FMO DATABASE

FMODB ID: QV2YY

Calculation Name: 4QXL-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4QXL

Chain ID: A

ChEMBL ID:

UniProt ID:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-853289.570302
FMO2-HF: Nuclear repulsion	809914.564238
FMO2-HF: Total energy	-43375.006064
FMO2-MP2: Total energy	-43501.185189

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:ALA)

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

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.
-17.044	-16.684	13.859	-7.333	-6.887	-0.075

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.027 / q_NPA : -0.028

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	GLU	-1	-0.901	-0.960	1.812	-21.158	-22.131	13.822	-6.910	-5.940	-0.076
4	A	4	GLY	0	0.005	0.008	4.699	1.116	1.213	-0.001	-0.013	-0.083	0.000
5	A	5	ALA	0	0.004	0.001	8.438	-0.188	-0.188	0.000	0.000	0.000	0.000
6	A	6	TRP	0	-0.043	0.004	11.884	0.144	0.144	0.000	0.000	0.000	0.000
7	A	7	GLN	0	-0.016	-0.013	15.410	-0.019	-0.019	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.757	-0.859	18.723	-0.162	-0.162	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.044	-0.041	22.247	-0.011	-0.011	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.055	0.039	25.761	0.011	0.011	0.000	0.000	0.000	0.000
11	A	11	MET	0	-0.018	-0.001	29.232	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.040	0.010	31.199	-0.010	-0.010	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.022	0.002	32.691	0.009	0.009	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.007	-0.012	35.416	0.002	0.002	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.022	0.001	37.145	0.002	0.002	0.000	0.000	0.000	0.000
16	A	16	ASN	0	0.047	-0.004	40.803	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	17	TYR	0	-0.009	-0.012	43.491	0.005	0.005	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.869	0.943	42.506	0.080	0.080	0.000	0.000	0.000	0.000
19	A	19	GLY	0	-0.004	0.000	42.266	0.003	0.003	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.038	-0.007	39.389	0.000	0.000	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.017	-0.042	35.211	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.004	0.004	35.109	0.004	0.004	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.004	-0.018	29.917	-0.012	-0.012	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.020	-0.028	29.175	0.012	0.012	0.000	0.000	0.000	0.000
25	A	25	SER	0	0.032	0.029	28.854	0.001	0.001	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.054	-0.029	25.412	-0.009	-0.009	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.029	0.002	22.836	0.009	0.009	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.040	-0.050	20.229	-0.017	-0.017	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.035	0.013	16.862	0.008	0.008	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.880	0.940	18.734	0.209	0.209	0.000	0.000	0.000	0.000
31	A	31	GLN	0	-0.024	-0.005	13.689	0.055	0.055	0.000	0.000	0.000	0.000
32	A	32	PRO	0	0.028	-0.002	16.140	-0.038	-0.038	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.021	0.003	12.729	-0.010	-0.010	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.003	-0.010	10.832	0.029	0.029	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.031	0.024	8.213	-0.180	-0.180	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.050	-0.021	7.520	0.219	0.219	0.000	0.000	0.000	0.000
37	A	37	MET	0	0.013	0.009	8.611	-0.315	-0.315	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.055	-0.026	6.415	0.086	0.086	0.000	0.000	0.000	0.000
39	A	39	LEU	0	0.039	0.015	9.817	0.155	0.155	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.005	0.009	12.806	-0.024	-0.024	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.021	0.012	15.965	0.043	0.043	0.000	0.000	0.000	0.000
42	A	42	TRP	0	-0.026	-0.003	18.439	0.012	0.012	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.942	0.962	21.898	0.204	0.204	0.000	0.000	0.000	0.000
44	A	44	TYR	0	-0.029	-0.024	25.535	0.004	0.004	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.841	-0.904	28.957	-0.123	-0.123	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.015	-0.007	32.474	0.001	0.001	0.000	0.000	0.000	0.000
47	A	47	ASN	0	0.023	0.026	36.034	0.004	0.004	0.000	0.000	0.000	0.000
48	A	48	GLY	0	-0.016	-0.014	39.353	0.005	0.005	0.000	0.000	0.000	0.000
49	A	49	PRO	0	0.024	0.020	39.342	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.056	0.018	35.799	0.000	0.000	0.000	0.000	0.000	0.000
