FMO DATABASE

FMODB ID: 52R9Z

Calculation Name: 4XUU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4XUU

Chain ID: A

ChEMBL ID:

UniProt ID: Q9Y2H2

Base Structure: X-ray

Registration Date: 2023-06-22

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	168
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1736779.492457
FMO2-HF: Nuclear repulsion	1667760.042174
FMO2-HF: Total energy	-69019.450283
FMO2-MP2: Total energy	-69218.164801

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:SER)

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

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.
1.223	3.318	-0.006	-1.22	-0.869	0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.038 / 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	3	SER	0	0.054	0.038	3.882	1.997	4.092	-0.006	-1.220	-0.869	0.004
4	A	4	HIS	0	0.050	0.007	6.443	-0.048	-0.048	0.000	0.000	0.000	0.000
5	A	5	GLN	0	0.074	0.039	8.933	-0.075	-0.075	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.920	-0.954	7.594	-0.761	-0.761	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.068	-0.035	7.425	-0.078	-0.078	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.030	0.018	9.126	-0.063	-0.063	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.018	-0.004	12.587	-0.032	-0.032	0.000	0.000	0.000	0.000
10	A	10	GLN	0	-0.032	-0.010	10.351	0.036	0.036	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.005	-0.006	11.966	0.008	0.008	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.014	0.018	14.237	-0.005	-0.005	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.031	-0.024	14.783	0.028	0.028	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.012	-0.001	15.460	0.006	0.006	0.000	0.000	0.000	0.000
15	A	15	TYR	0	0.035	0.009	17.484	0.007	0.007	0.000	0.000	0.000	0.000
16	A	16	MET	0	0.007	0.000	19.865	0.003	0.003	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.824	0.909	20.371	0.085	0.085	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.056	-0.044	19.176	0.002	0.002	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.048	-0.001	23.023	0.008	0.008	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.013	-0.004	25.663	0.005	0.005	0.000	0.000	0.000	0.000
21	A	21	PRO	0	0.007	0.011	27.167	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.873	-0.927	26.175	-0.082	-0.082	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.973	-0.981	28.546	-0.054	-0.054	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.764	-0.819	30.525	-0.028	-0.028	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.918	0.945	28.834	0.077	0.077	0.000	0.000	0.000	0.000
26	A	26	PHE	0	0.032	0.012	28.031	0.004	0.004	0.000	0.000	0.000	0.000
27	A	27	HIS	0	-0.069	-0.041	29.954	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.010	-0.005	32.082	0.000	0.000	0.000	0.000	0.000	0.000
29	A	29	GLY	0	-0.013	-0.004	31.378	0.000	0.000	0.000	0.000	0.000	0.000
30	A	30	TRP	0	-0.026	-0.022	32.356	0.000	0.000	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.028	0.025	32.585	0.001	0.001	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.069	-0.032	34.320	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.011	0.014	37.618	0.003	0.003	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.793	-0.904	40.367	0.012	0.012	0.000	0.000	0.000	0.000
35	A	35	CYS	0	-0.193	-0.091	43.190	0.002	0.002	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.766	-0.845	46.778	0.007	0.007	0.000	0.000	0.000	0.000
37	A	37	PRO	0	-0.045	-0.031	48.193	0.001	0.001	0.000	0.000	0.000	0.000
38	A	38	SER	0	0.025	0.023	45.597	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.046	-0.034	48.506	0.000	0.000	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.007	0.011	44.514	0.000	0.000	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.797	-0.900	47.561	0.027	0.027	0.000	0.000	0.000	0.000
42	A	42	ALA	0	-0.052	-0.007	49.249	0.000	0.000	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.063	-0.045	47.948	0.000	0.000	0.000	0.000	0.000	0.000
44	A	44	HIS	0	-0.056	-0.037	48.165	0.000	0.000	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.769	0.869	42.632	-0.032	-0.032	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.794	-0.868	41.067	0.023	0.023	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.029	0.018	39.743	0.002	0.002	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.877	-0.936	35.120	0.033	0.033	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.033	-0.031	36.578	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.036	0.002	29.499	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.003	0.009	33.877	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.002	-0.018	29.750	0.000	0.000	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.012	-0.007	33.209	0.001	0.001	0.000	0.000	0.000	0.000
