FMO DATABASE

FMODB ID: 94582

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	OptAll
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	-1355329.757891
FMO2-HF: Nuclear repulsion	1299146.609495
FMO2-HF: Total energy	-56183.148397
FMO2-MP2: Total energy	-56349.534155

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.
-5.067	0.755	3.55	-3.124	-6.247	-0.013

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 : 0.039 / q_NPA : 0.021

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	0.022	0.003	2.883	-5.559	0.047	3.542	-3.095	-6.053	-0.013
4	A	5	PRO	0	0.009	0.011	3.807	0.328	0.544	0.008	-0.029	-0.194	0.000
5	A	6	ARG	1	0.858	0.936	7.435	1.151	1.151	0.000	0.000	0.000	0.000
6	A	7	ILE	0	0.024	0.015	10.295	0.135	0.135	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.013	0.005	13.555	-0.039	-0.039	0.000	0.000	0.000	0.000
8	A	9	ILE	0	-0.017	-0.007	16.403	0.027	0.027	0.000	0.000	0.000	0.000
9	A	10	GLY	0	-0.008	0.013	20.132	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	11	ILE	0	-0.029	-0.012	23.255	0.013	0.013	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.024	-0.024	26.827	0.009	0.009	0.000	0.000	0.000	0.000
12	A	13	ILE	0	0.045	0.023	29.937	0.009	0.009	0.000	0.000	0.000	0.000
13	A	14	PHE	0	-0.006	-0.002	32.371	0.004	0.004	0.000	0.000	0.000	0.000
14	A	15	ASN	0	0.028	0.002	35.850	0.003	0.003	0.000	0.000	0.000	0.000
15	A	16	ASN	0	-0.036	-0.040	39.246	0.003	0.003	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.720	0.829	42.167	0.107	0.107	0.000	0.000	0.000	0.000
17	A	18	ASN	0	-0.067	-0.033	39.573	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.791	-0.847	38.607	-0.109	-0.109	0.000	0.000	0.000	0.000
19	A	20	ILE	0	-0.005	-0.014	31.667	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.028	-0.003	31.655	0.005	0.005	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.066	-0.031	29.511	-0.013	-0.013	0.000	0.000	0.000	0.000
22	A	23	GLY	0	0.069	0.014	29.399	0.012	0.012	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.829	0.921	28.873	0.123	0.123	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.921	0.956	22.633	0.296	0.296	0.000	0.000	0.000	0.000
25	A	26	ILE	0	0.003	-0.003	27.829	0.005	0.005	0.000	0.000	0.000	0.000
26	A	27	SER	0	-0.031	-0.043	24.448	-0.004	-0.004	0.000	0.000	0.000	0.000
27	A	28	SER	0	0.035	0.002	23.679	0.007	0.007	0.000	0.000	0.000	0.000
28	A	29	HIS	0	-0.076	-0.036	23.829	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.025	0.022	28.069	0.011	0.011	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.863	-0.902	25.598	-0.173	-0.173	0.000	0.000	0.000	0.000
31	A	32	SER	0	0.014	0.015	28.279	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	33	SER	0	-0.063	-0.014	26.475	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	34	TYR	0	0.045	0.016	28.408	0.004	0.004	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.007	0.001	24.519	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.006	0.002	24.356	0.018	0.018	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.051	0.031	25.813	-0.010	-0.010	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.007	-0.005	22.757	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	39	GLY	0	-0.070	-0.049	19.251	0.005	0.005	0.000	0.000	0.000	0.000
39	A	40	HIS	0	-0.056	-0.031	14.134	-0.172	-0.172	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.030	0.021	15.654	0.036	0.036	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.977	-0.982	15.030	-0.524	-0.524	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.085	-0.062	13.627	0.020	0.020	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.013	-0.001	16.096	0.041	0.041	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.724	-0.806	19.177	-0.341	-0.341	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.034	-0.047	20.032	-0.021	-0.021	0.000	0.000	0.000	0.000
