FMO DATABASE

FMODB ID: R89L8

Calculation Name: 2Q4P-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2Q4P

Chain ID: A

ChEMBL ID:

UniProt ID: Q9QY93

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	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	113
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-818554.36476
FMO2-HF: Nuclear repulsion	773399.877626
FMO2-HF: Total energy	-45154.487134
FMO2-MP2: Total energy	-45288.182197

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:22:PRO)

Summations of interaction energy for fragment #1(A:22:PRO)

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.
0.202	1.43	-0.013	-0.533	-0.682	0.002

Interaction energy analysis for fragmet #1(A:22:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.003 / q_NPA : -0.030

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	24	ARG	1	0.941	0.978	3.846	0.221	1.449	-0.013	-0.533	-0.682	0.002
4	A	25	PHE	0	0.041	0.019	6.642	0.103	0.103	0.000	0.000	0.000	0.000
5	A	26	SER	0	-0.022	-0.025	9.999	-0.197	-0.197	0.000	0.000	0.000	0.000
6	A	27	PRO	0	-0.070	-0.041	12.442	0.045	0.045	0.000	0.000	0.000	0.000
7	A	28	GLU	-1	-0.912	-0.922	15.050	-0.188	-0.188	0.000	0.000	0.000	0.000
8	A	29	PRO	0	0.069	0.023	16.736	-0.013	-0.013	0.000	0.000	0.000	0.000
9	A	30	THR	0	-0.037	-0.028	19.652	0.002	0.002	0.000	0.000	0.000	0.000
10	A	31	LEU	0	0.036	0.000	20.250	0.009	0.009	0.000	0.000	0.000	0.000
11	A	32	GLU	-1	-0.775	-0.848	22.884	-0.038	-0.038	0.000	0.000	0.000	0.000
12	A	33	ASP	-1	-0.768	-0.869	23.526	-0.088	-0.088	0.000	0.000	0.000	0.000
13	A	34	ILE	0	0.024	0.013	19.969	0.005	0.005	0.000	0.000	0.000	0.000
14	A	35	ARG	1	0.844	0.893	24.620	0.039	0.039	0.000	0.000	0.000	0.000
15	A	36	ARG	1	0.747	0.856	27.220	0.069	0.069	0.000	0.000	0.000	0.000
16	A	37	LEU	0	0.005	-0.004	24.332	0.003	0.003	0.000	0.000	0.000	0.000
17	A	38	HIS	0	0.059	0.012	27.840	0.006	0.006	0.000	0.000	0.000	0.000
18	A	39	ALA	0	-0.022	0.000	29.614	0.005	0.005	0.000	0.000	0.000	0.000
19	A	40	GLU	-1	-0.902	-0.963	32.491	-0.025	-0.025	0.000	0.000	0.000	0.000
20	A	41	PHE	0	-0.006	0.004	30.744	0.002	0.002	0.000	0.000	0.000	0.000
21	A	42	ALA	0	0.020	0.010	32.897	0.003	0.003	0.000	0.000	0.000	0.000
22	A	43	ALA	0	-0.076	-0.028	35.080	0.002	0.002	0.000	0.000	0.000	0.000
23	A	44	GLU	-1	-0.873	-0.903	34.867	-0.017	-0.017	0.000	0.000	0.000	0.000
24	A	45	ARG	1	0.765	0.857	34.134	0.010	0.010	0.000	0.000	0.000	0.000
25	A	46	ASP	-1	-0.844	-0.922	38.841	0.007	0.007	0.000	0.000	0.000	0.000
26	A	47	TRP	0	0.014	0.011	39.544	0.000	0.000	0.000	0.000	0.000	0.000
27	A	48	GLU	-1	-0.786	-0.903	39.932	0.008	0.008	0.000	0.000	0.000	0.000
28	A	49	GLN	0	-0.033	-0.008	37.325	0.000	0.000	0.000	0.000	0.000	0.000
29	A	50	PHE	0	0.017	0.007	32.331	0.002	0.002	0.000	0.000	0.000	0.000
30	A	51	HIS	1	0.825	0.915	35.348	0.000	0.000	0.000	0.000	0.000	0.000
31	A	52	GLN	0	-0.058	-0.034	37.473	0.002	0.002	0.000	0.000	0.000	0.000
32	A	53	PRO	0	-0.010	-0.003	35.248	0.002	0.002	0.000	0.000	0.000	0.000
33	A	54	ARG	1	0.962	0.963	35.022	-0.025	-0.025	0.000	0.000	0.000	0.000
