FMO DATABASE

FMODB ID: 22YLR

Calculation Name: 4JHY-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4JHY

Chain ID: A

ChEMBL ID:

UniProt ID: A6LHZ0

Base Structure: X-ray

Registration Date: 2023-06-20

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	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	155
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1514180.173891
FMO2-HF: Nuclear repulsion	1451519.193551
FMO2-HF: Total energy	-62660.98034
FMO2-MP2: Total energy	-62842.612576

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:27:GLU)

Summations of interaction energy for fragment #1(A:27:GLU)

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.
48.886	43.97	18.793	-7.902	-5.976	-0.011

Interaction energy analysis for fragmet #1(A:27:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.974 / q_NPA : -0.991

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	29	ALA	0	0.017	0.002	3.786	-8.557	-6.035	-0.018	-1.233	-1.271	0.004
4	A	30	PRO	0	0.008	0.038	4.703	-0.045	0.198	-0.001	-0.041	-0.201	0.000
5	A	31	MET	0	0.008	-0.017	6.139	-3.300	-3.300	0.000	0.000	0.000	0.000
6	A	32	LYS	1	0.791	0.850	9.286	-18.037	-18.037	0.000	0.000	0.000	0.000
7	A	33	ASN	0	-0.051	-0.041	12.537	-0.553	-0.553	0.000	0.000	0.000	0.000
8	A	34	GLY	0	0.011	0.004	14.289	-0.724	-0.724	0.000	0.000	0.000	0.000
9	A	35	LYS	1	0.838	0.911	13.901	-15.888	-15.888	0.000	0.000	0.000	0.000
10	A	36	VAL	0	0.011	0.006	9.041	0.855	0.855	0.000	0.000	0.000	0.000
11	A	37	CYM	-1	-0.880	-0.871	10.160	16.609	16.609	0.000	0.000	0.000	0.000
12	A	38	TYR	0	-0.005	0.009	6.912	0.529	0.529	0.000	0.000	0.000	0.000
13	A	39	SER	0	-0.005	-0.035	9.777	-1.866	-1.866	0.000	0.000	0.000	0.000
14	A	40	ASP	-1	-0.851	-0.918	10.670	21.740	21.740	0.000	0.000	0.000	0.000
15	A	41	ASP	-1	-0.892	-0.924	13.204	13.782	13.782	0.000	0.000	0.000	0.000
16	A	42	VAL	0	0.019	0.025	16.202	0.409	0.409	0.000	0.000	0.000	0.000
17	A	43	GLU	-1	-0.916	-0.964	18.403	11.582	11.582	0.000	0.000	0.000	0.000
18	A	44	ILE	0	-0.055	-0.046	21.682	0.230	0.230	0.000	0.000	0.000	0.000
19	A	45	GLU	-1	-0.900	-0.964	24.498	10.930	10.930	0.000	0.000	0.000	0.000
20	A	46	ASN	0	-0.055	-0.017	27.313	-0.382	-0.382	0.000	0.000	0.000	0.000
21	A	47	THR	0	0.034	0.029	28.095	-0.315	-0.315	0.000	0.000	0.000	0.000
22	A	48	SER	0	0.009	0.006	29.307	0.184	0.184	0.000	0.000	0.000	0.000
23	A	49	LYS	1	0.921	0.950	28.839	-9.723	-9.723	0.000	0.000	0.000	0.000
