FMO DATABASE

FMODB ID: LZ5N9

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1354242.426846
FMO2-HF: Nuclear repulsion	1298059.630149
FMO2-HF: Total energy	-56182.796697
FMO2-MP2: Total energy	-56349.208185

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.
-3.86	-0.168	5.966	-2.901	-6.759	-0.009

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 : 0.029 / q_NPA : 0.014

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	0.034	0.014	2.525	-4.490	-0.990	5.958	-2.881	-6.578	-0.009
4	A	5	PRO	0	0.007	0.004	3.805	0.276	0.468	0.008	-0.020	-0.181	0.000
5	A	6	ARG	1	0.886	0.957	7.434	1.238	1.238	0.000	0.000	0.000	0.000
6	A	7	ILE	0	0.021	0.009	10.061	0.117	0.117	0.000	0.000	0.000	0.000
7	A	8	GLY	0	-0.006	0.004	13.548	-0.014	-0.014	0.000	0.000	0.000	0.000
8	A	9	ILE	0	0.015	0.002	16.552	0.028	0.028	0.000	0.000	0.000	0.000
9	A	10	GLY	0	-0.032	-0.005	20.167	0.002	0.002	0.000	0.000	0.000	0.000
10	A	11	ILE	0	-0.013	-0.012	22.939	0.015	0.015	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.047	-0.033	26.567	0.007	0.007	0.000	0.000	0.000	0.000
12	A	13	ILE	0	0.050	0.028	29.551	0.008	0.008	0.000	0.000	0.000	0.000
13	A	14	PHE	0	-0.033	-0.021	32.254	0.003	0.003	0.000	0.000	0.000	0.000
14	A	15	ASN	0	0.015	-0.004	35.757	0.003	0.003	0.000	0.000	0.000	0.000
15	A	16	ASN	0	-0.017	-0.042	39.112	0.003	0.003	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.716	0.843	41.965	0.105	0.105	0.000	0.000	0.000	0.000
17	A	18	ASN	0	-0.050	-0.030	39.162	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.785	-0.841	38.189	-0.107	-0.107	0.000	0.000	0.000	0.000
19	A	20	ILE	0	0.018	-0.001	31.333	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.026	0.005	31.765	0.005	0.005	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.056	-0.031	29.141	-0.014	-0.014	0.000	0.000	0.000	0.000
22	A	23	GLY	0	0.057	0.017	29.261	0.013	0.013	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.849	0.932	28.772	0.125	0.125	0.000	0.000	0.000	0.000
24	A	25	ARG	1	1.000	1.000	21.998	0.298	0.298	0.000	0.000	0.000	0.000
25	A	26	ILE	0	0.011	0.004	28.000	0.007	0.007	0.000	0.000	0.000	0.000
26	A	27	SER	0	-0.039	-0.046	24.926	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	28	SER	0	0.062	0.018	24.361	0.007	0.007	0.000	0.000	0.000	0.000
28	A	29	HIS	0	-0.087	-0.042	24.069	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.026	0.021	28.403	0.011	0.011	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.889	-0.910	26.062	-0.164	-0.164	0.000	0.000	0.000	0.000
31	A	32	SER	0	0.021	0.009	28.512	-0.012	-0.012	0.000	0.000	0.000	0.000
32	A	33	SER	0	-0.065	-0.015	25.878	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	34	TYR	0	0.032	0.005	28.124	0.000	0.000	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.023	-0.009	24.176	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.001	0.006	24.364	0.015	0.015	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.039	0.022	25.359	-0.014	-0.014	0.000	0.000	0.000	0.000
37	A	38	GLY	0	-0.012	-0.021	22.678	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	39	GLY	0	-0.035	-0.005	19.345	0.001	0.001	0.000	0.000	0.000	0.000
39	A	40	HIS	0	-0.030	0.005	13.863	-0.135	-0.135	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.035	0.011	15.452	0.033	0.033	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.987	-0.982	14.977	-0.510	-0.510	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.068	-0.058	13.617	0.023	0.023	0.000	0.000	0.000	0.000
43	A	44	GLY	0	-0.022	-0.020	15.905	0.035	0.035	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.703	-0.801	18.864	-0.334	-0.334	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.037	-0.047	19.929	-0.017	-0.017	0.000	0.000	0.000	0.000
