FMO DATABASE

FMODB ID: K3R23

Calculation Name: 4JHY-A-Xray322

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: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	157
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1521369.362008
FMO2-HF: Nuclear repulsion	1458538.415933
FMO2-HF: Total energy	-62830.946074
FMO2-MP2: Total energy	-63013.126143

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:26:ACE )

Summations of interaction energy for fragment #1(A:26:ACE )

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.
3.13	2.074	5.913	-2.725	-2.133	-0.016

Interaction energy analysis for fragmet #1(A:26:ACE )

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 : -0.026

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	160	CYS	0	-0.070	-0.002	3.854	1.552	2.216	-0.005	-0.297	-0.362	0.000
4	A	29	ALA	0	0.016	0.011	4.708	0.292	0.360	0.000	-0.007	-0.061	0.000
5	A	30	PRO	0	0.004	0.036	5.204	0.497	0.497	0.000	0.000	0.000	0.000
6	A	31	MET	0	0.020	-0.011	6.072	0.045	0.045	0.000	0.000	0.000	0.000
7	A	32	LYS	1	0.881	0.906	8.290	0.009	0.009	0.000	0.000	0.000	0.000
8	A	33	ASN	0	-0.065	-0.039	11.436	-0.024	-0.024	0.000	0.000	0.000	0.000
9	A	34	GLY	0	0.015	0.006	12.706	-0.032	-0.032	0.000	0.000	0.000	0.000
10	A	35	LYS	1	0.850	0.919	12.874	-0.105	-0.105	0.000	0.000	0.000	0.000
11	A	36	VAL	0	0.017	0.013	9.292	0.044	0.044	0.000	0.000	0.000	0.000
12	A	37	CYM	-1	-0.915	-0.909	10.045	-0.017	-0.017	0.000	0.000	0.000	0.000
13	A	38	TYR	0	-0.004	-0.001	9.146	0.057	0.057	0.000	0.000	0.000	0.000
14	A	39	SER	0	-0.041	-0.049	11.758	0.070	0.070	0.000	0.000	0.000	0.000
15	A	40	ASP	-1	-0.795	-0.895	13.342	-0.318	-0.318	0.000	0.000	0.000	0.000
16	A	41	ASP	-1	-0.916	-0.929	15.990	-0.039	-0.039	0.000	0.000	0.000	0.000
17	A	42	VAL	0	0.040	0.031	18.754	-0.014	-0.014	0.000	0.000	0.000	0.000
18	A	43	GLU	-1	-0.910	-0.964	21.307	-0.059	-0.059	0.000	0.000	0.000	0.000
19	A	44	ILE	0	-0.056	-0.046	24.417	-0.008	-0.008	0.000	0.000	0.000	0.000
20	A	45	GLU	-1	-0.912	-0.967	27.576	-0.073	-0.073	0.000	0.000	0.000	0.000
21	A	46	ASN	0	-0.067	-0.018	30.175	0.005	0.005	0.000	0.000	0.000	0.000
22	A	47	THR	0	0.051	0.026	31.208	0.002	0.002	0.000	0.000	0.000	0.000
23	A	48	SER	0	-0.002	0.002	32.141	0.001	0.001	0.000	0.000	0.000	0.000
24	A	49	LYS	1	1.005	0.986	31.338	0.024	0.024	0.000	0.000	0.000	0.000
25	A	50	LEU	0	-0.087	-0.043	32.381	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	51	GLU	-1	-0.869	-0.937	34.565	-0.048	-0.048	0.000	0.000	0.000	0.000
27	A	52	ILE	0	0.057	0.037	27.810	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	53	PHE	0	-0.043	-0.031	30.104	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	54	ASN	0	-0.061	-0.052	31.198	0.000	0.000	0.000	0.000	0.000	0.000
30	A	55	ALA	0	0.037	0.045	30.603	0.001	0.001	0.000	0.000	0.000	0.000
31	A	56	ILE	0	0.077	0.042	25.142	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	57	ASN	0	-0.013	-0.009	28.724	0.001	0.001	0.000	0.000	0.000	0.000
33	A	58	ALA	0	-0.047	-0.021	31.047	0.003	0.003	0.000	0.000	0.000	0.000
34	A	59	TRP	0	0.091	0.053	23.316	0.008	0.008	0.000	0.000	0.000	0.000
