FMO DATABASE

FMODB ID: JQL99

Calculation Name: 3D7Q-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3D7Q

Chain ID: A

ChEMBL ID:

UniProt ID: B2JAN5

Base Structure: X-ray

Registration Date: 2023-09-21

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	112
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-945542.547139
FMO2-HF: Nuclear repulsion	898811.497708
FMO2-HF: Total energy	-46731.049431
FMO2-MP2: Total energy	-46866.330031

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:0:GLY)

Summations of interaction energy for fragment #1(A:0:GLY)

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.
-7.739	-2.993	1.583	-2.596	-3.735	0.005

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.012 / q_NPA : -0.003

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	2	ASP	-1	-0.904	-0.955	2.483	-1.233	1.102	0.392	-1.147	-1.581	-0.002
4	A	3	LYS	1	0.832	0.915	2.749	-5.805	-4.155	0.896	-0.957	-1.590	0.009
5	A	4	LEU	0	0.034	0.028	4.224	-1.614	-1.395	0.003	-0.075	-0.147	0.000
6	A	5	ASN	0	0.030	0.004	6.161	-0.056	-0.056	0.000	0.000	0.000	0.000
7	A	6	GLU	-1	-0.845	-0.910	7.340	1.030	1.030	0.000	0.000	0.000	0.000
8	A	7	TYR	0	-0.039	-0.045	8.294	-0.120	-0.120	0.000	0.000	0.000	0.000
9	A	8	ARG	1	0.838	0.885	10.078	0.078	0.078	0.000	0.000	0.000	0.000
10	A	9	THR	0	-0.043	-0.025	11.829	-0.086	-0.086	0.000	0.000	0.000	0.000
11	A	10	LYS	1	0.813	0.905	11.326	-0.872	-0.872	0.000	0.000	0.000	0.000
12	A	11	VAL	0	0.012	0.005	13.705	-0.053	-0.053	0.000	0.000	0.000	0.000
13	A	12	ARG	1	0.924	0.963	15.832	-0.083	-0.083	0.000	0.000	0.000	0.000
14	A	13	GLN	0	-0.022	0.002	16.932	0.002	0.002	0.000	0.000	0.000	0.000
15	A	14	LEU	0	-0.009	0.016	18.831	-0.025	-0.025	0.000	0.000	0.000	0.000
16	A	15	LEU	0	0.031	-0.007	19.026	-0.020	-0.020	0.000	0.000	0.000	0.000
17	A	16	THR	0	-0.014	-0.023	21.649	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	17	LYS	1	0.843	0.922	22.204	-0.186	-0.186	0.000	0.000	0.000	0.000
19	A	18	HIS	1	0.833	0.888	23.667	-0.138	-0.138	0.000	0.000	0.000	0.000
20	A	19	LEU	0	-0.011	0.011	26.261	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	20	GLN	0	-0.030	-0.026	27.081	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	21	TYR	0	-0.015	-0.012	27.608	0.001	0.001	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.922	0.994	31.265	-0.044	-0.044	0.000	0.000	0.000	0.000
24	A	23	PRO	0	-0.046	-0.017	33.219	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	24	SER	0	-0.030	-0.026	35.878	0.000	0.000	0.000	0.000	0.000	0.000
26	A	25	TYR	0	-0.022	-0.025	37.061	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	26	GLY	0	0.003	-0.010	40.140	0.000	0.000	0.000	0.000	0.000	0.000
28	A	27	ASP	-1	-0.935	-0.943	41.714	0.021	0.021	0.000	0.000	0.000	0.000
29	A	28	VAL	0	-0.039	-0.025	35.542	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	29	GLU	-1	-0.815	-0.911	34.510	0.034	0.034	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.058	-0.032	29.229	0.001	0.001	0.000	0.000	0.000	0.000
32	A	31	GLU	-1	-0.906	-0.954	29.514	0.017	0.017	0.000	0.000	0.000	0.000
