FMO DATABASE

FMODB ID: QYRZY

Calculation Name: 5EQZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5EQZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q9S0B8

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:

Apendix: None

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	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1124437.60743
FMO2-HF: Nuclear repulsion	1070733.116751
FMO2-HF: Total energy	-53704.490679
FMO2-MP2: Total energy	-53863.465464

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:20:HIS)

Summations of interaction energy for fragment #1(A:20:HIS)

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.
-16.993	-8.958	9.019	-6.733	-10.323	-0.03

Interaction energy analysis for fragmet #1(A:20:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.001 / q_NPA : -0.002

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	22	HIS	0	0.028	0.011	2.087	-8.706	-4.859	8.428	-4.903	-7.372	-0.024
4	A	23	TYR	0	0.006	0.002	4.559	0.336	0.751	0.000	-0.032	-0.383	0.000
5	A	24	VAL	0	0.019	0.009	7.425	0.018	0.018	0.000	0.000	0.000	0.000
6	A	25	GLU	-1	-0.783	-0.883	9.058	-1.145	-1.145	0.000	0.000	0.000	0.000
7	A	26	GLU	-1	-0.757	-0.887	10.288	-0.681	-0.681	0.000	0.000	0.000	0.000
8	A	27	LYS	1	0.767	0.881	3.773	2.828	2.960	0.000	-0.018	-0.114	0.000
9	A	28	LYS	1	0.810	0.896	10.553	1.427	1.427	0.000	0.000	0.000	0.000
10	A	29	GLU	-1	-0.938	-0.958	13.596	-0.276	-0.276	0.000	0.000	0.000	0.000
11	A	30	ILE	0	-0.043	-0.023	11.503	0.082	0.082	0.000	0.000	0.000	0.000
12	A	31	ASP	-1	-0.793	-0.877	12.578	-0.754	-0.754	0.000	0.000	0.000	0.000
13	A	32	SER	0	0.010	0.010	15.574	0.049	0.049	0.000	0.000	0.000	0.000
14	A	33	LEU	0	-0.010	-0.002	18.455	0.046	0.046	0.000	0.000	0.000	0.000
15	A	34	MET	0	-0.015	-0.005	16.985	0.065	0.065	0.000	0.000	0.000	0.000
16	A	35	GLU	-1	-0.927	-0.971	19.146	-0.327	-0.327	0.000	0.000	0.000	0.000
17	A	36	ASP	-1	-0.858	-0.887	21.422	-0.196	-0.196	0.000	0.000	0.000	0.000
18	A	37	VAL	0	-0.045	-0.031	22.257	0.033	0.033	0.000	0.000	0.000	0.000
19	A	38	LEU	0	0.028	-0.002	20.504	0.033	0.033	0.000	0.000	0.000	0.000
20	A	39	ALA	0	-0.012	0.012	24.546	0.012	0.012	0.000	0.000	0.000	0.000
21	A	40	LEU	0	-0.079	-0.017	26.876	0.010	0.010	0.000	0.000	0.000	0.000
22	A	41	VAL	0	0.027	0.015	29.443	0.005	0.005	0.000	0.000	0.000	0.000
23	A	42	ASN	0	0.051	0.005	32.684	0.005	0.005	0.000	0.000	0.000	0.000
24	A	43	ASP	-1	-0.884	-0.929	35.697	-0.073	-0.073	0.000	0.000	0.000	0.000
25	A	44	SER	0	-0.025	0.000	32.849	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	45	SER	0	0.026	0.006	34.877	0.010	0.010	0.000	0.000	0.000	0.000
27	A	46	GLY	0	0.097	0.030	34.289	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	47	GLY	0	-0.012	-0.013	33.835	0.004	0.004	0.000	0.000	0.000	0.000
29	A	48	LYS	1	0.931	0.962	29.275	0.136	0.136	0.000	0.000	0.000	0.000
30	A	49	PHE	0	0.033	0.017	29.530	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	50	LYS	1	0.800	0.882	29.016	0.018	0.018	0.000	0.000	0.000	0.000
32	A	51	ASP	-1	-0.798	-0.877	28.233	-0.116	-0.116	0.000	0.000	0.000	0.000
33	A	52	TYR	0	-0.019	-0.046	24.950	0.003	0.003	0.000	0.000	0.000	0.000
34	A	53	LYS	1	0.935	0.988	24.449	-0.015	-0.015	0.000	0.000	0.000	0.000
35	A	54	ASP	-1	-0.841	-0.913	25.158	0.004	0.004	0.000	0.000	0.000	0.000
36	A	55	LYS	1	0.898	0.930	22.599	0.158	0.158	0.000	0.000	0.000	0.000
37	A	56	ILE	0	-0.009	-0.001	20.168	0.005	0.005	0.000	0.000	0.000	0.000
38	A	57	ASN	0	-0.070	-0.046	20.487	0.053	0.053	0.000	0.000	0.000	0.000
39	A	58	GLU	-1	-0.926	-0.952	21.668	-0.050	-0.050	0.000	0.000	0.000	0.000
40	A	59	LEU	0	0.032	0.017	16.167	0.022	0.022	0.000	0.000	0.000	0.000
41	A	60	LYS	1	0.869	0.925	17.156	-0.204	-0.204	0.000	0.000	0.000	0.000
