FMO DATABASE

FMODB ID: 176YZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1200088.99765
FMO2-HF: Nuclear repulsion	1143993.433532
FMO2-HF: Total energy	-56095.564118
FMO2-MP2: Total energy	-56260.573345

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.
-11.39	-1.462	3.841	-5.485	-8.283	-0.005

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 : 0.019 / q_NPA : 0.017

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	0.036	0.010	2.647	-5.417	-0.838	0.706	-2.585	-2.699	-0.005
4	A	4	ILE	0	0.055	0.018	4.602	0.583	0.732	-0.001	-0.005	-0.144	0.000
5	A	5	GLU	-1	-0.796	-0.862	2.919	-4.986	-2.297	0.454	-1.515	-1.628	-0.013
6	A	6	LEU	0	-0.004	0.006	2.277	-2.001	0.339	2.680	-1.337	-3.682	0.013
7	A	7	MET	0	-0.040	-0.031	4.371	0.318	0.489	0.002	-0.043	-0.130	0.000
8	A	8	ILE	0	0.012	0.004	7.367	0.240	0.240	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.006	-0.004	5.609	0.138	0.138	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.004	-0.011	7.478	0.025	0.025	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.021	0.006	9.809	-0.040	-0.040	0.000	0.000	0.000	0.000
12	A	12	ILE	0	0.018	-0.003	10.892	0.011	0.011	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.007	-0.003	10.026	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.011	0.013	13.455	-0.023	-0.023	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.019	-0.012	15.601	-0.022	-0.022	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.005	-0.002	15.154	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.015	0.006	17.629	-0.011	-0.011	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.018	0.005	19.324	-0.014	-0.014	0.000	0.000	0.000	0.000
19	A	19	PHE	0	-0.010	-0.007	21.793	-0.012	-0.012	0.000	0.000	0.000	0.000
20	A	20	ALA	0	0.003	0.001	20.908	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	21	ILE	0	0.010	0.001	19.157	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	22	PRO	0	0.001	0.003	23.378	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.034	0.024	26.211	-0.006	-0.006	0.000	0.000	0.000	0.000
24	A	24	TYR	0	-0.012	-0.010	24.079	0.001	0.001	0.000	0.000	0.000	0.000
25	A	25	ASN	0	-0.004	-0.024	25.724	0.001	0.001	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.790	-0.885	28.248	0.066	0.066	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.053	-0.026	27.806	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.010	0.010	27.231	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	29	ALA	0	-0.029	-0.012	30.617	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.969	0.991	32.362	-0.091	-0.091	0.000	0.000	0.000	0.000
31	A	31	SER	0	-0.037	-0.013	32.736	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	32	GLN	0	0.015	0.002	32.085	-0.007	-0.007	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.033	0.021	36.088	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.012	0.020	38.384	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.776	-0.880	39.650	0.059	0.059	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.023	0.006	41.334	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.001	0.005	43.776	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	38	THR	0	0.002	0.005	42.933	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.020	-0.012	44.389	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	ALA	0	0.031	0.016	47.266	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.861	-0.931	48.474	0.046	0.046	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.016	0.001	49.589	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.022	-0.013	51.155	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.823	0.917	52.033	-0.044	-0.044	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.010	-0.001	55.788	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.881	0.942	52.912	-0.037	-0.037	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.035	-0.003	55.734	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	SER	0	0.005	-0.005	59.765	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.904	-0.954	61.628	0.030	0.030	0.000	0.000	0.000	0.000
50	A	50	HIS	1	0.742	0.859	59.545	-0.029	-0.029	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.020	0.003	62.677	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.970	-0.961	65.744	0.025	0.025	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.069	-0.028	68.021	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	54	GLY	0	-0.101	-0.052	68.919	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.921	-0.967	65.728	0.021	0.021	0.000	0.000	0.000	0.000
56	A	56	CYS	0	-0.069	-0.008	59.369	0.000	0.000	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.848	0.913	59.240	-0.022	-0.022	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.080	0.020	61.492	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.932	-0.952	61.666	0.024	0.024	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.066	-0.040	60.412	0.000	0.000	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.009	-0.003	62.475	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	62	PRO	0	-0.018	-0.020	64.621	0.001	0.001	0.000	0.000	0.000	0.000
63	A	63	ALA	0	-0.016	-0.005	65.653	0.001	0.001	0.000	0.000	0.000	0.000
64	A	64	SER	0	-0.006	-0.007	66.679	0.000	0.000	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.002	0.020	63.514	0.000	0.000	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.026	0.012	61.884	0.001	0.001	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.024	0.014	56.519	0.000	0.000	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.056	0.037	58.530	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	69	ASN	0	0.055	0.014	57.054	0.001	0.001	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.871	-0.897	52.250	0.032	0.032	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.844	-0.929	49.567	0.043	0.043	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.893	0.975	44.956	-0.039	-0.039	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.057	0.043	43.543	0.001	0.001	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.883	0.941	34.587	-0.074	-0.074	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.024	-0.057	34.384	0.001	0.001	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.021	0.015	39.727	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.005	0.019	43.364	0.001	0.001	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.022	-0.007	47.028	0.000	0.000	0.000	0.000	0.000	0.000