33	A	32	GLN	0	-0.005	-0.017	23.473	0.001	0.001	0.000	0.000	0.000	0.000
34	A	33	ILE	0	-0.009	-0.005	23.583	-0.008	-0.008	0.000	0.000	0.000	0.000
35	A	34	PHE	0	-0.037	-0.028	19.379	0.012	0.012	0.000	0.000	0.000	0.000
36	A	35	ASP	-1	-0.827	-0.895	19.011	-0.087	-0.087	0.000	0.000	0.000	0.000
37	A	36	GLU	-1	-0.854	-0.948	13.690	-0.081	-0.081	0.000	0.000	0.000	0.000
38	A	37	GLU	-1	-0.971	-0.969	14.421	-0.265	-0.265	0.000	0.000	0.000	0.000
39	A	38	HIS	0	-0.082	-0.064	15.045	-0.041	-0.041	0.000	0.000	0.000	0.000
40	A	39	ASP	-1	-0.787	-0.837	11.286	-0.139	-0.139	0.000	0.000	0.000	0.000
41	A	40	HIS	0	-0.079	-0.053	14.503	0.023	0.023	0.000	0.000	0.000	0.000
42	A	41	TYR	0	-0.044	-0.047	13.548	0.004	0.004	0.000	0.000	0.000	0.000
43	A	42	GLN	0	-0.011	-0.033	19.175	0.012	0.012	0.000	0.000	0.000	0.000
44	A	43	ILE	0	-0.002	0.008	22.750	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	44	ILE	0	-0.015	-0.016	25.694	0.002	0.002	0.000	0.000	0.000	0.000
46	A	45	SER	0	0.011	0.029	29.069	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	46	VAL	0	-0.015	-0.011	32.484	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	47	GLY	0	0.002	-0.002	35.229	0.000	0.000	0.000	0.000	0.000	0.000
49	A	48	TRP	0	-0.003	0.002	38.932	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	49	ASN	0	0.039	0.026	42.163	0.001	0.001	0.000	0.000	0.000	0.000
51	A	50	ASN	0	0.022	0.001	43.976	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	51	GLN	0	0.003	-0.006	46.636	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	52	HIS	0	-0.009	0.007	40.868	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	53	ARG	1	0.896	0.965	37.210	-0.014	-0.014	0.000	0.000	0.000	0.000
55	A	54	ILE	0	-0.016	-0.008	36.367	0.001	0.001	0.000	0.000	0.000	0.000
56	A	55	TYR	0	-0.002	-0.023	31.541	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	56	GLY	0	0.022	0.011	32.088	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	57	PRO	0	-0.024	-0.010	26.559	0.003	0.003	0.000	0.000	0.000	0.000
59	A	58	ILE	0	-0.014	0.014	27.799	0.001	0.001	0.000	0.000	0.000	0.000
60	A	59	MET	0	-0.029	-0.011	22.477	0.012	0.012	0.000	0.000	0.000	0.000
61	A	60	HIS	0	0.001	0.010	19.966	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	61	LEU	0	-0.030	-0.004	16.659	0.012	0.012	0.000	0.000	0.000	0.000
63	A	62	ASP	-1	-0.708	-0.831	15.463	0.012	0.012	0.000	0.000	0.000	0.000
64	A	63	ILE	0	-0.029	-0.004	8.957	0.063	0.063	0.000	0.000	0.000	0.000
65	A	64	LYS	1	0.892	0.945	11.249	-0.075	-0.075	0.000	0.000	0.000	0.000
66	A	65	ASN	0	-0.013	-0.007	8.228	0.009	0.009	0.000	0.000	0.000	0.000
67	A	66	ASN	0	-0.028	-0.032	2.803	0.389	0.931	0.292	-0.417	-0.417	-0.002
68	A	67	LYS	1	0.852	0.945	6.622	-0.161	-0.161	0.000	0.000	0.000	0.000
69	A	68	ILE	0	0.040	0.020	10.061	-0.097	-0.097	0.000	0.000	0.000	0.000
70	A	69	TRP	0	-0.022	-0.011	12.880	-0.022	-0.022	0.000	0.000	0.000	0.000
71	A	70	ILE	0	0.017	0.001	16.062	-0.015	-0.015	0.000	0.000	0.000	0.000
72	A	71	GLN	0	-0.048	-0.047	18.776	0.001	0.001	0.000	0.000	0.000	0.000
