FMO DATABASE

FMODB ID: 14LZZ

Calculation Name: 1SJ5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SJ5

Chain ID: A

ChEMBL ID:

UniProt ID: Q9WY07

Base Structure: X-ray

Registration Date: 2023-06-20

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	143
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1252207.317931
FMO2-HF: Nuclear repulsion	1197270.690434
FMO2-HF: Total energy	-54936.627497
FMO2-MP2: Total energy	-55099.016318

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:0:HIS)

Summations of interaction energy for fragment #1(A:0: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.
-0.238	2.606	0.072	-1.19	-1.726	-0.002

Interaction energy analysis for fragmet #1(A:0:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.000 / 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	2	ARG	1	0.980	1.009	3.775	-0.382	1.245	-0.026	-0.716	-0.885	0.000
4	A	3	LYS	1	0.858	0.936	6.385	-0.590	-0.590	0.000	0.000	0.000	0.000
5	A	4	ALA	0	0.004	-0.006	9.394	-0.089	-0.089	0.000	0.000	0.000	0.000
6	A	5	TRP	0	-0.010	-0.002	12.514	0.026	0.026	0.000	0.000	0.000	0.000
7	A	6	VAL	0	0.041	0.004	16.030	-0.013	-0.013	0.000	0.000	0.000	0.000
8	A	7	LYS	1	0.868	0.964	19.179	-0.155	-0.155	0.000	0.000	0.000	0.000
9	A	8	THR	0	0.027	-0.004	21.267	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	9	LEU	0	0.012	0.013	23.207	0.009	0.009	0.000	0.000	0.000	0.000
11	A	10	ALA	0	-0.016	0.014	25.567	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	11	LEU	0	0.045	0.009	28.124	0.006	0.006	0.000	0.000	0.000	0.000
13	A	12	ASP	-1	-0.838	-0.919	28.398	0.069	0.069	0.000	0.000	0.000	0.000
14	A	13	ARG	1	0.960	0.960	30.080	-0.071	-0.071	0.000	0.000	0.000	0.000
15	A	14	VAL	0	-0.025	0.003	32.350	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	15	SER	0	-0.054	-0.051	30.378	0.002	0.002	0.000	0.000	0.000	0.000
17	A	16	ASN	0	-0.055	-0.013	32.485	0.004	0.004	0.000	0.000	0.000	0.000
18	A	17	THR	0	0.015	0.024	28.228	0.000	0.000	0.000	0.000	0.000	0.000
19	A	18	PRO	0	-0.022	-0.018	27.312	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	19	VAL	0	-0.015	0.005	23.235	0.003	0.003	0.000	0.000	0.000	0.000
21	A	20	VAL	0	-0.003	-0.005	19.871	0.003	0.003	0.000	0.000	0.000	0.000
22	A	21	ILE	0	0.019	0.022	19.888	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	22	LEU	0	0.001	0.009	14.319	0.015	0.015	0.000	0.000	0.000	0.000
24	A	23	GLY	0	0.014	0.008	16.258	-0.028	-0.028	0.000	0.000	0.000	0.000
25	A	24	ILE	0	0.025	0.009	10.618	0.039	0.039	0.000	0.000	0.000	0.000
26	A	25	GLU	-1	-0.789	-0.897	11.951	0.359	0.359	0.000	0.000	0.000	0.000
27	A	26	GLY	0	-0.056	-0.016	11.578	0.040	0.040	0.000	0.000	0.000	0.000
28	A	27	THR	0	-0.086	-0.068	11.921	-0.040	-0.040	0.000	0.000	0.000	0.000
29	A	28	ASN	0	0.001	-0.011	15.037	0.015	0.015	0.000	0.000	0.000	0.000