46	A	47	PHE	0	-0.004	-0.030	18.243	-0.016	-0.016	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.861	-0.945	22.367	-0.252	-0.252	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.828	-0.886	24.336	-0.227	-0.227	0.000	0.000	0.000	0.000
49	A	50	CYS	0	-0.060	0.000	20.340	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	51	ALA	0	-0.007	-0.016	23.051	0.003	0.003	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.034	-0.028	25.386	0.010	0.010	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.779	0.864	19.788	0.364	0.364	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.740	-0.877	20.427	-0.404	-0.404	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.026	-0.013	24.942	0.009	0.009	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.004	0.031	28.318	0.011	0.011	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.847	-0.936	24.217	-0.267	-0.267	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.762	-0.868	25.234	-0.280	-0.280	0.000	0.000	0.000	0.000
58	A	59	THR	0	-0.058	-0.059	28.243	0.016	0.016	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.014	-0.006	31.837	0.011	0.011	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.040	-0.012	33.198	0.009	0.009	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.034	0.007	32.832	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	63	ILE	0	-0.027	-0.011	29.199	0.006	0.006	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.855	-0.922	33.449	-0.125	-0.125	0.000	0.000	0.000	0.000
64	A	65	ASN	0	-0.092	-0.067	32.932	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.021	0.033	28.579	0.004	0.004	0.000	0.000	0.000	0.000
66	A	67	GLN	0	0.035	0.017	29.613	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.052	0.028	22.157	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.054	-0.025	26.631	0.019	0.019	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.001	-0.010	24.804	0.014	0.014	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.029	0.032	18.521	-0.019	-0.019	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.070	-0.054	18.933	0.027	0.027	0.000	0.000	0.000	0.000
72	A	73	ASN	0	0.039	0.014	13.735	-0.100	-0.100	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.806	-0.880	14.877	-0.315	-0.315	0.000	0.000	0.000	0.000
74	A	75	ILE	0	0.039	0.011	11.426	-0.100	-0.100	0.000	0.000	0.000	0.000
75	A	76	PHE	0	-0.038	-0.011	13.436	0.078	0.078	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.860	-0.940	13.542	-0.289	-0.289	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.888	0.963	14.578	0.241	0.241	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.855	-0.945	14.450	-0.354	-0.354	0.000	0.000	0.000	0.000
79	A	80	GLN	0	-0.061	-0.026	9.594	-0.111	-0.111	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.831	0.914	7.869	1.229	1.229	0.000	0.000	0.000	0.000
81	A	82	HIS	0	-0.009	-0.019	8.543	0.073	0.073	0.000	0.000	0.000	0.000
82	A	83	TYR	0	-0.020	-0.021	9.997	-0.236	-0.236	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.017	-0.009	12.168	0.090	0.090	0.000	0.000	0.000	0.000
84	A	85	SER	0	0.008	0.012	14.592	-0.025	-0.025	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.005	0.003	17.734	0.041	0.041	0.000	0.000	0.000	0.000
86	A	87	PHE	0	0.002	-0.002	20.330	0.002	0.002	0.000	0.000	0.000	0.000
87	A	88	LEU	0	0.009	0.010	23.508	0.015	0.015	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.797	0.893	27.028	0.150	0.150	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.042	0.014	30.621	0.002	0.002	0.000	0.000	0.000	0.000
90	A	91	HIS	0	-0.017	0.004	33.147	-0.007	-0.007	0.000	0.000	0.000	0.000
