FMO DATABASE

FMODB ID: ZV46N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-853558.581253
FMO2-HF: Nuclear repulsion	810183.910354
FMO2-HF: Total energy	-43374.670899
FMO2-MP2: Total energy	-43500.808775

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.
-17.458	-21.205	22.124	-9.829	-8.547	-0.082

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 : -0.008 / q_NPA : -0.011

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	-0.883	-0.941	1.763	-21.460	-26.777	21.896	-9.201	-7.378	-0.085
4	A	4	GLY	0	-0.001	0.010	4.840	1.008	1.105	-0.001	-0.013	-0.082	0.000
5	A	5	ALA	0	0.005	-0.004	8.551	-0.007	-0.007	0.000	0.000	0.000	0.000
6	A	6	TRP	0	-0.040	0.011	11.787	0.147	0.147	0.000	0.000	0.000	0.000
7	A	7	GLN	0	-0.016	-0.015	15.029	0.023	0.023	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.796	-0.901	18.351	-0.361	-0.361	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.042	-0.034	21.757	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.042	0.024	25.114	0.005	0.005	0.000	0.000	0.000	0.000
11	A	11	MET	0	-0.031	-0.005	28.491	0.003	0.003	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.008	0.005	31.039	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.009	0.004	32.022	0.011	0.011	0.000	0.000	0.000	0.000
14	A	14	THR	0	0.001	-0.009	34.850	0.003	0.003	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.021	0.002	36.400	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	ASN	0	0.029	-0.012	39.912	0.003	0.003	0.000	0.000	0.000	0.000
17	A	17	TYR	0	-0.013	-0.010	42.680	0.007	0.007	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.935	0.981	41.926	0.091	0.091	0.000	0.000	0.000	0.000
19	A	19	GLY	0	0.003	0.008	41.414	0.003	0.003	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.027	-0.009	38.909	0.002	0.002	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.020	-0.005	33.930	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.018	0.006	34.780	0.003	0.003	0.000	0.000	0.000	0.000
23	A	23	SER	0	0.008	-0.014	29.506	-0.011	-0.011	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.041	-0.033	28.400	0.015	0.015	0.000	0.000	0.000	0.000
25	A	25	SER	0	0.022	0.015	28.685	0.002	0.002	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.073	-0.040	24.727	-0.007	-0.007	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.007	0.025	22.104	0.004	0.004	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.027	-0.030	19.649	-0.012	-0.012	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.032	0.012	16.257	0.008	0.008	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.937	0.976	18.194	0.476	0.476	0.000	0.000	0.000	0.000
31	A	31	GLN	0	-0.034	-0.011	13.290	0.159	0.159	0.000	0.000	0.000	0.000
32	A	32	PRO	0	0.021	-0.003	15.538	-0.020	-0.020	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.024	0.000	12.173	-0.109	-0.109	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.003	-0.009	10.687	0.083	0.083	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.044	0.026	8.154	-0.285	-0.285	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.058	-0.022	7.462	0.292	0.292	0.000	0.000	0.000	0.000
37	A	37	MET	0	0.005	-0.001	8.095	-0.404	-0.404	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.043	-0.026	6.245	0.172	0.172	0.000	0.000	0.000	0.000
39	A	39	LEU	0	0.033	0.026	9.585	0.219	0.219	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.011	-0.002	12.435	-0.099	-0.099	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.009	-0.007	15.400	0.076	0.076	0.000	0.000	0.000	0.000
42	A	42	TRP	0	-0.006	0.005	18.172	-0.015	-0.015	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.955	0.968	21.564	0.326	0.326	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.002	-0.008	25.044	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.876	-0.920	28.416	-0.182	-0.182	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.029	-0.017	31.866	0.000	0.000	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.009	-0.001	35.249	0.001	0.001	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.000	-0.010	38.588	0.004	0.004	0.000	0.000	0.000	0.000
