FMO DATABASE

FMODB ID: K9YJ3

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1128204.236699
FMO2-HF: Nuclear repulsion	1074499.510982
FMO2-HF: Total energy	-53704.725718
FMO2-MP2: Total energy	-53863.614614

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.
-24.037	-15.521	13.125	-8.299	-13.343	-0.018

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 : 0.016 / q_NPA : 0.006

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	0.008	2.128	-7.804	-3.183	9.111	-5.189	-8.543	-0.027
4	A	23	TYR	0	-0.009	0.002	4.275	-0.062	0.502	0.004	-0.009	-0.559	0.000
5	A	24	VAL	0	0.029	0.012	7.095	-0.132	-0.132	0.000	0.000	0.000	0.000
6	A	25	GLU	-1	-0.781	-0.877	8.713	-1.085	-1.085	0.000	0.000	0.000	0.000
7	A	26	GLU	-1	-0.753	-0.886	10.141	-0.190	-0.190	0.000	0.000	0.000	0.000
8	A	27	LYS	1	0.752	0.867	3.782	0.987	1.146	0.000	-0.026	-0.134	0.000
9	A	28	LYS	1	0.807	0.893	10.398	1.219	1.219	0.000	0.000	0.000	0.000
10	A	29	GLU	-1	-0.932	-0.960	13.447	-0.098	-0.098	0.000	0.000	0.000	0.000
11	A	30	ILE	0	-0.030	-0.016	11.399	0.055	0.055	0.000	0.000	0.000	0.000
12	A	31	ASP	-1	-0.784	-0.874	12.426	-0.558	-0.558	0.000	0.000	0.000	0.000
13	A	32	SER	0	-0.031	-0.017	15.415	0.018	0.018	0.000	0.000	0.000	0.000
14	A	33	LEU	0	-0.028	-0.001	18.131	0.027	0.027	0.000	0.000	0.000	0.000
15	A	34	MET	0	-0.013	-0.003	16.896	0.050	0.050	0.000	0.000	0.000	0.000
16	A	35	GLU	-1	-0.900	-0.956	18.993	-0.258	-0.258	0.000	0.000	0.000	0.000
17	A	36	ASP	-1	-0.809	-0.885	21.248	-0.105	-0.105	0.000	0.000	0.000	0.000
18	A	37	VAL	0	-0.017	-0.012	21.876	0.024	0.024	0.000	0.000	0.000	0.000
19	A	38	LEU	0	0.019	-0.002	20.426	0.023	0.023	0.000	0.000	0.000	0.000
20	A	39	ALA	0	-0.026	0.001	24.295	0.007	0.007	0.000	0.000	0.000	0.000
21	A	40	LEU	0	-0.069	-0.008	26.462	0.007	0.007	0.000	0.000	0.000	0.000
22	A	41	VAL	0	0.024	0.011	29.062	0.002	0.002	0.000	0.000	0.000	0.000
23	A	42	ASN	0	0.046	0.005	32.420	0.007	0.007	0.000	0.000	0.000	0.000
24	A	43	ASP	-1	-0.862	-0.920	35.489	-0.044	-0.044	0.000	0.000	0.000	0.000
25	A	44	SER	0	-0.013	0.005	32.620	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	45	SER	0	0.028	0.010	34.741	0.010	0.010	0.000	0.000	0.000	0.000
27	A	46	GLY	0	0.074	0.020	34.151	0.001	0.001	0.000	0.000	0.000	0.000
28	A	47	GLY	0	-0.013	-0.009	33.573	0.007	0.007	0.000	0.000	0.000	0.000
29	A	48	LYS	1	0.871	0.944	28.229	0.093	0.093	0.000	0.000	0.000	0.000
30	A	49	PHE	0	0.046	0.022	29.049	0.001	0.001	0.000	0.000	0.000	0.000
31	A	50	LYS	1	0.795	0.879	28.879	-0.041	-0.041	0.000	0.000	0.000	0.000
32	A	51	ASP	-1	-0.797	-0.884	27.695	-0.034	-0.034	0.000	0.000	0.000	0.000
33	A	52	TYR	0	-0.005	-0.030	24.530	0.008	0.008	0.000	0.000	0.000	0.000
