FMO DATABASE

FMODB ID: 392JL

Calculation Name: 4KYX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4KYX

Chain ID: A

ChEMBL ID:

UniProt ID: Q4ULX7

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	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	139
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1354121.170725
FMO2-HF: Nuclear repulsion	1297939.11516
FMO2-HF: Total energy	-56182.055565
FMO2-MP2: Total energy	-56348.471163

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:2:ILE)

Summations of interaction energy for fragment #1(A:2:ILE)

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.
1.632	-5.188	20.219	-3.652	-9.747	-0.015

Interaction energy analysis for fragmet #1(A:2:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.002 / q_NPA : -0.009

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	4	HIS	0	0.032	0.011	2.018	0.918	-6.094	20.208	-3.642	-9.554	-0.015
4	A	5	PRO	0	0.009	0.005	3.715	0.451	0.643	0.011	-0.010	-0.193	0.000
5	A	6	ARG	1	0.914	0.967	7.352	0.866	0.866	0.000	0.000	0.000	0.000
6	A	7	ILE	0	0.030	0.012	9.970	0.085	0.085	0.000	0.000	0.000	0.000
7	A	8	GLY	0	-0.015	0.000	13.467	0.010	0.010	0.000	0.000	0.000	0.000
8	A	9	ILE	0	0.023	0.008	16.459	0.001	0.001	0.000	0.000	0.000	0.000
9	A	10	GLY	0	-0.031	-0.006	20.078	0.013	0.013	0.000	0.000	0.000	0.000
10	A	11	ILE	0	-0.001	-0.007	22.845	0.003	0.003	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.055	-0.044	26.474	0.010	0.010	0.000	0.000	0.000	0.000
12	A	13	ILE	0	0.054	0.032	29.457	0.002	0.002	0.000	0.000	0.000	0.000
13	A	14	PHE	0	-0.048	-0.028	32.158	0.004	0.004	0.000	0.000	0.000	0.000
14	A	15	ASN	0	0.005	-0.002	35.663	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	16	ASN	0	0.031	-0.014	39.016	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.761	0.897	41.999	0.060	0.060	0.000	0.000	0.000	0.000
17	A	18	ASN	0	-0.045	-0.030	39.069	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.827	-0.889	38.084	-0.062	-0.062	0.000	0.000	0.000	0.000
19	A	20	ILE	0	0.014	-0.002	31.518	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.027	0.004	31.665	0.006	0.006	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.054	-0.031	29.052	-0.010	-0.010	0.000	0.000	0.000	0.000
22	A	23	GLY	0	0.059	0.021	29.151	0.009	0.009	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.899	0.959	28.659	0.036	0.036	0.000	0.000	0.000	0.000
24	A	25	ARG	1	1.011	1.005	21.557	0.143	0.143	0.000	0.000	0.000	0.000
25	A	26	ILE	0	0.006	0.002	27.884	0.001	0.001	0.000	0.000	0.000	0.000
26	A	27	SER	0	-0.022	-0.006	25.077	0.004	0.004	0.000	0.000	0.000	0.000
27	A	28	SER	0	0.058	0.012	24.647	0.002	0.002	0.000	0.000	0.000	0.000
28	A	29	HIS	0	-0.059	-0.023	24.114	0.005	0.005	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.028	0.022	28.448	0.000	0.000	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.915	-0.954	26.291	-0.019	-0.019	0.000	0.000	0.000	0.000
31	A	32	SER	0	-0.003	-0.009	28.461	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	33	SER	0	-0.051	-0.014	25.764	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	34	TYR	0	0.022	0.001	28.012	0.004	0.004	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.018	-0.007	24.084	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.004	0.009	24.235	0.011	0.011	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.039	0.022	25.252	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	38	GLY	0	-0.025	-0.019	22.577	-0.008	-0.008	0.000	0.000	0.000	0.000
38	A	39	GLY	0	-0.014	0.006	19.298	0.015	0.015	0.000	0.000	0.000	0.000
39	A	40	HIS	0	-0.056	0.005	14.124	-0.086	-0.086	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.051	0.025	15.875	0.022	0.022	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.990	-0.986	15.560	-0.327	-0.327	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.066	-0.057	13.908	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	44	GLY	0	-0.034	-0.026	16.245	0.034	0.034	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.731	-0.830	19.303	-0.243	-0.243	0.000	0.000	0.000	0.000
