FMO DATABASE

FMODB ID: 3QMVL

Calculation Name: 3OSG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3OSG

Chain ID: A

ChEMBL ID:

UniProt ID: Q58HP3

Base Structure: X-ray

Registration Date: 2023-03-14

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	111
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-865937.719822
FMO2-HF: Nuclear repulsion	820970.612907
FMO2-HF: Total energy	-44967.106915
FMO2-MP2: Total energy	-45099.760339

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:40:VAL)

Summations of interaction energy for fragment #1(A:40:VAL)

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.
-24.096	-15.797	11.37	-6.877	-12.792	-0.012

Interaction energy analysis for fragmet #1(A:40:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.014 / q_NPA : -0.002

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	42	VAL	0	0.015	0.029	3.698	-0.777	1.277	0.010	-0.938	-1.126	0.000
4	A	43	ASN	0	0.039	0.023	6.030	0.060	0.060	0.000	0.000	0.000	0.000
5	A	44	LEU	0	-0.038	-0.010	6.407	-0.167	-0.167	0.000	0.000	0.000	0.000
6	A	45	LYN	0	0.023	0.004	9.680	0.153	0.153	0.000	0.000	0.000	0.000
7	A	46	ALA	0	0.092	0.038	7.853	-0.323	-0.323	0.000	0.000	0.000	0.000
8	A	47	ALA	0	-0.014	0.002	3.467	0.282	0.574	0.008	-0.085	-0.215	0.000
9	A	48	LYS	1	0.942	0.960	5.347	0.890	0.941	-0.001	-0.002	-0.048	0.000
10	A	49	LYS	1	0.872	0.919	5.268	-0.589	-0.589	0.000	0.000	0.000	0.000
11	A	50	GLN	0	0.033	0.030	2.410	-0.479	1.390	1.833	-1.624	-2.077	-0.008
12	A	51	LYS	1	0.988	1.001	2.249	-13.025	-12.810	6.276	-2.189	-4.303	0.019
13	A	52	PHE	0	0.032	0.013	2.597	-4.659	-2.865	1.704	-1.130	-2.368	-0.019
14	A	53	THR	0	0.009	-0.007	2.556	-0.651	0.195	1.095	-0.432	-1.509	-0.004
15	A	54	PRO	0	0.042	0.014	4.469	0.137	0.189	0.000	-0.021	-0.031	0.000
16	A	55	GLU	-1	-0.828	-0.920	7.129	-0.198	-0.198	0.000	0.000	0.000	0.000
17	A	56	GLU	-1	-0.781	-0.848	3.829	-0.426	-0.027	0.007	-0.123	-0.283	-0.001
18	A	57	ASP	-1	-0.740	-0.851	8.110	1.116	1.116	0.000	0.000	0.000	0.000
19	A	58	GLU	-1	-0.817	-0.883	10.063	0.160	0.160	0.000	0.000	0.000	0.000
20	A	59	MET	0	-0.025	-0.001	10.803	-0.023	-0.023	0.000	0.000	0.000	0.000
21	A	60	LEU	0	-0.053	-0.014	10.588	0.005	0.005	0.000	0.000	0.000	0.000
22	A	61	LYS	1	0.853	0.906	13.025	-0.344	-0.344	0.000	0.000	0.000	0.000
23	A	62	ARG	1	0.879	0.929	15.260	-0.100	-0.100	0.000	0.000	0.000	0.000
24	A	63	ALA	0	0.027	0.023	15.419	-0.017	-0.017	0.000	0.000	0.000	0.000
25	A	64	VAL	0	-0.009	-0.018	16.710	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	65	ALA	0	-0.059	-0.030	18.987	-0.014	-0.014	0.000	0.000	0.000	0.000
27	A	66	GLN	0	-0.023	0.005	20.418	-0.017	-0.017	0.000	0.000	0.000	0.000
28	A	67	HIS	0	-0.003	-0.008	19.310	-0.007	-0.007	0.000	0.000	0.000	0.000
29	A	68	GLY	0	0.034	0.020	22.172	0.002	0.002	0.000	0.000	0.000	0.000
30	A	69	SER	0	-0.017	-0.027	20.561	0.022	0.022	0.000	0.000	0.000	0.000
31	A	70	ASP	-1	-0.810	-0.884	21.604	0.152	0.152	0.000	0.000	0.000	0.000
32	A	71	TRP	0	0.003	-0.033	16.003	0.018	0.018	0.000	0.000	0.000	0.000