34	A	53	LYS	1	0.891	0.962	24.306	-0.059	-0.059	0.000	0.000	0.000	0.000
35	A	54	ASP	-1	-0.828	-0.898	25.256	0.085	0.085	0.000	0.000	0.000	0.000
36	A	55	LYS	1	0.895	0.928	22.425	0.076	0.076	0.000	0.000	0.000	0.000
37	A	56	ILE	0	0.001	0.007	19.908	0.017	0.017	0.000	0.000	0.000	0.000
38	A	57	ASN	0	-0.090	-0.057	20.103	0.077	0.077	0.000	0.000	0.000	0.000
39	A	58	GLU	-1	-0.928	-0.953	21.519	0.072	0.072	0.000	0.000	0.000	0.000
40	A	59	LEU	0	0.028	0.013	16.016	0.033	0.033	0.000	0.000	0.000	0.000
41	A	60	LYS	1	0.870	0.930	16.833	-0.290	-0.290	0.000	0.000	0.000	0.000
42	A	61	GLU	-1	-0.844	-0.910	17.687	0.427	0.427	0.000	0.000	0.000	0.000
43	A	62	ASN	0	-0.064	-0.052	17.734	0.044	0.044	0.000	0.000	0.000	0.000
44	A	63	LEU	0	0.005	0.006	12.459	0.032	0.032	0.000	0.000	0.000	0.000
45	A	64	LYS	1	0.784	0.898	12.932	-0.199	-0.199	0.000	0.000	0.000	0.000
46	A	65	ASP	-1	-0.910	-0.955	13.833	0.835	0.835	0.000	0.000	0.000	0.000
47	A	66	ILE	0	-0.033	0.005	7.744	0.325	0.325	0.000	0.000	0.000	0.000
48	A	67	GLY	0	0.031	0.007	7.656	0.020	0.020	0.000	0.000	0.000	0.000
49	A	68	ASN	0	-0.052	-0.036	2.271	-9.093	-8.418	3.845	-1.749	-2.770	0.024
50	A	69	ALA	0	0.041	0.028	5.243	-2.028	-1.985	-0.001	-0.005	-0.037	0.000
51	A	70	GLU	-1	-0.740	-0.880	2.927	-3.569	-1.115	0.166	-1.321	-1.300	-0.015
52	A	71	LEU	0	0.013	0.008	6.494	-0.500	-0.500	0.000	0.000	0.000	0.000
53	A	72	LYS	1	0.860	0.924	8.393	-2.848	-2.848	0.000	0.000	0.000	0.000
54	A	73	GLU	-1	-0.908	-0.941	10.171	0.138	0.138	0.000	0.000	0.000	0.000
55	A	74	LYS	1	0.787	0.870	8.794	0.388	0.388	0.000	0.000	0.000	0.000
56	A	75	LEU	0	0.065	0.031	12.326	-0.082	-0.082	0.000	0.000	0.000	0.000
57	A	76	LEU	0	-0.062	-0.002	14.316	-0.063	-0.063	0.000	0.000	0.000	0.000
58	A	77	ASN	0	0.008	-0.015	14.196	-0.046	-0.046	0.000	0.000	0.000	0.000
59	A	78	LEU	0	0.039	0.033	16.402	-0.046	-0.046	0.000	0.000	0.000	0.000
60	A	79	GLN	0	-0.044	-0.039	17.481	-0.028	-0.028	0.000	0.000	0.000	0.000
61	A	80	ASN	0	-0.024	-0.014	19.114	-0.006	-0.006	0.000	0.000	0.000	0.000
62	A	81	SER	0	0.058	0.014	20.007	-0.026	-0.026	0.000	0.000	0.000	0.000
63	A	82	PHE	0	-0.014	-0.008	22.458	-0.020	-0.020	0.000	0.000	0.000	0.000
64	A	83	GLN	0	-0.004	-0.010	24.391	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	84	ASP	-1	-0.887	-0.931	24.692	0.079	0.079	0.000	0.000	0.000	0.000
66	A	85	LYS	1	0.761	0.878	26.302	0.041	0.041	0.000	0.000	0.000	0.000
67	A	86	LEU	0	-0.034	-0.010	28.450	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	87	ALA	0	0.018	0.007	30.194	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	88	ALA	0	-0.008	0.002	31.466	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	89	LYS	1	0.805	0.888	32.773	0.005	0.005	0.000	0.000	0.000	0.000
