FMO DATABASE

FMODB ID: 17Q5Z

Calculation Name: 4S0U-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4S0U

Chain ID: A

ChEMBL ID:

UniProt ID: P26718

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	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1118521.05271
FMO2-HF: Nuclear repulsion	1065788.043657
FMO2-HF: Total energy	-52733.009054
FMO2-MP2: Total energy	-52878.689286

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:92:THR)

Summations of interaction energy for fragment #1(A:92:THR)

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.
1.156	3.458	-0.023	-1.1	-1.179	0.004

Interaction energy analysis for fragmet #1(A:92:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.008 / q_NPA : -0.006

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	94	SER	0	-0.048	-0.023	3.812	0.700	2.991	-0.022	-1.099	-1.170	0.004
4	A	95	TYR	0	0.020	0.007	5.385	0.138	0.149	-0.001	-0.001	-0.009	0.000
5	A	96	CYS	0	-0.038	0.013	9.195	0.340	0.340	0.000	0.000	0.000	0.000
6	A	97	GLY	0	0.013	0.022	11.693	-0.017	-0.017	0.000	0.000	0.000	0.000
7	A	98	PRO	0	-0.052	-0.035	15.053	0.027	0.027	0.000	0.000	0.000	0.000
8	A	99	CYS	0	0.039	0.006	17.482	-0.022	-0.022	0.000	0.000	0.000	0.000
9	A	100	PRO	0	0.030	0.032	19.627	-0.018	-0.018	0.000	0.000	0.000	0.000
10	A	101	LYS	1	0.964	0.965	21.886	0.305	0.305	0.000	0.000	0.000	0.000
11	A	102	ASN	0	-0.039	-0.026	21.235	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	103	TRP	0	0.028	0.025	20.915	0.031	0.031	0.000	0.000	0.000	0.000
13	A	104	ILE	0	-0.005	0.001	17.219	-0.061	-0.061	0.000	0.000	0.000	0.000
14	A	106	TYR	0	-0.061	-0.061	12.588	-0.068	-0.068	0.000	0.000	0.000	0.000
15	A	107	LYS	1	0.845	0.920	12.195	-0.030	-0.030	0.000	0.000	0.000	0.000
16	A	108	ASN	0	0.055	-0.006	11.875	-0.034	-0.034	0.000	0.000	0.000	0.000
17	A	109	ASN	0	-0.037	0.012	14.625	0.013	0.013	0.000	0.000	0.000	0.000
18	A	111	TYR	0	0.012	-0.007	18.502	0.056	0.056	0.000	0.000	0.000	0.000
19	A	112	GLN	0	0.024	0.029	21.845	-0.033	-0.033	0.000	0.000	0.000	0.000
20	A	113	PHE	0	-0.032	-0.025	22.076	0.026	0.026	0.000	0.000	0.000	0.000
21	A	114	PHE	0	-0.008	0.001	26.852	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	115	ASP	-1	-0.863	-0.948	30.228	-0.152	-0.152	0.000	0.000	0.000	0.000
23	A	116	GLU	-1	-0.869	-0.944	32.674	-0.141	-0.141	0.000	0.000	0.000	0.000
24	A	117	SER	0	-0.029	-0.010	35.736	0.004	0.004	0.000	0.000	0.000	0.000
25	A	118	LYS	1	0.916	0.982	35.861	0.117	0.117	0.000	0.000	0.000	0.000
26	A	119	ASN	0	0.005	0.029	38.498	0.002	0.002	0.000	0.000	0.000	0.000
27	A	120	TRP	0	0.028	0.016	35.484	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	121	TYR	0	0.047	0.008	37.766	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	122	GLU	-1	-0.895	-0.945	39.013	-0.085	-0.085	0.000	0.000	0.000	0.000
30	A	123	SER	0	-0.030	-0.032	34.432	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	124	GLN	0	0.013	0.010	34.120	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	125	ALA	0	-0.020	-0.019	34.669	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	126	SER	0	-0.033	-0.029	33.586	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	127	CYS	0	-0.012	0.036	27.228	0.005	0.005	0.000	0.000	0.000	0.000