51	A	51	PRO	0	-0.009	-0.009	37.985	0.004	0.004	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.045	0.027	39.082	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.015	0.003	38.867	0.004	0.004	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.064	-0.026	34.196	0.001	0.001	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.798	0.871	31.062	0.140	0.140	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.003	-0.010	28.710	0.004	0.004	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.808	0.913	26.994	0.145	0.145	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.012	0.017	20.669	0.005	0.005	0.000	0.000	0.000	0.000
59	A	59	CYS	0	-0.033	-0.028	22.303	0.003	0.003	0.000	0.000	0.000	0.000
60	A	60	SER	0	-0.011	-0.029	19.612	-0.004	-0.004	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.059	-0.043	20.326	0.040	0.040	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.040	-0.024	21.250	0.023	0.023	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.837	0.917	15.044	0.433	0.433	0.000	0.000	0.000	0.000
64	A	65	VAL	0	-0.008	0.006	20.250	-0.011	-0.011	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.755	-0.856	23.732	-0.165	-0.165	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.075	-0.032	23.845	-0.018	-0.018	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.845	-0.920	27.075	-0.147	-0.147	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.009	0.010	28.020	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	70	GLN	0	-0.052	-0.043	29.486	0.004	0.004	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.028	-0.034	24.814	0.003	0.003	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.013	0.027	22.938	0.013	0.013	0.000	0.000	0.000	0.000
72	A	73	THR	0	0.008	0.002	17.572	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	74	THR	0	-0.008	-0.003	17.772	0.013	0.013	0.000	0.000	0.000	0.000
74	A	75	HIS	0	0.110	0.047	11.094	-0.056	-0.056	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.003	0.010	15.303	-0.020	-0.020	0.000	0.000	0.000	0.000
76	A	77	PHE	0	0.013	0.001	15.265	0.034	0.034	0.000	0.000	0.000	0.000
77	A	78	ALA	0	0.014	0.021	11.757	-0.053	-0.053	0.000	0.000	0.000	0.000
78	A	79	HIS	0	0.010	-0.010	9.009	0.027	0.027	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.004	0.023	11.595	0.083	0.083	0.000	0.000	0.000	0.000
80	A	81	PRO	0	0.055	0.024	12.691	-0.113	-0.113	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.011	-0.009	10.938	0.036	0.036	0.000	0.000	0.000	0.000
82	A	83	VAL	0	0.018	0.013	13.050	0.031	0.031	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.816	-0.878	16.470	-0.254	-0.254	0.000	0.000	0.000	0.000
84	A	85	PRO	0	-0.023	-0.004	18.651	-0.018	-0.018	0.000	0.000	0.000	0.000
85	A	86	LEU	0	0.009	0.000	17.809	0.010	0.010	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.935	0.961	21.901	0.207	0.207	0.000	0.000	0.000	0.000
87	A	88	PHE	0	0.035	0.027	24.435	-0.009	-0.009	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.006	-0.012	27.368	0.015	0.015	0.000	0.000	0.000	0.000
89	A	90	TRP	0	-0.023	-0.021	29.941	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.764	-0.848	33.174	-0.119	-0.119	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.024	0.014	36.194	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	93	PRO	0	0.041	0.027	38.012	0.006	0.006	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.025	0.016	41.053	0.002	0.002	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.040	0.012	44.876	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.032	0.023	47.238	0.001	0.001	0.000	0.000	0.000	0.000
96	A	97	ARG	1	0.968	0.973	47.254	0.054	0.054	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.052	-0.012	40.986	0.000	0.000	0.000	0.000	0.000	0.000
98	A	99	ILE	0	-0.048	-0.006	45.641	0.002	0.002	0.000	0.000	0.000	0.000
99	A	100	PRO	0	0.018	-0.005	43.976	0.001	0.001	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.050	0.023	43.134	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.014	0.020	35.611	0.000	0.000	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.862	0.909	38.659	0.084	0.084	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.009	0.021	31.725	0.001	0.001	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.916	0.957	34.575	0.094	0.094	0.000	0.000	0.000	0.000
105	A	106	SER	0	0.011	-0.003	30.122	0.006	0.006	0.000	0.000	0.000	0.000
106	A	107	ASN	0	-0.012	-0.003	27.498	0.002	0.002	0.000	0.000	0.000	0.000
107	A	108	GLN	0	0.010	0.005	23.417	0.017	0.017	0.000	0.000	0.000	0.000
108	A	109	VAL	0	-0.001	-0.001	19.324	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	110	ILE	0	0.009	-0.008	15.488	0.023	0.023	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.010	0.005	13.331	-0.034	-0.034	0.000	0.000	0.000	0.000
111	A	112	ASN	0	-0.019	-0.015	9.789	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	113	TYR	0	0.003	-0.008	8.261	0.181	0.181	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.938	0.990	3.300	1.453	1.899	0.028	-0.122	-0.352	0.001
114	A	115	HIS	0	-0.017	-0.005	3.670	0.678	1.468	0.010	-0.288	-0.512	0.000

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