71	A	90	LEU	0	-0.026	-0.018	33.678	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	91	ALA	0	-0.013	-0.002	36.001	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	92	ALA	0	-0.002	0.001	37.295	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	93	LEU	0	-0.028	-0.014	37.551	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	94	LYS	1	0.830	0.896	38.627	-0.057	-0.057	0.000	0.000	0.000	0.000
76	A	95	ALA	0	-0.012	0.007	41.833	0.000	0.000	0.000	0.000	0.000	0.000
77	A	96	ALA	0	0.030	0.017	43.194	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	97	LYS	1	0.789	0.891	44.871	-0.028	-0.028	0.000	0.000	0.000	0.000
79	A	98	ASN	0	0.032	0.022	46.448	0.001	0.001	0.000	0.000	0.000	0.000
80	A	99	THR	0	-0.045	-0.031	47.388	0.000	0.000	0.000	0.000	0.000	0.000
81	A	100	ILE	0	-0.048	-0.028	47.581	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	101	GLU	-1	-0.888	-0.953	50.168	0.020	0.020	0.000	0.000	0.000	0.000
83	A	102	ASN	0	-0.048	-0.042	51.400	0.000	0.000	0.000	0.000	0.000	0.000
84	A	103	ILE	0	-0.057	-0.010	52.611	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	104	THR	0	0.052	-0.006	56.009	0.001	0.001	0.000	0.000	0.000	0.000
86	A	105	ASP	-1	-0.885	-0.909	59.773	0.001	0.001	0.000	0.000	0.000	0.000
87	A	106	LYS	1	0.831	0.920	55.707	-0.010	-0.010	0.000	0.000	0.000	0.000
88	A	107	ASP	-1	-0.794	-0.913	59.073	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	108	GLN	0	-0.005	0.013	61.192	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	109	ASP	-1	-0.815	-0.883	59.918	-0.020	-0.020	0.000	0.000	0.000	0.000
91	A	110	ILE	0	0.013	0.001	57.102	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	111	SER	0	-0.007	-0.007	56.177	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	112	LYS	1	0.853	0.943	55.244	0.010	0.010	0.000	0.000	0.000	0.000
94	A	113	ARG	1	0.846	0.882	53.758	0.021	0.021	0.000	0.000	0.000	0.000
95	A	114	LYS	1	0.863	0.948	48.376	0.008	0.008	0.000	0.000	0.000	0.000
96	A	115	ILE	0	0.035	0.010	50.471	0.000	0.000	0.000	0.000	0.000	0.000
97	A	116	TRP	0	-0.024	-0.016	49.694	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	117	SER	0	-0.034	-0.041	47.664	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	118	GLU	-1	-0.799	-0.883	45.968	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	119	ALA	0	0.044	0.017	44.689	0.001	0.001	0.000	0.000	0.000	0.000
101	A	120	LYS	1	0.929	0.976	43.784	0.041	0.041	0.000	0.000	0.000	0.000
102	A	121	LEU	0	-0.039	-0.021	41.673	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	122	VAL	0	-0.007	0.012	39.546	0.000	0.000	0.000	0.000	0.000	0.000