46	A	47	PHE	0	-0.012	-0.031	18.152	-0.014	-0.014	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.882	-0.954	22.403	-0.239	-0.239	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.827	-0.893	24.085	-0.222	-0.222	0.000	0.000	0.000	0.000
49	A	50	CYS	0	-0.062	0.008	20.164	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.015	-0.004	22.909	0.004	0.004	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.039	-0.032	25.279	0.009	0.009	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.803	0.884	20.045	0.361	0.361	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.804	-0.926	20.442	-0.392	-0.392	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.011	-0.016	25.106	0.010	0.010	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.012	0.019	28.486	0.012	0.012	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.861	-0.948	24.300	-0.269	-0.269	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.805	-0.877	25.014	-0.281	-0.281	0.000	0.000	0.000	0.000
58	A	59	THR	0	-0.086	-0.073	28.530	0.015	0.015	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.010	-0.008	31.997	0.010	0.010	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.046	-0.006	33.133	0.010	0.010	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.036	0.006	32.817	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	63	ILE	0	-0.037	-0.016	29.012	0.007	0.007	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.857	-0.928	33.256	-0.122	-0.122	0.000	0.000	0.000	0.000
64	A	65	ASN	0	-0.107	-0.067	32.785	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.050	0.040	28.459	0.004	0.004	0.000	0.000	0.000	0.000
66	A	67	GLN	0	-0.004	-0.006	30.054	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.043	0.024	21.816	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.038	-0.028	26.290	0.018	0.018	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.014	-0.002	24.384	0.013	0.013	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.025	0.036	18.330	-0.019	-0.019	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.071	-0.059	18.721	0.031	0.031	0.000	0.000	0.000	0.000
72	A	73	ASN	0	0.040	0.021	13.503	-0.103	-0.103	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.821	-0.900	14.938	-0.328	-0.328	0.000	0.000	0.000	0.000
74	A	75	ILE	0	0.031	0.007	10.665	-0.092	-0.092	0.000	0.000	0.000	0.000
75	A	76	PHE	0	-0.037	-0.020	13.292	0.079	0.079	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.873	-0.952	13.444	-0.273	-0.273	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.904	0.975	14.080	0.237	0.237	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.865	-0.957	14.222	-0.363	-0.363	0.000	0.000	0.000	0.000
79	A	80	GLN	0	-0.044	-0.011	9.178	-0.108	-0.108	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.834	0.921	7.923	1.245	1.245	0.000	0.000	0.000	0.000
81	A	82	HIS	0	0.003	-0.009	8.312	0.078	0.078	0.000	0.000	0.000	0.000
82	A	83	TYR	0	-0.045	-0.031	9.842	-0.215	-0.215	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.003	0.004	12.010	0.093	0.093	0.000	0.000	0.000	0.000
84	A	85	SER	0	-0.004	0.000	14.322	-0.036	-0.036	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.012	-0.006	17.614	0.037	0.037	0.000	0.000	0.000	0.000
86	A	87	PHE	0	0.005	0.002	20.258	0.000	0.000	0.000	0.000	0.000	0.000
87	A	88	LEU	0	0.000	-0.001	23.453	0.014	0.014	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.833	0.921	26.710	0.146	0.146	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.050	0.024	30.260	0.002	0.002	0.000	0.000	0.000	0.000
90	A	91	HIS	0	0.013	0.020	32.871	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	92	CYS	0	-0.078	-0.033	35.188	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	93	LEU	0	0.013	0.001	36.591	0.007	0.007	0.000	0.000	0.000	0.000