54	A	54	SER	0	0.012	-0.022	32.598	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	55	ASN	0	0.020	0.008	33.595	0.002	0.002	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.012	-0.004	36.016	0.001	0.001	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.000	-0.001	35.842	0.003	0.003	0.000	0.000	0.000	0.000
58	A	58	TYR	0	0.030	0.019	36.284	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.047	-0.058	32.888	0.001	0.001	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.003	-0.004	35.602	0.001	0.001	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.013	-0.007	33.165	0.000	0.000	0.000	0.000	0.000	0.000
62	A	62	TYR	0	0.000	-0.012	35.180	0.002	0.002	0.000	0.000	0.000	0.000
63	A	63	TYR	0	-0.051	-0.029	28.821	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.878	-0.935	35.086	0.037	0.037	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.856	-0.927	35.875	0.038	0.038	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.903	-0.932	37.368	0.046	0.046	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.081	-0.047	31.467	0.006	0.006	0.000	0.000	0.000	0.000
68	A	68	ASP	-1	-0.886	-0.922	28.379	0.077	0.077	0.000	0.000	0.000	0.000
69	A	69	LYN	0	-0.086	-0.057	29.459	0.003	0.003	0.000	0.000	0.000	0.000
70	A	70	VAL	0	-0.040	-0.020	30.730	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.096	-0.052	33.128	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.038	-0.030	36.771	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	73	TYR	0	-0.019	-0.023	31.415	0.000	0.000	0.000	0.000	0.000	0.000
74	A	74	GLN	0	-0.027	-0.036	36.011	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	75	ARG	1	0.840	0.932	34.658	0.024	0.024	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.060	-0.036	36.802	0.000	0.000	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.010	-0.019	39.718	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.049	0.023	39.038	0.002	0.002	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.823	-0.900	42.307	-0.021	-0.021	0.000	0.000	0.000	0.000
80	A	80	ASN	0	-0.076	-0.042	43.933	0.002	0.002	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.001	0.013	42.980	0.002	0.002	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.806	-0.880	46.212	-0.008	-0.008	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.853	0.904	49.328	0.002	0.002	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.015	0.027	44.584	0.001	0.001	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.825	-0.881	48.729	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	86	ILE	0	0.029	0.012	47.331	0.001	0.001	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.040	0.020	50.626	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	88	PRO	0	-0.048	-0.031	51.543	0.001	0.001	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.718	-0.866	50.738	0.012	0.012	0.000	0.000	0.000	0.000
90	A	90	PRO	0	-0.013	0.005	51.331	0.000	0.000	0.000	0.000	0.000	0.000
91	A	91	THR	0	-0.049	-0.032	54.388	0.001	0.001	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.002	-0.002	55.427	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	93	PHE	0	-0.042	-0.023	58.096	0.000	0.000	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.005	0.009	58.738	0.001	0.001	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.933	0.964	58.504	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	96	PRO	0	0.024	0.025	54.524	0.001	0.001	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.793	0.890	51.301	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.063	0.029	47.895	0.000	0.000	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.070	-0.059	49.104	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	101	MET	0	0.010	0.008	42.304	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	102	ARG	1	0.787	0.868	45.883	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	103	LEU	0	0.032	0.012	41.718	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.025	-0.033	46.246	0.001	0.001	0.000	0.000	0.000	0.000
104	A	105	TYR	0	-0.037	-0.034	44.687	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	106	ARG	1	0.788	0.865	47.807	0.008	0.008	0.000	0.000	0.000	0.000
106	A	107	TYR	0	-0.013	-0.046	43.624	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.798	0.879	46.915	0.000	0.000	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.908	-0.945	49.686	-0.009	-0.009	0.000	0.000	0.000	0.000
109	A	110	ALA	0	-0.015	0.013	51.973	0.000	0.000	0.000	0.000	0.000	0.000
