FMO DATABASE

FMODB ID: 522MZ

Calculation Name: 5HYC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5HYC

Chain ID: A

ChEMBL ID:

UniProt ID: G4NCW2

Base Structure: X-ray

Registration Date: 2023-06-21

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	130
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1009772.784546
FMO2-HF: Nuclear repulsion	959212.376922
FMO2-HF: Total energy	-50560.407624
FMO2-MP2: Total energy	-50706.57285

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:5:GLY)

Summations of interaction energy for fragment #1(A:5:GLY)

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.
-10.974	-7.265	6.597	-4.903	-5.401	-0.042

Interaction energy analysis for fragmet #1(A:5:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.022 / q_NPA : 0.001

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	7	SER	0	-0.061	-0.056	3.839	-0.849	-0.129	-0.006	-0.425	-0.289	0.001
4	A	8	PRO	0	-0.004	0.007	6.448	0.196	0.196	0.000	0.000	0.000	0.000
5	A	9	ILE	0	0.018	0.022	9.126	0.178	0.178	0.000	0.000	0.000	0.000
6	A	10	PRO	0	0.078	0.073	10.399	-0.046	-0.046	0.000	0.000	0.000	0.000
7	A	11	THR	0	0.074	0.021	9.694	0.032	0.032	0.000	0.000	0.000	0.000
8	A	12	ASN	0	-0.011	-0.014	12.225	0.047	0.047	0.000	0.000	0.000	0.000
9	A	13	ARG	1	0.839	0.915	15.119	0.154	0.154	0.000	0.000	0.000	0.000
10	A	14	LEU	0	0.027	0.013	10.516	0.021	0.021	0.000	0.000	0.000	0.000
11	A	15	LYS	1	0.957	0.975	15.057	-0.003	-0.003	0.000	0.000	0.000	0.000
12	A	16	GLN	0	-0.002	-0.004	17.326	0.016	0.016	0.000	0.000	0.000	0.000
13	A	17	ILE	0	0.013	0.023	16.368	0.003	0.003	0.000	0.000	0.000	0.000
14	A	18	ALA	0	-0.012	-0.016	17.256	0.008	0.008	0.000	0.000	0.000	0.000
15	A	19	ALA	0	-0.012	-0.005	19.279	0.009	0.009	0.000	0.000	0.000	0.000
16	A	20	ASP	-1	-0.902	-0.946	22.410	-0.048	-0.048	0.000	0.000	0.000	0.000
17	A	21	ALA	0	0.018	0.011	21.716	0.003	0.003	0.000	0.000	0.000	0.000
18	A	22	CYS	0	-0.080	-0.032	21.999	0.008	0.008	0.000	0.000	0.000	0.000
19	A	23	ASN	0	-0.007	-0.010	24.864	0.008	0.008	0.000	0.000	0.000	0.000
20	A	24	ASP	-1	-0.891	-0.940	26.771	-0.046	-0.046	0.000	0.000	0.000	0.000
21	A	25	ALA	0	-0.069	-0.014	27.087	0.001	0.001	0.000	0.000	0.000	0.000
22	A	26	ILE	0	-0.020	-0.029	27.894	0.003	0.003	0.000	0.000	0.000	0.000
23	A	27	GLY	0	0.040	0.038	30.566	0.004	0.004	0.000	0.000	0.000	0.000
24	A	28	SER	0	-0.062	-0.038	31.806	0.002	0.002	0.000	0.000	0.000	0.000
25	A	29	ALA	0	-0.045	-0.012	33.755	0.001	0.001	0.000	0.000	0.000	0.000
26	A	30	GLU	-1	-0.872	-0.934	35.585	0.000	0.000	0.000	0.000	0.000	0.000
27	A	31	PHE	0	-0.014	-0.001	36.722	0.002	0.002	0.000	0.000	0.000	0.000
28	A	32	TYR	0	-0.002	-0.012	30.662	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	33	ASP	-1	-0.834	-0.932	34.466	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	34	HIS	0	0.010	-0.005	34.014	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	35	ALA	0	-0.011	0.006	34.402	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	36	LYS	1	0.958	0.977	34.129	0.010	0.010	0.000	0.000	0.000	0.000
33	A	37	THR	0	-0.033	-0.009	29.702	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	38	GLU	-1	-0.927	-0.953	28.788	-0.028	-0.028	0.000	0.000	0.000	0.000
35	A	39	GLN	0	0.024	-0.004	28.692	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	40	TRP	0	0.004	0.005	28.415	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	41	ASN	0	0.088	0.037	24.634	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	42	HIS	0	-0.008	0.016	24.049	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	43	GLN	0	0.031	-0.005	24.643	-0.011	-0.011	0.000	0.000	0.000	0.000