34	A	55	ASN	0	0.002	0.002	36.306	0.006	0.006	0.000	0.000	0.000	0.000
35	A	56	LEU	0	0.028	0.023	31.805	0.003	0.003	0.000	0.000	0.000	0.000
36	A	57	LEU	0	-0.021	-0.011	31.383	0.004	0.004	0.000	0.000	0.000	0.000
37	A	58	LEU	0	-0.028	-0.023	31.984	0.006	0.006	0.000	0.000	0.000	0.000
38	A	59	ALA	0	0.039	0.043	31.227	0.004	0.004	0.000	0.000	0.000	0.000
39	A	60	LEU	0	-0.015	0.001	25.960	0.006	0.006	0.000	0.000	0.000	0.000
40	A	61	VAL	0	-0.062	-0.047	28.042	0.009	0.009	0.000	0.000	0.000	0.000
41	A	62	GLY	0	0.005	0.016	30.121	0.007	0.007	0.000	0.000	0.000	0.000
42	A	63	GLU	-1	-0.803	-0.913	25.978	0.066	0.066	0.000	0.000	0.000	0.000
43	A	64	VAL	0	-0.079	-0.052	24.631	0.015	0.015	0.000	0.000	0.000	0.000
44	A	65	GLY	0	-0.016	0.002	26.240	0.013	0.013	0.000	0.000	0.000	0.000
45	A	66	GLU	-1	-0.863	-0.939	27.450	0.097	0.097	0.000	0.000	0.000	0.000
46	A	67	LEU	0	-0.055	-0.023	20.180	0.015	0.015	0.000	0.000	0.000	0.000
47	A	68	ALA	0	-0.040	-0.025	23.762	0.021	0.021	0.000	0.000	0.000	0.000
48	A	69	GLU	-1	-0.887	-0.940	25.807	0.110	0.110	0.000	0.000	0.000	0.000
49	A	70	LEU	0	-0.051	-0.031	22.787	0.007	0.007	0.000	0.000	0.000	0.000
50	A	71	PHE	0	-0.066	-0.057	17.631	0.042	0.042	0.000	0.000	0.000	0.000
51	A	72	GLN	0	-0.067	-0.022	23.654	0.004	0.004	0.000	0.000	0.000	0.000
52	A	73	TRP	0	-0.073	-0.036	26.709	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	74	LYS	1	0.793	0.916	21.315	-0.229	-0.229	0.000	0.000	0.000	0.000
54	A	75	SER	0	0.018	-0.015	23.183	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	76	ASP	-1	-0.864	-0.931	20.885	0.286	0.286	0.000	0.000	0.000	0.000
56	A	77	THR	0	-0.190	-0.114	19.255	0.020	0.020	0.000	0.000	0.000	0.000
57	A	78	GLU	-1	-0.871	-0.895	19.472	0.252	0.252	0.000	0.000	0.000	0.000
58	A	79	PRO	0	-0.029	-0.032	17.221	0.049	0.049	0.000	0.000	0.000	0.000
59	A	80	GLY	0	0.077	0.051	15.108	-0.029	-0.029	0.000	0.000	0.000	0.000
60	A	81	PRO	0	0.069	0.030	14.014	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	82	GLN	0	-0.028	-0.027	8.871	-0.219	-0.219	0.000	0.000	0.000	0.000
62	A	83	ALA	0	-0.059	-0.024	13.036	-0.058	-0.058	0.000	0.000	0.000	0.000
63	A	84	TRP	0	0.043	0.034	15.840	-0.040	-0.040	0.000	0.000	0.000	0.000
64	A	85	PRO	0	0.003	-0.007	18.241	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	86	PRO	0	0.001	-0.015	18.482	0.007	0.007	0.000	0.000	0.000	0.000
66	A	87	LYS	1	0.954	0.969	19.547	-0.075	-0.075	0.000	0.000	0.000	0.000
67	A	88	GLU	-1	-0.747	-0.853	20.843	0.179	0.179	0.000	0.000	0.000	0.000
68	A	89	ARG	1	0.838	0.923	11.554	-0.308	-0.308	0.000	0.000	0.000	0.000
69	A	90	ALA	0	-0.050	-0.012	17.711	0.004	0.004	0.000	0.000	0.000	0.000
70	A	91	ALA	0	0.124	0.069	19.684	0.001	0.001	0.000	0.000	0.000	0.000
71	A	92	LEU	0	0.010	0.018	16.221	0.006	0.006	0.000	0.000	0.000	0.000
72	A	93	GLN	0	-0.073	-0.038	15.320	0.000	0.000	0.000	0.000	0.000	0.000
73	A	94	GLU	-1	-0.906	-0.942	18.114	0.041	0.041	0.000	0.000	0.000	0.000
74	A	95	GLU	-1	-0.812	-0.911	21.585	0.090	0.090	0.000	0.000	0.000	0.000
