FMO DATABASE

FMODB ID: 3JMZL

Calculation Name: 2QGO-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QGO

Chain ID: A

ChEMBL ID:

UniProt ID: Q5FLQ3

Base Structure: X-ray

Registration Date: 2023-09-23

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	114
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-906848.676978
FMO2-HF: Nuclear repulsion	862647.554789
FMO2-HF: Total energy	-44201.122189
FMO2-MP2: Total energy	-44330.475766

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:4:LEU)

Summations of interaction energy for fragment #1(A:4:LEU)

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.
-10.421	-1.601	3.795	-3.433	-9.181	-0.007

Interaction energy analysis for fragmet #1(A:4:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.009 / q_NPA : -0.010

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	6	ILE	0	0.001	0.000	3.769	-1.237	0.637	-0.031	-0.851	-0.992	0.002
4	A	7	LYS	1	0.884	0.934	6.350	0.066	0.066	0.000	0.000	0.000	0.000
5	A	8	PHE	0	-0.003	-0.004	9.599	-0.040	-0.040	0.000	0.000	0.000	0.000
6	A	9	THR	0	0.042	-0.011	12.819	0.039	0.039	0.000	0.000	0.000	0.000
7	A	10	ASP	-1	-0.861	-0.940	16.139	-0.075	-0.075	0.000	0.000	0.000	0.000
8	A	11	ASN	0	-0.009	-0.002	19.367	0.001	0.001	0.000	0.000	0.000	0.000
9	A	12	ALA	0	-0.012	0.007	15.155	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	13	VAL	0	-0.002	-0.007	15.797	-0.013	-0.013	0.000	0.000	0.000	0.000
11	A	14	ASP	-1	-0.840	-0.923	17.699	-0.094	-0.094	0.000	0.000	0.000	0.000
12	A	15	TYR	0	-0.040	-0.017	18.629	0.002	0.002	0.000	0.000	0.000	0.000
13	A	16	LEU	0	0.035	-0.001	14.126	0.002	0.002	0.000	0.000	0.000	0.000
14	A	17	LYS	1	0.868	0.933	18.752	0.106	0.106	0.000	0.000	0.000	0.000
15	A	18	ARG	1	0.909	0.970	21.551	0.124	0.124	0.000	0.000	0.000	0.000
16	A	19	ARG	1	0.863	0.941	20.820	0.188	0.188	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.953	-0.969	22.675	-0.122	-0.122	0.000	0.000	0.000	0.000
18	A	21	ILE	0	-0.011	-0.021	16.869	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	22	LEU	0	-0.023	-0.009	15.145	-0.023	-0.023	0.000	0.000	0.000	0.000
20	A	23	ASP	-1	-0.890	-0.941	16.240	-0.181	-0.181	0.000	0.000	0.000	0.000
21	A	24	LYS	1	0.829	0.930	17.310	0.171	0.171	0.000	0.000	0.000	0.000
22	A	25	ILE	0	-0.071	-0.024	13.494	-0.021	-0.021	0.000	0.000	0.000	0.000
23	A	26	LEU	0	0.013	-0.006	11.452	0.007	0.007	0.000	0.000	0.000	0.000
24	A	27	ILE	0	-0.011	-0.003	10.129	-0.054	-0.054	0.000	0.000	0.000	0.000
25	A	28	LEU	0	0.011	0.021	6.019	0.071	0.071	0.000	0.000	0.000	0.000
26	A	29	ILE	0	-0.030	-0.006	7.879	-0.146	-0.146	0.000	0.000	0.000	0.000
27	A	30	THR	0	-0.012	-0.013	9.158	0.053	0.053	0.000	0.000	0.000	0.000
28	A	31	ASP	-1	-0.820	-0.906	11.598	-0.283	-0.283	0.000	0.000	0.000	0.000
29	A	32	ASP	-1	-0.871	-0.937	15.358	-0.321	-0.321	0.000	0.000	0.000	0.000
30	A	33	GLY	0	-0.042	-0.014	17.092	0.032	0.032	0.000	0.000	0.000	0.000
31	A	34	GLY	0	-0.029	-0.010	18.203	0.024	0.024	0.000	0.000	0.000	0.000