93	A	94	ASN	0	-0.025	-0.020	37.067	0.003	0.003	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.740	-0.863	38.786	-0.108	-0.108	0.000	0.000	0.000	0.000
95	A	96	HIS	0	-0.042	-0.033	39.864	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.912	-0.930	39.168	-0.107	-0.107	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.020	0.005	34.727	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.056	-0.030	35.619	0.006	0.006	0.000	0.000	0.000	0.000
99	A	100	ASN	0	-0.044	-0.043	31.622	-0.018	-0.018	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.006	0.009	30.680	0.008	0.008	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.826	-0.895	24.730	-0.293	-0.293	0.000	0.000	0.000	0.000
102	A	103	PRO	0	-0.014	-0.007	28.637	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.022	-0.010	26.979	0.004	0.004	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.733	0.866	22.609	0.310	0.310	0.000	0.000	0.000	0.000
105	A	106	VAL	0	-0.061	-0.036	26.039	-0.006	-0.006	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.914	-0.946	28.939	-0.127	-0.127	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.037	-0.035	32.151	0.010	0.010	0.000	0.000	0.000	0.000
108	A	109	TRP	0	0.072	0.034	27.365	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	110	GLN	0	-0.017	-0.005	33.931	0.009	0.009	0.000	0.000	0.000	0.000
110	A	111	TRP	0	0.034	0.014	35.058	-0.010	-0.010	0.000	0.000	0.000	0.000
111	A	112	PHE	0	-0.027	-0.021	34.377	0.007	0.007	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.067	0.038	37.034	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.022	-0.013	34.114	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.950	-0.965	36.716	-0.100	-0.100	0.000	0.000	0.000	0.000
115	A	116	ASN	0	-0.055	-0.034	38.374	0.006	0.006	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.011	0.009	32.047	-0.004	-0.004	0.000	0.000	0.000	0.000
117	A	118	PRO	0	0.011	0.016	32.466	0.005	0.005	0.000	0.000	0.000	0.000
118	A	119	SER	0	0.010	-0.006	32.619	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.088	-0.055	29.516	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.012	0.012	27.384	-0.008	-0.008	0.000	0.000	0.000	0.000
121	A	122	PHE	0	0.055	0.010	18.629	0.001	0.001	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.030	0.011	18.554	0.009	0.009	0.000	0.000	0.000	0.000
123	A	124	PRO	0	0.012	0.016	18.500	0.023	0.023	0.000	0.000	0.000	0.000
124	A	125	LEU	0	0.042	0.025	21.182	0.014	0.014	0.000	0.000	0.000	0.000
125	A	126	LYS	1	0.884	0.932	24.791	0.169	0.169	0.000	0.000	0.000	0.000
126	A	127	ARG	1	0.909	0.950	20.081	0.274	0.274	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.004	0.005	24.512	0.015	0.015	0.000	0.000	0.000	0.000
128	A	129	ILE	0	-0.003	-0.004	25.989	0.014	0.014	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.931	-0.942	27.899	-0.125	-0.125	0.000	0.000	0.000	0.000
130	A	131	LYS	1	0.852	0.898	27.978	0.143	0.143	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.852	0.942	24.307	0.153	0.153	0.000	0.000	0.000	0.000
132	A	133	CYS	0	-0.051	-0.011	22.508	-0.019	-0.019	0.000	0.000	0.000	0.000
133	A	134	TYR	0	0.000	0.011	18.911	0.013	0.013	0.000	0.000	0.000	0.000
134	A	135	LEU	0	0.007	-0.002	24.084	-0.013	-0.013	0.000	0.000	0.000	0.000
135	A	136	TYR	0	-0.030	-0.020	23.638	0.007	0.007	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.836	0.913	28.668	0.177	0.177	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.789	-0.877	30.815	-0.140	-0.140	0.000	0.000	0.000	0.000
138	A	139	ILE	0	0.061	0.021	29.854	0.000	0.000	0.000	0.000	0.000	0.000
139	A	140	ILE	0	0.014	0.031	32.955	0.000	0.000	0.000	0.000	0.000	0.000

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