30	A	29	ARG	1	0.968	0.992	12.626	-0.051	-0.051	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.043	-0.023	15.941	0.028	0.028	0.000	0.000	0.000	0.000
32	A	31	LEU	0	0.021	-0.007	13.097	-0.023	-0.023	0.000	0.000	0.000	0.000
33	A	32	PRO	0	-0.023	0.010	16.207	0.023	0.023	0.000	0.000	0.000	0.000
34	A	33	ILE	0	0.013	-0.011	15.692	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	34	TRP	0	0.028	0.009	20.001	0.007	0.007	0.000	0.000	0.000	0.000
36	A	35	ILE	0	-0.039	-0.011	22.140	0.008	0.008	0.000	0.000	0.000	0.000
37	A	36	GLY	0	0.060	0.029	24.627	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	37	ALA	0	0.034	-0.016	27.984	0.004	0.004	0.000	0.000	0.000	0.000
39	A	38	ALA	0	-0.009	0.004	30.498	0.000	0.000	0.000	0.000	0.000	0.000
40	A	39	GLU	-1	-0.865	-0.941	25.134	0.153	0.153	0.000	0.000	0.000	0.000
41	A	40	GLY	0	0.043	0.016	26.545	0.008	0.008	0.000	0.000	0.000	0.000
42	A	41	HIS	0	0.006	0.011	27.865	0.002	0.002	0.000	0.000	0.000	0.000
43	A	42	ALA	0	0.021	-0.003	27.207	0.000	0.000	0.000	0.000	0.000	0.000
44	A	43	LEU	0	-0.027	-0.003	22.231	0.009	0.009	0.000	0.000	0.000	0.000
45	A	44	ALA	0	0.046	0.009	25.868	0.004	0.004	0.000	0.000	0.000	0.000
46	A	45	LEU	0	-0.011	0.003	28.469	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	46	ALA	0	-0.036	-0.018	24.685	0.000	0.000	0.000	0.000	0.000	0.000
48	A	47	MET	0	-0.058	-0.041	23.859	0.006	0.006	0.000	0.000	0.000	0.000
49	A	48	GLU	-1	-0.969	-0.981	26.035	0.110	0.110	0.000	0.000	0.000	0.000
50	A	49	LYS	1	0.855	0.938	23.444	-0.202	-0.202	0.000	0.000	0.000	0.000
51	A	50	MET	0	-0.001	0.016	28.898	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	51	GLU	-1	-0.912	-0.948	31.974	0.127	0.127	0.000	0.000	0.000	0.000
53	A	52	PHE	0	-0.003	-0.012	33.726	-0.008	-0.008	0.000	0.000	0.000	0.000
54	A	53	PRO	0	-0.013	0.003	35.986	0.002	0.002	0.000	0.000	0.000	0.000
55	A	54	ARG	1	0.887	0.918	37.025	-0.104	-0.104	0.000	0.000	0.000	0.000
56	A	55	PRO	0	0.012	0.023	33.090	0.002	0.002	0.000	0.000	0.000	0.000
57	A	56	LEU	0	0.039	0.024	31.015	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	57	THR	0	0.011	-0.021	28.569	0.003	0.003	0.000	0.000	0.000	0.000
59	A	58	HIS	0	0.009	-0.002	23.798	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	59	ASP	-1	-0.824	-0.910	26.469	0.179	0.179	0.000	0.000	0.000	0.000
61	A	60	LEU	0	-0.015	-0.002	28.852	0.002	0.002	0.000	0.000	0.000	0.000
62	A	61	LEU	0	-0.015	-0.005	22.689	0.002	0.002	0.000	0.000	0.000	0.000
63	A	62	LEU	0	0.028	-0.009	22.242	0.013	0.013	0.000	0.000	0.000	0.000
64	A	63	SER	0	0.037	0.033	25.639	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	64	VAL	0	-0.041	-0.009	26.868	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	65	LEU	0	-0.059	-0.041	21.290	0.003	0.003	0.000	0.000	0.000	0.000
67	A	66	GLU	-1	-0.909	-0.944	25.170	0.171	0.171	0.000	0.000	0.000	0.000
