FMO DATABASE

FMODB ID: JLL19

Calculation Name: 5HXL-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5HXL

Chain ID: A

ChEMBL ID:

UniProt ID: G4NCW2

Base Structure: X-ray

Registration Date: 2023-06-21

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	OptHSide
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	123
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-953173.750633
FMO2-HF: Nuclear repulsion	904829.308514
FMO2-HF: Total energy	-48344.442118
FMO2-MP2: Total energy	-48483.099444

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:-2:HIS)

Summations of interaction energy for fragment #1(A:-2:HIS)

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.
-37.365	-28.122	25.425	-13.813	-20.853	-0.037

Interaction energy analysis for fragmet #1(A:-2:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.005 / q_NPA : -0.019

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	0	SER	0	0.024	0.013	3.183	-7.745	-3.180	0.144	-1.835	-2.873	0.010
4	A	1	MET	0	-0.059	-0.042	4.013	0.875	1.076	0.007	-0.037	-0.171	0.000
5	A	2	ALA	0	-0.023	-0.004	6.701	0.438	0.438	0.000	0.000	0.000	0.000
6	A	3	ALA	0	0.003	0.004	7.813	0.033	0.033	0.000	0.000	0.000	0.000
7	A	4	GLN	0	-0.035	-0.022	6.269	-0.637	-0.637	0.000	0.000	0.000	0.000
8	A	5	GLY	0	0.048	0.040	10.523	0.167	0.167	0.000	0.000	0.000	0.000
9	A	6	PRO	0	-0.065	-0.038	11.511	0.040	0.040	0.000	0.000	0.000	0.000
10	A	7	SER	0	0.012	-0.020	11.552	-0.084	-0.084	0.000	0.000	0.000	0.000
11	A	8	PRO	0	-0.030	-0.001	13.204	0.031	0.031	0.000	0.000	0.000	0.000
12	A	9	ILE	0	-0.007	0.010	15.081	0.021	0.021	0.000	0.000	0.000	0.000
13	A	10	PRO	0	0.047	0.035	14.754	0.062	0.062	0.000	0.000	0.000	0.000
14	A	11	THR	0	0.075	0.021	11.138	-0.012	-0.012	0.000	0.000	0.000	0.000
15	A	12	ASN	0	-0.035	-0.020	13.631	0.120	0.120	0.000	0.000	0.000	0.000
16	A	13	ARG	1	0.820	0.873	16.365	-0.319	-0.319	0.000	0.000	0.000	0.000
17	A	14	LEU	0	0.029	0.018	11.080	0.020	0.020	0.000	0.000	0.000	0.000
18	A	15	LYS	1	0.962	0.969	12.410	-0.811	-0.811	0.000	0.000	0.000	0.000
19	A	16	GLN	0	-0.007	0.011	13.636	0.003	0.003	0.000	0.000	0.000	0.000
20	A	17	ILE	0	-0.006	0.008	16.186	-0.022	-0.022	0.000	0.000	0.000	0.000
21	A	18	ALA	0	0.012	-0.001	12.161	-0.034	-0.034	0.000	0.000	0.000	0.000
22	A	19	ALA	0	-0.001	0.006	14.238	0.001	0.001	0.000	0.000	0.000	0.000
23	A	20	ASP	-1	-0.903	-0.960	15.488	0.468	0.468	0.000	0.000	0.000	0.000
24	A	21	ALA	0	0.005	0.008	16.270	-0.043	-0.043	0.000	0.000	0.000	0.000
25	A	22	CYS	0	-0.069	-0.037	13.847	0.002	0.002	0.000	0.000	0.000	0.000
26	A	23	ASN	0	-0.016	-0.014	16.572	-0.011	-0.011	0.000	0.000	0.000	0.000
27	A	24	ASP	-1	-0.904	-0.943	19.499	0.324	0.324	0.000	0.000	0.000	0.000
28	A	25	ALA	0	-0.077	-0.020	18.759	-0.039	-0.039	0.000	0.000	0.000	0.000
29	A	26	ILE	0	-0.027	-0.033	16.563	-0.029	-0.029	0.000	0.000	0.000	0.000
30	A	27	GLY	0	0.044	0.024	20.254	0.020	0.020	0.000	0.000	0.000	0.000
31	A	28	SER	0	-0.073	-0.039	21.563	0.000	0.000	0.000	0.000	0.000	0.000
32	A	29	ALA	0	-0.047	-0.011	21.469	-0.031	-0.031	0.000	0.000	0.000	0.000
33	A	30	GLU	-1	-0.908	-0.956	22.685	0.336	0.336	0.000	0.000	0.000	0.000
34	A	31	PHE	0	0.025	0.011	22.425	0.010	0.010	0.000	0.000	0.000	0.000
