FMO DATABASE

FMODB ID: GN291

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1253477.027189
FMO2-HF: Nuclear repulsion	1198539.181369
FMO2-HF: Total energy	-54937.845821
FMO2-MP2: Total energy	-55100.199893

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.
-12.171	-9.065	5.617	-4.557	-4.165	-0.03

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 : 0.004 / q_NPA : 0.009

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	0.960	1.000	3.775	1.697	4.282	-0.031	-1.337	-1.217	0.005
4	A	3	LYS	1	0.794	0.882	6.549	0.028	0.028	0.000	0.000	0.000	0.000
5	A	4	ALA	0	0.009	-0.005	9.425	-0.180	-0.180	0.000	0.000	0.000	0.000
6	A	5	TRP	0	0.020	0.009	12.529	0.105	0.105	0.000	0.000	0.000	0.000
7	A	6	VAL	0	0.034	0.000	16.048	-0.044	-0.044	0.000	0.000	0.000	0.000
8	A	7	LYS	1	0.871	0.960	18.589	0.206	0.206	0.000	0.000	0.000	0.000
9	A	8	THR	0	0.033	-0.004	21.280	0.015	0.015	0.000	0.000	0.000	0.000
10	A	9	LEU	0	0.006	0.016	23.229	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	10	ALA	0	-0.009	0.016	25.593	0.005	0.005	0.000	0.000	0.000	0.000
12	A	11	LEU	0	0.044	0.010	28.124	0.007	0.007	0.000	0.000	0.000	0.000
13	A	12	ASP	-1	-0.826	-0.910	28.595	-0.063	-0.063	0.000	0.000	0.000	0.000
14	A	13	ARG	1	0.902	0.942	30.297	0.066	0.066	0.000	0.000	0.000	0.000
15	A	14	VAL	0	-0.010	0.007	32.629	0.002	0.002	0.000	0.000	0.000	0.000
16	A	15	SER	0	-0.054	-0.052	30.647	0.008	0.008	0.000	0.000	0.000	0.000
17	A	16	ASN	0	-0.062	-0.021	32.701	0.011	0.011	0.000	0.000	0.000	0.000
18	A	17	THR	0	0.010	0.018	28.272	0.006	0.006	0.000	0.000	0.000	0.000
19	A	18	PRO	0	-0.026	-0.018	27.143	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	19	VAL	0	-0.035	-0.003	23.402	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	20	VAL	0	0.003	-0.002	19.589	0.007	0.007	0.000	0.000	0.000	0.000
22	A	21	ILE	0	0.015	0.023	19.913	-0.033	-0.033	0.000	0.000	0.000	0.000
23	A	22	LEU	0	0.012	0.008	14.250	0.029	0.029	0.000	0.000	0.000	0.000
24	A	23	GLY	0	0.017	0.009	16.114	-0.066	-0.066	0.000	0.000	0.000	0.000
25	A	24	ILE	0	0.016	0.005	10.247	0.022	0.022	0.000	0.000	0.000	0.000
26	A	25	GLU	-1	-0.759	-0.878	12.237	0.001	0.001	0.000	0.000	0.000	0.000
27	A	26	GLY	0	-0.042	-0.012	11.713	-0.114	-0.114	0.000	0.000	0.000	0.000
28	A	27	THR	0	-0.068	-0.043	11.365	-0.056	-0.056	0.000	0.000	0.000	0.000
29	A	28	ASN	0	-0.014	0.003	14.466	0.088	0.088	0.000	0.000	0.000	0.000
30	A	29	ARG	1	0.896	0.947	12.661	0.660	0.660	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.063	-0.042	15.629	0.025	0.025	0.000	0.000	0.000	0.000
32	A	31	LEU	0	0.026	0.003	12.959	-0.041	-0.041	0.000	0.000	0.000	0.000
33	A	32	PRO	0	-0.016	0.009	16.324	0.045	0.045	0.000	0.000	0.000	0.000
34	A	33	ILE	0	-0.005	-0.014	15.571	-0.005	-0.005	0.000	0.000	0.000	0.000