24	A	50	LEU	0	-0.077	-0.040	29.589	0.156	0.156	0.000	0.000	0.000	0.000
25	A	51	GLU	-1	-0.858	-0.932	31.359	9.051	9.051	0.000	0.000	0.000	0.000
26	A	52	ILE	0	0.048	0.032	24.837	0.174	0.174	0.000	0.000	0.000	0.000
27	A	53	PHE	0	-0.033	-0.027	26.955	0.096	0.096	0.000	0.000	0.000	0.000
28	A	54	ASN	0	-0.074	-0.054	28.323	0.102	0.102	0.000	0.000	0.000	0.000
29	A	55	ALA	0	0.030	0.038	27.319	-0.077	-0.077	0.000	0.000	0.000	0.000
30	A	56	ILE	0	0.082	0.044	22.110	0.093	0.093	0.000	0.000	0.000	0.000
31	A	57	ASN	0	-0.030	-0.025	25.525	0.058	0.058	0.000	0.000	0.000	0.000
32	A	58	ALA	0	-0.057	-0.025	28.131	-0.158	-0.158	0.000	0.000	0.000	0.000
33	A	59	TRP	0	0.091	0.052	20.143	-0.427	-0.427	0.000	0.000	0.000	0.000
34	A	60	ALA	0	0.039	0.029	24.801	0.062	0.062	0.000	0.000	0.000	0.000
35	A	61	LYS	1	0.899	0.942	25.961	-9.453	-9.453	0.000	0.000	0.000	0.000
36	A	62	LYS	1	0.906	0.954	27.473	-11.052	-11.052	0.000	0.000	0.000	0.000
37	A	63	SER	0	-0.028	-0.023	24.228	-0.098	-0.098	0.000	0.000	0.000	0.000
38	A	64	TYR	0	0.009	0.010	20.418	0.111	0.111	0.000	0.000	0.000	0.000
39	A	65	GLY	0	-0.011	0.005	27.236	-0.156	-0.156	0.000	0.000	0.000	0.000
40	A	66	LYS	1	0.896	0.932	30.957	-8.661	-8.661	0.000	0.000	0.000	0.000
41	A	67	ASP	-1	-0.795	-0.854	27.253	10.653	10.653	0.000	0.000	0.000	0.000
42	A	68	VAL	0	-0.012	-0.016	30.055	0.130	0.130	0.000	0.000	0.000	0.000
43	A	69	PHE	0	-0.028	-0.019	32.294	-0.057	-0.057	0.000	0.000	0.000	0.000
44	A	70	LEU	0	-0.063	-0.030	26.987	0.046	0.046	0.000	0.000	0.000	0.000
45	A	71	SER	0	0.011	-0.005	25.822	0.691	0.691	0.000	0.000	0.000	0.000
46	A	72	ASN	0	-0.101	-0.042	26.564	-0.690	-0.690	0.000	0.000	0.000	0.000
47	A	73	VAL	0	0.064	0.029	26.385	0.430	0.430	0.000	0.000	0.000	0.000
48	A	74	ASN	0	-0.069	-0.028	27.590	-0.360	-0.360	0.000	0.000	0.000	0.000
49	A	75	SER	0	0.030	-0.005	28.065	0.374	0.374	0.000	0.000	0.000	0.000
50	A	76	ASN	0	-0.060	-0.025	29.505	-0.522	-0.522	0.000	0.000	0.000	0.000
51	A	77	LYS	1	1.051	1.004	30.773	-8.140	-8.140	0.000	0.000	0.000	0.000
52	A	78	ASN	0	-0.052	-0.012	33.059	-0.027	-0.027	0.000	0.000	0.000	0.000
53	A	79	LYS	1	0.988	0.984	29.387	-9.426	-9.426	0.000	0.000	0.000	0.000
54	A	80	GLY	0	0.022	0.025	28.975	0.200	0.200	0.000	0.000	0.000	0.000
55	A	81	THR	0	0.001	0.004	25.202	0.231	0.231	0.000	0.000	0.000	0.000
56	A	82	ILE	0	0.003	0.007	24.278	-0.523	-0.523	0.000	0.000	0.000	0.000
57	A	83	PHE	0	-0.050	-0.019	23.502	0.471	0.471	0.000	0.000	0.000	0.000
