FMO DATABASE

FMODB ID: 6YN4Z

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:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
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
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-823460.846001
FMO2-HF: Nuclear repulsion	778310.198418
FMO2-HF: Total energy	-45150.647582
FMO2-MP2: Total energy	-45285.103996

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.
1.342	3.449	-0.03	-1.004	-1.072	0.001

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 : 0.023 / 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	24	ARG	1	0.983	0.997	3.819	1.448	3.555	-0.030	-1.004	-1.072	0.001
4	A	25	PHE	0	0.015	0.000	6.699	0.032	0.032	0.000	0.000	0.000	0.000
5	A	26	SER	0	0.009	-0.013	10.384	-0.167	-0.167	0.000	0.000	0.000	0.000
6	A	27	PRO	0	-0.103	-0.020	12.439	0.071	0.071	0.000	0.000	0.000	0.000
7	A	28	GLU	-1	-0.946	-0.963	14.805	-0.357	-0.357	0.000	0.000	0.000	0.000
8	A	29	PRO	0	0.035	-0.003	16.810	-0.043	-0.043	0.000	0.000	0.000	0.000
9	A	30	THR	0	0.014	0.003	19.635	0.004	0.004	0.000	0.000	0.000	0.000
10	A	31	LEU	0	0.067	-0.010	20.617	0.002	0.002	0.000	0.000	0.000	0.000
11	A	32	GLU	-1	-0.828	-0.874	22.690	-0.105	-0.105	0.000	0.000	0.000	0.000
12	A	33	ASP	-1	-0.818	-0.907	23.342	-0.182	-0.182	0.000	0.000	0.000	0.000
13	A	34	ILE	0	0.022	0.028	20.189	0.001	0.001	0.000	0.000	0.000	0.000
14	A	35	ARG	1	0.795	0.845	24.774	0.111	0.111	0.000	0.000	0.000	0.000
15	A	36	ARG	1	0.838	0.942	27.561	0.143	0.143	0.000	0.000	0.000	0.000
16	A	37	LEU	0	0.027	0.001	24.698	0.007	0.007	0.000	0.000	0.000	0.000
17	A	38	HIS	0	0.043	0.008	27.827	0.013	0.013	0.000	0.000	0.000	0.000
18	A	39	ALA	0	-0.025	-0.009	29.704	0.011	0.011	0.000	0.000	0.000	0.000
19	A	40	GLU	-1	-0.941	-0.971	32.902	-0.087	-0.087	0.000	0.000	0.000	0.000
20	A	41	PHE	0	0.059	0.042	29.099	0.005	0.005	0.000	0.000	0.000	0.000
21	A	42	ALA	0	-0.026	-0.022	32.894	0.005	0.005	0.000	0.000	0.000	0.000
22	A	43	ALA	0	-0.047	-0.021	34.803	0.007	0.007	0.000	0.000	0.000	0.000
23	A	44	GLU	-1	-0.951	-0.963	34.982	-0.091	-0.091	0.000	0.000	0.000	0.000
24	A	45	ARG	1	0.853	0.926	33.356	0.087	0.087	0.000	0.000	0.000	0.000
25	A	46	ASP	-1	-0.825	-0.917	38.713	-0.037	-0.037	0.000	0.000	0.000	0.000
26	A	47	TRP	0	0.061	0.012	39.344	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	48	GLU	-1	-0.863	-0.948	39.734	-0.035	-0.035	0.000	0.000	0.000	0.000
28	A	49	GLN	0	-0.019	0.015	36.301	0.002	0.002	0.000	0.000	0.000	0.000
29	A	50	PHE	0	-0.045	-0.030	31.123	0.003	0.003	0.000	0.000	0.000	0.000
30	A	51	HIS	1	0.811	0.912	35.263	0.053	0.053	0.000	0.000	0.000	0.000
31	A	52	GLN	0	0.031	0.027	37.639	0.003	0.003	0.000	0.000	0.000	0.000
32	A	53	PRO	0	0.007	0.003	35.099	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	54	ARG	1	0.932	0.936	34.851	0.005	0.005	0.000	0.000	0.000	0.000
34	A	55	ASN	0	-0.022	0.011	36.491	0.007	0.007	0.000	0.000	0.000	0.000