45	A	46	THR	0	0.002	0.010	20.458	-0.025	-0.025	0.000	0.000	0.000	0.000
46	A	47	PHE	0	0.015	-0.024	18.436	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.922	-0.965	22.736	-0.196	-0.196	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.885	-0.955	24.593	-0.184	-0.184	0.000	0.000	0.000	0.000
49	A	50	CYS	0	-0.034	0.027	21.097	0.004	0.004	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.022	-0.003	23.528	0.011	0.011	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.047	-0.033	25.558	0.012	0.012	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.853	0.923	20.666	0.238	0.238	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.791	-0.925	20.831	-0.247	-0.247	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.007	-0.011	25.571	0.013	0.013	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.013	0.027	28.757	0.012	0.012	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.900	-0.971	24.364	-0.150	-0.150	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.824	-0.900	24.154	-0.155	-0.155	0.000	0.000	0.000	0.000
58	A	59	THR	0	-0.081	-0.075	28.626	0.011	0.011	0.000	0.000	0.000	0.000
59	A	60	ASN	0	0.010	0.002	32.204	0.005	0.005	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.061	-0.014	33.462	0.004	0.004	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.050	0.015	33.221	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	63	ILE	0	-0.041	-0.018	29.328	0.004	0.004	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.897	-0.961	33.662	-0.091	-0.091	0.000	0.000	0.000	0.000
64	A	65	ASN	0	-0.053	-0.031	33.049	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.077	0.053	28.450	0.003	0.003	0.000	0.000	0.000	0.000
66	A	67	GLN	0	-0.082	-0.051	30.072	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.031	0.019	21.982	0.001	0.001	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.014	-0.012	26.219	0.014	0.014	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.017	-0.007	24.337	0.008	0.008	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.039	0.049	18.235	-0.014	-0.014	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.039	-0.025	18.752	0.022	0.022	0.000	0.000	0.000	0.000
72	A	73	ASN	0	0.040	0.020	13.371	-0.096	-0.096	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.838	-0.927	14.853	-0.243	-0.243	0.000	0.000	0.000	0.000
74	A	75	ILE	0	0.018	0.002	10.462	-0.072	-0.072	0.000	0.000	0.000	0.000
75	A	76	PHE	0	-0.032	-0.021	13.187	0.062	0.062	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.868	-0.941	13.455	-0.050	-0.050	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.897	0.973	14.101	0.042	0.042	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.880	-0.962	14.220	-0.049	-0.049	0.000	0.000	0.000	0.000
79	A	80	GLN	0	-0.045	-0.023	9.169	0.040	0.040	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.818	0.918	7.734	0.459	0.459	0.000	0.000	0.000	0.000
81	A	82	HIS	0	0.028	0.001	8.184	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	83	TYR	0	-0.055	-0.048	9.743	-0.171	-0.171	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.008	-0.002	12.138	0.063	0.063	0.000	0.000	0.000	0.000
84	A	85	SER	0	-0.013	-0.006	14.245	-0.010	-0.010	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.003	0.003	17.580	0.018	0.018	0.000	0.000	0.000	0.000
86	A	87	PHE	0	0.005	0.002	20.182	0.010	0.010	0.000	0.000	0.000	0.000
87	A	88	LEU	0	-0.004	-0.003	23.473	0.004	0.004	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.906	0.968	26.631	0.124	0.124	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.045	0.018	30.177	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	91	HIS	0	0.018	0.030	32.787	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	92	CYS	0	-0.075	-0.027	35.218	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	93	LEU	0	0.016	0.008	36.636	0.005	0.005	0.000	0.000	0.000	0.000