40	A	44	ILE	0	0.033	0.039	21.120	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	45	ILE	0	-0.007	-0.010	19.570	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	46	ASN	0	-0.087	-0.060	20.222	-0.023	-0.023	0.000	0.000	0.000	0.000
43	A	47	THR	0	-0.010	-0.007	21.878	-0.014	-0.014	0.000	0.000	0.000	0.000
44	A	48	ILE	0	0.000	0.002	16.192	-0.012	-0.012	0.000	0.000	0.000	0.000
45	A	49	LEU	0	0.003	0.003	16.086	-0.029	-0.029	0.000	0.000	0.000	0.000
46	A	50	LYS	1	0.956	0.976	17.856	0.074	0.074	0.000	0.000	0.000	0.000
47	A	51	ALA	0	0.032	0.022	18.975	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	52	VAL	0	-0.003	-0.009	13.437	-0.015	-0.015	0.000	0.000	0.000	0.000
49	A	53	ILE	0	-0.014	-0.004	14.828	-0.048	-0.048	0.000	0.000	0.000	0.000
50	A	54	ALA	0	-0.025	-0.015	16.736	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	55	GLU	-1	-0.849	-0.908	15.868	-0.179	-0.179	0.000	0.000	0.000	0.000
52	A	56	SER	0	-0.041	-0.024	12.862	-0.068	-0.068	0.000	0.000	0.000	0.000
53	A	57	GLN	0	-0.025	-0.009	14.543	-0.035	-0.035	0.000	0.000	0.000	0.000
54	A	58	PRO	0	-0.009	0.011	16.016	0.020	0.020	0.000	0.000	0.000	0.000
55	A	59	SER	0	-0.018	-0.017	18.505	0.012	0.012	0.000	0.000	0.000	0.000
56	A	60	ASP	-1	-0.854	-0.907	21.467	-0.138	-0.138	0.000	0.000	0.000	0.000
57	A	61	SER	0	0.029	-0.001	21.664	-0.011	-0.011	0.000	0.000	0.000	0.000
58	A	62	THR	0	-0.130	-0.062	23.555	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	63	THR	0	-0.029	-0.003	17.397	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	64	PRO	0	-0.013	-0.009	18.900	0.000	0.000	0.000	0.000	0.000	0.000
61	A	65	PRO	0	-0.009	-0.032	16.797	-0.026	-0.026	0.000	0.000	0.000	0.000
62	A	66	GLN	0	0.044	0.036	12.221	-0.021	-0.021	0.000	0.000	0.000	0.000
63	A	67	PHE	0	-0.003	0.013	6.653	-0.078	-0.078	0.000	0.000	0.000	0.000
64	A	68	LYS	1	0.914	0.964	11.236	0.412	0.412	0.000	0.000	0.000	0.000
65	A	69	PHE	0	0.039	0.007	10.158	-0.078	-0.078	0.000	0.000	0.000	0.000
66	A	70	ALA	0	-0.014	0.002	12.462	0.043	0.043	0.000	0.000	0.000	0.000
67	A	71	VAL	0	0.020	0.004	13.489	0.003	0.003	0.000	0.000	0.000	0.000
68	A	72	ASN	0	-0.015	0.001	16.027	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	73	SER	0	0.013	-0.003	17.943	0.012	0.012	0.000	0.000	0.000	0.000
70	A	74	THR	0	-0.070	-0.032	20.678	0.003	0.003	0.000	0.000	0.000	0.000
71	A	75	ILE	0	0.038	0.018	23.189	0.003	0.003	0.000	0.000	0.000	0.000
72	A	76	VAL	0	-0.072	-0.036	25.660	0.000	0.000	0.000	0.000	0.000	0.000
73	A	77	GLN	0	0.006	0.005	28.410	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	78	HIS	0	-0.071	-0.045	29.865	0.003	0.003	0.000	0.000	0.000	0.000
75	A	79	LEU	0	-0.086	-0.048	33.253	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	80	VAL	0	0.042	0.029	36.051	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	81	PRO	0	0.047	0.029	39.414	0.001	0.001	0.000	0.000	0.000	0.000
78	A	82	SER	0	-0.007	-0.016	42.423	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	83	SER	0	0.010	-0.003	45.269	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	84	LYS	1	0.920	0.979	43.387	-0.016	-0.016	0.000	0.000	0.000	0.000
81	A	104	ASP	-1	-0.909	-0.954	44.624	0.016	0.016	0.000	0.000	0.000	0.000
82	A	105	GLY	0	-0.071	-0.034	44.239	0.002	0.002	0.000	0.000	0.000	0.000
83	A	106	LYS	1	0.874	0.918	39.456	-0.027	-0.027	0.000	0.000	0.000	0.000
84	A	107	PRO	0	0.089	0.052	36.962	0.001	0.001	0.000	0.000	0.000	0.000
