FMO DATABASE

FMODB ID: JQQ99

Calculation Name: 5X5J-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5X5J

Chain ID: A

ChEMBL ID:

UniProt ID: Q6TA00

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	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	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1046003.718135
FMO2-HF: Nuclear repulsion	998175.474832
FMO2-HF: Total energy	-47828.243303
FMO2-MP2: Total energy	-47967.074159

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:10:CYS)

Summations of interaction energy for fragment #1(A:10:CYS)

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.
-7.079	-4.333	10.764	-4.141	-9.367	-0.013

Interaction energy analysis for fragmet #1(A:10:CYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.030 / q_NPA : -0.018

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	12	ASP	-1	-0.929	-0.960	3.791	-0.753	0.484	0.000	-0.371	-0.866	0.002
4	A	13	LYS	1	0.886	0.969	2.664	1.234	2.145	1.066	-0.582	-1.396	-0.003
5	A	14	VAL	0	0.011	-0.001	5.231	-0.217	-0.198	-0.001	-0.004	-0.014	0.000
6	A	15	ILE	0	-0.028	-0.015	5.059	0.224	0.224	0.000	0.000	0.000	0.000
7	A	16	LEU	0	-0.009	0.002	8.943	0.105	0.105	0.000	0.000	0.000	0.000
8	A	17	VAL	0	0.007	-0.007	11.900	0.048	0.048	0.000	0.000	0.000	0.000
9	A	18	VAL	0	-0.032	-0.021	14.217	0.032	0.032	0.000	0.000	0.000	0.000
10	A	19	GLH	0	-0.072	-0.093	17.731	0.033	0.033	0.000	0.000	0.000	0.000
11	A	20	ASP	-1	-0.924	-0.969	19.835	-0.172	-0.172	0.000	0.000	0.000	0.000
12	A	21	ASP	-1	-0.855	-0.902	22.466	-0.156	-0.156	0.000	0.000	0.000	0.000
13	A	22	TYR	0	0.010	-0.034	21.224	-0.024	-0.024	0.000	0.000	0.000	0.000
14	A	23	ASP	-1	-0.834	-0.898	20.341	-0.191	-0.191	0.000	0.000	0.000	0.000
15	A	24	ILE	0	-0.046	-0.033	18.413	-0.015	-0.015	0.000	0.000	0.000	0.000
16	A	25	GLY	0	-0.008	-0.015	16.782	-0.024	-0.024	0.000	0.000	0.000	0.000
17	A	26	ASP	-1	-0.807	-0.891	15.538	-0.351	-0.351	0.000	0.000	0.000	0.000
18	A	27	ILE	0	-0.092	-0.044	15.330	-0.037	-0.037	0.000	0.000	0.000	0.000
19	A	28	ILE	0	-0.007	-0.010	11.800	-0.019	-0.019	0.000	0.000	0.000	0.000
20	A	29	GLU	-1	-0.844	-0.916	11.095	-0.686	-0.686	0.000	0.000	0.000	0.000
21	A	30	ASN	0	0.009	-0.001	10.630	-0.134	-0.134	0.000	0.000	0.000	0.000
22	A	31	TYR	0	-0.009	-0.012	10.235	-0.037	-0.037	0.000	0.000	0.000	0.000
23	A	32	LEU	0	0.017	-0.002	6.671	0.029	0.029	0.000	0.000	0.000	0.000
24	A	33	LYS	1	0.930	0.966	5.836	0.271	0.271	0.000	0.000	0.000	0.000
25	A	34	ARG	1	0.810	0.916	7.586	0.145	0.145	0.000	0.000	0.000	0.000
26	A	35	GLU	-1	-0.918	-0.956	3.964	0.589	0.942	0.012	-0.065	-0.300	0.000
27	A	36	GLY	0	-0.012	-0.001	3.342	-2.822	-1.923	0.060	-0.502	-0.457	-0.004
28	A	37	MET	0	-0.072	-0.026	2.426	-1.577	-0.825	2.145	-0.675	-2.223	-0.004
29	A	38	SER	0	0.007	-0.003	4.757	1.251	1.336	-0.001	-0.008	-0.075	0.000
30	A	39	VAL	0	-0.029	-0.017	8.417	-0.094	-0.094	0.000	0.000	0.000	0.000
31	A	40	ILE	0	0.007	0.013	10.831	0.123	0.123	0.000	0.000	0.000	0.000
32	A	41	ARG	1	0.827	0.903	14.280	0.388	0.388	0.000	0.000	0.000	0.000
33	A	42	ALA	0	0.002	0.005	16.903	0.028	0.028	0.000	0.000	0.000	0.000
34	A	43	MET	0	0.018	0.009	19.375	0.002	0.002	0.000	0.000	0.000	0.000
35	A	44	ASN	0	0.020	0.007	22.348	0.017	0.017	0.000	0.000	0.000	0.000