49	A	49	PRO	0	-0.003	0.000	39.090	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.075	0.030	36.214	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	51	PRO	0	-0.039	-0.011	37.360	0.007	0.007	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.043	0.008	38.561	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	53	GLY	0	-0.008	-0.015	38.564	0.003	0.003	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.067	-0.021	33.635	0.000	0.000	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.849	0.909	30.297	0.153	0.153	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.003	-0.006	27.962	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.915	0.971	26.622	0.176	0.176	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.016	0.020	20.379	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	59	CYS	0	-0.049	-0.034	21.957	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	60	SER	0	0.045	0.032	19.012	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.021	-0.018	20.635	0.016	0.016	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.016	-0.013	21.226	0.025	0.025	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.862	0.939	15.546	0.386	0.386	0.000	0.000	0.000	0.000
64	A	65	VAL	0	-0.011	0.005	19.858	0.006	0.006	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.767	-0.873	23.256	-0.182	-0.182	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.066	-0.028	23.238	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.880	-0.938	26.372	-0.155	-0.155	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.028	0.023	27.554	-0.012	-0.012	0.000	0.000	0.000	0.000
69	A	70	GLN	0	-0.031	-0.029	28.902	0.003	0.003	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.044	-0.040	24.578	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.031	0.026	22.707	0.025	0.025	0.000	0.000	0.000	0.000
72	A	73	THR	0	-0.014	-0.008	17.477	-0.033	-0.033	0.000	0.000	0.000	0.000
73	A	74	THR	0	0.021	0.019	17.364	0.041	0.041	0.000	0.000	0.000	0.000
74	A	75	HIS	0	0.083	0.032	10.993	-0.135	-0.135	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.013	0.005	15.107	0.001	0.001	0.000	0.000	0.000	0.000
76	A	77	PHE	0	-0.010	-0.015	14.973	0.040	0.040	0.000	0.000	0.000	0.000
77	A	78	ALA	0	0.019	0.022	11.675	-0.068	-0.068	0.000	0.000	0.000	0.000
78	A	79	HIS	0	-0.034	-0.044	9.936	0.089	0.089	0.000	0.000	0.000	0.000
79	A	80	VAL	0	-0.013	0.017	11.890	0.078	0.078	0.000	0.000	0.000	0.000
80	A	81	PRO	0	0.055	0.032	12.503	-0.154	-0.154	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.024	-0.005	10.686	0.036	0.036	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.005	-0.004	12.791	0.019	0.019	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.885	-0.942	15.945	-0.328	-0.328	0.000	0.000	0.000	0.000
84	A	85	PRO	0	-0.014	-0.005	17.904	-0.036	-0.036	0.000	0.000	0.000	0.000
85	A	86	LEU	0	-0.019	-0.017	17.318	0.013	0.013	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.939	0.967	21.454	0.275	0.275	0.000	0.000	0.000	0.000
87	A	88	PHE	0	0.036	0.026	23.851	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.021	-0.015	26.930	0.014	0.014	0.000	0.000	0.000	0.000
89	A	90	TRP	0	-0.022	-0.017	29.454	0.001	0.001	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.883	-0.956	32.853	-0.124	-0.124	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.008	0.011	35.972	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	93	PRO	0	0.040	0.029	37.495	0.006	0.006	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.005	-0.001	40.357	0.003	0.003	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.041	0.009	44.116	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.024	0.017	46.610	0.001	0.001	0.000	0.000	0.000	0.000
96	A	97	ARG	1	0.957	0.971	46.458	0.074	0.074	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.037	-0.007	40.311	0.002	0.002	0.000	0.000	0.000	0.000
98	A	99	ILE	0	-0.065	-0.004	45.020	0.000	0.000	0.000	0.000	0.000	0.000
99	A	100	PRO	0	0.012	-0.005	43.476	0.002	0.002	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.028	-0.009	42.528	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.034	0.030	34.896	0.000	0.000	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.914	0.953	38.097	0.119	0.119	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.039	0.030	31.198	0.000	0.000	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.930	0.981	33.819	0.166	0.166	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.034	-0.023	29.283	-0.007	-0.007	0.000	0.000	0.000	0.000
106	A	107	ASN	0	0.048	0.018	26.669	0.019	0.019	0.000	0.000	0.000	0.000
107	A	108	GLN	0	0.005	0.002	22.422	0.025	0.025	0.000	0.000	0.000	0.000
108	A	109	VAL	0	0.011	0.005	18.762	0.011	0.011	0.000	0.000	0.000	0.000
109	A	110	ILE	0	-0.002	-0.003	14.821	0.001	0.001	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.007	-0.003	12.347	0.016	0.016	0.000	0.000	0.000	0.000
111	A	112	ASN	0	-0.013	-0.002	9.173	-0.183	-0.183	0.000	0.000	0.000	0.000
112	A	113	TYR	0	0.003	-0.006	7.770	0.361	0.361	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.985	1.013	2.588	0.404	1.011	0.223	-0.273	-0.557	0.002
114	A	115	HIS	0	-0.025	-0.006	3.830	1.247	2.113	0.006	-0.342	-0.530	0.001

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