85	A	108	HIS	0	-0.043	-0.024	34.654	0.004	0.004	0.000	0.000	0.000	0.000
86	A	109	VAL	0	0.025	0.030	31.573	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	110	GLY	0	-0.016	0.003	33.580	0.004	0.004	0.000	0.000	0.000	0.000
88	A	111	ARG	1	0.906	0.926	28.118	-0.052	-0.052	0.000	0.000	0.000	0.000
89	A	112	ARG	1	0.980	0.992	29.506	-0.033	-0.033	0.000	0.000	0.000	0.000
90	A	113	GLY	0	0.014	0.009	28.553	0.004	0.004	0.000	0.000	0.000	0.000
91	A	114	MET	0	-0.035	-0.030	23.393	-0.008	-0.008	0.000	0.000	0.000	0.000
92	A	115	HIS	0	0.001	0.000	18.934	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	116	SER	0	-0.001	0.009	18.743	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	117	ALA	0	0.006	-0.001	15.907	0.026	0.026	0.000	0.000	0.000	0.000
95	A	118	THR	0	0.022	-0.001	11.848	-0.049	-0.049	0.000	0.000	0.000	0.000
96	A	119	GLY	0	-0.002	0.013	11.924	0.086	0.086	0.000	0.000	0.000	0.000
97	A	120	ALA	0	-0.015	-0.014	8.766	-0.040	-0.040	0.000	0.000	0.000	0.000
98	A	121	PHE	0	-0.031	-0.007	10.707	0.017	0.017	0.000	0.000	0.000	0.000
99	A	122	TRP	0	0.022	0.006	5.523	-0.067	-0.067	0.000	0.000	0.000	0.000
100	A	123	ASN	0	-0.003	0.008	6.848	0.075	0.075	0.000	0.000	0.000	0.000
101	A	124	ASP	-1	-0.905	-0.966	3.986	-0.935	-0.460	0.000	-0.216	-0.259	-0.001
102	A	125	LYS	1	0.929	0.964	1.995	-6.431	-6.643	4.962	-2.283	-2.467	-0.026
103	A	126	THR	0	-0.039	-0.029	3.345	-0.131	0.800	0.080	-0.512	-0.498	-0.003
104	A	127	ASP	-1	-0.793	-0.887	3.591	-2.119	-1.807	0.022	-0.129	-0.204	-0.001
105	A	128	GLY	0	0.032	-0.005	2.489	-1.147	-0.038	1.538	-1.212	-1.436	-0.012
106	A	129	MET	0	-0.030	-0.017	4.216	-0.725	-0.624	0.000	-0.031	-0.070	0.000
107	A	130	TRP	0	0.003	0.009	7.601	0.174	0.174	0.000	0.000	0.000	0.000
108	A	131	THR	0	-0.046	-0.032	10.094	-0.024	-0.024	0.000	0.000	0.000	0.000
109	A	132	TYR	0	-0.043	-0.048	13.763	0.003	0.003	0.000	0.000	0.000	0.000
110	A	133	LYS	1	0.935	0.959	16.455	-0.157	-0.157	0.000	0.000	0.000	0.000
111	A	134	HIS	0	0.046	0.043	20.567	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	135	GLU	-1	-0.985	-0.994	23.754	0.065	0.065	0.000	0.000	0.000	0.000
113	A	136	GLY	0	0.026	0.023	26.355	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	137	ASP	-1	-0.864	-0.924	29.944	0.021	0.021	0.000	0.000	0.000	0.000
115	A	138	GLU	-1	-0.876	-0.982	32.770	0.022	0.022	0.000	0.000	0.000	0.000
116	A	139	SER	0	-0.075	-0.037	35.801	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	140	LYS	1	0.812	0.901	31.506	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	141	GLY	0	0.057	0.025	34.181	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	142	MET	0	-0.075	-0.046	30.138	0.000	0.000	0.000	0.000	0.000	0.000
120	A	143	ASP	-1	-0.755	-0.821	25.734	0.041	0.041	0.000	0.000	0.000	0.000
121	A	144	VAL	0	0.008	0.002	22.326	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	145	VAL	0	-0.042	-0.014	18.472	0.009	0.009	0.000	0.000	0.000	0.000
123	A	146	VAL	0	0.021	0.007	15.975	-0.011	-0.011	0.000	0.000	0.000	0.000
124	A	147	MET	0	-0.034	-0.011	12.472	0.044	0.044	0.000	0.000	0.000	0.000
125	A	148	LEU	0	-0.003	0.007	10.320	-0.030	-0.030	0.000	0.000	0.000	0.000
126	A	149	ILE	0	0.009	-0.007	8.584	0.076	0.076	0.000	0.000	0.000	0.000
127	A	150	TRP	0	0.006	0.013	3.364	0.864	1.137	0.001	-0.095	-0.178	0.000
128	A	151	ILE	0	-0.025	-0.014	6.616	-0.182	-0.182	0.000	0.000	0.000	0.000
129	A	152	ALA	0	0.028	0.015	7.236	0.138	0.138	0.000	0.000	0.000	0.000
130	A	153	VAL	0	-0.067	-0.036	8.836	0.154	0.154	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:GLY)