42	A	61	GLU	-1	-0.865	-0.915	18.038	0.273	0.273	0.000	0.000	0.000	0.000
43	A	62	ASN	0	-0.041	-0.032	17.936	0.041	0.041	0.000	0.000	0.000	0.000
44	A	63	LEU	0	-0.028	-0.016	12.593	0.011	0.011	0.000	0.000	0.000	0.000
45	A	64	LYS	1	0.828	0.919	13.637	-0.095	-0.095	0.000	0.000	0.000	0.000
46	A	65	ASP	-1	-0.928	-0.964	14.317	0.601	0.601	0.000	0.000	0.000	0.000
47	A	66	ILE	0	-0.024	0.004	8.360	0.277	0.277	0.000	0.000	0.000	0.000
48	A	67	GLY	0	-0.005	-0.014	9.019	-0.042	-0.042	0.000	0.000	0.000	0.000
49	A	68	ASN	0	-0.030	-0.035	2.744	-4.763	-3.249	0.396	-0.683	-1.228	0.007
50	A	69	ALA	0	0.030	0.011	5.805	-1.409	-1.409	0.000	0.000	0.000	0.000
51	A	70	GLU	-1	-0.745	-0.877	2.882	-2.739	-0.612	0.195	-1.097	-1.226	-0.013
52	A	71	LEU	0	0.006	0.005	6.574	-0.471	-0.471	0.000	0.000	0.000	0.000
53	A	72	LYS	1	0.907	0.959	8.422	-2.350	-2.350	0.000	0.000	0.000	0.000
54	A	73	GLU	-1	-0.913	-0.945	10.232	0.153	0.153	0.000	0.000	0.000	0.000
55	A	74	LYS	1	0.800	0.880	8.947	0.640	0.640	0.000	0.000	0.000	0.000
56	A	75	LEU	0	0.059	0.034	12.378	-0.058	-0.058	0.000	0.000	0.000	0.000
57	A	76	LEU	0	-0.055	-0.004	14.489	-0.039	-0.039	0.000	0.000	0.000	0.000
58	A	77	ASN	0	-0.002	-0.015	14.069	-0.020	-0.020	0.000	0.000	0.000	0.000
59	A	78	LEU	0	0.036	0.028	16.540	-0.026	-0.026	0.000	0.000	0.000	0.000
60	A	79	GLN	0	-0.031	-0.036	17.671	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	80	ASN	0	-0.005	-0.007	19.537	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	81	SER	0	0.051	0.021	20.290	-0.020	-0.020	0.000	0.000	0.000	0.000
63	A	82	PHE	0	-0.009	-0.009	22.661	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	83	GLN	0	-0.004	-0.014	24.568	-0.010	-0.010	0.000	0.000	0.000	0.000
65	A	84	ASP	-1	-0.884	-0.922	25.386	0.044	0.044	0.000	0.000	0.000	0.000
66	A	85	LYS	1	0.747	0.874	26.524	0.088	0.088	0.000	0.000	0.000	0.000
67	A	86	LEU	0	-0.041	-0.020	28.641	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	87	ALA	0	0.012	0.004	30.329	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	88	ALA	0	-0.009	0.001	31.661	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	89	LYS	1	0.833	0.913	33.017	0.041	0.041	0.000	0.000	0.000	0.000
71	A	90	LEU	0	-0.020	-0.021	34.117	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	91	ALA	0	-0.016	-0.001	36.260	0.001	0.001	0.000	0.000	0.000	0.000
73	A	92	ALA	0	0.003	0.000	37.549	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	93	LEU	0	-0.030	-0.008	37.985	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	94	LYS	1	0.872	0.910	38.771	-0.027	-0.027	0.000	0.000	0.000	0.000
76	A	95	ALA	0	-0.008	0.011	42.125	0.001	0.001	0.000	0.000	0.000	0.000
77	A	96	ALA	0	0.029	0.018	43.443	0.000	0.000	0.000	0.000	0.000	0.000
78	A	97	LYS	1	0.787	0.888	45.099	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	98	ASN	0	0.033	0.018	46.712	0.002	0.002	0.000	0.000	0.000	0.000
80	A	99	THR	0	-0.026	-0.008	47.451	0.002	0.002	0.000	0.000	0.000	0.000
81	A	100	ILE	0	-0.037	-0.025	48.323	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	101	GLU	-1	-0.893	-0.961	50.530	0.004	0.004	0.000	0.000	0.000	0.000
83	A	102	ASN	0	-0.045	-0.031	51.653	0.002	0.002	0.000	0.000	0.000	0.000
84	A	103	ILE	0	-0.047	-0.004	52.722	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	104	THR	0	0.041	0.007	56.164	0.001	0.001	0.000	0.000	0.000	0.000
86	A	105	ASP	-1	-0.878	-0.916	59.891	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	106	LYS	1	0.844	0.925	56.044	0.004	0.004	0.000	0.000	0.000	0.000
88	A	107	ASP	-1	-0.807	-0.916	59.743	-0.019	-0.019	0.000	0.000	0.000	0.000
89	A	108	GLN	0	-0.011	0.009	61.524	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	109	ASP	-1	-0.801	-0.885	60.375	-0.031	-0.031	0.000	0.000	0.000	0.000