58	A	84	VAL	0	0.023	0.012	21.860	-0.537	-0.537	0.000	0.000	0.000	0.000
59	A	85	SER	0	-0.066	-0.029	22.214	0.318	0.318	0.000	0.000	0.000	0.000
60	A	86	SER	0	0.032	0.013	21.569	-0.347	-0.347	0.000	0.000	0.000	0.000
61	A	87	LYS	1	0.905	0.949	21.772	-10.856	-10.856	0.000	0.000	0.000	0.000
62	A	88	VAL	0	0.018	0.022	19.646	-0.485	-0.485	0.000	0.000	0.000	0.000
63	A	89	GLU	-1	-0.914	-0.971	20.907	12.511	12.511	0.000	0.000	0.000	0.000
64	A	90	LEU	0	0.008	0.000	13.874	0.007	0.007	0.000	0.000	0.000	0.000
65	A	91	LEU	0	0.034	-0.004	18.370	-0.181	-0.181	0.000	0.000	0.000	0.000
66	A	92	LEU	0	-0.070	-0.011	14.441	1.015	1.015	0.000	0.000	0.000	0.000
67	A	93	ASN	0	0.024	0.002	15.233	0.351	0.351	0.000	0.000	0.000	0.000
68	A	94	ASP	-1	-0.897	-0.929	17.732	15.310	15.310	0.000	0.000	0.000	0.000
69	A	95	THR	0	-0.086	-0.050	21.363	-0.731	-0.731	0.000	0.000	0.000	0.000
70	A	96	ASP	-1	-0.749	-0.845	18.960	13.994	13.994	0.000	0.000	0.000	0.000
71	A	97	LYS	1	0.883	0.928	19.101	-12.279	-12.279	0.000	0.000	0.000	0.000
72	A	98	THR	0	0.013	0.000	16.690	-0.544	-0.544	0.000	0.000	0.000	0.000
73	A	99	ILE	0	-0.051	-0.004	19.949	-0.059	-0.059	0.000	0.000	0.000	0.000
74	A	100	ILE	0	0.020	0.020	14.463	0.315	0.315	0.000	0.000	0.000	0.000
75	A	101	LYS	1	0.913	0.948	18.861	-12.688	-12.688	0.000	0.000	0.000	0.000
76	A	102	TYR	0	0.040	0.023	16.790	0.648	0.648	0.000	0.000	0.000	0.000
77	A	103	LYS	1	0.833	0.900	18.289	-13.297	-13.297	0.000	0.000	0.000	0.000
78	A	104	MET	0	0.051	0.030	17.320	0.905	0.905	0.000	0.000	0.000	0.000
79	A	105	ARG	1	0.782	0.877	18.613	-14.300	-14.300	0.000	0.000	0.000	0.000
80	A	106	ILE	0	0.053	0.031	19.221	0.487	0.487	0.000	0.000	0.000	0.000
81	A	107	THR	0	-0.048	-0.030	21.227	-0.903	-0.903	0.000	0.000	0.000	0.000
82	A	108	CYS	0	-0.012	0.018	22.623	0.395	0.395	0.000	0.000	0.000	0.000
83	A	109	PHE	0	-0.053	-0.047	22.439	-0.532	-0.532	0.000	0.000	0.000	0.000
84	A	110	ASP	-1	-0.836	-0.924	26.864	9.544	9.544	0.000	0.000	0.000	0.000
85	A	111	ASN	0	-0.018	-0.007	26.823	0.004	0.004	0.000	0.000	0.000	0.000
86	A	112	ARG	1	0.854	0.909	19.222	-13.375	-13.375	0.000	0.000	0.000	0.000
87	A	113	TYR	0	-0.022	-0.008	17.731	-0.762	-0.762	0.000	0.000	0.000	0.000
88	A	114	THR	0	0.034	0.027	17.917	0.368	0.368	0.000	0.000	0.000	0.000
89	A	115	ILE	0	0.013	-0.003	14.703	-0.930	-0.930	0.000	0.000	0.000	0.000
90	A	116	GLU	-1	-0.795	-0.870	14.338	16.193	16.193	0.000	0.000	0.000	0.000