110	A	111	SER	0	-0.003	-0.015	51.422	0.000	0.000	0.000	0.000	0.000	0.000
111	A	112	GLY	0	-0.016	-0.003	52.598	0.001	0.001	0.000	0.000	0.000	0.000
112	A	113	TYR	0	-0.025	0.005	47.721	0.001	0.001	0.000	0.000	0.000	0.000
113	A	114	PHE	0	-0.017	-0.034	47.487	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	115	HIS	0	0.031	0.055	42.213	0.003	0.003	0.000	0.000	0.000	0.000
115	A	116	THR	0	-0.021	-0.040	45.122	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	117	LEU	0	0.039	0.032	40.065	0.001	0.001	0.000	0.000	0.000	0.000
117	A	118	ARG	1	0.815	0.864	42.664	-0.022	-0.022	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.047	0.021	40.054	0.001	0.001	0.000	0.000	0.000	0.000
119	A	120	VAL	0	0.047	0.041	36.132	0.001	0.001	0.000	0.000	0.000	0.000
120	A	121	MET	0	-0.009	-0.009	39.631	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.918	0.935	38.760	-0.030	-0.030	0.000	0.000	0.000	0.000
122	A	123	ASN	0	0.049	0.030	42.085	0.002	0.002	0.000	0.000	0.000	0.000
123	A	124	PRO	0	-0.023	-0.009	45.723	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	125	GLU	-1	-0.994	-0.992	48.506	0.011	0.011	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.957	-0.972	45.709	0.007	0.007	0.000	0.000	0.000	0.000
126	A	127	ASP	-1	-0.830	-0.898	47.524	0.007	0.007	0.000	0.000	0.000	0.000
127	A	128	GLY	0	0.051	0.019	45.238	0.000	0.000	0.000	0.000	0.000	0.000
128	A	129	LYS	1	0.823	0.900	45.164	0.001	0.001	0.000	0.000	0.000	0.000
129	A	130	ASP	-1	-0.891	-0.948	45.782	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	131	THR	0	-0.019	-0.016	40.039	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	132	LEU	0	0.001	0.005	41.532	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	133	GLN	0	-0.037	-0.031	43.654	0.000	0.000	0.000	0.000	0.000	0.000
133	A	134	CYS	0	-0.014	-0.009	40.729	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	135	ILE	0	-0.010	0.003	38.605	-0.002	-0.002	0.000	0.000	0.000	0.000
135	A	136	ALA	0	0.004	-0.009	40.785	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.848	-0.912	43.604	-0.013	-0.013	0.000	0.000	0.000	0.000
137	A	138	MET	0	-0.018	0.005	35.551	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	139	LEU	0	0.014	0.002	39.590	-0.003	-0.003	0.000	0.000	0.000	0.000
139	A	140	GLN	0	-0.032	-0.012	41.659	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	141	ILE	0	0.006	-0.002	40.329	-0.002	-0.002	0.000	0.000	0.000	0.000
141	A	142	THR	0	-0.037	-0.018	38.038	-0.004	-0.004	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.817	0.907	40.918	0.014	0.014	0.000	0.000	0.000	0.000
143	A	144	GLN	0	-0.046	-0.042	43.814	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.057	-0.019	41.080	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	146	MET	0	-0.079	-0.021	41.337	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	147	GLY	0	-0.037	-0.011	43.287	0.000	0.000	0.000	0.000	0.000	0.000
147	A	148	SER	0	-0.071	-0.035	46.745	0.002	0.002	0.000	0.000	0.000	0.000
148	A	149	ASP	-1	-0.821	-0.916	48.468	-0.017	-0.017	0.000	0.000	0.000	0.000
149	A	150	LEU	0	-0.036	-0.017	45.159	0.001	0.001	0.000	0.000	0.000	0.000
150	A	151	PRO	0	-0.010	0.010	48.995	0.000	0.000	0.000	0.000	0.000	0.000
151	A	152	ILE	0	0.044	0.027	46.876	0.001	0.001	0.000	0.000	0.000	0.000
152	A	153	ILE	0	-0.065	-0.041	50.564	0.000	0.000	0.000	0.000	0.000	0.000
153	A	154	GLU	-1	-0.790	-0.874	52.764	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.746	0.855	54.532	0.000	0.000	0.000	0.000	0.000	0.000
155	A	156	LYS	1	0.942	0.964	55.252	-0.003	-0.003	0.000	0.000	0.000	0.000
156	A	157	LEU	0	0.067	0.052	50.647	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	158	GLU	-1	-0.866	-0.916	55.017	0.002	0.002	0.000	0.000	0.000	0.000
158	A	159	ALA	0	0.042	0.026	55.728	0.000	0.000	0.000	0.000	0.000	0.000
159	A	160	LYS	1	0.809	0.889	55.514	-0.002	-0.002	0.000	0.000	0.000	0.000
160	A	161	ALA	0	0.091	0.048	52.133	0.000	0.000	0.000	0.000	0.000	0.000
161	A	162	SER	0	0.005	0.000	49.049	-0.002	-0.002	0.000	0.000	0.000	0.000
162	A	163	LYS	1	0.836	0.912	51.026	0.000	0.000	0.000	0.000	0.000	0.000
163	A	164	PRO	0	-0.002	0.014	48.541	0.000	0.000	0.000	0.000	0.000	0.000
164	A	165	HIS	0	0.075	0.055	43.596	-0.002	-0.002	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.768	-0.838	43.814	0.004	0.004	0.000	0.000	0.000	0.000
166	A	167	ASP	-1	-0.768	-0.872	38.115	0.012	0.012	0.000	0.000	0.000	0.000
167	A	168	ILE	0	-0.040	-0.017	38.619	-0.001	-0.001	0.000	0.000	0.000	0.000
168	A	169	ILE	0	0.025	0.016	33.596	-0.002	-0.002	0.000	0.000	0.000	0.000

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