33	A	72	LYS	1	0.923	0.958	16.758	-0.113	-0.113	0.000	0.000	0.000	0.000
34	A	73	MET	0	0.039	0.030	17.914	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	74	ILE	0	0.009	0.007	14.365	0.000	0.000	0.000	0.000	0.000	0.000
36	A	75	ALA	0	-0.036	-0.024	13.252	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	76	ALA	0	-0.012	0.007	13.543	-0.013	-0.013	0.000	0.000	0.000	0.000
38	A	77	THR	0	-0.032	-0.016	14.201	-0.027	-0.027	0.000	0.000	0.000	0.000
39	A	78	PHE	0	-0.021	-0.022	8.393	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	79	PRO	0	0.034	0.014	9.463	0.037	0.037	0.000	0.000	0.000	0.000
41	A	80	ASN	0	-0.025	-0.011	5.729	-0.128	-0.128	0.000	0.000	0.000	0.000
42	A	81	ARG	1	0.720	0.831	2.349	-2.013	-1.286	0.438	-0.333	-0.832	0.001
43	A	82	ASN	0	0.077	0.038	9.260	-0.059	-0.059	0.000	0.000	0.000	0.000
44	A	83	ALA	0	0.092	0.036	12.588	0.069	0.069	0.000	0.000	0.000	0.000
45	A	84	ARG	1	0.839	0.912	13.731	-0.529	-0.529	0.000	0.000	0.000	0.000
46	A	85	GLN	0	0.005	-0.009	7.818	-0.106	-0.106	0.000	0.000	0.000	0.000
47	A	86	CYS	0	0.015	0.022	11.542	0.092	0.092	0.000	0.000	0.000	0.000
48	A	87	ARG	1	0.917	0.950	12.416	-0.378	-0.378	0.000	0.000	0.000	0.000
49	A	88	ASP	-1	-0.817	-0.880	13.692	0.535	0.535	0.000	0.000	0.000	0.000
50	A	89	ARG	1	0.787	0.870	8.401	-1.214	-1.214	0.000	0.000	0.000	0.000
51	A	90	TRP	0	0.107	0.038	12.134	-0.014	-0.014	0.000	0.000	0.000	0.000
52	A	91	LYS	1	0.819	0.879	15.122	-0.420	-0.420	0.000	0.000	0.000	0.000
53	A	92	ASN	0	-0.007	0.001	14.891	-0.104	-0.104	0.000	0.000	0.000	0.000
54	A	93	TYR	0	-0.016	-0.017	12.301	0.093	0.093	0.000	0.000	0.000	0.000
55	A	94	LEU	0	-0.056	0.002	11.131	-0.031	-0.031	0.000	0.000	0.000	0.000
56	A	95	ALA	0	0.028	0.036	15.135	-0.052	-0.052	0.000	0.000	0.000	0.000
57	A	96	PRO	0	0.028	0.000	18.752	0.011	0.011	0.000	0.000	0.000	0.000
58	A	97	SER	0	0.005	0.012	21.260	-0.015	-0.015	0.000	0.000	0.000	0.000
59	A	98	ILE	0	-0.088	-0.035	17.189	0.001	0.001	0.000	0.000	0.000	0.000
60	A	99	SER	0	0.035	0.034	20.377	-0.012	-0.012	0.000	0.000	0.000	0.000
61	A	100	HIS	0	-0.028	-0.027	15.361	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	101	THR	0	0.001	0.008	18.696	0.001	0.001	0.000	0.000	0.000	0.000
63	A	102	PRO	0	0.004	-0.009	21.278	0.024	0.024	0.000	0.000	0.000	0.000
64	A	103	TRP	0	0.007	-0.002	20.642	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	104	THR	0	-0.003	-0.026	24.066	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	105	ALA	0	0.024	0.010	27.779	0.006	0.006	0.000	0.000	0.000	0.000
67	A	106	GLU	-1	-0.817	-0.893	30.774	0.141	0.141	0.000	0.000	0.000	0.000
68	A	107	GLU	-1	-0.775	-0.870	25.595	0.247	0.247	0.000	0.000	0.000	0.000
69	A	108	ASP	-1	-0.750	-0.865	27.161	0.215	0.215	0.000	0.000	0.000	0.000
70	A	109	ALA	0	0.000	0.001	29.599	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	110	LEU	0	-0.004	0.007	30.849	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	111	LEU	0	-0.044	-0.016	26.044	0.001	0.001	0.000	0.000	0.000	0.000
