FMO DATABASE

FMODB ID: 39YVL

Calculation Name: 2EMQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EMQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q5L147

Base Structure: X-ray

Registration Date: 2023-09-20

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	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	135
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1183582.466482
FMO2-HF: Nuclear repulsion	1128517.057487
FMO2-HF: Total energy	-55065.408995
FMO2-MP2: Total energy	-55222.258075

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:10:GLN)

Summations of interaction energy for fragment #1(A:10: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.
-9.641	-7.162	-0.01	-0.914	-1.553	0.005

Interaction energy analysis for fragmet #1(A:10:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.026 / 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	12	THR	0	-0.006	-0.010	3.786	-0.387	1.178	-0.014	-0.719	-0.831	0.004
4	A	13	VAL	0	-0.018	-0.011	6.303	0.134	0.134	0.000	0.000	0.000	0.000
5	A	14	LYS	1	0.850	0.898	9.787	-0.071	-0.071	0.000	0.000	0.000	0.000
6	A	15	PRO	0	-0.052	-0.014	8.890	-0.044	-0.044	0.000	0.000	0.000	0.000
7	A	16	PHE	0	-0.009	-0.008	8.332	0.011	0.011	0.000	0.000	0.000	0.000
8	A	17	LEU	0	-0.070	-0.012	13.498	-0.026	-0.026	0.000	0.000	0.000	0.000
9	A	18	ILE	0	0.001	0.018	15.848	-0.062	-0.062	0.000	0.000	0.000	0.000
10	A	19	PRO	0	0.028	-0.002	19.542	0.010	0.010	0.000	0.000	0.000	0.000
11	A	20	ALA	0	0.058	0.018	21.198	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	21	ASP	-1	-0.867	-0.921	23.569	0.246	0.246	0.000	0.000	0.000	0.000
13	A	22	LYS	1	0.828	0.915	24.480	-0.279	-0.279	0.000	0.000	0.000	0.000
14	A	23	VAL	0	-0.076	-0.039	22.801	0.020	0.020	0.000	0.000	0.000	0.000
15	A	24	ALA	0	-0.001	0.014	26.203	-0.019	-0.019	0.000	0.000	0.000	0.000
16	A	25	HIS	0	-0.021	-0.024	28.109	0.012	0.012	0.000	0.000	0.000	0.000
17	A	26	VAL	0	0.009	0.008	29.840	-0.014	-0.014	0.000	0.000	0.000	0.000
18	A	27	GLN	0	0.075	0.021	31.852	0.004	0.004	0.000	0.000	0.000	0.000
19	A	28	PRO	0	0.013	-0.029	32.292	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	29	GLY	0	0.082	0.044	34.713	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	30	ASN	0	-0.081	-0.038	36.429	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	31	TYR	0	0.072	0.047	38.952	0.003	0.003	0.000	0.000	0.000	0.000
23	A	32	LEU	0	0.028	0.009	37.867	0.009	0.009	0.000	0.000	0.000	0.000
24	A	33	ASP	-1	-0.815	-0.916	39.377	0.146	0.146	0.000	0.000	0.000	0.000
25	A	34	HIS	0	-0.004	0.003	37.465	0.000	0.000	0.000	0.000	0.000	0.000
26	A	35	ALA	0	0.001	-0.010	35.069	0.008	0.008	0.000	0.000	0.000	0.000