36	A	45	GLY	0	0.073	0.023	22.407	-0.019	-0.019	0.000	0.000	0.000	0.000
37	A	46	LYS	1	0.848	0.919	23.226	0.148	0.148	0.000	0.000	0.000	0.000
38	A	47	GLN	0	0.038	0.024	21.860	-0.022	-0.022	0.000	0.000	0.000	0.000
39	A	48	ALA	0	0.026	0.016	18.946	-0.022	-0.022	0.000	0.000	0.000	0.000
40	A	49	ILE	0	-0.019	-0.013	19.245	-0.018	-0.018	0.000	0.000	0.000	0.000
41	A	50	GLU	-1	-0.936	-0.967	21.379	-0.223	-0.223	0.000	0.000	0.000	0.000
42	A	51	LEU	0	-0.009	-0.015	17.521	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	52	HIS	0	-0.023	-0.031	15.167	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	53	ALA	0	-0.113	-0.066	17.539	0.003	0.003	0.000	0.000	0.000	0.000
45	A	54	SER	0	0.002	0.009	19.767	0.003	0.003	0.000	0.000	0.000	0.000
46	A	55	GLN	0	-0.023	-0.002	15.015	-0.036	-0.036	0.000	0.000	0.000	0.000
47	A	56	PRO	0	-0.012	-0.003	12.294	0.027	0.027	0.000	0.000	0.000	0.000
48	A	57	ILE	0	-0.033	-0.006	11.203	-0.127	-0.127	0.000	0.000	0.000	0.000
49	A	58	ASP	-1	-0.856	-0.926	6.948	-1.248	-1.248	0.000	0.000	0.000	0.000
50	A	59	LEU	0	-0.058	-0.032	7.453	0.128	0.128	0.000	0.000	0.000	0.000
51	A	60	ILE	0	-0.015	-0.004	9.493	-0.063	-0.063	0.000	0.000	0.000	0.000
52	A	61	LEU	0	-0.011	-0.001	10.213	0.059	0.059	0.000	0.000	0.000	0.000
53	A	62	LEU	0	0.010	-0.007	13.284	-0.007	-0.007	0.000	0.000	0.000	0.000
54	A	63	ASP	-1	-0.731	-0.812	17.028	-0.141	-0.141	0.000	0.000	0.000	0.000
55	A	64	ILE	0	-0.023	-0.017	19.831	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	65	LYS	1	0.894	0.954	22.875	0.127	0.127	0.000	0.000	0.000	0.000
57	A	66	LEU	0	-0.009	-0.010	21.398	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	67	PRO	0	0.011	0.010	25.500	0.011	0.011	0.000	0.000	0.000	0.000
59	A	68	GLU	-1	-0.841	-0.926	28.141	-0.142	-0.142	0.000	0.000	0.000	0.000
60	A	69	LEU	0	-0.059	-0.017	26.392	0.007	0.007	0.000	0.000	0.000	0.000
61	A	70	ASN	0	0.092	0.030	27.505	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	71	GLY	0	0.093	0.031	23.779	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	72	TRP	0	0.046	0.015	22.548	-0.018	-0.018	0.000	0.000	0.000	0.000
64	A	73	GLU	-1	-0.869	-0.943	24.651	-0.109	-0.109	0.000	0.000	0.000	0.000
65	A	74	VAL	0	-0.065	-0.011	20.932	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	75	LEU	0	0.017	0.009	18.455	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	76	ASN	0	-0.036	-0.016	21.334	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	77	LYS	1	0.958	0.971	24.336	0.140	0.140	0.000	0.000	0.000	0.000
69	A	78	ILE	0	-0.002	0.002	17.747	0.001	0.001	0.000	0.000	0.000	0.000
70	A	79	ARG	1	0.786	0.878	15.847	0.223	0.223	0.000	0.000	0.000	0.000
71	A	80	GLN	0	-0.021	0.013	21.519	0.012	0.012	0.000	0.000	0.000	0.000
72	A	81	LYS	1	0.863	0.953	20.209	0.246	0.246	0.000	0.000	0.000	0.000
73	A	82	ALA	0	0.000	-0.011	17.638	0.004	0.004	0.000	0.000	0.000	0.000
74	A	83	GLN	0	-0.009	-0.018	17.528	0.003	0.003	0.000	0.000	0.000	0.000
75	A	84	THR	0	0.028	0.039	12.324	0.024	0.024	0.000	0.000	0.000	0.000
76	A	85	PRO	0	0.060	0.046	10.128	0.048	0.048	0.000	0.000	0.000	0.000
77	A	86	VAL	0	-0.034	-0.015	12.346	-0.063	-0.063	0.000	0.000	0.000	0.000
78	A	87	ILE	0	0.006	0.010	10.024	0.045	0.045	0.000	0.000	0.000	0.000