73	A	112	VAL	0	0.006	-0.013	30.353	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	113	GLN	0	0.056	0.049	32.678	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	114	LYS	1	0.821	0.886	31.799	-0.133	-0.133	0.000	0.000	0.000	0.000
76	A	115	ILE	0	-0.031	-0.018	28.036	0.003	0.003	0.000	0.000	0.000	0.000
77	A	116	GLN	0	-0.034	-0.018	32.401	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	117	GLU	-1	-0.825	-0.861	35.979	0.118	0.118	0.000	0.000	0.000	0.000
79	A	118	TYR	0	-0.042	-0.043	33.056	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	119	GLY	0	0.066	0.044	32.847	0.002	0.002	0.000	0.000	0.000	0.000
81	A	120	ARG	1	0.930	0.941	24.879	-0.189	-0.189	0.000	0.000	0.000	0.000
82	A	121	GLN	0	-0.016	-0.002	27.914	0.015	0.015	0.000	0.000	0.000	0.000
83	A	122	TRP	0	0.025	-0.011	24.051	0.004	0.004	0.000	0.000	0.000	0.000
84	A	123	ALA	0	0.003	-0.007	26.103	0.006	0.006	0.000	0.000	0.000	0.000
85	A	124	ILE	0	0.002	0.017	27.053	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	125	ILE	0	0.019	0.016	28.271	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	126	ALA	0	-0.012	-0.023	25.187	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	127	LYS	1	0.911	0.967	27.028	-0.189	-0.189	0.000	0.000	0.000	0.000
89	A	128	PHE	0	-0.001	0.007	29.929	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	129	PHE	0	-0.023	-0.009	26.192	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	130	PRO	0	0.026	0.018	26.080	0.021	0.021	0.000	0.000	0.000	0.000
92	A	131	GLY	0	0.048	0.028	23.360	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	132	ARG	1	0.760	0.848	20.786	-0.273	-0.273	0.000	0.000	0.000	0.000
94	A	133	THR	0	-0.009	-0.023	18.875	-0.009	-0.009	0.000	0.000	0.000	0.000
95	A	134	ASP	-1	-0.768	-0.883	21.049	0.385	0.385	0.000	0.000	0.000	0.000
96	A	135	ILE	0	-0.060	-0.038	15.617	0.007	0.007	0.000	0.000	0.000	0.000
97	A	136	HIS	0	-0.009	0.007	16.321	-0.023	-0.023	0.000	0.000	0.000	0.000
98	A	137	ILE	0	0.037	0.028	19.755	-0.012	-0.012	0.000	0.000	0.000	0.000
99	A	138	LYS	1	0.885	0.950	16.890	-0.518	-0.518	0.000	0.000	0.000	0.000
100	A	139	ASN	0	-0.008	-0.004	15.637	-0.043	-0.043	0.000	0.000	0.000	0.000
101	A	140	ARG	1	0.835	0.911	19.787	-0.272	-0.272	0.000	0.000	0.000	0.000
102	A	141	TRP	0	0.094	0.040	22.632	-0.022	-0.022	0.000	0.000	0.000	0.000
103	A	142	VAL	0	-0.007	0.018	20.180	-0.019	-0.019	0.000	0.000	0.000	0.000
104	A	143	THR	0	-0.032	-0.007	21.306	-0.010	-0.010	0.000	0.000	0.000	0.000
105	A	144	ILE	0	-0.017	-0.009	23.373	-0.020	-0.020	0.000	0.000	0.000	0.000
106	A	145	SER	0	-0.012	-0.025	25.796	-0.015	-0.015	0.000	0.000	0.000	0.000
107	A	146	ASN	0	-0.020	-0.019	23.792	-0.027	-0.027	0.000	0.000	0.000	0.000
108	A	147	LYS	1	0.832	0.911	26.028	-0.201	-0.201	0.000	0.000	0.000	0.000
109	A	148	LEU	0	-0.031	-0.009	29.029	-0.010	-0.010	0.000	0.000	0.000	0.000
110	A	149	GLY	0	0.044	0.041	30.594	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	150	ILE	0	-0.110	-0.053	29.407	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:40:VAL)