35	A	34	TRP	0	0.039	0.011	20.070	0.013	0.013	0.000	0.000	0.000	0.000
36	A	35	ILE	0	-0.033	-0.007	22.094	0.016	0.016	0.000	0.000	0.000	0.000
37	A	36	GLY	0	0.051	0.030	24.646	-0.009	-0.009	0.000	0.000	0.000	0.000
38	A	37	ALA	0	0.048	-0.011	28.004	0.002	0.002	0.000	0.000	0.000	0.000
39	A	38	ALA	0	-0.012	0.002	30.605	0.000	0.000	0.000	0.000	0.000	0.000
40	A	39	GLU	-1	-0.817	-0.898	25.163	0.101	0.101	0.000	0.000	0.000	0.000
41	A	40	GLY	0	0.033	0.007	26.591	0.004	0.004	0.000	0.000	0.000	0.000
42	A	41	HIS	0	-0.003	0.011	27.906	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	42	ALA	0	0.018	-0.007	27.372	0.002	0.002	0.000	0.000	0.000	0.000
44	A	43	LEU	0	-0.018	-0.001	22.112	0.011	0.011	0.000	0.000	0.000	0.000
45	A	44	ALA	0	0.048	0.011	25.911	0.002	0.002	0.000	0.000	0.000	0.000
46	A	45	LEU	0	-0.013	0.006	28.507	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	46	ALA	0	-0.014	-0.007	24.666	0.005	0.005	0.000	0.000	0.000	0.000
48	A	47	MET	0	-0.066	-0.048	23.736	0.005	0.005	0.000	0.000	0.000	0.000
49	A	48	GLU	-1	-0.962	-0.977	26.069	0.045	0.045	0.000	0.000	0.000	0.000
50	A	49	LYS	1	0.832	0.930	23.023	-0.151	-0.151	0.000	0.000	0.000	0.000
51	A	50	MET	0	0.010	0.023	28.934	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	51	GLU	-1	-0.921	-0.954	32.017	0.120	0.120	0.000	0.000	0.000	0.000
53	A	52	PHE	0	-0.013	-0.021	34.317	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	53	PRO	0	-0.007	0.011	36.033	0.005	0.005	0.000	0.000	0.000	0.000
55	A	54	ARG	1	0.898	0.924	37.099	-0.102	-0.102	0.000	0.000	0.000	0.000
56	A	55	PRO	0	0.017	0.024	32.977	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	56	LEU	0	0.053	0.035	30.915	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	57	THR	0	0.018	-0.013	29.022	0.007	0.007	0.000	0.000	0.000	0.000
59	A	58	HIS	0	0.012	-0.011	23.918	0.003	0.003	0.000	0.000	0.000	0.000
60	A	59	ASP	-1	-0.804	-0.889	26.526	0.176	0.176	0.000	0.000	0.000	0.000
61	A	60	LEU	0	0.004	0.016	28.907	0.009	0.009	0.000	0.000	0.000	0.000
62	A	61	LEU	0	-0.019	-0.003	22.724	0.008	0.008	0.000	0.000	0.000	0.000
63	A	62	LEU	0	0.033	-0.005	22.203	0.021	0.021	0.000	0.000	0.000	0.000
64	A	63	SER	0	0.019	0.016	25.697	0.001	0.001	0.000	0.000	0.000	0.000
65	A	64	VAL	0	-0.034	0.001	27.317	0.001	0.001	0.000	0.000	0.000	0.000
66	A	65	LEU	0	-0.044	-0.034	21.415	0.010	0.010	0.000	0.000	0.000	0.000
67	A	66	GLU	-1	-0.918	-0.947	25.229	0.222	0.222	0.000	0.000	0.000	0.000
68	A	67	SER	0	-0.067	-0.065	27.158	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	68	LEU	0	-0.118	-0.049	26.676	-0.014	-0.014	0.000	0.000	0.000	0.000
70	A	69	GLU	-1	-0.921	-0.950	26.504	0.259	0.259	0.000	0.000	0.000	0.000
