FMO DATABASE

FMODB ID: G6YR1

Calculation Name: 3SOK-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3SOK

Chain ID: A

ChEMBL ID:

UniProt ID: P02975

Base Structure: X-ray

Registration Date: 2023-06-22

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	150
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1201925.300977
FMO2-HF: Nuclear repulsion	1145829.334212
FMO2-HF: Total energy	-56095.966765
FMO2-MP2: Total energy	-56260.923872

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:1:PHE)

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

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.
-11.373	-1.639	3.597	-5.283	-8.05	-0.008

Interaction energy analysis for fragmet #1(A:1:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.022 / q_NPA : 0.018

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	3	LEU	0	0.025	-0.002	2.671	-4.974	-0.846	0.704	-2.368	-2.464	-0.009
4	A	4	ILE	0	0.045	0.016	4.501	0.626	0.780	-0.001	-0.005	-0.148	0.000
5	A	5	GLU	-1	-0.797	-0.860	2.626	-5.359	-2.527	0.557	-1.562	-1.828	-0.013
6	A	6	LEU	0	0.001	0.011	2.301	-1.903	0.541	2.335	-1.299	-3.481	0.014
7	A	7	MET	0	-0.026	-0.020	4.336	0.216	0.392	0.002	-0.049	-0.129	0.000
8	A	8	ILE	0	0.014	0.013	7.451	0.232	0.232	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.011	0.003	5.555	0.111	0.111	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.002	-0.004	7.458	0.020	0.020	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.006	0.006	9.994	-0.044	-0.044	0.000	0.000	0.000	0.000
12	A	12	ILE	0	-0.012	-0.006	10.546	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.007	-0.003	10.172	-0.013	-0.013	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.010	0.010	13.593	-0.034	-0.034	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.018	-0.015	15.849	-0.021	-0.021	0.000	0.000	0.000	0.000
16	A	16	LEU	0	0.011	0.006	15.222	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.002	-0.006	17.401	-0.015	-0.015	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.017	-0.005	19.388	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	19	PHE	0	-0.015	0.002	21.878	-0.017	-0.017	0.000	0.000	0.000	0.000
20	A	20	ALA	0	0.003	-0.007	20.843	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	21	ILE	0	0.007	0.004	19.085	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	22	PRO	0	-0.014	-0.009	23.351	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.037	0.024	26.055	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	24	TYR	0	0.005	0.005	24.153	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	25	ASN	0	0.015	-0.004	25.723	0.000	0.000	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.803	-0.900	28.428	0.067	0.067	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.047	-0.021	27.801	-0.007	-0.007	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.006	0.000	27.477	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	29	ALA	0	-0.041	-0.017	30.780	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.914	0.952	32.257	-0.089	-0.089	0.000	0.000	0.000	0.000
31	A	31	SER	0	-0.043	-0.010	32.714	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	32	GLN	0	0.014	-0.002	32.228	-0.008	-0.008	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.033	0.018	36.305	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.018	0.025	38.582	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.762	-0.868	39.909	0.058	0.058	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.034	0.010	41.627	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.000	0.001	44.093	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.019	-0.013	43.022	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.027	-0.012	44.723	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	ALA	0	0.029	0.019	47.603	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.854	-0.933	48.742	0.046	0.046	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.012	0.003	49.736	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.019	-0.020	51.315	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.831	0.931	52.427	-0.044	-0.044	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.003	0.003	55.917	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.851	0.904	52.909	-0.037	-0.037	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.030	-0.009	55.900	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	SER	0	0.005	0.002	59.852	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.898	-0.958	61.434	0.030	0.030	0.000	0.000	0.000	0.000
50	A	50	HIS	1	0.746	0.866	59.827	-0.029	-0.029	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.024	0.007	62.676	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.975	-0.968	65.868	0.025	0.025	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.054	-0.021	67.925	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	54	GLY	0	-0.037	-0.008	68.879	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.958	-0.986	65.944	0.022	0.022	0.000	0.000	0.000	0.000
56	A	56	CYS	0	-0.027	0.021	59.617	0.000	0.000	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.858	0.937	59.840	-0.022	-0.022	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.101	0.037	61.862	0.000	0.000	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.950	-0.969	61.724	0.024	0.024	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.051	-0.031	60.454	0.001	0.001	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.026	0.007	62.512	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	62	PRO	0	-0.022	-0.025	64.489	0.001	0.001	0.000	0.000	0.000	0.000
63	A	63	ALA	0	-0.031	-0.008	65.724	0.000	0.000	0.000	0.000	0.000	0.000
64	A	64	SER	0	-0.010	-0.017	66.716	0.000	0.000	0.000	0.000	0.000	0.000