35	A	128	MET	0	0.038	0.026	30.746	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	129	SER	0	-0.106	-0.053	32.623	-0.006	-0.006	0.000	0.000	0.000	0.000
37	A	130	GLN	0	-0.044	-0.025	28.876	-0.022	-0.022	0.000	0.000	0.000	0.000
38	A	131	ASN	0	-0.078	-0.036	28.168	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	132	ALA	0	-0.023	0.007	26.693	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	133	SER	0	0.008	0.008	27.739	0.011	0.011	0.000	0.000	0.000	0.000
41	A	134	LEU	0	0.008	0.004	28.466	-0.016	-0.016	0.000	0.000	0.000	0.000
42	A	135	LEU	0	-0.057	-0.025	24.782	0.005	0.005	0.000	0.000	0.000	0.000
43	A	136	LYS	1	0.860	0.912	26.461	0.037	0.037	0.000	0.000	0.000	0.000
44	A	137	VAL	0	-0.005	-0.019	25.449	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	138	TYR	0	-0.091	-0.089	18.765	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	139	SER	0	0.010	-0.005	20.882	0.018	0.018	0.000	0.000	0.000	0.000
47	A	140	LYS	1	0.873	0.945	21.856	-0.069	-0.069	0.000	0.000	0.000	0.000
48	A	141	GLU	-1	-0.865	-0.931	17.794	0.113	0.113	0.000	0.000	0.000	0.000
49	A	142	ASP	-1	-0.810	-0.879	16.639	0.092	0.092	0.000	0.000	0.000	0.000
50	A	143	GLN	0	0.030	0.001	17.411	-0.030	-0.030	0.000	0.000	0.000	0.000
51	A	144	ASP	-1	-0.725	-0.841	16.432	0.007	0.007	0.000	0.000	0.000	0.000
52	A	145	LEU	0	-0.025	-0.011	15.359	0.002	0.002	0.000	0.000	0.000	0.000
53	A	146	LEU	0	0.031	0.028	19.136	-0.022	-0.022	0.000	0.000	0.000	0.000
54	A	147	LYS	1	0.824	0.915	19.181	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	148	LEU	0	-0.031	-0.005	19.813	0.008	0.008	0.000	0.000	0.000	0.000
56	A	149	VAL	0	-0.015	0.027	23.068	-0.017	-0.017	0.000	0.000	0.000	0.000
57	A	150	LYS	1	0.986	0.986	25.174	0.134	0.134	0.000	0.000	0.000	0.000
58	A	151	SER	0	-0.020	-0.023	28.546	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	152	TYR	0	-0.016	-0.003	31.298	0.007	0.007	0.000	0.000	0.000	0.000
60	A	153	HIS	0	0.029	0.027	29.064	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	154	TRP	0	-0.061	-0.029	32.185	0.009	0.009	0.000	0.000	0.000	0.000
62	A	155	MET	0	-0.042	-0.007	30.000	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	156	GLY	0	0.053	0.013	31.007	0.002	0.002	0.000	0.000	0.000	0.000
64	A	157	LEU	0	-0.082	-0.035	32.682	0.005	0.005	0.000	0.000	0.000	0.000
65	A	158	VAL	0	0.042	0.003	34.671	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	159	HIS	0	-0.074	-0.036	38.458	0.005	0.005	0.000	0.000	0.000	0.000
67	A	160	ILE	0	0.017	0.005	40.997	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	161	PRO	0	0.075	0.038	43.518	0.004	0.004	0.000	0.000	0.000	0.000
69	A	162	THR	0	-0.065	-0.030	46.984	0.001	0.001	0.000	0.000	0.000	0.000
70	A	163	ASN	0	-0.004	-0.003	43.904	0.001	0.001	0.000	0.000	0.000	0.000
71	A	164	GLY	0	0.045	0.033	44.944	0.003	0.003	0.000	0.000	0.000	0.000
72	A	165	SER	0	-0.093	-0.051	40.425	0.002	0.002	0.000	0.000	0.000	0.000
73	A	166	TRP	0	0.034	0.014	36.867	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	167	GLN	0	0.015	-0.007	35.625	0.002	0.002	0.000	0.000	0.000	0.000
75	A	168	TRP	0	0.011	0.004	30.066	-0.010	-0.010	0.000	0.000	0.000	0.000
76	A	169	GLU	-1	-0.736	-0.887	32.036	-0.078	-0.078	0.000	0.000	0.000	0.000
77	A	170	ASP	-1	-0.807	-0.840	30.022	-0.032	-0.032	0.000	0.000	0.000	0.000
78	A	171	GLY	0	0.020	0.021	33.344	0.004	0.004	0.000	0.000	0.000	0.000