93	A	94	ASN	0	-0.018	-0.013	37.477	0.001	0.001	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.769	-0.900	38.824	-0.064	-0.064	0.000	0.000	0.000	0.000
95	A	96	HIS	0	-0.056	-0.040	39.899	0.000	0.000	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.923	-0.937	39.598	-0.059	-0.059	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.021	-0.001	34.636	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.059	-0.032	35.732	0.006	0.006	0.000	0.000	0.000	0.000
99	A	100	ASN	0	-0.045	-0.042	31.445	-0.012	-0.012	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.005	0.011	30.597	0.008	0.008	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.825	-0.909	25.022	-0.123	-0.123	0.000	0.000	0.000	0.000
102	A	103	PRO	0	0.003	-0.002	28.501	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.032	-0.015	27.134	0.007	0.007	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.730	0.890	22.751	0.152	0.152	0.000	0.000	0.000	0.000
105	A	106	VAL	0	-0.066	-0.042	26.014	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.931	-0.955	28.873	-0.026	-0.026	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.061	-0.053	32.173	0.005	0.005	0.000	0.000	0.000	0.000
108	A	109	TRP	0	0.072	0.038	27.490	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	110	GLN	0	-0.027	-0.005	33.819	0.005	0.005	0.000	0.000	0.000	0.000
110	A	111	TRP	0	0.032	0.005	34.950	-0.007	-0.007	0.000	0.000	0.000	0.000
111	A	112	PHE	0	-0.025	-0.019	34.164	0.006	0.006	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.081	0.043	36.933	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.030	-0.013	33.761	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.974	-0.970	36.622	-0.062	-0.062	0.000	0.000	0.000	0.000
115	A	116	ASN	0	-0.047	-0.030	38.275	0.005	0.005	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.002	0.008	31.692	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	118	PRO	0	0.008	0.013	32.435	0.004	0.004	0.000	0.000	0.000	0.000
118	A	119	SER	0	0.041	0.016	32.516	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.072	-0.039	29.412	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.015	0.010	27.274	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	122	PHE	0	0.050	0.010	18.433	0.002	0.002	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.024	0.011	18.356	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	124	PRO	0	0.023	0.013	18.355	0.009	0.009	0.000	0.000	0.000	0.000
124	A	125	LEU	0	0.045	0.034	21.087	0.002	0.002	0.000	0.000	0.000	0.000
125	A	126	LYS	1	0.914	0.958	24.695	0.096	0.096	0.000	0.000	0.000	0.000
126	A	127	ARG	1	0.910	0.958	20.313	0.206	0.206	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.017	0.010	24.428	0.005	0.005	0.000	0.000	0.000	0.000
128	A	129	ILE	0	-0.021	-0.011	25.905	0.007	0.007	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.993	-0.987	27.886	-0.084	-0.084	0.000	0.000	0.000	0.000
130	A	131	LYS	1	0.862	0.920	27.910	0.108	0.108	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.886	0.955	23.779	0.114	0.114	0.000	0.000	0.000	0.000
132	A	133	CYS	0	-0.042	-0.022	22.421	-0.013	-0.013	0.000	0.000	0.000	0.000
133	A	134	TYR	0	-0.030	0.001	18.935	0.006	0.006	0.000	0.000	0.000	0.000
134	A	135	LEU	0	-0.005	-0.009	24.030	-0.010	-0.010	0.000	0.000	0.000	0.000
135	A	136	TYR	0	-0.025	-0.014	23.842	0.003	0.003	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.854	0.925	28.614	0.157	0.157	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.834	-0.913	30.746	-0.113	-0.113	0.000	0.000	0.000	0.000
138	A	139	ILE	0	0.016	0.004	29.714	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	140	ILE	0	-0.012	0.006	32.875	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ILE)