FMO DATABASE

FMODB ID: ZV5YN

Calculation Name: 1X91-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1X91

Chain ID: A

ChEMBL ID:

UniProt ID: Q9LNF2

Base Structure: X-ray

Registration Date: 2023-09-23

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	147
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1302433.655344
FMO2-HF: Nuclear repulsion	1244340.375089
FMO2-HF: Total energy	-58093.280255
FMO2-MP2: Total energy	-58256.35249

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.
-2.565	-0.321	0.014	-0.944	-1.314	0.002

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 : 0.004 / q_NPA : -0.013

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	GLU	-1	-0.746	-0.892	3.861	-3.888	-2.324	-0.011	-0.725	-0.829	0.003
4	A	4	MET	0	-0.030	0.012	6.401	0.361	0.361	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.023	-0.021	3.598	0.341	0.789	0.020	-0.178	-0.290	-0.001
6	A	6	THR	0	-0.062	-0.035	3.607	0.089	0.321	0.005	-0.041	-0.195	0.000
7	A	7	ILE	0	0.009	0.004	6.445	0.210	0.210	0.000	0.000	0.000	0.000
8	A	8	CYS	0	0.013	0.021	9.524	0.116	0.116	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.821	-0.894	9.543	-0.768	-0.768	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.803	0.908	8.369	1.238	1.238	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.049	-0.035	13.792	0.056	0.056	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.040	0.004	16.440	0.018	0.018	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.020	-0.006	18.530	0.038	0.038	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.092	0.050	14.255	0.025	0.025	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.027	0.008	15.451	0.037	0.037	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.031	-0.012	17.839	0.036	0.036	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.060	0.027	11.039	0.033	0.033	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.949	0.986	14.348	-0.075	-0.075	0.000	0.000	0.000	0.000
19	A	20	PHE	0	-0.005	0.005	16.462	0.038	0.038	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.037	0.006	11.153	0.019	0.019	0.000	0.000	0.000	0.000
21	A	22	ASN	0	-0.042	-0.030	12.200	0.132	0.132	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.078	-0.056	14.549	0.018	0.018	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.845	0.932	16.759	-0.125	-0.125	0.000	0.000	0.000	0.000
24	A	25	PHE	0	-0.037	-0.006	12.199	0.010	0.010	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.021	0.013	11.449	0.006	0.006	0.000	0.000	0.000	0.000
26	A	27	SER	0	0.050	0.020	10.860	0.126	0.126	0.000	0.000	0.000	0.000
27	A	28	ALA	0	0.039	0.005	7.519	-0.115	-0.115	0.000	0.000	0.000	0.000
28	A	29	ASN	0	-0.030	-0.008	9.166	-0.273	-0.273	0.000	0.000	0.000	0.000
29	A	30	LEU	0	0.094	0.030	10.294	0.031	0.031	0.000	0.000	0.000	0.000
30	A	31	GLN	0	0.056	0.037	13.365	-0.016	-0.016	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.011	-0.009	15.580	0.015	0.015	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.010	0.004	11.620	0.015	0.015	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.036	0.034	15.499	0.002	0.002	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.876	0.925	18.135	-0.014	-0.014	0.000	0.000	0.000	0.000
35	A	36	THR	0	0.008	-0.012	17.719	0.007	0.007	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.027	-0.021	17.426	0.021	0.021	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.034	0.039	20.014	0.004	0.004	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.809	-0.883	23.156	0.042	0.042	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.074	-0.054	21.670	0.014	0.014	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.023	-0.028	23.173	0.000	0.000	0.000	0.000	0.000	0.000
41	A	42	GLN	0	0.077	0.031	25.558	0.001	0.001	0.000	0.000	0.000	0.000
42	A	43	ALA	0	-0.027	0.007	27.569	0.003	0.003	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.897	0.942	26.713	-0.049	-0.049	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.065	0.051	29.506	0.000	0.000	0.000	0.000	0.000	0.000