71	A	70	ALA	0	-0.028	-0.008	21.831	0.033	0.033	0.000	0.000	0.000	0.000
72	A	71	ARG	1	0.913	0.960	16.525	-0.595	-0.595	0.000	0.000	0.000	0.000
73	A	72	VAL	0	0.021	0.008	16.363	0.066	0.066	0.000	0.000	0.000	0.000
74	A	73	ASP	-1	-0.823	-0.881	12.980	1.073	1.073	0.000	0.000	0.000	0.000
75	A	74	LYS	1	0.872	0.932	8.568	-1.775	-1.775	0.000	0.000	0.000	0.000
76	A	75	VAL	0	-0.004	0.012	11.631	0.042	0.042	0.000	0.000	0.000	0.000
77	A	76	ILE	0	0.000	0.006	6.880	-0.078	-0.078	0.000	0.000	0.000	0.000
78	A	77	ILE	0	0.015	0.015	9.994	-0.013	-0.013	0.000	0.000	0.000	0.000
79	A	78	HIS	0	0.061	0.005	8.463	-0.276	-0.276	0.000	0.000	0.000	0.000
80	A	79	SER	0	-0.020	-0.010	9.468	-0.170	-0.170	0.000	0.000	0.000	0.000
81	A	80	LEU	0	-0.007	0.000	12.244	0.024	0.024	0.000	0.000	0.000	0.000
82	A	81	LYS	1	0.855	0.928	15.582	-0.049	-0.049	0.000	0.000	0.000	0.000
83	A	82	ASP	-1	-0.852	-0.932	18.252	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	83	ASN	0	-0.016	-0.021	20.818	0.003	0.003	0.000	0.000	0.000	0.000
85	A	84	THR	0	-0.007	0.026	19.652	0.011	0.011	0.000	0.000	0.000	0.000
86	A	85	PHE	0	0.049	0.014	14.619	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	86	TYR	0	-0.023	-0.015	14.372	0.028	0.028	0.000	0.000	0.000	0.000
88	A	87	ALA	0	-0.007	-0.011	13.043	-0.015	-0.015	0.000	0.000	0.000	0.000
89	A	88	THR	0	0.023	0.025	11.372	-0.073	-0.073	0.000	0.000	0.000	0.000
90	A	89	LEU	0	-0.030	-0.023	12.910	0.048	0.048	0.000	0.000	0.000	0.000
91	A	90	VAL	0	-0.004	0.001	10.519	0.020	0.020	0.000	0.000	0.000	0.000
92	A	91	ILE	0	0.019	0.007	14.006	-0.051	-0.051	0.000	0.000	0.000	0.000
93	A	92	ARG	1	0.845	0.884	13.608	-0.776	-0.776	0.000	0.000	0.000	0.000
94	A	93	ASP	-1	-0.819	-0.869	17.767	0.349	0.349	0.000	0.000	0.000	0.000
95	A	94	LEU	0	-0.057	-0.054	20.979	0.010	0.010	0.000	0.000	0.000	0.000
96	A	95	THR	0	-0.087	-0.039	22.803	-0.027	-0.027	0.000	0.000	0.000	0.000
97	A	104	ALA	0	-0.043	-0.039	11.501	0.005	0.005	0.000	0.000	0.000	0.000
98	A	105	ALA	0	0.053	0.038	13.526	-0.045	-0.045	0.000	0.000	0.000	0.000
99	A	106	LEU	0	-0.057	-0.035	11.135	0.011	0.011	0.000	0.000	0.000	0.000
100	A	107	ILE	0	0.010	0.002	14.947	-0.014	-0.014	0.000	0.000	0.000	0.000
101	A	108	ASP	-1	-0.898	-0.945	11.488	1.647	1.647	0.000	0.000	0.000	0.000
102	A	109	ILE	0	-0.034	-0.024	14.692	-0.098	-0.098	0.000	0.000	0.000	0.000
103	A	110	ASP	-1	-0.912	-0.942	16.329	0.440	0.440	0.000	0.000	0.000	0.000
104	A	111	SER	0	-0.008	-0.019	16.957	-0.047	-0.047	0.000	0.000	0.000	0.000
105	A	112	ARG	1	0.819	0.885	17.580	-0.166	-0.166	0.000	0.000	0.000	0.000
106	A	113	PRO	0	0.048	0.007	16.482	0.035	0.035	0.000	0.000	0.000	0.000
107	A	114	SER	0	0.044	0.025	17.747	0.011	0.011	0.000	0.000	0.000	0.000
108	A	115	ASP	-1	-0.825	-0.883	20.785	0.191	0.191	0.000	0.000	0.000	0.000