32	A	35	GLY	0	-0.001	0.005	16.179	0.006	0.006	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.776	0.844	16.319	0.297	0.297	0.000	0.000	0.000	0.000
34	A	37	TYR	0	-0.122	-0.104	14.852	0.037	0.037	0.000	0.000	0.000	0.000
35	A	38	SER	0	-0.054	-0.018	17.884	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	39	ILE	0	-0.020	-0.019	18.874	0.024	0.024	0.000	0.000	0.000	0.000
37	A	49	HIS	1	0.824	0.907	13.600	0.345	0.345	0.000	0.000	0.000	0.000
38	A	50	PHE	0	-0.024	-0.040	7.876	-0.048	-0.048	0.000	0.000	0.000	0.000
39	A	51	SER	0	0.019	0.005	12.444	0.051	0.051	0.000	0.000	0.000	0.000
40	A	52	ILE	0	-0.035	-0.023	10.431	-0.069	-0.069	0.000	0.000	0.000	0.000
41	A	53	ILE	0	0.010	0.007	13.286	0.068	0.068	0.000	0.000	0.000	0.000
42	A	54	TRP	0	0.004	0.005	14.424	-0.020	-0.020	0.000	0.000	0.000	0.000
43	A	55	LEU	0	-0.012	-0.007	16.022	0.027	0.027	0.000	0.000	0.000	0.000
44	A	56	ASP	-1	-0.814	-0.917	18.469	-0.169	-0.169	0.000	0.000	0.000	0.000
45	A	57	LYS	1	0.884	0.933	18.823	0.165	0.165	0.000	0.000	0.000	0.000
46	A	58	VAL	0	0.009	0.007	13.936	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	59	ASP	-1	-0.731	-0.833	14.457	-0.261	-0.261	0.000	0.000	0.000	0.000
48	A	60	PRO	0	-0.023	-0.019	14.006	-0.031	-0.031	0.000	0.000	0.000	0.000
49	A	61	ASP	-1	-0.821	-0.883	14.246	-0.260	-0.260	0.000	0.000	0.000	0.000
50	A	62	TYR	0	-0.098	-0.050	9.601	-0.012	-0.012	0.000	0.000	0.000	0.000
51	A	63	PRO	0	0.009	0.004	9.670	-0.012	-0.012	0.000	0.000	0.000	0.000
52	A	64	VAL	0	-0.021	-0.008	3.697	-0.198	0.051	0.005	-0.038	-0.217	0.000
53	A	65	LYS	1	0.932	0.967	5.968	0.239	0.239	0.000	0.000	0.000	0.000
54	A	66	ILE	0	0.012	0.025	2.270	-1.880	-0.693	1.302	-0.578	-1.911	0.000
55	A	67	ALA	0	0.000	0.000	3.848	0.205	0.551	0.002	-0.047	-0.301	0.000
56	A	68	ASN	0	0.032	0.005	5.951	-0.039	-0.039	0.000	0.000	0.000	0.000
57	A	69	GLU	-1	-0.878	-0.931	8.789	0.246	0.246	0.000	0.000	0.000	0.000
58	A	70	GLN	0	-0.012	-0.021	11.935	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	71	ASN	0	-0.065	-0.022	13.259	0.008	0.008	0.000	0.000	0.000	0.000
60	A	72	VAL	0	0.050	0.036	10.840	0.012	0.012	0.000	0.000	0.000	0.000
61	A	73	LYS	1	0.845	0.925	10.739	0.141	0.141	0.000	0.000	0.000	0.000
62	A	74	ILE	0	0.018	0.014	6.994	0.037	0.037	0.000	0.000	0.000	0.000
63	A	75	TYR	0	-0.052	-0.040	7.116	-0.033	-0.033	0.000	0.000	0.000	0.000
64	A	76	THR	0	0.048	0.011	3.381	-0.375	-0.078	0.011	-0.054	-0.253	0.000
65	A	77	SER	0	0.005	-0.016	6.762	0.141	0.141	0.000	0.000	0.000	0.000
66	A	78	ASP	-1	-0.871	-0.944	6.194	-0.647	-0.647	0.000	0.000	0.000	0.000
67	A	79	PHE	0	0.013	0.008	6.889	-0.117	-0.117	0.000	0.000	0.000	0.000
68	A	80	ASP	-1	-0.722	-0.850	7.368	-0.779	-0.779	0.000	0.000	0.000	0.000
69	A	81	LYS	1	0.839	0.912	2.327	-0.912	0.065	1.303	-0.429	-1.851	0.001
70	A	82	THR	0	-0.085	-0.040	3.243	-2.072	-0.921	0.055	-0.557	-0.650	-0.005
71	A	83	MET	0	-0.008	0.008	5.896	0.226	0.226	0.000	0.000	0.000	0.000
72	A	84	LEU	0	-0.046	-0.007	2.841	-0.695	0.114	0.305	-0.218	-0.896	-0.001
73	A	85	GLY	0	0.085	0.037	4.113	-0.179	0.054	0.002	-0.059	-0.176	0.000
74	A	86	PRO	0	-0.060	-0.034	3.397	-1.132	-0.206	0.053	-0.360	-0.619	-0.002
