FMO DATABASE

FMODB ID: 949J2

Calculation Name: 1Q2Y-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1Q2Y

Chain ID: A

ChEMBL ID:

UniProt ID: O31628

Base Structure: X-ray

Registration Date: 2023-09-20

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	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	140
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1300021.38707
FMO2-HF: Nuclear repulsion	1244646.575969
FMO2-HF: Total energy	-55374.811101
FMO2-MP2: Total energy	-55534.964817

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:MET)

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

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.
-19.497	-9.941	9.954	-7.091	-12.415	-0.046

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.010 / q_NPA : -0.008

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	ALA	0	0.033	0.026	3.875	-0.602	0.971	-0.016	-0.756	-0.801	0.001
4	A	4	VAL	0	-0.062	-0.047	6.253	0.034	0.034	0.000	0.000	0.000	0.000
5	A	5	ILE	0	0.011	0.017	9.750	0.053	0.053	0.000	0.000	0.000	0.000
6	A	6	ALA	0	-0.024	-0.006	13.089	-0.013	-0.013	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.862	0.901	14.671	-0.015	-0.015	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.021	0.000	15.755	0.003	0.003	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.808	-0.904	17.983	0.047	0.047	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.799	-0.890	15.701	0.053	0.053	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.054	0.029	12.647	0.012	0.012	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.004	-0.004	14.392	0.014	0.014	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.807	0.887	17.194	-0.037	-0.037	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.805	-0.879	11.591	0.043	0.043	0.000	0.000	0.000	0.000
15	A	15	ALA	0	-0.037	-0.034	13.223	0.041	0.041	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.009	0.001	14.192	0.036	0.036	0.000	0.000	0.000	0.000
17	A	17	TYR	0	-0.022	-0.008	13.127	0.003	0.003	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.036	-0.028	10.058	0.034	0.034	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.733	0.834	13.193	-0.112	-0.112	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.726	-0.866	16.264	0.147	0.147	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.904	-0.934	13.269	0.223	0.223	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.027	-0.018	13.487	0.004	0.004	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.038	-0.033	16.538	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.011	0.010	20.003	-0.015	-0.015	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.765	0.890	16.479	-0.179	-0.179	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.820	-0.903	14.475	0.376	0.376	0.000	0.000	0.000	0.000
27	A	27	GLN	0	-0.073	-0.053	17.819	-0.017	-0.017	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.023	-0.018	22.150	-0.013	-0.013	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.014	0.016	23.814	-0.010	-0.010	0.000	0.000	0.000	0.000
30	A	30	PRO	0	-0.012	-0.017	25.652	0.001	0.001	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.008	-0.013	25.675	0.006	0.006	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.884	-0.930	24.639	0.078	0.078	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.911	-0.962	25.828	0.078	0.078	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.895	-0.960	20.234	0.154	0.154	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.023	-0.004	21.696	0.012	0.012	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.741	-0.838	24.202	0.094	0.094	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.899	-0.965	26.200	0.059	0.059	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.063	-0.022	25.239	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.700	-0.809	21.209	0.121	0.121	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.015	-0.012	22.452	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.907	-0.939	25.092	0.055	0.055	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.069	-0.042	20.097	0.003	0.003	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.827	-0.891	16.556	0.028	0.028	0.000	0.000	0.000	0.000
44	A	44	HIS	0	-0.002	-0.013	15.435	0.031	0.031	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.062	-0.037	9.412	-0.035	-0.035	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.034	0.031	8.503	0.088	0.088	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.060	-0.039	2.992	-0.732	-0.086	0.180	-0.173	-0.652	0.000
48	A	48	TYR	0	-0.039	-0.051	4.728	0.029	0.356	-0.001	-0.065	-0.260	0.000
49	A	49	ASP	-1	-0.885	-0.954	2.337	-9.615	-6.085	4.117	-3.779	-3.867	-0.037
50	A	50	GLY	0	0.003	0.004	3.603	0.398	0.549	0.024	0.033	-0.208	-0.001
51	A	51	GLU	-1	-0.936	-0.969	5.886	0.031	0.031	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.889	0.965	7.227	-0.295	-0.295	0.000	0.000	0.000	0.000
53	A	53	PRO	0	0.031	0.029	6.250	-0.283	-0.283	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.049	-0.046	2.946	-0.443	0.198	0.100	-0.142	-0.598	-0.001
55	A	55	GLY	0	0.001	-0.021	6.350	0.471	0.471	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.009	0.014	8.196	-0.226	-0.226	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.042	0.020	10.829	0.078	0.078	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.748	0.851	13.750	-0.150	-0.150	0.000	0.000	0.000	0.000
59	A	59	TRP	0	-0.052	-0.032	16.620	0.016	0.016	0.000	0.000	0.000	0.000
60	A	60	ARG	1	0.889	0.923	18.741	-0.092	-0.092	0.000	0.000	0.000	0.000