79	A	79	THR	0	0.022	-0.014	49.404	0.000	0.000	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.040	-0.011	53.017	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.834	-0.922	56.067	0.024	0.024	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.033	-0.013	58.007	0.001	0.001	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.928	-0.948	60.497	0.020	0.020	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.016	-0.031	64.183	0.000	0.000	0.000	0.000	0.000	0.000
85	A	85	ASN	0	-0.008	-0.008	65.441	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.927	0.957	67.485	-0.020	-0.020	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.935	-0.954	70.374	0.019	0.019	0.000	0.000	0.000	0.000
88	A	88	ALA	0	-0.057	-0.003	65.953	0.000	0.000	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.927	0.949	67.924	-0.021	-0.021	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.106	-0.080	66.787	0.001	0.001	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.000	-0.014	62.159	0.000	0.000	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.861	-0.936	59.034	0.033	0.033	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.794	-0.856	61.471	0.023	0.023	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.862	0.903	57.276	-0.026	-0.026	0.000	0.000	0.000	0.000
95	A	95	ASN	0	0.043	0.002	60.567	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.048	0.031	61.689	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.847	0.902	55.187	-0.025	-0.025	0.000	0.000	0.000	0.000
98	A	99	VAL	0	-0.019	0.001	50.720	0.000	0.000	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.003	-0.007	50.596	0.001	0.001	0.000	0.000	0.000	0.000
100	A	101	ILE	0	0.008	0.018	44.911	0.001	0.001	0.000	0.000	0.000	0.000
101	A	102	THR	0	0.002	0.004	45.596	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	103	TYR	0	0.016	-0.029	40.390	0.001	0.001	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.000	-0.002	40.128	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	105	GLN	0	-0.034	-0.012	41.072	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.055	0.035	42.321	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.055	-0.063	40.968	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.082	-0.033	36.481	0.000	0.000	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.009	0.012	37.653	0.000	0.000	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.881	-0.956	37.776	0.035	0.035	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.854	0.939	33.358	-0.055	-0.055	0.000	0.000	0.000	0.000
111	A	112	ILE	0	-0.030	-0.008	33.684	0.006	0.006	0.000	0.000	0.000	0.000
112	A	113	SER	0	0.016	0.010	32.001	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	114	LYS	1	1.016	0.986	30.453	-0.051	-0.051	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.067	-0.038	31.224	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.001	0.003	35.093	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.006	0.009	36.752	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	118	GLY	0	0.003	0.001	38.911	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.843	0.941	40.296	-0.036	-0.036	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.931	0.949	43.141	-0.029	-0.029	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.007	0.006	44.194	0.000	0.000	0.000	0.000	0.000	0.000
121	A	122	VAL	0	0.011	0.012	46.817	0.000	0.000	0.000	0.000	0.000	0.000
122	A	123	LEU	0	-0.021	-0.011	47.937	0.001	0.001	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.749	-0.848	51.850	0.028	0.028	0.000	0.000	0.000	0.000
124	A	125	GLN	0	-0.002	-0.015	55.130	0.000	0.000	0.000	0.000	0.000	0.000
125	A	126	PHE	0	-0.028	-0.016	55.620	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	127	VAL	0	0.034	0.026	59.526	0.001	0.001	0.000	0.000	0.000	0.000
127	A	128	ASN	0	-0.019	-0.004	58.756	0.001	0.001	0.000	0.000	0.000	0.000
128	A	129	GLY	0	0.033	0.027	58.447	0.001	0.001	0.000	0.000	0.000	0.000
129	A	130	SER	0	-0.069	-0.036	54.848	0.002	0.002	0.000	0.000	0.000	0.000
130	A	131	TYR	0	-0.022	-0.045	50.838	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.832	0.916	51.268	-0.032	-0.032	0.000	0.000	0.000	0.000
132	A	133	TYR	0	-0.050	-0.069	48.022	0.000	0.000	0.000	0.000	0.000	0.000
133	A	134	ASN	0	-0.050	-0.027	50.530	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.864	-0.911	50.174	0.031	0.031	0.000	0.000	0.000	0.000
135	A	136	GLY	0	0.007	0.004	50.832	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.793	-0.883	52.197	0.025	0.025	0.000	0.000	0.000	0.000
137	A	138	THR	0	-0.100	-0.048	46.228	0.002	0.002	0.000	0.000	0.000	0.000
138	A	139	ASP	-1	-0.856	-0.923	44.522	0.029	0.029	0.000	0.000	0.000	0.000
139	A	140	LEU	0	-0.095	-0.040	39.851	0.001	0.001	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.882	-0.950	38.294	0.040	0.040	0.000	0.000	0.000	0.000
141	A	142	LEU	0	0.114	0.044	41.084	0.004	0.004	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.766	0.873	33.959	-0.058	-0.058	0.000	0.000	0.000	0.000
143	A	144	PHE	0	-0.073	-0.056	34.218	0.006	0.006	0.000	0.000	0.000	0.000
144	A	145	ILE	0	0.029	0.044	38.679	0.002	0.002	0.000	0.000	0.000	0.000
145	A	146	PRO	0	0.036	0.021	41.352	0.002	0.002	0.000	0.000	0.000	0.000
146	A	147	ASN	0	0.049	-0.020	40.367	-0.005	-0.005	0.000	0.000	0.000	0.000
147	A	148	ALA	0	0.002	0.015	43.842	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	149	VAL	0	0.004	0.015	45.962	-0.002	-0.002	0.000	0.000	0.000	0.000
149	A	150	LYS	1	0.863	0.949	41.724	-0.057	-0.057	0.000	0.000	0.000	0.000
150	A	151	ASN	0	-0.033	0.005	48.121	-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)