35	A	60	ALA	0	0.047	0.029	27.594	0.000	0.000	0.000	0.000	0.000	0.000
36	A	61	LYS	1	0.892	0.936	28.837	0.045	0.045	0.000	0.000	0.000	0.000
37	A	62	LYS	1	0.909	0.954	31.780	0.077	0.077	0.000	0.000	0.000	0.000
38	A	63	SER	0	-0.026	-0.017	27.506	0.000	0.000	0.000	0.000	0.000	0.000
39	A	64	TYR	0	0.013	0.019	23.307	0.001	0.001	0.000	0.000	0.000	0.000
40	A	65	GLY	0	-0.017	-0.002	29.828	0.005	0.005	0.000	0.000	0.000	0.000
41	A	66	LYS	1	0.891	0.929	33.397	0.038	0.038	0.000	0.000	0.000	0.000
42	A	67	ASP	-1	-0.797	-0.872	29.573	-0.046	-0.046	0.000	0.000	0.000	0.000
43	A	68	VAL	0	-0.009	-0.015	32.106	0.001	0.001	0.000	0.000	0.000	0.000
44	A	69	PHE	0	-0.029	-0.019	34.015	0.003	0.003	0.000	0.000	0.000	0.000
45	A	70	LEU	0	-0.061	-0.027	28.884	0.004	0.004	0.000	0.000	0.000	0.000
46	A	71	SER	0	0.019	0.032	27.913	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	72	ASN	0	-0.089	-0.032	28.262	0.005	0.005	0.000	0.000	0.000	0.000
48	A	73	VAL	0	0.062	0.028	28.207	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	74	ASN	0	-0.075	-0.035	29.437	0.005	0.005	0.000	0.000	0.000	0.000
50	A	75	SER	0	0.021	-0.014	29.995	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	76	ASN	0	-0.065	-0.021	31.498	0.003	0.003	0.000	0.000	0.000	0.000
52	A	77	LYS	1	1.047	0.999	32.760	0.027	0.027	0.000	0.000	0.000	0.000
53	A	78	ASN	0	-0.036	-0.001	35.218	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	79	LYS	1	0.936	0.944	30.930	0.005	0.005	0.000	0.000	0.000	0.000
55	A	80	GLY	0	0.020	0.029	30.838	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	81	THR	0	0.003	0.003	27.100	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	82	ILE	0	0.003	0.003	26.679	0.004	0.004	0.000	0.000	0.000	0.000
58	A	83	PHE	0	-0.043	-0.014	24.997	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	84	VAL	0	0.029	0.015	23.907	0.003	0.003	0.000	0.000	0.000	0.000
60	A	85	SER	0	-0.071	-0.030	23.748	0.003	0.003	0.000	0.000	0.000	0.000
61	A	86	SER	0	0.034	-0.010	23.540	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	87	LYS	1	0.925	0.967	23.264	0.023	0.023	0.000	0.000	0.000	0.000
63	A	88	VAL	0	0.018	0.020	22.117	0.001	0.001	0.000	0.000	0.000	0.000
64	A	89	GLU	-1	-0.945	-0.978	22.994	-0.052	-0.052	0.000	0.000	0.000	0.000
65	A	90	LEU	0	-0.006	-0.007	16.459	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	91	LEU	0	0.043	-0.003	21.151	0.010	0.010	0.000	0.000	0.000	0.000
67	A	92	LEU	0	-0.071	-0.010	17.022	-0.017	-0.017	0.000	0.000	0.000	0.000
68	A	93	ASN	0	0.028	0.006	18.841	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	94	ASP	-1	-0.890	-0.929	21.394	-0.104	-0.104	0.000	0.000	0.000	0.000
70	A	95	THR	0	-0.064	-0.053	24.525	0.007	0.007	0.000	0.000	0.000	0.000
71	A	96	ASP	-1	-0.766	-0.845	21.612	-0.032	-0.032	0.000	0.000	0.000	0.000
72	A	97	LYS	1	0.922	0.971	21.843	0.035	0.035	0.000	0.000	0.000	0.000
73	A	98	THR	0	0.005	-0.006	18.429	0.021	0.021	0.000	0.000	0.000	0.000
74	A	99	ILE	0	-0.041	0.001	21.887	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	100	ILE	0	0.020	0.019	16.126	0.011	0.011	0.000	0.000	0.000	0.000