79	A	88	MET	0	-0.049	-0.013	13.872	-0.031	-0.031	0.000	0.000	0.000	0.000
80	A	89	LEU	0	0.020	0.012	14.924	0.024	0.024	0.000	0.000	0.000	0.000
81	A	90	THR	0	0.016	-0.024	18.520	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	91	ALA	0	0.039	0.008	22.037	0.005	0.005	0.000	0.000	0.000	0.000
83	A	92	LEU	0	-0.031	-0.016	23.799	0.006	0.006	0.000	0.000	0.000	0.000
84	A	93	ASP	-1	-0.853	-0.881	26.301	-0.047	-0.047	0.000	0.000	0.000	0.000
85	A	94	GLN	0	-0.082	-0.081	29.474	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	95	ASP	-1	-0.896	-0.941	29.090	-0.076	-0.076	0.000	0.000	0.000	0.000
87	A	96	ILE	0	-0.075	-0.050	26.061	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	97	ASP	-1	-0.850	-0.920	26.887	-0.051	-0.051	0.000	0.000	0.000	0.000
89	A	98	LYS	1	0.982	0.994	26.561	0.042	0.042	0.000	0.000	0.000	0.000
90	A	99	VAL	0	-0.018	-0.017	24.693	0.001	0.001	0.000	0.000	0.000	0.000
91	A	100	MET	0	0.015	0.019	21.393	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	101	ALA	0	0.037	0.018	21.963	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	102	LEU	0	-0.099	-0.054	23.083	0.003	0.003	0.000	0.000	0.000	0.000
94	A	103	ARG	1	0.849	0.945	17.472	0.148	0.148	0.000	0.000	0.000	0.000
95	A	104	ILE	0	-0.026	0.027	17.992	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	105	GLY	0	-0.001	-0.009	19.307	0.013	0.013	0.000	0.000	0.000	0.000
97	A	106	ALA	0	-0.060	-0.047	14.451	0.015	0.015	0.000	0.000	0.000	0.000
98	A	107	ASP	-1	-0.838	-0.908	13.734	-0.237	-0.237	0.000	0.000	0.000	0.000
99	A	108	ASP	-1	-0.802	-0.909	13.634	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	109	PHE	0	-0.073	-0.057	15.434	-0.031	-0.031	0.000	0.000	0.000	0.000
101	A	110	VAL	0	0.015	0.011	14.127	0.020	0.020	0.000	0.000	0.000	0.000
102	A	111	VAL	0	0.010	0.002	17.248	-0.018	-0.018	0.000	0.000	0.000	0.000
103	A	112	LYS	1	0.808	0.923	20.489	0.136	0.136	0.000	0.000	0.000	0.000
104	A	113	PRO	0	0.001	-0.007	22.154	0.004	0.004	0.000	0.000	0.000	0.000
105	A	114	PHE	0	0.082	0.021	15.894	0.008	0.008	0.000	0.000	0.000	0.000
106	A	115	ASN	0	0.041	0.026	16.182	-0.011	-0.011	0.000	0.000	0.000	0.000
107	A	116	PRO	0	0.046	0.011	14.075	0.013	0.013	0.000	0.000	0.000	0.000
108	A	117	ASN	0	-0.011	-0.024	11.688	0.032	0.032	0.000	0.000	0.000	0.000
109	A	118	GLU	-1	-0.866	-0.908	11.348	0.082	0.082	0.000	0.000	0.000	0.000
110	A	119	VAL	0	0.010	0.005	10.236	0.026	0.026	0.000	0.000	0.000	0.000
111	A	120	ILE	0	0.020	0.023	5.834	-0.106	-0.055	-0.001	-0.001	-0.049	0.000
112	A	121	ALA	0	0.004	0.006	6.950	0.356	0.356	0.000	0.000	0.000	0.000
113	A	122	ARG	1	0.821	0.890	8.517	0.008	0.008	0.000	0.000	0.000	0.000
114	A	123	VAL	0	0.022	0.014	4.720	-0.160	-0.098	-0.001	-0.003	-0.057	0.000
115	A	124	GLN	0	-0.007	-0.014	2.519	-2.090	-4.312	7.301	-1.776	-3.303	-0.003
116	A	125	ALA	0	-0.073	-0.035	4.724	-0.595	-0.519	-0.001	-0.009	-0.065	0.000
117	A	126	VAL	0	-0.011	-0.013	7.720	-0.057	-0.057	0.000	0.000	0.000	0.000
118	A	127	LEU	0	-0.016	-0.007	2.836	-0.722	-0.199	0.185	-0.145	-0.562	-0.001
119	A	128	ARG	1	0.903	0.970	5.799	-0.040	-0.040	0.000	0.000	0.000	0.000
120	A	129	ARG	1	0.929	0.978	6.670	0.146	0.146	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:CYS)