104	A	123	GLY	0	0.007	0.007	39.360	0.003	0.003	0.000	0.000	0.000	0.000
105	A	124	VAL	0	-0.090	-0.027	40.351	0.001	0.001	0.000	0.000	0.000	0.000
106	A	125	THR	0	-0.008	-0.007	43.730	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	126	VAL	0	0.007	0.014	46.813	0.002	0.002	0.000	0.000	0.000	0.000
108	A	127	PRO	0	-0.010	-0.005	50.510	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	128	LEU	0	0.062	0.012	53.691	0.002	0.002	0.000	0.000	0.000	0.000
110	A	129	LEU	0	-0.025	-0.019	55.385	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	130	GLY	0	0.027	-0.012	58.731	0.002	0.002	0.000	0.000	0.000	0.000
112	A	131	SER	0	0.015	0.025	60.609	0.001	0.001	0.000	0.000	0.000	0.000
113	A	132	ASN	0	0.019	-0.009	63.783	0.000	0.000	0.000	0.000	0.000	0.000
114	A	133	THR	0	-0.031	-0.009	64.613	0.001	0.001	0.000	0.000	0.000	0.000
115	A	134	SER	0	0.027	0.009	64.713	0.000	0.000	0.000	0.000	0.000	0.000
116	A	135	GLY	0	0.041	0.028	63.376	0.001	0.001	0.000	0.000	0.000	0.000
117	A	136	ASN	0	-0.039	-0.039	60.658	0.001	0.001	0.000	0.000	0.000	0.000
118	A	137	GLY	0	0.027	0.011	58.575	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	138	ASP	-1	-0.798	-0.905	57.179	0.005	0.005	0.000	0.000	0.000	0.000
120	A	139	LYS	1	0.911	0.976	56.937	0.006	0.006	0.000	0.000	0.000	0.000
121	A	140	MET	0	-0.078	-0.009	53.773	0.000	0.000	0.000	0.000	0.000	0.000
122	A	141	SER	0	-0.013	-0.008	52.873	0.001	0.001	0.000	0.000	0.000	0.000
123	A	142	LYS	1	0.856	0.912	52.067	-0.012	-0.012	0.000	0.000	0.000	0.000
124	A	143	ASN	0	-0.005	0.005	50.827	0.002	0.002	0.000	0.000	0.000	0.000
125	A	144	ALA	0	0.051	0.013	48.639	0.000	0.000	0.000	0.000	0.000	0.000
126	A	145	VAL	0	0.003	0.008	47.369	0.001	0.001	0.000	0.000	0.000	0.000
127	A	146	GLU	-1	-0.801	-0.887	47.319	0.016	0.016	0.000	0.000	0.000	0.000
128	A	147	GLN	0	-0.092	-0.057	45.114	0.000	0.000	0.000	0.000	0.000	0.000
129	A	148	ILE	0	0.018	0.010	42.706	0.001	0.001	0.000	0.000	0.000	0.000
130	A	149	ASP	-1	-0.764	-0.868	42.433	0.030	0.030	0.000	0.000	0.000	0.000
131	A	150	LYS	1	0.792	0.903	39.899	-0.027	-0.027	0.000	0.000	0.000	0.000
132	A	151	VAL	0	-0.016	-0.017	38.109	0.003	0.003	0.000	0.000	0.000	0.000
133	A	152	ILE	0	0.038	0.011	38.239	0.004	0.004	0.000	0.000	0.000	0.000
134	A	153	LYS	1	0.870	0.915	38.093	-0.043	-0.043	0.000	0.000	0.000	0.000
135	A	154	PHE	0	-0.096	-0.039	34.703	0.006	0.006	0.000	0.000	0.000	0.000
136	A	155	LEU	0	-0.020	0.000	32.990	0.003	0.003	0.000	0.000	0.000	0.000
137	A	156	GLU	-1	-0.768	-0.878	33.495	0.074	0.074	0.000	0.000	0.000	0.000
138	A	157	GLU	-1	-0.836	-0.900	33.749	0.056	0.056	0.000	0.000	0.000	0.000

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