	-0.694	0.000	0.000	0.000	0.000
110	A	127	GLU	-1	-0.994	-0.977	13.249	-0.689	-0.689	0.000	0.000	0.000	0.000
111	A	128	ARG	1	0.904	0.955	9.396	1.136	1.136	0.000	0.000	0.000	0.000
112	A	129	ASN	0	-0.030	-0.007	8.475	-0.321	-0.321	0.000	0.000	0.000	0.000
113	A	130	LEU	0	0.031	0.023	5.982	-0.468	-0.468	0.000	0.000	0.000	0.000
114	A	131	THR	0	-0.010	-0.028	5.326	0.272	0.272	0.000	0.000	0.000	0.000
115	A	132	TYR	0	-0.064	-0.059	4.750	0.112	0.200	-0.001	-0.007	-0.079	0.000
116	A	133	ILE	0	0.039	0.006	6.543	0.356	0.356	0.000	0.000	0.000	0.000
117	A	134	LEU	0	0.067	0.037	8.952	0.252	0.252	0.000	0.000	0.000	0.000
118	A	135	LYS	1	0.902	0.989	9.005	0.247	0.247	0.000	0.000	0.000	0.000
119	A	136	ILE	0	-0.016	-0.012	10.061	0.127	0.127	0.000	0.000	0.000	0.000
120	A	137	LEU	0	0.010	0.008	12.513	0.100	0.100	0.000	0.000	0.000	0.000
121	A	138	ASN	0	-0.012	-0.015	14.472	0.102	0.102	0.000	0.000	0.000	0.000
122	A	139	GLN	0	-0.023	-0.016	14.151	0.053	0.053	0.000	0.000	0.000	0.000
123	A	140	HIS	0	0.012	0.000	14.193	0.033	0.033	0.000	0.000	0.000	0.000
124	A	141	LEU	0	-0.064	-0.016	15.394	0.022	0.022	0.000	0.000	0.000	0.000
125	A	142	ASP	-1	-0.910	-0.948	18.744	-0.115	-0.115	0.000	0.000	0.000	0.000
126	A	143	ILE	0	0.021	0.003	17.997	0.009	0.009	0.000	0.000	0.000	0.000
127	A	144	LYS	1	0.981	0.995	22.555	0.118	0.118	0.000	0.000	0.000	0.000
128	A	145	VAL	0	0.014	0.003	23.620	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	146	TYR	0	-0.055	-0.027	26.303	0.014	0.014	0.000	0.000	0.000	0.000
130	A	147	VAL	0	0.003	-0.013	29.258	-0.013	-0.013	0.000	0.000	0.000	0.000
131	A	148	GLY	0	-0.002	0.009	31.336	0.007	0.007	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:18:GLN)