FMO DATABASE

FMODB ID: 39GGL

Calculation Name: 2Q3A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2Q3A

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-06-26

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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-966573.921668
FMO2-HF: Nuclear repulsion	920136.910045
FMO2-HF: Total energy	-46437.011623
FMO2-MP2: Total energy	-46572.654113

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:ASN)

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

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.
-36.336	-25.603	13.219	-10.286	-13.666	0.005

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

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 : -0.016

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	PHE	0	0.031	0.011	2.310	-12.243	-5.548	3.549	-4.650	-5.595	0.038
4	A	4	ARG	1	0.927	0.974	3.639	-1.591	-1.112	0.039	-0.137	-0.382	0.000
5	A	5	VAL	0	-0.006	0.001	5.491	-0.514	-0.514	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.065	-0.002	7.902	-0.473	-0.473	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.014	0.002	11.488	0.053	0.053	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.042	-0.003	9.162	-0.051	-0.051	0.000	0.000	0.000	0.000
9	A	9	GLY	0	-0.003	0.003	13.734	-0.043	-0.043	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.834	0.904	16.766	-0.345	-0.345	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.002	0.012	18.564	0.007	0.007	0.000	0.000	0.000	0.000
12	A	12	TRP	0	0.035	0.020	15.856	0.031	0.031	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.010	-0.026	22.784	-0.038	-0.038	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.035	0.003	25.937	0.012	0.012	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.011	0.012	27.584	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.865	-0.900	24.021	0.241	0.241	0.000	0.000	0.000	0.000
17	A	17	THR	0	-0.049	-0.041	22.907	0.002	0.002	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.009	0.000	17.786	0.010	0.010	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.863	-0.922	17.873	0.578	0.578	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.004	0.012	12.866	0.033	0.033	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.840	0.893	12.323	-0.765	-0.765	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.028	-0.009	6.881	-0.083	-0.083	0.000	0.000	0.000	0.000
23	A	23	GLN	0	-0.012	-0.011	8.076	-0.271	-0.271	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.010	-0.018	6.799	1.325	1.325	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.004	-0.012	5.677	-0.646	-0.646	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.006	0.010	7.198	-0.623	-0.623	0.000	0.000	0.000	0.000
27	A	27	SER	0	0.012	0.013	9.026	-0.009	-0.009	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.021	-0.017	11.841	-0.017	-0.017	0.000	0.000	0.000	0.000
29	A	29	PRO	0	-0.016	0.010	11.773	-0.040	-0.040	0.000	0.000	0.000	0.000
30	A	30	THR	0	0.013	-0.005	13.534	-0.049	-0.049	0.000	0.000	0.000	0.000
31	A	31	SER	0	-0.017	-0.012	13.624	-0.073	-0.073	0.000	0.000	0.000	0.000
32	A	32	GLY	0	-0.035	-0.016	14.303	0.080	0.080	0.000	0.000	0.000	0.000
33	A	33	CYS	0	-0.032	-0.003	10.325	0.181	0.181	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.010	-0.003	11.515	-0.191	-0.191	0.000	0.000	0.000	0.000
35	A	35	TRP	0	0.025	0.006	11.010	0.167	0.167	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.047	-0.032	9.573	-0.154	-0.154	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.012	-0.013	12.553	0.075	0.075	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.017	-0.009	12.625	-0.090	-0.090	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.007	0.019	14.394	0.021	0.021	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.902	0.926	17.088	-0.053	-0.053	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.007	0.007	19.079	0.004	0.004	0.000	0.000	0.000	0.000
42	A	42	THR	0	0.001	-0.012	18.754	-0.028	-0.028	0.000	0.000	0.000	0.000
43	A	43	ALA	0	-0.008	-0.001	18.285	0.014	0.014	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.024	0.042	16.711	0.021	0.021	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.985	0.978	16.082	0.046	0.046	0.000	0.000	0.000	0.000
46	A	46	PRO	0	-0.003	-0.010	12.435	0.043	0.043	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.016	0.026	14.462	0.011	0.011	0.000	0.000	0.000	0.000
48	A	48	PHE	0	-0.020	-0.013	14.814	0.037	0.037	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.000	0.008	15.473	-0.012	-0.012	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.002	-0.002	16.211	-0.027	-0.027	0.000	0.000	0.000	0.000
51	A	51	TYR	0	0.016	0.025	15.757	0.076	0.076	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.031	-0.011	15.087	-0.062	-0.062	0.000	0.000	0.000	0.000
53	A	53	SER	0	0.020	-0.017	16.416	0.026	0.026	0.000	0.000	0.000	0.000
54	A	54	GLN	0	-0.001	-0.006	18.482	0.030	0.030	0.000	0.000	0.000	0.000