91	A	117	ALA	0	0.032	0.014	13.445	-1.106	-1.106	0.000	0.000	0.000	0.000
92	A	118	SER	0	0.055	-0.006	13.274	0.751	0.751	0.000	0.000	0.000	0.000
93	A	119	ASP	-1	-0.912	-0.949	15.381	12.958	12.958	0.000	0.000	0.000	0.000
94	A	120	ILE	0	0.020	0.033	12.820	-0.731	-0.731	0.000	0.000	0.000	0.000
95	A	121	VAL	0	-0.047	-0.031	16.156	-0.130	-0.130	0.000	0.000	0.000	0.000
96	A	122	TYR	0	0.006	-0.005	12.514	-0.237	-0.237	0.000	0.000	0.000	0.000
97	A	123	GLN	0	-0.072	-0.039	18.952	-0.857	-0.857	0.000	0.000	0.000	0.000
98	A	124	TYR	0	0.010	-0.026	20.237	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	125	ASP	-1	-0.748	-0.878	22.371	10.665	10.665	0.000	0.000	0.000	0.000
100	A	126	PRO	0	0.019	0.019	22.716	0.087	0.087	0.000	0.000	0.000	0.000
101	A	127	LEU	0	-0.013	-0.001	23.868	0.020	0.020	0.000	0.000	0.000	0.000
102	A	128	ASN	0	-0.088	-0.055	22.587	-0.109	-0.109	0.000	0.000	0.000	0.000
103	A	129	ASP	-1	-0.789	-0.885	26.425	9.175	9.175	0.000	0.000	0.000	0.000
104	A	130	LYS	1	0.862	0.934	27.280	-11.428	-11.428	0.000	0.000	0.000	0.000
105	A	131	LYS	1	0.780	0.885	29.148	-9.580	-9.580	0.000	0.000	0.000	0.000
106	A	132	TYR	0	-0.038	-0.014	24.451	-0.017	-0.017	0.000	0.000	0.000	0.000
107	A	133	LYS	1	0.932	0.974	24.289	-10.699	-10.699	0.000	0.000	0.000	0.000
108	A	134	THR	0	-0.016	-0.019	22.491	0.352	0.352	0.000	0.000	0.000	0.000
109	A	135	TYR	0	0.034	0.023	18.397	-0.383	-0.383	0.000	0.000	0.000	0.000
110	A	136	LYS	1	0.874	0.920	17.682	-14.016	-14.016	0.000	0.000	0.000	0.000
111	A	137	ALA	0	0.066	0.032	12.526	0.227	0.227	0.000	0.000	0.000	0.000
112	A	138	GLU	-1	-0.838	-0.918	12.510	18.567	18.567	0.000	0.000	0.000	0.000
113	A	139	ASP	-1	-0.859	-0.902	13.401	15.163	15.163	0.000	0.000	0.000	0.000
114	A	140	VAL	0	-0.015	0.000	13.113	-0.442	-0.442	0.000	0.000	0.000	0.000
115	A	141	ILE	0	0.024	-0.009	8.617	0.722	0.722	0.000	0.000	0.000	0.000
116	A	142	ALA	0	0.067	0.041	7.770	2.870	2.870	0.000	0.000	0.000	0.000
117	A	143	ASN	0	-0.059	-0.050	6.231	0.952	0.952	0.000	0.000	0.000	0.000
118	A	144	ASN	0	0.068	0.028	1.832	-2.233	-10.222	18.814	-6.592	-4.233	-0.015
119	A	145	GLY	0	0.035	0.009	5.082	0.673	0.764	-0.001	-0.007	-0.083	0.000
120	A	146	ASP	-1	-0.872	-0.918	7.775	29.004	29.004	0.000	0.000	0.000	0.000
121	A	147	SER	0	-0.065	-0.027	9.840	-1.762	-1.762	0.000	0.000	0.000	0.000
122	A	148	ASN	0	0.033	0.027	11.870	-1.055	-1.055	0.000	0.000	0.000	0.000
123	A	149	THR	0	-0.056	-0.038	13.824	-1.004	-1.004	0.000	0.000	0.000	0.000