75	A	87	ASN	0	-0.040	-0.039	4.226	-0.011	0.054	-0.001	-0.008	-0.055	0.000
76	A	88	MET	0	0.001	0.024	2.494	-1.059	-0.353	0.789	-0.234	-1.260	-0.002
77	A	89	VAL	0	0.004	-0.002	6.893	0.050	0.050	0.000	0.000	0.000	0.000
78	A	90	MET	0	-0.017	0.005	10.205	-0.028	-0.028	0.000	0.000	0.000	0.000
79	A	91	ASP	-1	-0.796	-0.886	11.978	-0.090	-0.090	0.000	0.000	0.000	0.000
80	A	92	TYR	0	-0.033	-0.028	15.741	-0.017	-0.017	0.000	0.000	0.000	0.000
81	A	93	ASN	0	-0.050	-0.035	18.941	0.028	0.028	0.000	0.000	0.000	0.000
82	A	94	ALA	0	0.039	0.020	21.811	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	95	GLY	0	-0.037	-0.011	24.163	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	96	SER	0	-0.045	-0.017	19.573	0.000	0.000	0.000	0.000	0.000	0.000
85	A	97	LEU	0	0.017	0.000	14.863	0.012	0.012	0.000	0.000	0.000	0.000
86	A	98	SER	0	-0.037	0.003	14.907	0.000	0.000	0.000	0.000	0.000	0.000
87	A	99	LEU	0	0.046	0.013	7.286	0.003	0.003	0.000	0.000	0.000	0.000
88	A	100	SER	0	-0.005	-0.004	10.190	0.043	0.043	0.000	0.000	0.000	0.000
89	A	101	SER	0	0.009	0.008	6.975	-0.102	-0.102	0.000	0.000	0.000	0.000
90	A	102	ASP	-1	-0.818	-0.893	8.851	0.588	0.588	0.000	0.000	0.000	0.000
91	A	103	GLU	-1	-0.980	-0.990	8.455	-0.118	-0.118	0.000	0.000	0.000	0.000
92	A	104	GLY	0	-0.015	0.007	11.639	-0.012	-0.012	0.000	0.000	0.000	0.000
93	A	105	LEU	0	-0.078	-0.057	11.544	-0.050	-0.050	0.000	0.000	0.000	0.000
94	A	106	LEU	0	-0.009	0.003	7.049	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	107	ASP	-1	-0.740	-0.866	11.442	-0.343	-0.343	0.000	0.000	0.000	0.000
96	A	108	GLY	0	0.000	0.010	13.893	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	109	SER	0	-0.067	-0.041	16.749	0.031	0.031	0.000	0.000	0.000	0.000
98	A	110	VAL	0	-0.026	0.005	12.557	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	111	ASP	-1	-0.837	-0.904	15.586	-0.238	-0.238	0.000	0.000	0.000	0.000
100	A	112	ILE	0	-0.035	-0.024	16.228	-0.033	-0.033	0.000	0.000	0.000	0.000
101	A	113	GLY	0	0.023	0.011	17.712	0.028	0.028	0.000	0.000	0.000	0.000
102	A	114	ASN	0	-0.030	-0.002	18.612	-0.019	-0.019	0.000	0.000	0.000	0.000
103	A	115	GLY	0	0.136	0.043	18.991	0.008	0.008	0.000	0.000	0.000	0.000
104	A	116	ALA	0	0.014	0.005	19.732	0.010	0.010	0.000	0.000	0.000	0.000
105	A	117	ALA	0	-0.075	-0.050	22.968	0.012	0.012	0.000	0.000	0.000	0.000
106	A	118	LEU	0	0.032	0.030	19.437	0.014	0.014	0.000	0.000	0.000	0.000
107	A	119	LEU	0	0.035	0.021	20.185	0.013	0.013	0.000	0.000	0.000	0.000
108	A	120	LYS	1	0.904	0.958	23.766	0.137	0.137	0.000	0.000	0.000	0.000
109	A	121	ALA	0	-0.001	-0.001	26.765	0.011	0.011	0.000	0.000	0.000	0.000
110	A	122	ASN	0	0.025	0.017	22.519	0.016	0.016	0.000	0.000	0.000	0.000
111	A	123	LYS	1	0.967	0.981	26.724	0.115	0.115	0.000	0.000	0.000	0.000
112	A	124	ASN	0	-0.062	-0.049	28.994	0.008	0.008	0.000	0.000	0.000	0.000
113	A	125	VAL	0	-0.026	0.009	29.387	0.007	0.007	0.000	0.000	0.000	0.000
114	A	126	GLN	0	-0.078	-0.025	27.990	0.008	0.008	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:LEU)