FMO DATABASE

FMODB ID: N9RMQ

Calculation Name: 1O5L-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1O5L

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X0Q3

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	129
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1108035.422186
FMO2-HF: Nuclear repulsion	1057227.591243
FMO2-HF: Total energy	-50807.830943
FMO2-MP2: Total energy	-50958.176299

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:MET)

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

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.
-24.379	-18.391	31.639	-12.29	-25.334	-0.038

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.015 / q_NPA : 0.023

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

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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	0.021	-0.003	2.538	0.199	4.150	2.495	-1.850	-4.596	-0.011
4	A	4	LYS	1	0.850	0.921	3.940	-0.584	-0.406	0.004	0.053	-0.234	0.000
5	A	5	LYS	1	0.819	0.903	2.226	-13.174	-18.089	15.924	-5.597	-5.412	0.045
6	A	6	LEU	0	0.004	-0.003	4.382	-0.975	-0.704	0.002	-0.035	-0.237	0.000
7	A	7	LEU	0	0.000	-0.002	7.627	-0.429	-0.429	0.000	0.000	0.000	0.000
8	A	8	PRO	0	-0.034	-0.020	10.297	-0.148	-0.148	0.000	0.000	0.000	0.000
9	A	9	CYS	0	-0.046	-0.009	8.850	-0.056	-0.056	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.016	-0.001	12.226	-0.111	-0.111	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.794	0.918	14.571	0.101	0.101	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.023	-0.009	14.810	0.000	0.000	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.009	0.004	17.148	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.010	-0.017	18.264	0.007	0.007	0.000	0.000	0.000	0.000
15	A	15	PHE	0	0.041	0.037	19.200	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.842	0.897	22.681	-0.026	-0.026	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.855	0.916	25.193	-0.007	-0.007	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.011	0.008	25.728	0.005	0.005	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.856	-0.918	25.059	-0.008	-0.008	0.000	0.000	0.000	0.000
20	A	20	ILE	0	0.002	-0.001	24.302	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.073	-0.030	18.445	0.008	0.008	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.781	0.873	20.117	0.167	0.167	0.000	0.000	0.000	0.000
23	A	23	HIS	0	0.009	0.002	22.835	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	24	GLN	0	0.015	0.007	24.735	-0.021	-0.021	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.906	-0.955	25.741	-0.159	-0.159	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.843	-0.901	24.036	-0.130	-0.130	0.000	0.000	0.000	0.000
27	A	27	PRO	0	-0.020	-0.015	23.695	-0.023	-0.023	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.002	0.021	16.968	0.003	0.003	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.825	-0.901	19.859	-0.194	-0.194	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.782	-0.873	16.327	-0.112	-0.112	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.007	-0.005	10.101	-0.028	-0.028	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.000	0.008	12.577	0.075	0.075	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.003	-0.004	7.017	-0.124	-0.124	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.009	0.016	10.614	0.143	0.143	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.004	-0.012	9.911	-0.026	-0.026	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.821	-0.928	11.804	0.402	0.402	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.015	0.025	14.752	-0.020	-0.020	0.000	0.000	0.000	0.000
38	A	38	THR	0	0.004	-0.020	16.531	-0.025	-0.025	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.056	-0.018	15.916	0.017	0.017	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.805	0.891	18.962	0.087	0.087	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.020	-0.014	18.813	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.846	-0.938	22.017	-0.101	-0.101	0.000	0.000	0.000	0.000
43	A	43	HIS	0	0.028	0.022	25.580	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	44	VAL	0	-0.030	-0.022	27.810	0.014	0.014	0.000	0.000	0.000	0.000
45	A	45	SER	0	0.013	-0.003	30.909	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.867	-0.948	33.827	-0.110	-0.110	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.104	-0.052	36.807	0.005	0.005	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.015	0.015	35.374	0.006	0.006	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.847	0.924	33.962	0.087	0.087	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.085	0.051	29.459	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.059	-0.023	29.304	0.012	0.012	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.793	-0.888	24.025	-0.124	-0.124	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.110	-0.048	22.817	0.004	0.004	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.850	-0.921	19.197	-0.268	-0.268	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.857	-0.909	19.247	-0.072	-0.072	0.000	0.000	0.000	0.000
56	A	56	ILE	0	-0.023	-0.004	13.330	-0.047	-0.047	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.837	0.897	13.928	0.156	0.156	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.037	-0.004	11.286	-0.094	-0.094	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.034	-0.018	6.755	0.102	0.102	0.000	0.000	0.000	0.000
60	A	60	GLN	0	0.042	0.019	7.267	-0.304	-0.304	0.000	0.000	0.000	0.000