45	A	46	THR	0	0.021	0.000	31.493	0.000	0.000	0.000	0.000	0.000	0.000
46	A	47	GLN	0	-0.022	-0.019	30.107	0.001	0.001	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.009	-0.023	32.318	0.002	0.002	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.024	0.037	34.986	0.001	0.001	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.936	0.965	37.561	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.836	0.926	37.272	-0.019	-0.019	0.000	0.000	0.000	0.000
51	A	52	LEU	0	-0.005	-0.007	37.227	0.001	0.001	0.000	0.000	0.000	0.000
52	A	53	GLN	0	-0.022	-0.016	40.568	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.013	-0.011	42.603	0.001	0.001	0.000	0.000	0.000	0.000
54	A	55	ILE	0	-0.069	-0.021	40.292	0.001	0.001	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.048	-0.026	43.647	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.840	-0.916	46.725	0.005	0.005	0.000	0.000	0.000	0.000
57	A	58	GLY	0	-0.031	-0.004	47.747	0.001	0.001	0.000	0.000	0.000	0.000
58	A	59	GLY	0	-0.010	0.002	49.100	0.001	0.001	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.065	-0.028	46.097	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.754	-0.856	48.981	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	62	PRO	0	0.048	-0.001	49.710	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.922	0.977	45.561	0.015	0.015	0.000	0.000	0.000	0.000
63	A	64	SER	0	0.000	-0.044	45.298	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.818	0.921	45.087	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.019	-0.004	46.335	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.025	0.022	42.009	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	68	TYR	0	0.039	-0.006	39.904	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.951	0.972	41.772	0.009	0.009	0.000	0.000	0.000	0.000
69	A	70	SER	0	0.049	0.021	40.888	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	71	CYS	0	-0.050	-0.018	34.342	0.005	0.005	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.017	-0.010	37.798	0.000	0.000	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.883	-0.935	39.296	-0.022	-0.022	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.868	-0.937	35.677	-0.050	-0.050	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.037	-0.057	31.194	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.944	-0.978	35.085	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	77	SER	0	0.009	0.001	36.427	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.029	-0.012	31.220	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	79	ILE	0	-0.029	-0.020	31.485	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.091	0.057	32.455	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	81	ASN	0	-0.035	-0.029	30.561	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.016	-0.022	26.378	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.975	-0.988	28.550	-0.017	-0.017	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.810	-0.904	30.127	-0.062	-0.062	0.000	0.000	0.000	0.000
84	A	85	ALA	0	-0.028	-0.011	25.573	-0.010	-0.010	0.000	0.000	0.000	0.000
85	A	86	PHE	0	-0.058	-0.037	24.824	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.901	-0.937	26.721	-0.033	-0.033	0.000	0.000	0.000	0.000
87	A	88	HIS	0	-0.078	-0.043	26.572	0.003	0.003	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.013	0.001	20.071	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	90	ALA	0	-0.038	-0.018	23.462	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	91	SER	0	-0.069	-0.042	25.806	0.002	0.002	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.005	-0.002	22.417	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.800	-0.878	22.317	-0.190	-0.190	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.027	-0.006	20.775	0.008	0.008	0.000	0.000	0.000	0.000
94	A	95	MET	0	-0.028	-0.009	21.713	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.039	0.012	24.071	0.006	0.006	0.000	0.000	0.000	0.000
96	A	97	MET	0	-0.027	-0.001	20.078	0.007	0.007	0.000	0.000	0.000	0.000