75	A	96	LEU	0	-0.069	-0.040	16.252	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	97	SER	0	-0.083	-0.055	19.333	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	98	ASP	-1	-0.868	-0.945	20.702	0.023	0.023	0.000	0.000	0.000	0.000
78	A	99	VAL	0	-0.020	0.002	22.274	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	100	LEU	0	-0.041	-0.022	18.328	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	101	ILE	0	0.008	-0.001	22.203	-0.014	-0.014	0.000	0.000	0.000	0.000
81	A	102	TYR	0	0.036	0.012	24.892	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	103	LEU	0	-0.036	-0.004	22.833	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	104	VAL	0	-0.028	-0.018	23.037	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	105	ALA	0	0.026	0.013	26.191	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	106	LEU	0	-0.024	-0.006	29.483	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	107	ALA	0	-0.004	-0.004	27.844	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	108	ALA	0	0.026	-0.001	29.789	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	109	ARG	1	0.868	0.950	31.362	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	110	CYS	0	-0.088	-0.043	32.864	0.001	0.001	0.000	0.000	0.000	0.000
90	A	111	HIS	0	-0.087	-0.045	33.515	0.000	0.000	0.000	0.000	0.000	0.000
91	A	112	VAL	0	-0.011	0.005	28.920	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	113	ASP	-1	-0.788	-0.910	27.486	-0.029	-0.029	0.000	0.000	0.000	0.000
93	A	114	LEU	0	0.006	0.002	23.046	0.002	0.002	0.000	0.000	0.000	0.000
94	A	115	PRO	0	-0.008	-0.004	22.692	0.006	0.006	0.000	0.000	0.000	0.000
95	A	116	GLN	0	0.022	0.006	23.684	0.008	0.008	0.000	0.000	0.000	0.000
96	A	117	ALA	0	-0.028	-0.003	26.307	0.006	0.006	0.000	0.000	0.000	0.000
97	A	118	VAL	0	-0.006	-0.014	20.064	0.010	0.010	0.000	0.000	0.000	0.000
98	A	119	ILE	0	0.028	0.021	21.849	0.009	0.009	0.000	0.000	0.000	0.000
99	A	120	SER	0	0.075	0.052	23.394	0.009	0.009	0.000	0.000	0.000	0.000
100	A	121	LYS	1	0.882	0.953	24.672	-0.056	-0.056	0.000	0.000	0.000	0.000
101	A	122	MET	0	-0.012	-0.011	17.004	0.010	0.010	0.000	0.000	0.000	0.000
102	A	123	ASP	-1	-0.811	-0.888	22.714	0.014	0.014	0.000	0.000	0.000	0.000
103	A	124	THR	0	-0.051	-0.039	24.928	0.003	0.003	0.000	0.000	0.000	0.000
104	A	125	ASN	0	-0.028	-0.026	22.776	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	126	ARG	1	0.853	0.909	20.789	-0.022	-0.022	0.000	0.000	0.000	0.000
106	A	127	GLN	0	-0.043	-0.010	24.138	0.001	0.001	0.000	0.000	0.000	0.000
107	A	128	ARG	1	0.917	0.942	27.954	-0.049	-0.049	0.000	0.000	0.000	0.000
108	A	129	TYR	0	-0.025	0.002	23.497	0.004	0.004	0.000	0.000	0.000	0.000
109	A	130	PRO	0	0.015	0.012	24.669	0.003	0.003	0.000	0.000	0.000	0.000
110	A	131	VAL	0	-0.009	-0.002	21.166	0.009	0.009	0.000	0.000	0.000	0.000
111	A	132	HIS	0	-0.006	-0.002	23.862	-0.011	-0.011	0.000	0.000	0.000	0.000
112	A	133	LEU	0	-0.006	-0.002	23.615	0.005	0.005	0.000	0.000	0.000	0.000
113	A	134	SER	0	0.004	0.010	25.897	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:PRO)