35	A	56	LEU	0	0.027	0.023	31.221	0.001	0.001	0.000	0.000	0.000	0.000
36	A	57	LEU	0	0.019	0.014	30.912	0.000	0.000	0.000	0.000	0.000	0.000
37	A	58	LEU	0	-0.031	-0.008	31.330	0.004	0.004	0.000	0.000	0.000	0.000
38	A	59	ALA	0	0.003	0.014	31.288	0.004	0.004	0.000	0.000	0.000	0.000
39	A	60	LEU	0	0.009	0.042	25.271	0.001	0.001	0.000	0.000	0.000	0.000
40	A	61	VAL	0	-0.036	-0.031	27.852	0.006	0.006	0.000	0.000	0.000	0.000
41	A	62	GLY	0	0.021	0.022	29.469	0.008	0.008	0.000	0.000	0.000	0.000
42	A	63	GLU	-1	-0.711	-0.845	25.030	-0.032	-0.032	0.000	0.000	0.000	0.000
43	A	64	VAL	0	-0.162	-0.108	24.328	0.007	0.007	0.000	0.000	0.000	0.000
44	A	65	GLY	0	-0.078	-0.054	25.730	0.014	0.014	0.000	0.000	0.000	0.000
45	A	66	GLU	-1	-0.848	-0.928	26.565	0.014	0.014	0.000	0.000	0.000	0.000
46	A	67	LEU	0	-0.046	-0.026	19.571	0.008	0.008	0.000	0.000	0.000	0.000
47	A	68	ALA	0	-0.060	-0.026	23.336	0.017	0.017	0.000	0.000	0.000	0.000
48	A	69	GLU	-1	-0.858	-0.947	25.007	0.049	0.049	0.000	0.000	0.000	0.000
49	A	70	LEU	0	-0.097	-0.031	21.655	0.008	0.008	0.000	0.000	0.000	0.000
50	A	71	PHE	0	-0.079	-0.078	16.769	0.023	0.023	0.000	0.000	0.000	0.000
51	A	72	GLN	0	-0.036	-0.003	22.699	0.012	0.012	0.000	0.000	0.000	0.000
52	A	73	TRP	0	-0.081	-0.036	26.095	0.007	0.007	0.000	0.000	0.000	0.000
53	A	74	LYS	1	0.905	0.987	19.869	-0.119	-0.119	0.000	0.000	0.000	0.000
54	A	75	SER	0	-0.038	-0.048	22.444	0.007	0.007	0.000	0.000	0.000	0.000
55	A	76	ASP	-1	-0.936	-0.965	20.376	0.267	0.267	0.000	0.000	0.000	0.000
56	A	77	THR	0	-0.116	-0.063	18.824	0.046	0.046	0.000	0.000	0.000	0.000
57	A	78	GLU	-1	-0.856	-0.916	18.242	0.208	0.208	0.000	0.000	0.000	0.000
58	A	79	PRO	0	0.003	-0.002	16.654	0.031	0.031	0.000	0.000	0.000	0.000
59	A	80	GLY	0	0.108	0.067	14.517	-0.038	-0.038	0.000	0.000	0.000	0.000
60	A	81	PRO	0	0.032	-0.022	13.412	-0.022	-0.022	0.000	0.000	0.000	0.000
61	A	82	GLN	0	-0.111	-0.084	8.548	0.027	0.027	0.000	0.000	0.000	0.000
62	A	83	ALA	0	-0.022	0.001	12.785	-0.048	-0.048	0.000	0.000	0.000	0.000
63	A	84	TRP	0	0.012	0.042	15.407	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	85	PRO	0	-0.043	-0.014	18.248	-0.028	-0.028	0.000	0.000	0.000	0.000
65	A	86	PRO	0	-0.009	-0.034	18.128	0.002	0.002	0.000	0.000	0.000	0.000
66	A	87	LYS	1	0.996	0.989	19.161	0.033	0.033	0.000	0.000	0.000	0.000
67	A	88	GLU	-1	-0.796	-0.900	19.710	0.049	0.049	0.000	0.000	0.000	0.000
68	A	89	ARG	1	0.943	0.980	10.344	0.156	0.156	0.000	0.000	0.000	0.000
69	A	90	ALA	0	-0.078	-0.023	16.974	-0.017	-0.017	0.000	0.000	0.000	0.000
70	A	91	ALA	0	0.166	0.082	18.911	-0.017	-0.017	0.000	0.000	0.000	0.000
71	A	92	LEU	0	-0.040	0.028	15.445	0.008	0.008	0.000	0.000	0.000	0.000
72	A	93	GLN	0	-0.096	-0.067	14.660	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	94	GLU	-1	-0.879	-0.925	17.213	-0.125	-0.125	0.000	0.000	0.000	0.000
74	A	95	GLU	-1	-0.781	-0.889	20.812	-0.038	-0.038	0.000	0.000	0.000	0.000