91	A	110	ILE	0	0.000	-0.010	57.406	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	111	SER	0	-0.003	-0.009	56.549	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	112	LYS	1	0.865	0.943	55.710	0.022	0.022	0.000	0.000	0.000	0.000
94	A	113	ARG	1	0.848	0.894	54.365	0.031	0.031	0.000	0.000	0.000	0.000
95	A	114	LYS	1	0.873	0.949	48.866	0.023	0.023	0.000	0.000	0.000	0.000
96	A	115	ILE	0	0.048	0.017	50.870	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	116	TRP	0	-0.034	-0.017	49.808	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	117	SER	0	-0.040	-0.042	48.273	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	118	GLU	-1	-0.821	-0.908	46.474	-0.025	-0.025	0.000	0.000	0.000	0.000
100	A	119	ALA	0	0.027	0.011	45.173	0.000	0.000	0.000	0.000	0.000	0.000
101	A	120	LYS	1	0.942	0.980	44.229	0.061	0.061	0.000	0.000	0.000	0.000
102	A	121	LEU	0	-0.028	-0.012	42.221	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	122	VAL	0	-0.012	0.005	39.889	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	123	GLY	0	0.005	-0.004	39.902	0.001	0.001	0.000	0.000	0.000	0.000
105	A	124	VAL	0	-0.088	-0.025	40.887	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	125	THR	0	0.004	0.000	44.183	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	126	VAL	0	0.010	0.014	46.994	0.002	0.002	0.000	0.000	0.000	0.000
108	A	127	PRO	0	-0.030	-0.018	50.513	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	128	LEU	0	0.046	0.004	53.660	0.003	0.003	0.000	0.000	0.000	0.000
110	A	129	LEU	0	-0.052	-0.047	55.574	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	130	GLY	0	0.038	0.004	58.988	0.002	0.002	0.000	0.000	0.000	0.000
112	A	131	SER	0	0.007	0.017	60.978	0.001	0.001	0.000	0.000	0.000	0.000
113	A	132	ASN	0	0.026	-0.012	64.090	0.000	0.000	0.000	0.000	0.000	0.000
114	A	133	THR	0	-0.033	-0.004	64.979	0.001	0.001	0.000	0.000	0.000	0.000
115	A	134	SER	0	0.033	0.015	65.255	0.000	0.000	0.000	0.000	0.000	0.000
116	A	135	GLY	0	0.048	0.029	63.708	0.000	0.000	0.000	0.000	0.000	0.000
117	A	136	ASN	0	-0.021	-0.022	60.960	0.000	0.000	0.000	0.000	0.000	0.000
118	A	137	GLY	0	0.022	0.008	58.751	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	138	ASP	-1	-0.847	-0.935	57.627	-0.009	-0.009	0.000	0.000	0.000	0.000
120	A	139	LYS	1	0.919	0.980	57.704	0.021	0.021	0.000	0.000	0.000	0.000
121	A	140	MET	0	-0.051	0.005	54.183	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	141	SER	0	-0.003	0.009	53.448	0.000	0.000	0.000	0.000	0.000	0.000
123	A	142	LYS	1	0.868	0.922	52.546	0.006	0.006	0.000	0.000	0.000	0.000
124	A	143	ASN	0	-0.008	-0.002	51.180	0.000	0.000	0.000	0.000	0.000	0.000
125	A	144	ALA	0	0.050	0.014	49.167	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	145	VAL	0	0.015	0.007	47.929	0.000	0.000	0.000	0.000	0.000	0.000
127	A	146	GLU	-1	-0.822	-0.893	47.959	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	147	GLN	0	-0.098	-0.060	45.710	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	148	ILE	0	0.002	-0.002	43.064	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	149	ASP	-1	-0.769	-0.873	42.991	0.006	0.006	0.000	0.000	0.000	0.000
131	A	150	LYS	1	0.891	0.962	40.941	0.012	0.012	0.000	0.000	0.000	0.000
132	A	151	VAL	0	-0.025	-0.022	38.422	0.000	0.000	0.000	0.000	0.000	0.000
133	A	152	ILE	0	0.039	0.017	38.711	0.002	0.002	0.000	0.000	0.000	0.000
134	A	153	LYS	1	0.855	0.909	38.820	-0.010	-0.010	0.000	0.000	0.000	0.000
135	A	154	PHE	0	-0.105	-0.056	35.121	0.003	0.003	0.000	0.000	0.000	0.000
136	A	155	LEU	0	-0.033	-0.010	33.386	0.001	0.001	0.000	0.000	0.000	0.000
137	A	156	GLU	-1	-0.824	-0.893	34.103	0.038	0.038	0.000	0.000	0.000	0.000
138	A	157	GLU	-1	-0.922	-0.933	33.863	0.017	0.017	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:20:HIS)