35	A	32	TYR	0	0.004	-0.005	16.827	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	33	ASP	-1	-0.826	-0.924	20.573	0.200	0.200	0.000	0.000	0.000	0.000
37	A	34	HIS	0	0.034	0.009	20.908	0.021	0.021	0.000	0.000	0.000	0.000
38	A	35	ALA	0	-0.036	-0.018	21.974	-0.023	-0.023	0.000	0.000	0.000	0.000
39	A	36	LYS	1	0.870	0.931	23.115	-0.261	-0.261	0.000	0.000	0.000	0.000
40	A	37	THR	0	-0.018	-0.003	17.838	0.000	0.000	0.000	0.000	0.000	0.000
41	A	38	GLU	-1	-0.877	-0.916	18.712	0.067	0.067	0.000	0.000	0.000	0.000
42	A	39	GLN	0	0.030	0.004	20.452	0.015	0.015	0.000	0.000	0.000	0.000
43	A	40	TRP	0	0.023	0.012	18.507	0.004	0.004	0.000	0.000	0.000	0.000
44	A	41	ASN	0	0.047	0.016	13.878	0.136	0.136	0.000	0.000	0.000	0.000
45	A	42	HIS	0	-0.060	-0.033	17.138	0.004	0.004	0.000	0.000	0.000	0.000
46	A	43	GLN	0	0.009	0.015	19.977	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	44	ILE	0	0.053	0.036	14.235	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	45	ILE	0	0.006	-0.001	14.550	0.012	0.012	0.000	0.000	0.000	0.000
49	A	46	ASN	0	-0.068	-0.047	17.078	-0.059	-0.059	0.000	0.000	0.000	0.000
50	A	47	THR	0	-0.030	-0.018	19.255	-0.033	-0.033	0.000	0.000	0.000	0.000
51	A	48	ILE	0	0.014	0.001	13.507	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	49	LEU	0	-0.004	0.002	16.494	-0.031	-0.031	0.000	0.000	0.000	0.000
53	A	50	LYS	1	0.966	0.983	17.917	-0.157	-0.157	0.000	0.000	0.000	0.000
54	A	51	ALA	0	0.006	0.006	18.836	-0.022	-0.022	0.000	0.000	0.000	0.000
55	A	52	VAL	0	0.021	0.003	14.473	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	53	ILE	0	-0.009	0.013	17.824	-0.044	-0.044	0.000	0.000	0.000	0.000
57	A	54	ALA	0	-0.015	0.000	20.314	-0.019	-0.019	0.000	0.000	0.000	0.000
58	A	55	GLU	-1	-0.788	-0.868	19.965	0.264	0.264	0.000	0.000	0.000	0.000
59	A	56	SER	0	-0.067	-0.039	18.159	-0.014	-0.014	0.000	0.000	0.000	0.000
60	A	57	GLN	0	-0.078	-0.047	20.235	-0.050	-0.050	0.000	0.000	0.000	0.000
61	A	58	PRO	0	-0.001	0.007	23.744	0.018	0.018	0.000	0.000	0.000	0.000
62	A	59	SER	0	0.004	0.001	25.891	0.006	0.006	0.000	0.000	0.000	0.000
63	A	60	ASP	-1	-0.869	-0.893	28.835	-0.036	-0.036	0.000	0.000	0.000	0.000
64	A	61	SER	0	0.051	0.006	30.200	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	62	THR	0	-0.121	-0.073	32.159	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	63	THR	0	-0.053	-0.034	26.562	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	64	PRO	0	-0.005	0.007	26.938	0.008	0.008	0.000	0.000	0.000	0.000
68	A	65	PRO	0	0.075	0.022	22.563	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	66	GLN	0	-0.044	-0.020	21.291	-0.036	-0.036	0.000	0.000	0.000	0.000
70	A	67	PHE	0	-0.013	0.003	15.361	-0.030	-0.030	0.000	0.000	0.000	0.000
71	A	68	LYS	1	0.883	0.949	16.527	0.466	0.466	0.000	0.000	0.000	0.000
72	A	69	PHE	0	0.037	-0.004	13.188	-0.034	-0.034	0.000	0.000	0.000	0.000
73	A	70	ALA	0	-0.022	0.002	11.149	0.006	0.006	0.000	0.000	0.000	0.000
74	A	71	VAL	0	0.021	0.003	11.111	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	72	ASN	0	-0.032	-0.014	8.706	0.116	0.116	0.000	0.000	0.000	0.000
76	A	73	SER	0	0.032	0.004	10.312	0.372	0.372	0.000	0.000	0.000	0.000
77	A	74	THR	0	-0.029	-0.007	8.742	-0.332	-0.332	0.000	0.000	0.000	0.000
78	A	75	ILE	0	0.011	0.009	10.585	0.266	0.266	0.000	0.000	0.000	0.000
79	A	76	VAL	0	-0.040	-0.026	9.279	-0.135	-0.135	0.000	0.000	0.000	0.000