76	A	101	LYS	1	0.901	0.940	20.141	0.002	0.002	0.000	0.000	0.000	0.000
77	A	102	TYR	0	0.048	0.026	18.164	0.005	0.005	0.000	0.000	0.000	0.000
78	A	103	LYS	1	0.896	0.943	19.309	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	104	MET	0	0.049	0.028	19.124	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	105	ARG	1	0.780	0.884	20.341	0.017	0.017	0.000	0.000	0.000	0.000
81	A	106	ILE	0	0.045	0.029	21.172	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	107	THR	0	-0.060	-0.040	23.391	0.014	0.014	0.000	0.000	0.000	0.000
83	A	108	CYS	0	-0.009	0.019	24.949	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	109	PHE	0	-0.064	-0.046	24.647	0.012	0.012	0.000	0.000	0.000	0.000
85	A	110	ASP	-1	-0.834	-0.922	29.176	-0.040	-0.040	0.000	0.000	0.000	0.000
86	A	111	ASN	0	-0.027	-0.011	29.392	0.000	0.000	0.000	0.000	0.000	0.000
87	A	112	ARG	1	0.855	0.908	20.777	0.059	0.059	0.000	0.000	0.000	0.000
88	A	113	TYR	0	-0.020	-0.008	21.360	0.013	0.013	0.000	0.000	0.000	0.000
89	A	114	THR	0	0.021	0.022	19.942	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	115	ILE	0	0.013	-0.003	17.544	0.016	0.016	0.000	0.000	0.000	0.000
91	A	116	GLU	-1	-0.805	-0.891	16.131	-0.019	-0.019	0.000	0.000	0.000	0.000
92	A	117	ALA	0	0.019	0.015	15.227	0.009	0.009	0.000	0.000	0.000	0.000
93	A	118	SER	0	0.037	-0.013	14.348	0.008	0.008	0.000	0.000	0.000	0.000
94	A	119	ASP	-1	-0.973	-0.998	15.913	0.031	0.031	0.000	0.000	0.000	0.000
95	A	120	ILE	0	0.026	0.038	13.640	-0.007	-0.007	0.000	0.000	0.000	0.000
96	A	121	VAL	0	-0.041	-0.032	16.602	0.027	0.027	0.000	0.000	0.000	0.000
97	A	122	TYR	0	-0.008	-0.008	13.562	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	123	GLN	0	-0.083	-0.044	19.626	0.008	0.008	0.000	0.000	0.000	0.000
99	A	124	TYR	0	-0.017	-0.057	21.297	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	125	ASP	-1	-0.767	-0.894	23.408	0.005	0.005	0.000	0.000	0.000	0.000
101	A	126	PRO	0	0.024	0.024	24.085	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	127	LEU	0	-0.014	-0.006	25.373	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	128	ASN	0	-0.105	-0.062	24.936	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	129	ASP	-1	-0.863	-0.924	28.491	-0.014	-0.014	0.000	0.000	0.000	0.000
105	A	130	LYS	1	0.886	0.935	29.828	0.031	0.031	0.000	0.000	0.000	0.000
106	A	131	LYS	1	0.843	0.925	30.441	0.008	0.008	0.000	0.000	0.000	0.000
107	A	132	TYR	0	-0.014	-0.003	25.865	0.004	0.004	0.000	0.000	0.000	0.000
108	A	133	LYS	1	0.937	0.973	24.756	-0.022	-0.022	0.000	0.000	0.000	0.000
109	A	134	THR	0	-0.017	-0.020	22.381	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	135	TYR	0	0.023	0.014	18.501	0.011	0.011	0.000	0.000	0.000	0.000
111	A	136	LYS	1	0.977	0.990	16.984	-0.139	-0.139	0.000	0.000	0.000	0.000
112	A	137	ALA	0	0.076	0.035	12.661	0.012	0.012	0.000	0.000	0.000	0.000
113	A	138	GLU	-1	-0.868	-0.930	11.791	0.161	0.161	0.000	0.000	0.000	0.000
114	A	139	ASP	-1	-0.926	-0.949	12.574	0.227	0.227	0.000	0.000	0.000	0.000
115	A	140	VAL	0	-0.026	-0.010	13.567	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	141	ILE	0	0.012	-0.015	9.248	0.015	0.015	0.000	0.000	0.000	0.000