75	A	96	LEU	0	-0.124	-0.051	15.547	0.005	0.005	0.000	0.000	0.000	0.000
76	A	97	SER	0	-0.084	-0.081	18.628	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	98	ASP	-1	-0.817	-0.904	20.172	-0.091	-0.091	0.000	0.000	0.000	0.000
78	A	99	VAL	0	-0.053	-0.024	22.098	0.006	0.006	0.000	0.000	0.000	0.000
79	A	100	LEU	0	-0.035	-0.032	18.648	0.004	0.004	0.000	0.000	0.000	0.000
80	A	101	ILE	0	0.028	0.025	22.315	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	102	TYR	0	0.003	-0.007	24.780	0.001	0.001	0.000	0.000	0.000	0.000
82	A	103	LEU	0	-0.060	-0.013	22.654	0.008	0.008	0.000	0.000	0.000	0.000
83	A	104	VAL	0	-0.045	-0.049	22.989	0.005	0.005	0.000	0.000	0.000	0.000
84	A	105	ALA	0	0.028	0.010	25.935	0.002	0.002	0.000	0.000	0.000	0.000
85	A	106	LEU	0	-0.005	0.002	29.314	0.005	0.005	0.000	0.000	0.000	0.000
86	A	107	ALA	0	0.017	0.009	27.567	0.002	0.002	0.000	0.000	0.000	0.000
87	A	108	ALA	0	0.034	0.013	29.455	0.002	0.002	0.000	0.000	0.000	0.000
88	A	109	ARG	1	0.943	0.991	30.933	0.039	0.039	0.000	0.000	0.000	0.000
89	A	110	CYS	0	-0.135	-0.064	32.617	0.006	0.006	0.000	0.000	0.000	0.000
90	A	111	HIS	0	-0.068	-0.034	33.357	0.005	0.005	0.000	0.000	0.000	0.000
91	A	112	VAL	0	-0.023	-0.011	28.625	0.003	0.003	0.000	0.000	0.000	0.000
92	A	113	ASP	-1	-0.835	-0.932	27.228	-0.080	-0.080	0.000	0.000	0.000	0.000
93	A	114	LEU	0	0.030	0.005	23.383	0.004	0.004	0.000	0.000	0.000	0.000
94	A	115	PRO	0	-0.025	0.007	22.590	0.009	0.009	0.000	0.000	0.000	0.000
95	A	116	GLN	0	0.070	0.018	23.554	0.017	0.017	0.000	0.000	0.000	0.000
96	A	117	ALA	0	-0.062	-0.020	26.211	0.012	0.012	0.000	0.000	0.000	0.000
97	A	118	VAL	0	-0.005	-0.022	19.926	0.016	0.016	0.000	0.000	0.000	0.000
98	A	119	ILE	0	0.064	0.049	22.454	0.019	0.019	0.000	0.000	0.000	0.000
99	A	120	SER	0	0.139	0.067	23.653	0.018	0.018	0.000	0.000	0.000	0.000
100	A	121	LYS	1	0.916	0.989	24.058	-0.047	-0.047	0.000	0.000	0.000	0.000
101	A	122	MET	0	-0.025	-0.030	16.795	0.012	0.012	0.000	0.000	0.000	0.000
102	A	123	ASP	-1	-0.793	-0.924	22.461	0.034	0.034	0.000	0.000	0.000	0.000
103	A	124	THR	0	-0.107	-0.055	24.723	0.004	0.004	0.000	0.000	0.000	0.000
104	A	125	ASN	0	-0.058	-0.054	22.736	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	126	ARG	1	0.803	0.933	20.443	-0.049	-0.049	0.000	0.000	0.000	0.000
106	A	127	GLN	0	-0.014	-0.005	23.772	0.003	0.003	0.000	0.000	0.000	0.000
107	A	128	ARG	1	0.878	0.923	27.505	-0.054	-0.054	0.000	0.000	0.000	0.000
108	A	129	TYR	0	-0.051	0.012	24.192	0.005	0.005	0.000	0.000	0.000	0.000
109	A	130	PRO	0	0.036	0.030	24.766	0.006	0.006	0.000	0.000	0.000	0.000
110	A	131	VAL	0	0.014	0.005	21.212	0.011	0.011	0.000	0.000	0.000	0.000
111	A	132	HIS	0	-0.030	-0.024	23.397	-0.021	-0.021	0.000	0.000	0.000	0.000
112	A	133	LEU	0	-0.040	-0.005	23.479	0.018	0.018	0.000	0.000	0.000	0.000
113	A	134	SER	0	0.045	0.016	25.492	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)