FMO DATABASE

FMODB ID: 98QG2

Calculation Name: 3ZQC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3ZQC

Chain ID: A

ChEMBL ID:

UniProt ID: A2D9X4

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	118
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-953450.826956
FMO2-HF: Nuclear repulsion	905431.551404
FMO2-HF: Total energy	-48019.275552
FMO2-MP2: Total energy	-48161.69023

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:52:MET)

Summations of interaction energy for fragment #1(A:52:MET)

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.
-15.887	-12.471	17.632	-9.959	-11.09	-0.061

Interaction energy analysis for fragmet #1(A:52:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.046 / q_NPA : 0.036

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

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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	54	GLY	0	0.024	-0.002	2.699	-3.124	0.898	1.343	-2.431	-2.934	-0.004
4	A	55	PRO	0	0.011	0.003	4.622	-1.150	-1.031	-0.001	-0.028	-0.090	0.000
5	A	56	PHE	0	0.023	0.017	4.255	-1.804	-1.697	-0.001	-0.022	-0.085	0.000
6	A	57	THR	0	-0.020	-0.019	5.435	0.643	0.643	0.000	0.000	0.000	0.000
7	A	58	GLU	-1	-0.761	-0.857	7.723	-0.983	-0.983	0.000	0.000	0.000	0.000
8	A	59	ALA	0	0.030	0.011	9.532	0.084	0.084	0.000	0.000	0.000	0.000
9	A	60	GLU	-1	-0.786	-0.857	4.276	-6.374	-6.203	-0.001	-0.030	-0.140	0.000
10	A	61	ASP	-1	-0.735	-0.851	8.837	-1.672	-1.672	0.000	0.000	0.000	0.000
11	A	62	ASP	-1	-0.816	-0.892	11.691	-0.678	-0.678	0.000	0.000	0.000	0.000
12	A	63	LEU	0	-0.029	-0.007	10.588	0.108	0.108	0.000	0.000	0.000	0.000
13	A	64	ILE	0	-0.073	-0.031	9.424	0.078	0.078	0.000	0.000	0.000	0.000
14	A	65	ARG	1	0.786	0.835	13.053	1.064	1.064	0.000	0.000	0.000	0.000
15	A	66	GLU	-1	-0.869	-0.928	16.039	-0.403	-0.403	0.000	0.000	0.000	0.000
16	A	67	TYR	0	-0.009	-0.023	14.713	0.082	0.082	0.000	0.000	0.000	0.000
17	A	68	VAL	0	-0.044	-0.032	16.431	0.072	0.072	0.000	0.000	0.000	0.000
18	A	69	LYS	1	0.873	0.941	18.762	0.419	0.419	0.000	0.000	0.000	0.000
19	A	70	GLU	-1	-0.881	-0.927	19.880	-0.273	-0.273	0.000	0.000	0.000	0.000
20	A	71	ASN	0	-0.091	-0.046	19.227	0.046	0.046	0.000	0.000	0.000	0.000
21	A	72	GLY	0	0.058	0.045	20.048	0.041	0.041	0.000	0.000	0.000	0.000
22	A	73	PRO	0	-0.005	0.000	18.461	-0.050	-0.050	0.000	0.000	0.000	0.000
23	A	74	GLN	0	0.017	-0.004	19.509	-0.037	-0.037	0.000	0.000	0.000	0.000
24	A	75	ASN	0	0.003	0.005	18.757	0.007	0.007	0.000	0.000	0.000	0.000
25	A	76	TRP	0	0.027	0.003	13.414	-0.035	-0.035	0.000	0.000	0.000	0.000
26	A	77	PRO	0	-0.009	-0.016	13.343	-0.085	-0.085	0.000	0.000	0.000	0.000
27	A	78	ARG	1	0.929	0.970	13.412	0.323	0.323	0.000	0.000	0.000	0.000
28	A	79	ILE	0	0.035	0.035	10.539	0.036	0.036	0.000	0.000	0.000	0.000
29	A	80	THR	0	-0.018	-0.019	8.970	-0.117	-0.117	0.000	0.000	0.000	0.000
30	A	81	SER	0	-0.068	-0.030	10.999	0.156	0.156	0.000	0.000	0.000	0.000
31	A	82	PHE	0	-0.004	0.001	11.503	0.080	0.080	0.000	0.000	0.000	0.000
32	A	83	LEU	0	-0.013	-0.002	6.295	-0.098	-0.098	0.000	0.000	0.000	0.000
33	A	84	PRO	0	0.062	0.031	6.673	-0.469	-0.469	0.000	0.000	0.000	0.000