73	A	72	GLN	0	0.012	-0.003	21.581	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	73	ASN	0	0.021	0.008	23.772	0.007	0.007	0.000	0.000	0.000	0.000
75	A	74	THR	0	-0.023	0.004	26.148	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	75	THR	0	-0.063	-0.046	27.661	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	76	GLU	-1	-0.914	-0.961	29.707	0.084	0.084	0.000	0.000	0.000	0.000
78	A	77	ALA	0	-0.022	0.003	26.022	0.005	0.005	0.000	0.000	0.000	0.000
79	A	78	ASP	-1	-0.838	-0.919	23.583	0.159	0.159	0.000	0.000	0.000	0.000
80	A	79	ILE	0	0.033	-0.008	19.509	0.012	0.012	0.000	0.000	0.000	0.000
81	A	80	ALA	0	0.019	0.016	19.006	0.027	0.027	0.000	0.000	0.000	0.000
82	A	81	LEU	0	-0.006	-0.009	19.278	0.034	0.034	0.000	0.000	0.000	0.000
83	A	82	GLU	-1	-0.784	-0.865	21.194	0.175	0.175	0.000	0.000	0.000	0.000
84	A	83	LEU	0	-0.027	-0.016	15.157	0.018	0.018	0.000	0.000	0.000	0.000
85	A	84	MET	0	-0.044	-0.024	16.539	0.038	0.038	0.000	0.000	0.000	0.000
86	A	85	GLU	-1	-0.942	-0.953	17.811	0.237	0.237	0.000	0.000	0.000	0.000
87	A	86	MET	0	-0.095	-0.034	16.230	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	87	GLY	0	0.009	0.001	14.662	0.073	0.073	0.000	0.000	0.000	0.000
89	A	88	ILE	0	-0.064	-0.019	11.476	0.138	0.138	0.000	0.000	0.000	0.000
90	A	89	ASP	-1	-0.820	-0.914	11.872	0.355	0.355	0.000	0.000	0.000	0.000
91	A	90	LYS	1	0.965	0.961	13.481	-0.247	-0.247	0.000	0.000	0.000	0.000
92	A	91	GLN	0	-0.026	-0.018	13.483	-0.053	-0.053	0.000	0.000	0.000	0.000
93	A	92	ASP	-1	-0.800	-0.875	8.835	0.992	0.992	0.000	0.000	0.000	0.000
94	A	93	ILE	0	0.026	0.030	11.492	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	94	VAL	0	-0.020	-0.009	14.200	-0.024	-0.024	0.000	0.000	0.000	0.000
96	A	95	ILE	0	0.026	0.011	16.711	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	96	GLY	0	0.035	0.017	20.136	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	97	PHE	0	-0.013	-0.004	20.901	-0.014	-0.014	0.000	0.000	0.000	0.000
99	A	98	HIS	0	0.009	0.022	23.436	0.000	0.000	0.000	0.000	0.000	0.000
100	A	99	THR	0	0.049	-0.013	23.723	0.001	0.001	0.000	0.000	0.000	0.000
101	A	100	PRO	0	0.082	0.020	22.503	0.008	0.008	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.881	0.940	23.584	-0.062	-0.062	0.000	0.000	0.000	0.000
103	A	102	MET	0	0.018	0.025	26.460	0.003	0.003	0.000	0.000	0.000	0.000
104	A	103	ARG	1	0.872	0.959	19.126	-0.090	-0.090	0.000	0.000	0.000	0.000
105	A	104	GLN	0	-0.022	0.000	22.274	0.005	0.005	0.000	0.000	0.000	0.000
106	A	105	LEU	0	-0.049	-0.025	23.806	0.001	0.001	0.000	0.000	0.000	0.000
107	A	106	SER	0	-0.039	-0.022	23.780	0.004	0.004	0.000	0.000	0.000	0.000
108	A	107	GLY	0	0.042	0.028	22.636	0.005	0.005	0.000	0.000	0.000	0.000
109	A	108	PHE	0	-0.034	-0.023	17.824	0.019	0.019	0.000	0.000	0.000	0.000
110	A	109	ALA	0	-0.018	0.012	14.692	-0.019	-0.019	0.000	0.000	0.000	0.000
111	A	110	VAL	0	-0.022	-0.029	16.643	-0.016	-0.016	0.000	0.000	0.000	0.000
112	A	111	GLU	-1	-0.905	-0.953	13.367	0.098	0.098	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:GLY)