27	A	36	LEU	0	-0.017	-0.004	35.928	0.013	0.013	0.000	0.000	0.000	0.000
28	A	37	LEU	0	-0.009	0.017	37.894	0.007	0.007	0.000	0.000	0.000	0.000
29	A	38	VAL	0	0.019	-0.010	33.081	0.006	0.006	0.000	0.000	0.000	0.000
30	A	39	LEU	0	-0.031	-0.022	31.235	0.012	0.012	0.000	0.000	0.000	0.000
31	A	40	THR	0	-0.068	-0.049	33.999	0.007	0.007	0.000	0.000	0.000	0.000
32	A	41	LYS	1	0.867	0.939	35.827	-0.177	-0.177	0.000	0.000	0.000	0.000
33	A	42	THR	0	-0.027	0.022	30.244	0.013	0.013	0.000	0.000	0.000	0.000
34	A	43	GLY	0	0.013	-0.003	29.530	-0.006	-0.006	0.000	0.000	0.000	0.000
35	A	44	TYR	0	-0.071	-0.042	23.149	0.048	0.048	0.000	0.000	0.000	0.000
36	A	45	SER	0	0.000	0.001	25.689	-0.016	-0.016	0.000	0.000	0.000	0.000
37	A	46	ALA	0	0.005	-0.004	26.470	-0.022	-0.022	0.000	0.000	0.000	0.000
38	A	47	ILE	0	-0.009	0.003	27.388	0.017	0.017	0.000	0.000	0.000	0.000
39	A	48	PRO	0	0.014	-0.015	24.366	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	49	VAL	0	-0.001	0.017	26.700	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	50	LEU	0	-0.023	0.005	25.259	0.010	0.010	0.000	0.000	0.000	0.000
42	A	51	ASP	-1	-0.753	-0.873	29.205	0.158	0.158	0.000	0.000	0.000	0.000
43	A	52	THR	0	0.017	-0.017	31.434	0.005	0.005	0.000	0.000	0.000	0.000
44	A	53	SER	0	-0.058	-0.028	30.011	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	54	TYR	0	0.015	0.007	25.012	0.008	0.008	0.000	0.000	0.000	0.000
46	A	55	LYS	1	0.871	0.941	25.166	-0.134	-0.134	0.000	0.000	0.000	0.000
47	A	56	LEU	0	-0.010	-0.017	21.655	0.000	0.000	0.000	0.000	0.000	0.000
48	A	57	HIS	0	-0.025	-0.028	25.422	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	58	GLY	0	0.034	-0.013	26.176	0.000	0.000	0.000	0.000	0.000	0.000
50	A	59	LEU	0	-0.033	0.005	23.224	0.007	0.007	0.000	0.000	0.000	0.000
51	A	60	ILE	0	0.095	0.023	27.595	-0.012	-0.012	0.000	0.000	0.000	0.000
52	A	61	SER	0	0.045	0.003	29.928	0.006	0.006	0.000	0.000	0.000	0.000
53	A	62	MET	0	0.079	0.012	31.878	-0.015	-0.015	0.000	0.000	0.000	0.000
54	A	63	THR	0	-0.008	0.005	32.714	-0.011	-0.011	0.000	0.000	0.000	0.000
55	A	64	MET	0	-0.044	0.017	28.890	-0.008	-0.008	0.000	0.000	0.000	0.000
56	A	65	MET	0	0.005	0.016	34.563	-0.012	-0.012	0.000	0.000	0.000	0.000
57	A	66	MET	0	0.001	-0.008	37.795	-0.012	-0.012	0.000	0.000	0.000	0.000
58	A	67	ASP	-1	-0.922	-0.966	36.561	0.188	0.188	0.000	0.000	0.000	0.000
59	A	68	ALA	0	-0.035	0.001	38.648	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	69	ILE	0	-0.066	-0.027	40.356	-0.009	-0.009	0.000	0.000	0.000	0.000
61	A	70	LEU	0	-0.030	-0.014	41.055	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	71	GLY	0	0.025	0.021	44.394	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	72	LEU	0	-0.052	-0.039	47.750	0.002	0.002	0.000	0.000	0.000	0.000