65	A	65	GLY	0	-0.024	0.004	63.293	0.001	0.001	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.051	0.029	61.721	0.001	0.001	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.008	0.011	56.567	0.000	0.000	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.059	0.039	58.828	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	69	ASN	0	0.057	0.025	57.277	0.001	0.001	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.848	-0.892	52.537	0.032	0.032	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.831	-0.909	49.406	0.043	0.043	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.855	0.944	44.976	-0.041	-0.041	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.059	0.054	43.241	0.001	0.001	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.907	0.955	34.384	-0.075	-0.075	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.038	-0.056	34.246	0.001	0.001	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.009	0.002	39.595	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.005	0.011	43.272	0.001	0.001	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.013	-0.014	46.934	0.000	0.000	0.000	0.000	0.000	0.000
79	A	79	THR	0	0.013	-0.010	49.393	0.000	0.000	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.036	-0.008	53.128	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.829	-0.918	56.067	0.024	0.024	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.037	-0.015	58.019	0.001	0.001	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.921	-0.969	60.504	0.021	0.021	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.024	-0.023	64.229	0.000	0.000	0.000	0.000	0.000	0.000
85	A	85	ASN	0	-0.001	-0.006	65.551	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.872	0.917	67.479	-0.020	-0.020	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.925	-0.948	70.195	0.019	0.019	0.000	0.000	0.000	0.000
88	A	88	ALA	0	-0.051	-0.002	65.674	0.000	0.000	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.902	0.944	67.676	-0.022	-0.022	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.096	-0.082	66.967	0.000	0.000	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.038	0.010	62.206	0.000	0.000	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.820	-0.913	58.622	0.034	0.034	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.798	-0.864	61.144	0.023	0.023	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.863	0.911	56.580	-0.027	-0.027	0.000	0.000	0.000	0.000
95	A	95	ASN	0	0.020	-0.009	60.501	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.031	0.016	61.536	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.825	0.886	55.071	-0.026	-0.026	0.000	0.000	0.000	0.000
98	A	99	VAL	0	-0.011	0.006	50.789	0.000	0.000	0.000	0.000	0.000	0.000
99	A	100	VAL	0	0.011	0.005	50.731	0.001	0.001	0.000	0.000	0.000	0.000
100	A	101	ILE	0	-0.011	0.007	44.951	0.001	0.001	0.000	0.000	0.000	0.000
101	A	102	THR	0	-0.013	-0.003	45.149	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	103	TYR	0	0.020	-0.015	40.101	0.001	0.001	0.000	0.000	0.000	0.000
103	A	104	GLY	0	-0.013	-0.009	39.910	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	105	GLN	0	-0.024	-0.013	40.852	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.065	0.044	41.908	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.068	-0.067	41.185	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.063	-0.027	36.417	0.000	0.000	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.015	0.016	37.751	0.000	0.000	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.885	-0.965	37.921	0.036	0.036	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.864	0.952	33.552	-0.054	-0.054	0.000	0.000	0.000	0.000
111	A	112	ILE	0	-0.026	-0.010	33.644	0.006	0.006	0.000	0.000	0.000	0.000
112	A	113	SER	0	0.032	0.017	31.947	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	114	LYS	1	0.959	0.961	30.221	-0.052	-0.052	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.047	-0.021	31.090	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.000	0.001	34.986	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.022	-0.002	36.473	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	118	GLY	0	0.002	0.008	38.669	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.775	0.904	40.196	-0.040	-0.040	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.973	0.972	42.997	-0.030	-0.030	0.000	0.000	0.000	0.000
120	A	121	LEU	0	-0.012	-0.013	44.195	0.001	0.001	0.000	0.000	0.000	0.000
121	A	122	VAL	0	0.001	0.019	46.982	0.000	0.000	0.000	0.000	0.000	0.000
122	A	123	LEU	0	-0.007	-0.012	47.727	0.001	0.001	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.742	-0.851	51.777	0.029	0.029	0.000	0.000	0.000	0.000
124	A	125	GLN	0	0.008	-0.001	55.078	0.001	0.001	0.000	0.000	0.000	0.000
125	A	126	PHE	0	-0.014	-0.009	55.609	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	127	VAL	0	0.011	0.018	59.554	0.001	0.001	0.000	0.000	0.000	0.000
127	A	128	ASN	0	-0.040	-0.006	58.483	0.001	0.001	0.000	0.000	0.000	0.000
128	A	129	GLY	0	0.042	0.032	58.527	0.001	0.001	0.000	0.000	0.000	0.000
129	A	130	SER	0	-0.082	-0.051	54.469	0.002	0.002	0.000	0.000	0.000	0.000
130	A	131	TYR	0	-0.026	-0.053	51.112	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.793	0.881	51.479	-0.033	-0.033	0.000	0.000	0.000	0.000
132	A	133	TYR	0	-0.053	-0.072	47.910	0.000	0.000	0.000	0.000	0.000	0.000
133	A	134	ASN	0	-0.048	-0.028	50.527	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.878	-0.911	50.145	0.032	0.032	0.000	0.000	0.000	0.000
135	A	136	GLY	0	0.025	0.008	51.139	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.795	-0.869	52.259	0.025	0.025	0.000	0.000	0.000	0.000
137	A	138	THR	0	-0.102	-0.048	46.355	0.002	0.002	0.000	0.000	0.000	0.000
138	A	139	ASP	-1	-0.863	-0.935	44.084	0.031	0.031	0.000	0.000	0.000	0.000
139	A	140	LEU	0	-0.074	-0.025	39.649	0.001	0.001	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.814	-0.923	38.216	0.041	0.041	0.000	0.000	0.000	0.000
141	A	142	LEU	0	0.075	0.029	40.831	0.004	0.004	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.795	0.896	33.969	-0.061	-0.061	0.000	0.000	0.000	0.000
143	A	144	PHE	0	-0.038	-0.035	34.206	0.007	0.007	0.000	0.000	0.000	0.000
144	A	145	ILE	0	0.056	0.053	38.564	0.002	0.002	0.000	0.000	0.000	0.000
145	A	146	PRO	0	0.048	0.028	41.356	0.002	0.002	0.000	0.000	0.000	0.000
146	A	147	ASN	0	0.036	-0.022	40.437	-0.005	-0.005	0.000	0.000	0.000	0.000
147	A	148	ALA	0	0.020	0.016	43.915	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	149	VAL	0	0.009	0.029	46.101	-0.002	-0.002	0.000	0.000	0.000	0.000
149	A	150	LYS	1	0.828	0.933	41.779	-0.057	-0.057	0.000	0.000	0.000	0.000
150	A	151	ASN	0	-0.027	-0.002	48.086	-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:1:PHE)