97	A	98	ASN	0	-0.081	-0.035	20.265	0.018	0.018	0.000	0.000	0.000	0.000
98	A	99	MET	0	0.030	0.011	23.294	0.009	0.009	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.823	0.911	26.993	0.085	0.085	0.000	0.000	0.000	0.000
100	A	101	VAL	0	-0.008	-0.017	22.090	0.014	0.014	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.045	-0.015	25.435	0.003	0.003	0.000	0.000	0.000	0.000
102	A	103	ALA	0	0.027	0.024	26.561	0.009	0.009	0.000	0.000	0.000	0.000
103	A	104	ALA	0	-0.007	-0.003	27.406	0.010	0.010	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.065	-0.033	23.620	0.010	0.010	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.839	-0.928	27.527	-0.098	-0.098	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.080	0.063	30.573	0.006	0.006	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.051	-0.030	29.050	0.008	0.008	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.798	-0.898	28.760	-0.067	-0.067	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.007	-0.001	31.398	0.005	0.005	0.000	0.000	0.000	0.000
110	A	112	LEU	0	-0.064	-0.052	30.226	0.007	0.007	0.000	0.000	0.000	0.000
111	A	113	ASP	-1	-0.820	-0.893	34.583	-0.042	-0.042	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.820	-0.893	36.574	-0.026	-0.026	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.048	-0.027	37.006	0.004	0.004	0.000	0.000	0.000	0.000
114	A	116	LYS	1	0.754	0.882	37.328	0.045	0.045	0.000	0.000	0.000	0.000
115	A	117	ARG	1	0.847	0.904	39.027	0.022	0.022	0.000	0.000	0.000	0.000
116	A	118	LEU	0	0.001	0.030	41.804	0.001	0.001	0.000	0.000	0.000	0.000
117	A	119	ARG	1	0.918	0.959	42.920	0.001	0.001	0.000	0.000	0.000	0.000
118	A	120	SER	0	-0.014	-0.016	42.877	0.002	0.002	0.000	0.000	0.000	0.000
119	A	121	VAL	0	0.037	0.017	38.250	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.710	-0.834	38.323	0.021	0.021	0.000	0.000	0.000	0.000
121	A	123	SER	0	0.024	0.002	35.520	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	124	SER	0	-0.081	-0.056	34.133	0.001	0.001	0.000	0.000	0.000	0.000
123	A	125	VAL	0	0.075	0.032	33.524	0.000	0.000	0.000	0.000	0.000	0.000
124	A	126	VAL	0	0.015	0.017	32.749	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	127	ASN	0	0.019	-0.009	30.057	-0.009	-0.009	0.000	0.000	0.000	0.000
126	A	128	ASN	0	-0.010	0.001	28.819	0.006	0.006	0.000	0.000	0.000	0.000
127	A	129	SER	0	0.072	0.050	28.754	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	130	LYS	1	0.878	0.951	26.828	-0.012	-0.012	0.000	0.000	0.000	0.000
129	A	131	THR	0	-0.078	-0.042	24.629	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	132	ILE	0	0.014	0.007	24.022	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	133	LYS	1	0.866	0.926	24.633	0.069	0.069	0.000	0.000	0.000	0.000
132	A	134	ASN	0	-0.042	-0.028	20.699	-0.029	-0.029	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.057	-0.024	20.024	-0.017	-0.017	0.000	0.000	0.000	0.000
134	A	136	CYS	0	0.016	0.015	20.306	-0.016	-0.016	0.000	0.000	0.000	0.000
135	A	137	GLY	0	0.036	0.016	20.026	-0.024	-0.024	0.000	0.000	0.000	0.000
136	A	138	ILE	0	-0.030	-0.026	14.834	-0.035	-0.035	0.000	0.000	0.000	0.000
137	A	139	ALA	0	0.013	0.004	16.285	-0.050	-0.050	0.000	0.000	0.000	0.000
138	A	140	LEU	0	-0.005	0.024	18.719	-0.025	-0.025	0.000	0.000	0.000	0.000
139	A	141	VAL	0	0.008	0.000	12.754	-0.039	-0.039	0.000	0.000	0.000	0.000
140	A	142	ILE	0	-0.029	-0.025	13.605	-0.069	-0.069	0.000	0.000	0.000	0.000
141	A	143	SER	0	-0.006	-0.033	15.030	-0.035	-0.035	0.000	0.000	0.000	0.000
142	A	144	ASN	0	-0.051	-0.014	16.661	-0.049	-0.049	0.000	0.000	0.000	0.000
143	A	145	MET	0	-0.025	-0.008	10.576	-0.099	-0.099	0.000	0.000	0.000	0.000
144	A	146	LEU	0	-0.025	0.005	14.703	-0.041	-0.041	0.000	0.000	0.000	0.000
145	A	147	PRO	0	-0.043	-0.035	15.814	-0.025	-0.025	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.955	0.994	15.572	0.534	0.534	0.000	0.000	0.000	0.000
147	A	149	ASN	0	0.007	0.014	21.126	0.015	0.015	0.000	0.000	0.000	0.000

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