64	A	73	GLU	-1	-0.948	-0.974	49.860	0.089	0.089	0.000	0.000	0.000	0.000
65	A	74	ARG	1	0.787	0.864	50.060	-0.105	-0.105	0.000	0.000	0.000	0.000
66	A	75	ILE	0	0.009	0.023	44.352	0.002	0.002	0.000	0.000	0.000	0.000
67	A	76	GLU	-1	-0.904	-0.962	47.053	0.111	0.111	0.000	0.000	0.000	0.000
68	A	77	PHE	0	-0.004	-0.036	43.924	0.003	0.003	0.000	0.000	0.000	0.000
69	A	78	GLU	-1	-0.729	-0.813	47.033	0.110	0.110	0.000	0.000	0.000	0.000
70	A	79	ARG	1	0.878	0.927	44.377	-0.129	-0.129	0.000	0.000	0.000	0.000
71	A	80	LEU	0	-0.036	-0.014	41.378	0.004	0.004	0.000	0.000	0.000	0.000
72	A	81	GLU	-1	-0.842	-0.932	43.598	0.124	0.124	0.000	0.000	0.000	0.000
73	A	82	THR	0	-0.099	-0.045	46.122	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	83	MET	0	0.009	0.031	41.269	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	84	LYS	1	0.915	0.963	39.272	-0.118	-0.118	0.000	0.000	0.000	0.000
76	A	85	VAL	0	-0.004	0.008	34.293	0.005	0.005	0.000	0.000	0.000	0.000
77	A	86	GLU	-1	-0.987	-1.001	34.567	0.155	0.155	0.000	0.000	0.000	0.000
78	A	87	GLU	-1	-0.946	-0.974	35.526	0.140	0.140	0.000	0.000	0.000	0.000
79	A	88	VAL	0	-0.022	0.002	35.087	0.002	0.002	0.000	0.000	0.000	0.000
80	A	89	MET	0	-0.103	-0.027	30.450	0.013	0.013	0.000	0.000	0.000	0.000
81	A	90	ASN	0	0.031	0.013	26.285	-0.021	-0.021	0.000	0.000	0.000	0.000
82	A	91	ARG	1	0.977	0.974	27.697	-0.182	-0.182	0.000	0.000	0.000	0.000
83	A	92	ASN	0	-0.014	0.004	25.379	0.016	0.016	0.000	0.000	0.000	0.000
84	A	93	ILE	0	-0.049	0.002	22.539	0.019	0.019	0.000	0.000	0.000	0.000
85	A	94	PRO	0	-0.020	-0.006	17.388	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	95	ARG	1	0.856	0.908	17.506	-0.383	-0.383	0.000	0.000	0.000	0.000
87	A	96	LEU	0	-0.044	-0.016	11.426	0.093	0.093	0.000	0.000	0.000	0.000
88	A	97	ARG	1	0.979	0.993	10.918	-0.259	-0.259	0.000	0.000	0.000	0.000
89	A	98	LEU	0	0.008	-0.011	11.470	0.140	0.140	0.000	0.000	0.000	0.000
90	A	99	ASP	-1	-0.849	-0.904	8.984	-0.042	-0.042	0.000	0.000	0.000	0.000
91	A	100	ASP	-1	-0.718	-0.847	8.138	1.002	1.002	0.000	0.000	0.000	0.000
92	A	101	SER	0	0.009	0.001	4.095	-0.760	-0.507	0.000	-0.069	-0.185	0.000
93	A	102	LEU	0	0.031	0.008	4.375	-0.323	-0.192	-0.001	-0.009	-0.120	0.000
94	A	103	MET	0	-0.015	-0.019	3.679	-2.028	-1.541	0.006	-0.118	-0.375	0.001
95	A	104	LYS	1	0.933	0.971	5.590	-2.937	-2.894	-0.001	0.001	-0.042	0.000
96	A	105	ALA	0	0.026	0.015	8.382	-0.659	-0.659	0.000	0.000	0.000	0.000
97	A	106	VAL	0	0.004	-0.012	9.141	-0.466	-0.466	0.000	0.000	0.000	0.000
98	A	107	GLY	0	0.025	0.015	10.214	-0.349	-0.349	0.000	0.000	0.000	0.000
99	A	108	LEU	0	0.032	0.015	12.064	-0.296	-0.296	0.000	0.000	0.000	0.000