68	A	67	SER	0	-0.062	-0.053	27.103	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	68	LEU	0	-0.122	-0.048	26.581	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	69	GLU	-1	-0.923	-0.956	26.447	0.158	0.158	0.000	0.000	0.000	0.000
71	A	70	ALA	0	-0.027	-0.006	21.658	0.017	0.017	0.000	0.000	0.000	0.000
72	A	71	ARG	1	0.935	0.967	17.120	-0.395	-0.395	0.000	0.000	0.000	0.000
73	A	72	VAL	0	0.008	0.009	16.407	0.041	0.041	0.000	0.000	0.000	0.000
74	A	73	ASP	-1	-0.918	-0.965	12.183	0.835	0.835	0.000	0.000	0.000	0.000
75	A	74	LYS	1	0.947	0.966	7.687	-1.786	-1.786	0.000	0.000	0.000	0.000
76	A	75	VAL	0	-0.021	0.002	11.627	0.013	0.013	0.000	0.000	0.000	0.000
77	A	76	ILE	0	0.006	0.011	6.710	0.007	0.007	0.000	0.000	0.000	0.000
78	A	77	ILE	0	0.020	0.018	9.938	-0.050	-0.050	0.000	0.000	0.000	0.000
79	A	78	HIS	0	0.071	0.010	8.358	-0.087	-0.087	0.000	0.000	0.000	0.000
80	A	79	SER	0	-0.036	-0.019	9.461	-0.104	-0.104	0.000	0.000	0.000	0.000
81	A	80	LEU	0	-0.003	-0.001	12.237	0.011	0.011	0.000	0.000	0.000	0.000
82	A	81	LYS	1	0.925	0.965	15.541	-0.142	-0.142	0.000	0.000	0.000	0.000
83	A	82	ASP	-1	-0.918	-0.962	18.250	0.082	0.082	0.000	0.000	0.000	0.000
84	A	83	ASN	0	-0.024	-0.029	20.750	0.007	0.007	0.000	0.000	0.000	0.000
85	A	84	THR	0	0.010	0.036	19.360	0.005	0.005	0.000	0.000	0.000	0.000
86	A	85	PHE	0	0.033	0.010	14.241	0.003	0.003	0.000	0.000	0.000	0.000
87	A	86	TYR	0	-0.015	-0.014	14.177	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	87	ALA	0	-0.016	-0.018	13.023	0.026	0.026	0.000	0.000	0.000	0.000
89	A	88	THR	0	0.009	0.020	11.260	-0.078	-0.078	0.000	0.000	0.000	0.000
90	A	89	LEU	0	-0.023	-0.024	12.848	0.055	0.055	0.000	0.000	0.000	0.000
91	A	90	VAL	0	-0.009	0.007	10.496	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	91	ILE	0	0.023	0.005	13.943	-0.033	-0.033	0.000	0.000	0.000	0.000
93	A	92	ARG	1	0.922	0.943	13.856	-0.463	-0.463	0.000	0.000	0.000	0.000
94	A	93	ASP	-1	-0.869	-0.933	17.713	0.224	0.224	0.000	0.000	0.000	0.000
95	A	94	LEU	0	-0.088	-0.055	21.102	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	95	THR	0	-0.010	0.030	22.872	-0.031	-0.031	0.000	0.000	0.000	0.000
97	A	104	ALA	0	-0.035	-0.038	12.049	0.007	0.007	0.000	0.000	0.000	0.000
98	A	105	ALA	0	0.034	0.031	14.088	-0.033	-0.033	0.000	0.000	0.000	0.000
99	A	106	LEU	0	-0.074	-0.038	11.524	0.015	0.015	0.000	0.000	0.000	0.000
100	A	107	ILE	0	0.014	0.005	15.465	-0.021	-0.021	0.000	0.000	0.000	0.000
101	A	108	ASP	-1	-0.904	-0.945	11.950	1.212	1.212	0.000	0.000	0.000	0.000
102	A	109	ILE	0	-0.023	-0.016	14.660	-0.082	-0.082	0.000	0.000	0.000	0.000
103	A	110	ASP	-1	-0.929	-0.955	16.309	0.413	0.413	0.000	0.000	0.000	0.000
104	A	111	SER	0	0.009	-0.015	16.974	-0.045	-0.045	0.000	0.000	0.000	0.000
105	A	112	ARG	1	0.873	0.943	17.557	-0.201	-0.201	0.000	0.000	0.000	0.000
106	A	113	PRO	0	0.035	0.009	16.540	0.027	0.027	0.000	0.000	0.000	0.000