91	A	92	CYS	0	-0.074	-0.018	35.192	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.017	-0.017	36.633	0.007	0.007	0.000	0.000	0.000	0.000
93	A	94	ASN	0	-0.012	-0.013	37.005	0.002	0.002	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.737	-0.863	38.751	-0.108	-0.108	0.000	0.000	0.000	0.000
95	A	96	HIS	0	-0.028	-0.022	39.829	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.904	-0.931	39.176	-0.107	-0.107	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.022	0.003	34.509	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.061	-0.033	35.516	0.009	0.009	0.000	0.000	0.000	0.000
99	A	100	ASN	0	-0.055	-0.050	31.580	-0.018	-0.018	0.000	0.000	0.000	0.000
100	A	101	LEU	0	0.006	0.019	30.247	0.008	0.008	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.821	-0.899	24.592	-0.293	-0.293	0.000	0.000	0.000	0.000
102	A	103	PRO	0	0.022	0.005	28.458	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.046	-0.024	26.747	0.003	0.003	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.723	0.856	22.041	0.308	0.308	0.000	0.000	0.000	0.000
105	A	106	VAL	0	-0.050	-0.029	25.761	-0.011	-0.011	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.912	-0.927	28.731	-0.123	-0.123	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.026	-0.036	31.893	0.011	0.011	0.000	0.000	0.000	0.000
108	A	109	TRP	0	0.055	0.045	27.144	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	110	GLN	0	-0.005	0.003	33.802	0.010	0.010	0.000	0.000	0.000	0.000
110	A	111	TRP	0	0.026	0.013	35.162	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	112	PHE	0	-0.011	-0.017	34.611	0.006	0.006	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.064	0.041	37.159	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.011	-0.013	34.424	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.937	-0.965	36.854	-0.104	-0.104	0.000	0.000	0.000	0.000
115	A	116	ASN	0	-0.060	-0.031	38.788	0.004	0.004	0.000	0.000	0.000	0.000
116	A	117	LEU	0	0.003	0.014	32.487	-0.004	-0.004	0.000	0.000	0.000	0.000
117	A	118	PRO	0	0.005	0.011	32.421	0.005	0.005	0.000	0.000	0.000	0.000
118	A	119	SER	0	0.011	-0.004	32.686	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.085	-0.052	29.688	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	121	LEU	0	-0.006	-0.002	27.555	-0.009	-0.009	0.000	0.000	0.000	0.000
121	A	122	PHE	0	0.061	0.014	18.812	0.003	0.003	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.033	0.021	19.024	0.005	0.005	0.000	0.000	0.000	0.000
123	A	124	PRO	0	0.004	0.008	18.630	0.023	0.023	0.000	0.000	0.000	0.000
124	A	125	LEU	0	0.050	0.025	21.364	0.015	0.015	0.000	0.000	0.000	0.000
125	A	126	LYS	1	0.864	0.921	24.987	0.173	0.173	0.000	0.000	0.000	0.000
126	A	127	ARG	1	0.859	0.903	19.499	0.295	0.295	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.001	0.002	24.978	0.014	0.014	0.000	0.000	0.000	0.000
128	A	129	ILE	0	0.004	0.000	26.563	0.014	0.014	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.872	-0.915	27.765	-0.128	-0.128	0.000	0.000	0.000	0.000
130	A	131	LYS	1	0.862	0.921	28.542	0.150	0.150	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.799	0.904	25.208	0.153	0.153	0.000	0.000	0.000	0.000
132	A	133	CYS	0	-0.036	0.001	22.875	-0.016	-0.016	0.000	0.000	0.000	0.000
133	A	134	TYR	0	0.015	0.012	18.885	0.013	0.013	0.000	0.000	0.000	0.000
134	A	135	LEU	0	0.011	-0.002	24.038	-0.012	-0.012	0.000	0.000	0.000	0.000
135	A	136	TYR	0	-0.025	-0.011	23.478	0.005	0.005	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.812	0.894	28.655	0.184	0.184	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.772	-0.879	30.984	-0.145	-0.145	0.000	0.000	0.000	0.000
138	A	139	ILE	0	0.041	0.033	30.264	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	140	ILE	0	0.022	0.029	33.272	-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)