124	A	150	ILE	0	-0.039	-0.017	17.048	-1.092	-1.092	0.000	0.000	0.000	0.000
125	A	151	ALA	0	0.021	0.008	18.858	0.299	0.299	0.000	0.000	0.000	0.000
126	A	152	LEU	0	-0.044	-0.021	20.937	0.014	0.014	0.000	0.000	0.000	0.000
127	A	153	ILE	0	-0.032	-0.005	15.899	-0.216	-0.216	0.000	0.000	0.000	0.000
128	A	154	LYS	1	0.833	0.904	17.713	-14.937	-14.937	0.000	0.000	0.000	0.000
129	A	155	ASP	-1	-0.824	-0.914	15.052	17.572	17.572	0.000	0.000	0.000	0.000
130	A	156	PRO	0	0.040	0.024	11.877	0.716	0.716	0.000	0.000	0.000	0.000
131	A	157	LYS	1	0.844	0.890	7.397	-33.233	-33.233	0.000	0.000	0.000	0.000
132	A	158	LEU	0	0.008	0.018	8.938	2.018	2.018	0.000	0.000	0.000	0.000
133	A	159	PHE	0	0.031	0.015	11.497	0.042	0.042	0.000	0.000	0.000	0.000
134	A	161	ASN	0	0.032	0.002	5.843	3.725	3.725	0.000	0.000	0.000	0.000
135	A	162	ALA	0	0.038	0.022	7.883	-0.022	-0.022	0.000	0.000	0.000	0.000
136	A	163	THR	0	-0.019	-0.018	10.048	-1.999	-1.999	0.000	0.000	0.000	0.000
137	A	164	PHE	0	0.025	0.018	4.791	-0.624	-0.407	-0.001	-0.029	-0.188	0.000
138	A	165	PHE	0	0.024	0.007	7.543	-0.535	-0.535	0.000	0.000	0.000	0.000
139	A	166	PHE	0	-0.016	-0.002	9.870	-1.680	-1.680	0.000	0.000	0.000	0.000
140	A	167	VAL	0	-0.012	-0.016	10.948	-1.339	-1.339	0.000	0.000	0.000	0.000
141	A	168	GLU	-1	-0.855	-0.935	7.640	25.573	25.573	0.000	0.000	0.000	0.000
142	A	169	ASN	0	-0.036	-0.021	11.016	-1.152	-1.152	0.000	0.000	0.000	0.000
143	A	170	LEU	0	-0.034	-0.001	13.872	-1.389	-1.389	0.000	0.000	0.000	0.000
144	A	171	PHE	0	-0.037	-0.036	11.004	-1.533	-1.533	0.000	0.000	0.000	0.000
145	A	172	ALA	0	0.040	0.023	14.408	-0.739	-0.739	0.000	0.000	0.000	0.000
146	A	173	ASP	-1	-0.885	-0.939	16.142	14.303	14.303	0.000	0.000	0.000	0.000
147	A	174	VAL	0	-0.110	-0.062	18.324	-0.942	-0.942	0.000	0.000	0.000	0.000
148	A	175	PHE	0	-0.015	-0.002	17.610	-0.670	-0.670	0.000	0.000	0.000	0.000
149	A	176	ASP	-1	-0.846	-0.920	19.672	14.064	14.064	0.000	0.000	0.000	0.000
150	A	177	ALA	0	-0.086	-0.049	22.137	-0.760	-0.760	0.000	0.000	0.000	0.000
151	A	178	ALA	0	-0.041	-0.034	22.424	-0.641	-0.641	0.000	0.000	0.000	0.000
152	A	179	GLN	0	-0.004	-0.001	22.743	-0.491	-0.491	0.000	0.000	0.000	0.000
153	A	180	ASN	0	-0.116	-0.055	25.439	-0.653	-0.653	0.000	0.000	0.000	0.000
154	A	181	ALA	0	-0.067	-0.017	27.948	-0.414	-0.414	0.000	0.000	0.000	0.000
155	A	182	GLU	-1	-0.962	-0.976	29.827	8.914	8.914	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:27:GLU)