117	A	142	ALA	0	0.059	0.035	7.778	0.064	0.064	0.000	0.000	0.000	0.000
118	A	143	ASN	0	-0.046	-0.041	4.786	0.276	0.331	0.000	-0.006	-0.049	0.000
119	A	144	ASN	0	0.033	0.014	2.475	1.417	-0.426	5.918	-2.415	-1.661	-0.016
120	A	145	GLY	0	0.031	0.005	5.603	-0.220	-0.220	0.000	0.000	0.000	0.000
121	A	146	ASP	-1	-0.889	-0.930	7.540	0.290	0.290	0.000	0.000	0.000	0.000
122	A	147	SER	0	-0.083	-0.039	9.366	0.036	0.036	0.000	0.000	0.000	0.000
123	A	148	ASN	0	0.032	0.028	11.152	-0.028	-0.028	0.000	0.000	0.000	0.000
124	A	149	THR	0	-0.041	-0.026	13.640	-0.011	-0.011	0.000	0.000	0.000	0.000
125	A	150	ILE	0	-0.041	-0.018	16.868	-0.023	-0.023	0.000	0.000	0.000	0.000
126	A	151	ALA	0	0.020	0.005	19.049	-0.012	-0.012	0.000	0.000	0.000	0.000
127	A	152	LEU	0	-0.052	-0.023	21.071	-0.009	-0.009	0.000	0.000	0.000	0.000
128	A	153	ILE	0	-0.040	-0.007	16.742	-0.014	-0.014	0.000	0.000	0.000	0.000
129	A	154	LYS	1	0.846	0.921	18.382	0.038	0.038	0.000	0.000	0.000	0.000
130	A	155	ASP	-1	-0.820	-0.914	16.817	-0.033	-0.033	0.000	0.000	0.000	0.000
131	A	156	PRO	0	0.042	0.025	12.581	-0.028	-0.028	0.000	0.000	0.000	0.000
132	A	157	LYS	1	0.891	0.920	8.623	-0.048	-0.048	0.000	0.000	0.000	0.000
133	A	158	LEU	0	0.009	0.018	11.745	-0.083	-0.083	0.000	0.000	0.000	0.000
134	A	159	PHE	0	0.024	0.019	13.714	-0.026	-0.026	0.000	0.000	0.000	0.000
135	A	161	ASN	0	0.041	0.006	10.009	-0.194	-0.194	0.000	0.000	0.000	0.000
136	A	162	ALA	0	0.039	0.022	11.457	-0.026	-0.026	0.000	0.000	0.000	0.000
137	A	163	THR	0	-0.023	-0.012	11.869	0.034	0.034	0.000	0.000	0.000	0.000
138	A	164	PHE	0	0.023	0.019	8.602	-0.014	-0.014	0.000	0.000	0.000	0.000
139	A	165	PHE	0	0.013	0.002	11.284	0.005	0.005	0.000	0.000	0.000	0.000
140	A	166	PHE	0	-0.031	-0.011	14.429	0.038	0.038	0.000	0.000	0.000	0.000
141	A	167	VAL	0	-0.014	-0.021	13.596	0.030	0.030	0.000	0.000	0.000	0.000
142	A	168	GLU	-1	-0.885	-0.946	11.765	-0.452	-0.452	0.000	0.000	0.000	0.000
143	A	169	ASN	0	0.009	0.005	14.916	0.009	0.009	0.000	0.000	0.000	0.000
144	A	170	LEU	0	-0.038	0.002	18.169	0.032	0.032	0.000	0.000	0.000	0.000
145	A	171	PHE	0	-0.030	-0.034	13.959	0.040	0.040	0.000	0.000	0.000	0.000
146	A	172	ALA	0	0.035	0.022	18.742	0.016	0.016	0.000	0.000	0.000	0.000
147	A	173	ASP	-1	-0.885	-0.937	20.409	-0.135	-0.135	0.000	0.000	0.000	0.000
148	A	174	VAL	0	-0.121	-0.068	21.729	0.019	0.019	0.000	0.000	0.000	0.000
149	A	175	PHE	0	-0.011	-0.004	21.469	0.012	0.012	0.000	0.000	0.000	0.000
150	A	176	ASP	-1	-0.861	-0.924	23.493	-0.140	-0.140	0.000	0.000	0.000	0.000
151	A	177	ALA	0	-0.107	-0.061	26.337	0.013	0.013	0.000	0.000	0.000	0.000
152	A	178	ALA	0	-0.038	-0.035	26.159	0.011	0.011	0.000	0.000	0.000	0.000
153	A	179	GLN	0	-0.009	-0.005	26.671	0.005	0.005	0.000	0.000	0.000	0.000
154	A	180	ASN	0	-0.077	-0.027	29.271	0.004	0.004	0.000	0.000	0.000	0.000
155	A	181	ALA	0	-0.074	-0.020	31.651	0.006	0.006	0.000	0.000	0.000	0.000
156	A	182	GLU	-1	-0.939	-0.968	33.456	-0.057	-0.057	0.000	0.000	0.000	0.000
157	A	183	NME	0	-0.037	-0.013	35.835	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:26:ACE )