34	A	85	ASN	0	-0.028	-0.007	2.544	-2.254	-1.122	1.136	-0.805	-1.464	0.000
35	A	86	ARG	1	0.732	0.820	1.793	-4.809	-7.283	15.158	-6.536	-6.147	-0.057
36	A	87	SER	0	0.044	0.023	4.434	1.193	1.364	-0.001	-0.032	-0.138	0.000
37	A	88	PRO	0	0.086	0.034	6.994	-0.130	-0.130	0.000	0.000	0.000	0.000
38	A	89	LYS	1	0.837	0.921	9.984	1.077	1.077	0.000	0.000	0.000	0.000
39	A	90	GLN	0	-0.010	-0.015	4.490	0.261	0.429	-0.001	-0.075	-0.092	0.000
40	A	91	CYS	0	0.006	0.019	8.392	-0.096	-0.096	0.000	0.000	0.000	0.000
41	A	92	ARG	1	0.972	0.997	10.412	0.799	0.799	0.000	0.000	0.000	0.000
42	A	93	GLU	-1	-0.921	-0.953	11.889	-0.963	-0.963	0.000	0.000	0.000	0.000
43	A	94	ARG	1	0.844	0.884	10.053	1.772	1.772	0.000	0.000	0.000	0.000
44	A	95	TRP	0	0.073	0.020	12.185	0.079	0.079	0.000	0.000	0.000	0.000
45	A	96	PHE	0	-0.021	-0.017	15.318	0.070	0.070	0.000	0.000	0.000	0.000
46	A	97	ASN	0	-0.131	-0.082	15.175	0.159	0.159	0.000	0.000	0.000	0.000
47	A	98	HIS	0	-0.045	-0.026	12.626	-0.082	-0.082	0.000	0.000	0.000	0.000
48	A	99	LEU	0	-0.027	0.008	13.233	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	100	ASP	-1	-0.830	-0.886	16.698	-0.487	-0.487	0.000	0.000	0.000	0.000
50	A	101	PRO	0	0.009	-0.013	19.896	0.012	0.012	0.000	0.000	0.000	0.000
51	A	102	ALA	0	-0.021	0.003	23.057	0.032	0.032	0.000	0.000	0.000	0.000
52	A	103	VAL	0	-0.077	-0.025	19.026	0.027	0.027	0.000	0.000	0.000	0.000
53	A	104	VAL	0	-0.018	-0.004	22.322	0.002	0.002	0.000	0.000	0.000	0.000
54	A	105	LYS	1	0.970	0.971	22.415	0.377	0.377	0.000	0.000	0.000	0.000
55	A	106	HIS	0	-0.012	0.005	23.716	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	107	ALA	0	0.047	0.016	25.840	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	108	TRP	0	-0.021	-0.025	23.204	0.006	0.006	0.000	0.000	0.000	0.000
58	A	109	THR	0	0.027	0.000	28.356	0.016	0.016	0.000	0.000	0.000	0.000
59	A	110	PRO	0	0.019	0.007	32.104	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	111	GLU	-1	-0.808	-0.917	34.404	-0.178	-0.178	0.000	0.000	0.000	0.000
61	A	112	GLU	-1	-0.768	-0.823	29.240	-0.293	-0.293	0.000	0.000	0.000	0.000
62	A	113	ASP	-1	-0.745	-0.840	29.953	-0.235	-0.235	0.000	0.000	0.000	0.000
63	A	114	GLU	-1	-0.794	-0.891	32.125	-0.144	-0.144	0.000	0.000	0.000	0.000
64	A	115	THR	0	-0.051	-0.038	33.513	0.009	0.009	0.000	0.000	0.000	0.000
65	A	116	ILE	0	-0.044	-0.023	28.219	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	117	PHE	0	0.011	0.006	32.226	0.006	0.006	0.000	0.000	0.000	0.000
67	A	118	ARG	1	0.888	0.929	34.709	0.149	0.149	0.000	0.000	0.000	0.000
68	A	119	ASN	0	-0.065	-0.038	34.033	0.016	0.016	0.000	0.000	0.000	0.000
69	A	120	TYR	0	-0.005	0.000	29.262	0.004	0.004	0.000	0.000	0.000	0.000
70	A	121	LEU	0	-0.023	0.009	34.032	0.007	0.007	0.000	0.000	0.000	0.000
71	A	122	LYS	1	0.853	0.931	36.893	0.155	0.155	0.000	0.000	0.000	0.000
72	A	123	LEU	0	-0.026	-0.005	33.590	0.003	0.003	0.000	0.000	0.000	0.000
73	A	124	GLY	0	0.086	0.043	33.234	0.005	0.005	0.000	0.000	0.000	0.000
74	A	125	SER	0	0.027	0.017	27.740	-0.010	-0.010	0.000	0.000	0.000	0.000
75	A	126	LYS	1	0.853	0.911	28.221	0.187	0.187	0.000	0.000	0.000	0.000