107	A	114	SER	0	0.061	0.019	17.723	0.012	0.012	0.000	0.000	0.000	0.000
108	A	115	ASP	-1	-0.857	-0.900	20.742	0.227	0.227	0.000	0.000	0.000	0.000
109	A	116	ALA	0	0.040	0.016	15.471	0.005	0.005	0.000	0.000	0.000	0.000
110	A	117	ILE	0	0.002	-0.017	16.320	0.016	0.016	0.000	0.000	0.000	0.000
111	A	118	ILE	0	0.005	0.010	18.049	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	119	LEU	0	0.014	-0.002	19.160	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	120	ALA	0	0.010	0.030	16.120	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	121	VAL	0	-0.025	-0.008	17.879	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	122	LYS	1	0.865	0.931	20.656	-0.198	-0.198	0.000	0.000	0.000	0.000
116	A	123	THR	0	-0.028	-0.027	19.216	0.002	0.002	0.000	0.000	0.000	0.000
117	A	124	GLY	0	-0.011	0.006	19.541	-0.012	-0.012	0.000	0.000	0.000	0.000
118	A	125	ALA	0	-0.052	-0.013	15.329	0.020	0.020	0.000	0.000	0.000	0.000
119	A	126	PRO	0	-0.074	-0.025	11.025	-0.015	-0.015	0.000	0.000	0.000	0.000
120	A	127	ILE	0	0.046	0.014	11.901	0.032	0.032	0.000	0.000	0.000	0.000
121	A	128	PHE	0	-0.012	-0.015	6.220	0.086	0.086	0.000	0.000	0.000	0.000
122	A	129	VAL	0	0.018	0.010	8.012	-0.017	-0.017	0.000	0.000	0.000	0.000
123	A	130	SER	0	-0.017	-0.005	5.355	-0.442	-0.442	0.000	0.000	0.000	0.000
124	A	131	ASP	-1	-0.819	-0.940	2.831	-0.186	0.920	0.099	-0.468	-0.737	-0.002
125	A	132	ASN	0	0.009	0.000	4.796	0.540	0.651	-0.001	-0.006	-0.104	0.000
126	A	133	LEU	0	-0.053	-0.008	7.234	0.183	0.183	0.000	0.000	0.000	0.000
127	A	134	VAL	0	0.035	0.012	7.943	0.090	0.090	0.000	0.000	0.000	0.000
128	A	135	GLU	-1	-0.944	-0.889	7.557	-0.120	-0.120	0.000	0.000	0.000	0.000
129	A	136	LYS	1	0.902	0.952	10.422	0.143	0.143	0.000	0.000	0.000	0.000
130	A	137	HIS	0	-0.010	-0.023	12.500	0.028	0.028	0.000	0.000	0.000	0.000
131	A	138	SER	0	-0.139	-0.107	12.406	0.029	0.029	0.000	0.000	0.000	0.000
132	A	139	ILE	0	0.014	-0.007	14.598	-0.012	-0.012	0.000	0.000	0.000	0.000
133	A	140	GLU	-1	-0.943	-0.981	17.320	0.073	0.073	0.000	0.000	0.000	0.000
134	A	141	LEU	0	-0.007	0.016	18.767	-0.003	-0.003	0.000	0.000	0.000	0.000
135	A	142	GLU	-1	-0.874	-0.944	22.111	0.033	0.033	0.000	0.000	0.000	0.000
136	A	143	VAL	0	-0.035	-0.024	24.844	0.007	0.007	0.000	0.000	0.000	0.000
137	A	144	ASN	0	0.026	-0.016	27.865	0.006	0.006	0.000	0.000	0.000	0.000
138	A	145	GLU	-1	-0.876	-0.938	24.232	0.047	0.047	0.000	0.000	0.000	0.000
139	A	146	ARG	1	0.820	0.920	21.181	-0.079	-0.079	0.000	0.000	0.000	0.000
140	A	147	ASP	-1	-0.893	-0.943	26.300	0.065	0.065	0.000	0.000	0.000	0.000
141	A	148	LEU	0	-0.087	-0.036	29.322	0.001	0.001	0.000	0.000	0.000	0.000
142	A	149	ILE	0	-0.091	-0.038	25.879	0.000	0.000	0.000	0.000	0.000	0.000
143	A	150	ASN	0	0.002	0.019	28.496	0.012	0.012	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:HIS)