61	A	61	ILE	0	-0.001	-0.001	6.033	0.177	0.177	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.002	-0.008	9.678	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.028	0.011	13.517	0.003	0.003	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.011	-0.018	10.895	0.094	0.094	0.000	0.000	0.000	0.000
65	A	65	GLY	0	-0.009	-0.009	12.661	0.002	0.002	0.000	0.000	0.000	0.000
66	A	66	PHE	0	-0.003	-0.006	15.234	0.040	0.040	0.000	0.000	0.000	0.000
67	A	67	ILE	0	0.008	0.010	12.203	0.040	0.040	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.010	-0.017	12.182	0.038	0.038	0.000	0.000	0.000	0.000
69	A	69	SER	0	0.002	0.013	17.589	0.002	0.002	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.011	-0.006	20.882	0.010	0.010	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.879	-0.926	24.296	-0.180	-0.180	0.000	0.000	0.000	0.000
72	A	72	PRO	0	-0.017	0.026	19.955	0.007	0.007	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.838	0.875	22.000	0.192	0.192	0.000	0.000	0.000	0.000
74	A	74	PHE	0	0.004	-0.007	17.127	-0.036	-0.036	0.000	0.000	0.000	0.000
75	A	75	PRO	0	-0.009	-0.001	20.512	0.025	0.025	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.048	-0.025	21.483	0.012	0.012	0.000	0.000	0.000	0.000
77	A	77	ASN	0	0.010	0.009	23.083	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.016	-0.012	18.267	-0.017	-0.017	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.034	0.016	21.649	0.018	0.018	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.030	0.018	21.119	-0.011	-0.011	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.042	0.017	21.415	0.009	0.009	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.933	-0.954	20.166	0.047	0.047	0.000	0.000	0.000	0.000
83	A	83	ASN	0	0.004	0.010	22.281	-0.012	-0.012	0.000	0.000	0.000	0.000
84	A	84	SER	0	0.017	0.004	17.860	0.011	0.011	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.838	0.904	15.878	-0.226	-0.226	0.000	0.000	0.000	0.000
86	A	86	ILE	0	0.022	0.015	13.905	-0.015	-0.015	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.003	0.023	9.136	0.035	0.035	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.059	-0.058	12.977	-0.094	-0.094	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.028	0.021	9.208	0.052	0.052	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.030	0.015	13.349	-0.074	-0.074	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.870	0.938	14.219	0.324	0.324	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.865	-0.946	13.732	-0.367	-0.367	0.000	0.000	0.000	0.000
93	A	93	VAL	0	-0.014	0.001	11.657	-0.027	-0.027	0.000	0.000	0.000	0.000
94	A	94	PHE	0	0.026	0.008	6.855	-0.051	-0.051	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.016	0.011	9.375	-0.188	-0.188	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.838	-0.910	11.388	-0.351	-0.351	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.006	-0.004	6.820	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.011	-0.003	6.421	-0.279	-0.279	0.000	0.000	0.000	0.000
99	A	99	MET	0	-0.071	-0.027	8.113	-0.068	-0.068	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.752	0.865	9.112	0.407	0.407	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.820	-0.900	2.608	-7.340	-5.450	0.946	-1.293	-1.542	-0.017
102	A	102	ARG	1	0.982	0.975	5.630	0.603	0.603	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.847	-0.931	2.375	-1.328	2.722	5.903	-3.754	-6.199	-0.038
104	A	104	LEU	0	0.002	-0.005	2.205	-3.741	-2.446	4.233	-1.770	-3.758	-0.007
105	A	105	LEU	0	-0.003	0.001	2.721	3.492	0.637	0.264	2.938	-0.348	-0.001
106	A	106	LEU	0	-0.040	-0.028	6.362	0.361	0.361	0.000	0.000	0.000	0.000
107	A	107	PHE	0	0.001	0.003	2.517	-2.486	-0.444	1.869	-0.978	-2.932	-0.009
108	A	108	PHE	0	0.035	0.007	4.978	0.630	0.711	-0.001	-0.004	-0.076	0.000
109	A	109	LEU	0	0.023	0.011	6.886	0.393	0.393	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.956	0.998	7.660	1.450	1.450	0.000	0.000	0.000	0.000
111	A	111	ASP	-1	-0.839	-0.899	7.600	-1.098	-1.098	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.033	0.016	9.464	0.255	0.255	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.046	-0.040	12.370	0.188	0.188	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.848	-0.894	11.549	-0.517	-0.517	0.000	0.000	0.000	0.000
115	A	115	HIS	0	-0.055	-0.024	11.412	0.217	0.217	0.000	0.000	0.000	0.000
116	A	116	PHE	0	-0.022	-0.008	15.422	0.091	0.091	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.759	0.833	15.641	0.534	0.534	0.000	0.000	0.000	0.000
118	A	118	VAL	0	0.032	0.017	17.036	0.059	0.059	0.000	0.000	0.000	0.000
119	A	119	VAL	0	-0.017	-0.011	19.470	0.052	0.052	0.000	0.000	0.000	0.000
120	A	120	SER	0	0.020	0.011	21.459	0.037	0.037	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.887	-0.936	21.121	-0.306	-0.306	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.945	0.975	23.672	0.252	0.252	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.017	0.012	25.536	0.024	0.024	0.000	0.000	0.000	0.000
124	A	124	PHE	0	0.049	0.030	25.757	0.021	0.021	0.000	0.000	0.000	0.000
125	A	125	PHE	0	0.000	0.023	25.513	0.018	0.018	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.011	0.006	29.338	0.014	0.014	0.000	0.000	0.000	0.000
127	A	127	THR	0	-0.053	-0.053	31.143	0.013	0.013	0.000	0.000	0.000	0.000
128	A	128	THR	0	-0.045	-0.036	32.156	0.011	0.011	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.851	0.944	34.689	0.135	0.135	0.000	0.000	0.000	0.000

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