55	A	55	ASN	0	0.002	0.010	21.704	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.969	0.992	23.181	-0.235	-0.235	0.000	0.000	0.000	0.000
57	A	57	PRO	0	0.024	0.015	20.976	0.015	0.015	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.819	0.906	20.739	-0.210	-0.210	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.035	0.014	20.161	0.030	0.030	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.015	0.007	20.149	-0.021	-0.021	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.824	-0.909	22.075	0.130	0.130	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.003	0.003	25.098	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.048	-0.015	20.643	0.001	0.001	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.751	-0.882	24.443	0.166	0.166	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.006	-0.004	24.414	0.015	0.015	0.000	0.000	0.000	0.000
66	A	66	GLN	0	-0.047	-0.002	25.945	0.014	0.014	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.733	0.857	25.231	-0.158	-0.158	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.002	0.000	19.150	0.031	0.031	0.000	0.000	0.000	0.000
69	A	69	SER	0	0.001	-0.004	21.262	-0.012	-0.012	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.061	0.014	18.489	0.044	0.044	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.908	0.961	18.045	-0.440	-0.440	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.977	1.003	15.948	-0.492	-0.492	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.035	-0.012	16.693	-0.089	-0.089	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.044	0.023	16.626	0.053	0.053	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.818	-0.894	12.329	1.011	1.011	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.025	-0.020	11.490	0.413	0.413	0.000	0.000	0.000	0.000
77	A	77	PHE	0	-0.013	-0.018	11.360	-0.306	-0.306	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.011	-0.017	12.975	0.145	0.145	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.002	0.024	14.855	-0.081	-0.081	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.053	-0.046	16.636	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.020	0.010	19.958	-0.024	-0.024	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.946	0.974	21.702	-0.218	-0.218	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.839	-0.921	25.381	0.132	0.132	0.000	0.000	0.000	0.000
84	A	84	PHE	0	-0.011	0.012	20.122	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.926	0.949	24.447	-0.145	-0.145	0.000	0.000	0.000	0.000
86	A	86	GLN	0	0.053	0.011	23.993	0.010	0.010	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.877	-0.930	23.644	0.107	0.107	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.017	-0.012	20.682	0.002	0.002	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.752	-0.839	19.050	0.096	0.096	0.000	0.000	0.000	0.000
90	A	90	GLY	0	-0.021	-0.017	16.752	-0.030	-0.030	0.000	0.000	0.000	0.000
91	A	91	TYR	0	-0.004	0.001	11.240	0.035	0.035	0.000	0.000	0.000	0.000
92	A	92	TYR	0	0.004	-0.004	11.836	-0.042	-0.042	0.000	0.000	0.000	0.000
93	A	93	PHE	0	-0.037	-0.018	6.578	0.054	0.054	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.016	0.008	6.382	-0.116	-0.116	0.000	0.000	0.000	0.000
95	A	96	ALA	0	0.033	0.002	8.493	0.205	0.205	0.000	0.000	0.000	0.000
96	A	97	LEU	0	0.031	0.013	9.488	-0.131	-0.131	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.020	-0.001	10.972	0.048	0.048	0.000	0.000	0.000	0.000
98	A	99	ASN	0	0.025	-0.005	12.648	-0.079	-0.079	0.000	0.000	0.000	0.000
99	A	100	SER	0	0.013	0.003	15.451	-0.033	-0.033	0.000	0.000	0.000	0.000
100	A	101	ILE	0	-0.020	0.012	9.814	-0.038	-0.038	0.000	0.000	0.000	0.000
101	A	102	MET	0	-0.002	0.009	8.977	0.124	0.124	0.000	0.000	0.000	0.000
102	A	103	TYR	0	-0.012	0.003	5.112	-0.323	-0.323	0.000	0.000	0.000	0.000
103	A	104	PHE	0	0.034	-0.003	4.312	0.790	1.158	-0.001	-0.209	-0.157	-0.001
104	A	105	SER	0	-0.012	0.014	1.905	-14.915	-14.440	8.584	-4.658	-4.401	-0.029
105	A	106	HIS	0	0.013	0.004	2.878	-6.994	-4.376	1.048	-0.616	-3.049	-0.003
106	A	107	PHE	0	0.019	0.000	4.446	0.490	0.588	0.000	-0.016	-0.082	0.000
107	A	108	VAL	0	0.009	0.005	7.888	0.163	0.163	0.000	0.000	0.000	0.000
108	A	109	PRO	0	-0.045	-0.029	10.834	-0.087	-0.087	0.000	0.000	0.000	0.000
109	A	110	VAL	0	-0.022	-0.008	13.880	0.052	0.052	0.000	0.000	0.000	0.000
110	A	111	PHE	0	0.005	-0.005	15.868	-0.045	-0.045	0.000	0.000	0.000	0.000
111	A	112	LEU	0	0.032	0.009	20.034	0.026	0.026	0.000	0.000	0.000	0.000
112	A	113	PRO	0	-0.054	-0.018	23.602	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.013	0.016	25.335	-0.010	-0.010	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.962	0.965	27.027	-0.048	-0.048	0.000	0.000	0.000	0.000
115	A	116	PRO	0	0.033	0.019	30.678	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	117	THR	0	-0.028	0.000	31.650	-0.007	-0.007	0.000	0.000	0.000	0.000

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