80	A	77	GLN	0	0.029	0.025	12.582	0.048	0.048	0.000	0.000	0.000	0.000
81	A	78	HIS	0	-0.058	-0.035	13.889	-0.055	-0.055	0.000	0.000	0.000	0.000
82	A	79	LEU	0	-0.007	0.003	14.341	-0.120	-0.120	0.000	0.000	0.000	0.000
83	A	113	GLY	0	0.010	-0.005	10.304	0.059	0.059	0.000	0.000	0.000	0.000
84	A	114	MET	0	-0.015	-0.005	6.065	-0.441	-0.441	0.000	0.000	0.000	0.000
85	A	115	HIS	0	-0.015	-0.003	4.047	1.303	1.767	0.001	-0.094	-0.371	0.000
86	A	116	SER	0	0.007	0.006	2.391	-7.207	-4.314	1.647	-2.011	-2.530	-0.006
87	A	117	ALA	0	0.028	0.004	2.268	-2.200	0.414	4.305	-3.429	-3.490	-0.028
88	A	118	THR	0	0.002	0.009	1.862	-13.750	-15.778	8.800	-2.874	-3.898	-0.029
89	A	119	GLY	0	0.043	0.032	3.416	1.764	2.079	0.012	-0.124	-0.202	-0.001
90	A	120	ALA	0	-0.015	-0.009	6.967	-0.251	-0.251	0.000	0.000	0.000	0.000
91	A	121	PHE	0	-0.020	-0.001	9.485	0.263	0.263	0.000	0.000	0.000	0.000
92	A	122	TRP	0	-0.029	-0.019	6.431	-0.117	-0.117	0.000	0.000	0.000	0.000
93	A	123	ASN	0	0.007	0.003	13.967	0.083	0.083	0.000	0.000	0.000	0.000
94	A	124	ASP	-1	-0.872	-0.941	12.810	-0.873	-0.873	0.000	0.000	0.000	0.000
95	A	125	LYS	1	0.895	0.939	13.846	0.458	0.458	0.000	0.000	0.000	0.000
96	A	126	THR	0	-0.048	-0.054	15.162	0.087	0.087	0.000	0.000	0.000	0.000
97	A	127	ASP	-1	-0.754	-0.855	11.857	-0.636	-0.636	0.000	0.000	0.000	0.000
98	A	128	GLY	0	0.045	0.020	8.284	0.019	0.019	0.000	0.000	0.000	0.000
99	A	129	MET	0	-0.046	-0.004	2.273	-2.094	-4.510	7.285	-1.598	-3.271	-0.003
100	A	130	TRP	0	0.013	0.011	5.720	0.551	0.551	0.000	0.000	0.000	0.000
101	A	131	THR	0	-0.029	-0.017	2.536	-8.477	-6.003	3.226	-1.801	-3.899	0.020
102	A	132	TYR	0	-0.037	-0.040	5.440	-0.574	-0.525	-0.001	-0.002	-0.045	0.000
103	A	133	LYS	1	0.812	0.895	6.269	-1.977	-1.977	0.000	0.000	0.000	0.000
104	A	134	HIS	0	0.036	0.028	7.924	-0.167	-0.167	0.000	0.000	0.000	0.000
105	A	135	GLU	-1	-0.917	-0.945	10.858	1.469	1.469	0.000	0.000	0.000	0.000
106	A	136	GLY	0	0.011	0.014	12.639	-0.142	-0.142	0.000	0.000	0.000	0.000
107	A	137	ASP	-1	-0.880	-0.959	15.764	0.602	0.602	0.000	0.000	0.000	0.000
108	A	138	GLU	-1	-0.944	-0.992	18.374	0.451	0.451	0.000	0.000	0.000	0.000
109	A	139	SER	0	-0.008	-0.002	20.200	-0.016	-0.016	0.000	0.000	0.000	0.000
110	A	140	LYS	1	0.786	0.923	17.965	-0.564	-0.564	0.000	0.000	0.000	0.000
111	A	141	GLY	0	0.048	0.018	18.762	-0.034	-0.034	0.000	0.000	0.000	0.000
112	A	142	MET	0	-0.082	-0.042	15.257	-0.037	-0.037	0.000	0.000	0.000	0.000
113	A	143	ASP	-1	-0.791	-0.870	10.389	1.636	1.636	0.000	0.000	0.000	0.000
114	A	144	VAL	0	-0.004	-0.003	11.274	-0.130	-0.130	0.000	0.000	0.000	0.000
115	A	145	VAL	0	-0.025	-0.006	4.587	0.249	0.361	-0.001	-0.008	-0.103	0.000
116	A	146	VAL	0	0.000	0.000	7.681	-0.580	-0.580	0.000	0.000	0.000	0.000
117	A	147	MET	0	-0.017	-0.007	4.815	0.867	0.867	0.000	0.000	0.000	0.000
118	A	148	LEU	0	-0.013	0.006	7.211	-0.558	-0.558	0.000	0.000	0.000	0.000
119	A	149	ILE	0	0.007	-0.006	5.852	-0.149	-0.149	0.000	0.000	0.000	0.000
120	A	150	TRP	0	-0.004	-0.001	8.653	0.223	0.223	0.000	0.000	0.000	0.000
121	A	151	ILE	0	-0.024	-0.017	11.462	-0.154	-0.154	0.000	0.000	0.000	0.000
122	A	152	ALA	0	0.033	0.027	14.200	0.104	0.104	0.000	0.000	0.000	0.000
123	A	153	VAL	0	-0.052	-0.032	17.341	-0.033	-0.033	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-2:HIS)