79	A	172	SER	0	-0.117	-0.080	31.368	0.009	0.009	0.000	0.000	0.000	0.000
80	A	173	ILE	0	0.030	0.003	33.601	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	174	LEU	0	-0.041	-0.014	31.379	0.001	0.001	0.000	0.000	0.000	0.000
82	A	175	SER	0	-0.019	-0.006	29.615	0.007	0.007	0.000	0.000	0.000	0.000
83	A	176	PRO	0	0.040	0.001	31.727	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	177	ASN	0	0.005	-0.004	28.517	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	178	LEU	0	0.007	0.022	26.068	0.007	0.007	0.000	0.000	0.000	0.000
86	A	179	LEU	0	0.022	0.005	28.621	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	180	THR	0	-0.048	-0.014	31.257	0.008	0.008	0.000	0.000	0.000	0.000
88	A	181	ILE	0	-0.003	0.003	34.148	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	182	ILE	0	-0.051	-0.028	36.750	0.004	0.004	0.000	0.000	0.000	0.000
90	A	183	GLU	-1	-0.768	-0.884	39.260	-0.023	-0.023	0.000	0.000	0.000	0.000
91	A	184	MET	0	-0.033	-0.028	41.855	0.001	0.001	0.000	0.000	0.000	0.000
92	A	185	GLN	0	-0.068	-0.046	44.742	0.000	0.000	0.000	0.000	0.000	0.000
93	A	186	LYS	1	0.902	0.960	44.530	0.027	0.027	0.000	0.000	0.000	0.000
94	A	187	GLY	0	0.014	0.001	44.657	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	188	ASP	-1	-0.863	-0.917	42.649	-0.024	-0.024	0.000	0.000	0.000	0.000
96	A	189	CYS	0	0.021	0.030	38.611	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	190	ALA	0	0.016	0.011	34.795	0.001	0.001	0.000	0.000	0.000	0.000
98	A	191	LEU	0	0.017	0.009	34.264	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	192	TYR	0	-0.032	-0.052	25.761	0.014	0.014	0.000	0.000	0.000	0.000
100	A	193	ALA	0	0.020	-0.003	30.624	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	194	SER	0	-0.066	-0.033	26.659	0.013	0.013	0.000	0.000	0.000	0.000
102	A	195	SER	0	-0.016	-0.018	26.576	0.011	0.011	0.000	0.000	0.000	0.000
103	A	196	PHE	0	-0.037	-0.009	22.379	0.010	0.010	0.000	0.000	0.000	0.000
104	A	197	LYS	1	0.936	0.971	28.434	0.028	0.028	0.000	0.000	0.000	0.000
105	A	198	GLY	0	0.050	0.015	31.782	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	199	TYR	0	-0.014	-0.009	34.257	0.008	0.008	0.000	0.000	0.000	0.000
107	A	200	ILE	0	-0.006	0.009	37.198	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	201	GLU	-1	-0.853	-0.920	39.783	-0.041	-0.041	0.000	0.000	0.000	0.000
109	A	202	ASN	0	0.028	0.015	41.531	0.000	0.000	0.000	0.000	0.000	0.000
110	A	204	SER	0	-0.055	-0.049	41.899	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	205	THR	0	-0.003	-0.006	41.626	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	206	PRO	0	-0.009	-0.016	40.498	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	207	ASN	0	-0.035	-0.025	36.043	0.002	0.002	0.000	0.000	0.000	0.000
114	A	208	THR	0	0.040	0.039	31.942	0.001	0.001	0.000	0.000	0.000	0.000
115	A	209	TYR	0	-0.027	-0.024	31.447	0.011	0.011	0.000	0.000	0.000	0.000
116	A	210	ILE	0	-0.002	0.005	25.391	-0.012	-0.012	0.000	0.000	0.000	0.000
117	A	212	MET	0	-0.049	-0.026	21.611	-0.011	-0.011	0.000	0.000	0.000	0.000
118	A	213	GLN	0	-0.021	-0.024	22.715	-0.007	-0.007	0.000	0.000	0.000	0.000
119	A	214	ARG	1	0.898	0.953	19.324	0.025	0.025	0.000	0.000	0.000	0.000
120	A	215	THR	0	0.056	0.030	17.033	-0.003	-0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:92:THR)