109	A	116	ALA	0	0.039	0.017	15.656	0.010	0.010	0.000	0.000	0.000	0.000
110	A	117	ILE	0	0.007	-0.011	16.404	0.017	0.017	0.000	0.000	0.000	0.000
111	A	118	ILE	0	0.002	0.007	18.096	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	119	LEU	0	0.014	0.000	19.220	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	120	ALA	0	0.001	0.024	16.122	0.011	0.011	0.000	0.000	0.000	0.000
114	A	121	VAL	0	-0.010	0.002	17.925	-0.007	-0.007	0.000	0.000	0.000	0.000
115	A	122	LYS	1	0.798	0.878	20.696	-0.172	-0.172	0.000	0.000	0.000	0.000
116	A	123	THR	0	-0.030	-0.027	19.310	0.009	0.009	0.000	0.000	0.000	0.000
117	A	124	GLY	0	-0.016	0.003	19.577	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	125	ALA	0	-0.053	-0.011	15.392	0.020	0.020	0.000	0.000	0.000	0.000
119	A	126	PRO	0	-0.043	-0.029	11.063	-0.040	-0.040	0.000	0.000	0.000	0.000
120	A	127	ILE	0	0.039	0.020	11.923	0.069	0.069	0.000	0.000	0.000	0.000
121	A	128	PHE	0	-0.016	-0.016	6.226	0.100	0.100	0.000	0.000	0.000	0.000
122	A	129	VAL	0	0.005	0.004	8.037	0.116	0.116	0.000	0.000	0.000	0.000
123	A	130	SER	0	-0.006	0.000	5.371	-0.894	-0.894	0.000	0.000	0.000	0.000
124	A	131	ASP	-1	-0.795	-0.921	2.053	-14.707	-14.311	5.649	-3.215	-2.830	-0.035
125	A	132	ASN	0	0.023	0.001	5.138	0.960	1.085	-0.001	-0.005	-0.118	0.000
126	A	133	LEU	0	-0.034	-0.006	7.368	0.308	0.308	0.000	0.000	0.000	0.000
127	A	134	VAL	0	0.013	0.003	8.141	0.188	0.188	0.000	0.000	0.000	0.000
128	A	135	GLU	-1	-0.969	-0.945	8.063	-1.287	-1.287	0.000	0.000	0.000	0.000
129	A	136	LYS	1	0.877	0.942	10.736	0.762	0.762	0.000	0.000	0.000	0.000
130	A	137	HIS	0	-0.001	-0.018	12.772	0.109	0.109	0.000	0.000	0.000	0.000
131	A	138	SER	0	-0.122	-0.056	12.675	0.087	0.087	0.000	0.000	0.000	0.000
132	A	139	ILE	0	0.042	0.011	14.806	0.006	0.006	0.000	0.000	0.000	0.000
133	A	140	GLU	-1	-0.859	-0.939	16.504	-0.528	-0.528	0.000	0.000	0.000	0.000
134	A	141	LEU	0	-0.003	0.015	18.618	0.032	0.032	0.000	0.000	0.000	0.000
135	A	142	GLU	-1	-0.872	-0.924	21.876	-0.236	-0.236	0.000	0.000	0.000	0.000
136	A	143	VAL	0	-0.031	-0.026	24.525	0.005	0.005	0.000	0.000	0.000	0.000
137	A	144	ASN	0	0.016	-0.013	27.459	0.009	0.009	0.000	0.000	0.000	0.000
138	A	145	GLU	-1	-0.833	-0.918	24.272	-0.203	-0.203	0.000	0.000	0.000	0.000
139	A	146	ARG	1	0.792	0.880	21.185	0.222	0.222	0.000	0.000	0.000	0.000
140	A	147	ASP	-1	-0.870	-0.940	26.014	-0.094	-0.094	0.000	0.000	0.000	0.000
141	A	148	LEU	0	-0.055	-0.023	29.235	0.013	0.013	0.000	0.000	0.000	0.000
142	A	149	ILE	0	-0.075	-0.037	25.541	0.008	0.008	0.000	0.000	0.000	0.000
143	A	150	ASN	0	-0.040	0.012	28.007	0.013	0.013	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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