76	A	127	TRP	0	0.111	0.043	24.977	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	128	SER	0	0.012	0.016	25.129	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	129	VAL	0	-0.033	-0.015	26.525	0.000	0.000	0.000	0.000	0.000	0.000
79	A	130	ILE	0	0.029	0.006	29.038	0.000	0.000	0.000	0.000	0.000	0.000
80	A	131	ALA	0	0.035	0.014	25.549	0.003	0.003	0.000	0.000	0.000	0.000
81	A	132	LYS	1	0.888	0.958	27.498	0.238	0.238	0.000	0.000	0.000	0.000
82	A	133	LEU	0	-0.038	-0.017	30.013	0.016	0.016	0.000	0.000	0.000	0.000
83	A	134	ILE	0	-0.001	0.005	29.245	0.011	0.011	0.000	0.000	0.000	0.000
84	A	135	PRO	0	0.021	0.014	28.597	-0.023	-0.023	0.000	0.000	0.000	0.000
85	A	136	GLY	0	0.095	0.045	25.676	0.001	0.001	0.000	0.000	0.000	0.000
86	A	137	ARG	1	0.699	0.842	24.197	0.313	0.313	0.000	0.000	0.000	0.000
87	A	138	THR	0	0.033	0.015	19.314	0.038	0.038	0.000	0.000	0.000	0.000
88	A	139	ASP	-1	-0.788	-0.920	20.961	-0.421	-0.421	0.000	0.000	0.000	0.000
89	A	140	ASN	0	0.024	0.004	16.197	0.099	0.099	0.000	0.000	0.000	0.000
90	A	141	ALA	0	0.003	0.022	20.110	0.002	0.002	0.000	0.000	0.000	0.000
91	A	142	ILE	0	0.027	0.009	21.540	0.029	0.029	0.000	0.000	0.000	0.000
92	A	143	LYS	1	0.801	0.904	20.271	0.451	0.451	0.000	0.000	0.000	0.000
93	A	144	ASN	0	-0.006	-0.008	17.805	0.054	0.054	0.000	0.000	0.000	0.000
94	A	145	ARG	1	0.791	0.892	21.810	0.278	0.278	0.000	0.000	0.000	0.000
95	A	146	TRP	0	0.060	0.015	24.897	0.022	0.022	0.000	0.000	0.000	0.000
96	A	147	ASN	0	0.019	0.004	22.324	0.038	0.038	0.000	0.000	0.000	0.000
97	A	148	SER	0	-0.060	-0.046	22.652	0.025	0.025	0.000	0.000	0.000	0.000
98	A	149	SER	0	-0.033	-0.019	24.696	0.021	0.021	0.000	0.000	0.000	0.000
99	A	150	ILE	0	0.010	0.008	28.137	0.016	0.016	0.000	0.000	0.000	0.000
100	A	151	SER	0	-0.023	-0.016	29.148	0.014	0.014	0.000	0.000	0.000	0.000
101	A	152	LYS	1	0.813	0.909	25.996	0.197	0.197	0.000	0.000	0.000	0.000
102	A	153	ARG	1	0.790	0.883	30.411	0.193	0.193	0.000	0.000	0.000	0.000
103	A	154	ILE	0	0.023	0.023	34.606	0.000	0.000	0.000	0.000	0.000	0.000
104	A	155	SER	0	-0.011	-0.005	37.039	0.007	0.007	0.000	0.000	0.000	0.000
105	A	156	THR	0	0.039	0.024	40.697	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	157	ASN	0	0.030	0.020	44.323	0.002	0.002	0.000	0.000	0.000	0.000
107	A	158	SER	0	0.001	-0.009	46.774	0.002	0.002	0.000	0.000	0.000	0.000
108	A	159	ASN	0	-0.050	-0.043	49.612	0.003	0.003	0.000	0.000	0.000	0.000
109	A	160	HIS	0	-0.007	0.012	48.176	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	161	LYS	1	0.857	0.924	43.670	0.094	0.094	0.000	0.000	0.000	0.000
111	A	162	GLU	-1	-0.822	-0.908	39.998	-0.100	-0.100	0.000	0.000	0.000	0.000
112	A	163	ILE	0	-0.034	-0.016	41.256	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	164	LEU	0	-0.001	0.008	34.163	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	165	LEU	0	0.014	0.011	37.431	0.003	0.003	0.000	0.000	0.000	0.000
115	A	166	PRO	0	0.034	0.030	35.682	-0.010	-0.010	0.000	0.000	0.000	0.000
116	A	167	ASP	-1	-0.784	-0.890	29.859	-0.204	-0.204	0.000	0.000	0.000	0.000
117	A	168	ARG	1	0.895	0.931	32.774	0.130	0.130	0.000	0.000	0.000	0.000
118	A	169	SER	0	0.021	0.033	28.454	0.003	0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:52:MET)