100	A	109	ILE	0	-0.012	0.018	13.558	-0.198	-0.198	0.000	0.000	0.000	0.000
101	A	110	VAL	0	0.001	0.026	14.103	-0.116	-0.116	0.000	0.000	0.000	0.000
102	A	111	ASN	0	0.007	0.004	16.848	-0.109	-0.109	0.000	0.000	0.000	0.000
103	A	112	HIS	0	-0.049	-0.027	17.810	-0.141	-0.141	0.000	0.000	0.000	0.000
104	A	113	PRO	0	-0.035	-0.038	19.042	0.065	0.065	0.000	0.000	0.000	0.000
105	A	114	PHE	0	-0.019	-0.033	18.781	0.042	0.042	0.000	0.000	0.000	0.000
106	A	115	VAL	0	0.002	0.015	16.220	-0.030	-0.030	0.000	0.000	0.000	0.000
107	A	116	CYS	0	-0.022	0.013	17.822	0.014	0.014	0.000	0.000	0.000	0.000
108	A	117	VAL	0	-0.015	-0.003	14.385	0.061	0.061	0.000	0.000	0.000	0.000
109	A	118	GLU	-1	-0.814	-0.892	16.851	0.301	0.301	0.000	0.000	0.000	0.000
110	A	119	ASN	0	0.031	-0.014	16.602	0.010	0.010	0.000	0.000	0.000	0.000
111	A	120	ASP	-1	-0.884	-0.973	14.667	0.146	0.146	0.000	0.000	0.000	0.000
112	A	121	ASP	-1	-0.933	-0.938	17.495	0.061	0.061	0.000	0.000	0.000	0.000
113	A	122	GLY	0	-0.016	-0.014	20.675	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	123	TYR	0	-0.084	-0.033	21.680	0.010	0.010	0.000	0.000	0.000	0.000
115	A	124	PHE	0	0.015	0.007	21.001	0.032	0.032	0.000	0.000	0.000	0.000
116	A	125	ALA	0	0.015	-0.018	17.982	-0.029	-0.029	0.000	0.000	0.000	0.000
117	A	126	GLY	0	0.033	0.010	19.483	-0.014	-0.014	0.000	0.000	0.000	0.000
118	A	127	ILE	0	-0.039	-0.001	18.561	0.022	0.022	0.000	0.000	0.000	0.000
119	A	128	PHE	0	0.030	0.015	11.286	0.033	0.033	0.000	0.000	0.000	0.000
120	A	129	THR	0	0.049	0.011	16.185	-0.019	-0.019	0.000	0.000	0.000	0.000
121	A	130	ARG	1	0.933	0.964	16.284	-0.597	-0.597	0.000	0.000	0.000	0.000
122	A	131	ARG	1	0.963	0.994	17.899	-0.447	-0.447	0.000	0.000	0.000	0.000
123	A	132	GLU	-1	-0.874	-0.945	15.939	0.637	0.637	0.000	0.000	0.000	0.000
124	A	133	VAL	0	0.012	0.020	12.588	0.044	0.044	0.000	0.000	0.000	0.000
125	A	134	LEU	0	0.006	-0.013	14.613	0.017	0.017	0.000	0.000	0.000	0.000
126	A	135	LYS	1	0.882	0.945	17.354	-0.574	-0.574	0.000	0.000	0.000	0.000
127	A	136	GLN	0	-0.007	-0.014	12.153	-0.193	-0.193	0.000	0.000	0.000	0.000
128	A	137	LEU	0	0.056	0.028	14.770	-0.035	-0.035	0.000	0.000	0.000	0.000
129	A	138	ASN	0	0.035	0.011	15.753	-0.072	-0.072	0.000	0.000	0.000	0.000
130	A	139	LYS	1	0.870	0.940	16.062	-0.765	-0.765	0.000	0.000	0.000	0.000
131	A	140	GLN	0	-0.054	-0.009	11.582	0.006	0.006	0.000	0.000	0.000	0.000
132	A	141	LEU	0	-0.017	0.007	16.691	-0.029	-0.029	0.000	0.000	0.000	0.000
133	A	142	HIS	0	-0.046	-0.043	19.858	-0.050	-0.050	0.000	0.000	0.000	0.000
134	A	143	ARG	1	0.928	0.958	22.691	-0.376	-0.376	0.000	0.000	0.000	0.000
135	A	144	PRO	0	0.045	0.052	24.962	-0.020	-0.020	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:GLN)