61	A	61	MET	0	-0.006	0.012	22.415	0.004	0.004	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.802	0.877	25.303	-0.050	-0.050	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.827	-0.907	27.772	0.046	0.046	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.018	0.019	29.209	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	65	TYR	0	-0.004	-0.011	25.337	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.063	0.011	21.876	0.000	0.000	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.776	0.900	21.740	-0.093	-0.093	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.004	-0.002	16.315	0.006	0.006	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.768	-0.876	18.141	0.104	0.104	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.835	0.895	17.236	-0.114	-0.114	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.003	0.014	12.176	0.026	0.026	0.000	0.000	0.000	0.000
72	A	72	CYS	0	-0.047	-0.009	12.642	-0.042	-0.042	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.006	-0.022	7.474	0.146	0.146	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.076	0.058	8.564	-0.107	-0.107	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.810	0.887	10.148	-0.071	-0.071	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.033	-0.020	9.250	-0.052	-0.052	0.000	0.000	0.000	0.000
77	A	77	HIS	0	0.037	0.009	4.325	-0.584	-0.240	0.014	-0.075	-0.283	0.001
78	A	78	ARG	1	0.836	0.924	6.527	0.038	0.038	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.019	-0.008	8.014	0.028	0.028	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.009	0.012	3.106	-0.800	-0.302	0.211	-0.149	-0.560	0.000
81	A	81	GLY	0	0.013	0.002	2.396	-4.373	-3.254	1.510	-1.006	-1.624	-0.017
82	A	82	VAL	0	0.023	0.006	2.865	-0.711	-0.382	1.873	-0.522	-1.680	0.004
83	A	83	GLY	0	0.063	0.033	4.857	-0.911	-0.889	0.003	-0.019	-0.005	0.000
84	A	84	GLY	0	-0.003	-0.008	7.656	-0.240	-0.240	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.060	-0.025	2.803	-1.213	-0.837	1.939	-0.438	-1.877	0.004
86	A	86	ILE	0	0.016	0.017	6.643	-0.364	-0.364	0.000	0.000	0.000	0.000
87	A	87	MET	0	0.002	0.017	8.832	-0.179	-0.179	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.950	0.976	8.363	0.080	0.080	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.015	-0.002	8.894	-0.077	-0.077	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.029	0.009	10.958	-0.037	-0.037	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.790	-0.844	13.884	0.069	0.069	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.869	0.948	13.821	0.034	0.034	0.000	0.000	0.000	0.000
93	A	93	ALA	0	-0.013	-0.001	14.778	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.037	0.016	16.516	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	95	ALA	0	-0.028	-0.019	18.810	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.907	-0.967	17.967	-0.025	-0.025	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.035	-0.012	20.609	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.034	-0.016	22.456	0.002	0.002	0.000	0.000	0.000	0.000
99	A	99	ALA	0	-0.048	-0.021	22.193	0.001	0.001	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.029	-0.013	24.272	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.017	0.022	23.735	0.001	0.001	0.000	0.000	0.000	0.000
102	A	102	PHE	0	-0.016	-0.025	19.331	0.006	0.006	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.005	-0.006	22.240	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.015	0.005	17.385	0.004	0.004	0.000	0.000	0.000	0.000
105	A	105	ASN	0	0.015	0.010	20.889	-0.022	-0.022	0.000	0.000	0.000	0.000
106	A	106	ALA	0	-0.016	-0.012	19.053	0.026	0.026	0.000	0.000	0.000	0.000
107	A	107	GLN	0	0.057	0.034	15.668	-0.033	-0.033	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.005	-0.040	19.847	0.011	0.011	0.000	0.000	0.000	0.000
109	A	109	GLN	0	0.002	-0.008	19.412	0.006	0.006	0.000	0.000	0.000	0.000
110	A	110	ALA	0	0.001	0.008	15.782	0.001	0.001	0.000	0.000	0.000	0.000
111	A	111	VAL	0	0.028	0.011	17.214	0.002	0.002	0.000	0.000	0.000	0.000
112	A	112	PRO	0	-0.017	-0.019	18.134	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	113	PHE	0	0.017	0.012	9.842	-0.017	-0.017	0.000	0.000	0.000	0.000
114	A	114	TYR	0	0.066	0.020	14.299	-0.020	-0.020	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.965	0.998	17.108	-0.089	-0.089	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.856	0.943	12.860	-0.025	-0.025	0.000	0.000	0.000	0.000
117	A	117	HIS	0	-0.075	-0.045	11.945	-0.053	-0.053	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.021	0.008	16.510	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	119	TYR	0	-0.052	-0.053	17.295	-0.004	-0.004	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.916	0.949	21.431	-0.036	-0.036	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.005	-0.009	24.818	0.005	0.005	0.000	0.000	0.000	0.000
122	A	122	LEU	0	0.008	0.008	26.384	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.011	-0.009	28.968	-0.006	-0.006	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.930	-0.962	29.420	0.050	0.050	0.000	0.000	0.000	0.000
125	A	125	LYS	1	0.855	0.927	31.026	-0.059	-0.059	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.825	-0.893	26.918	0.096	0.096	0.000	0.000	0.000	0.000
127	A	127	PHE	0	-0.067	-0.030	25.318	-0.009	-0.009	0.000	0.000	0.000	0.000
128	A	128	LEU	0	-0.001	-0.003	26.990	0.007	0.007	0.000	0.000	0.000	0.000
129	A	129	ASP	-1	-0.869	-0.904	23.283	0.131	0.131	0.000	0.000	0.000	0.000
130	A	130	ALA	0	0.103	0.044	23.297	-0.006	-0.006	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.020	0.012	24.731	0.006	0.006	0.000	0.000	0.000	0.000
132	A	132	ILE	0	-0.004	0.001	21.233	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	133	PRO	0	-0.018	-0.004	24.617	0.001	0.001	0.000	0.000	0.000	0.000
134	A	134	HIS	0	-0.042	-0.033	20.693	0.035	0.035	0.000	0.000	0.000	0.000
135	A	135	LEU	0	0.025	0.029	23.500	-0.015	-0.015	0.000	0.000	0.000	0.000
136	A	136	GLN	0	-0.006	-0.007	23.688	0.006	0.006	0.000	0.000	0.000	0.000
137	A	137	MET	0	-0.076	-0.033	21.144	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	138	MET	0	0.020	0.023	23.827	0.004	0.004	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.815	0.884	18.086	-0.070	-0.070	0.000	0.000	0.000	0.000
140	A	140	ASP	-1	-0.846	-0.898	23.123	0.039	0.039	0.000	0.000	0.000	0.000

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