FMO DATABASE

FMODB ID: YNQM2

Calculation Name: 1Q67-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1Q67

Chain ID: A

ChEMBL ID:

UniProt ID: Q12517

Base Structure: X-ray

Registration Date: 2023-09-26

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1480250.062508
FMO2-HF: Nuclear repulsion	1420447.753974
FMO2-HF: Total energy	-59802.308535
FMO2-MP2: Total energy	-59979.679388

3D Structure Molmil

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:22:LEU)

Summations of interaction energy for fragment #1(A:22:LEU)

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.
-7.726	-2.242	3.253	-3.209	-5.527	-0.007

Interaction energy analysis for fragmet #1(A:22:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.017 / q_NPA : -0.006

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	24	PHE	0	0.022	0.029	2.989	-3.432	-0.076	0.008	-1.738	-1.626	0.000
4	A	25	ASN	0	0.053	0.011	4.970	-0.464	-0.339	-0.001	-0.006	-0.117	0.000
5	A	26	VAL	0	-0.040	-0.005	6.576	-0.306	-0.306	0.000	0.000	0.000	0.000
6	A	27	ILE	0	0.048	0.025	6.336	-0.143	-0.143	0.000	0.000	0.000	0.000
7	A	28	GLY	0	0.043	0.018	9.063	-0.112	-0.112	0.000	0.000	0.000	0.000
8	A	29	ARG	1	0.859	0.931	11.022	-0.423	-0.423	0.000	0.000	0.000	0.000
9	A	30	TYR	0	-0.026	-0.008	12.737	-0.045	-0.045	0.000	0.000	0.000	0.000
10	A	31	ASP	-1	-0.726	-0.813	13.194	0.173	0.173	0.000	0.000	0.000	0.000
11	A	32	PRO	0	0.002	-0.003	13.218	0.056	0.056	0.000	0.000	0.000	0.000
12	A	33	LYS	1	0.860	0.935	14.871	-0.157	-0.157	0.000	0.000	0.000	0.000
13	A	34	ILE	0	-0.056	-0.004	7.237	-0.034	-0.034	0.000	0.000	0.000	0.000
14	A	35	LYS	1	0.887	0.951	11.096	-0.130	-0.130	0.000	0.000	0.000	0.000
15	A	36	GLN	0	0.003	-0.015	7.133	0.134	0.134	0.000	0.000	0.000	0.000
16	A	37	LEU	0	-0.029	-0.010	2.376	-0.769	-0.389	1.950	-0.513	-1.817	-0.001
17	A	38	LEU	0	-0.051	-0.022	5.526	-0.111	-0.111	0.000	0.000	0.000	0.000
18	A	39	PHE	0	0.044	0.018	6.446	-0.125	-0.125	0.000	0.000	0.000	0.000
19	A	40	HIS	0	-0.042	-0.028	2.521	-1.952	-0.329	1.296	-0.952	-1.967	-0.006
20	A	41	THR	0	0.015	-0.002	6.363	-0.038	-0.038	0.000	0.000	0.000	0.000
21	A	42	PRO	0	-0.024	-0.015	8.279	0.004	0.004	0.000	0.000	0.000	0.000
22	A	43	HIS	0	0.056	0.012	9.538	0.029	0.029	0.000	0.000	0.000	0.000
23	A	44	ALA	0	0.027	0.031	13.186	0.011	0.011	0.000	0.000	0.000	0.000
24	A	45	SER	0	-0.019	-0.005	15.479	0.013	0.013	0.000	0.000	0.000	0.000
25	A	46	LEU	0	0.004	0.018	18.870	0.001	0.001	0.000	0.000	0.000	0.000
26	A	47	TYR	0	0.013	0.006	20.522	0.005	0.005	0.000	0.000	0.000	0.000
27	A	48	LYS	1	0.839	0.892	23.803	0.016	0.016	0.000	0.000	0.000	0.000
28	A	49	TRP	0	-0.043	-0.020	26.474	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	50	ASP	-1	-0.845	-0.919	29.668	-0.019	-0.019	0.000	0.000	0.000	0.000
30	A	51	PHE	0	0.022	-0.013	31.471	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	52	LYS	1	0.879	0.950	35.329	0.014	0.014	0.000	0.000	0.000	0.000
32	A	53	LYS	1	0.827	0.896	35.749	0.033	0.033	0.000	0.000	0.000	0.000
33	A	54	ASP	-1	-0.874	-0.912	35.302	-0.035	-0.035	0.000	0.000	0.000	0.000
34	A	55	GLU	-1	-0.869	-0.921	32.978	-0.043	-0.043	0.000	0.000	0.000	0.000
35	A	56	TRP	0	0.009	-0.001	26.109	0.001	0.001	0.000	0.000	0.000	0.000
36	A	57	ASN	0	-0.025	-0.006	29.605	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	58	LYS	1	0.806	0.894	21.409	0.092	0.092	0.000	0.000	0.000	0.000
38	A	59	LEU	0	-0.006	-0.001	23.002	0.008	0.008	0.000	0.000	0.000	0.000
39	A	60	GLU	-1	-0.907	-0.958	23.056	-0.037	-0.037	0.000	0.000	0.000	0.000
40	A	61	TYR	0	-0.002	0.011	17.955	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	62	GLN	0	-0.027	-0.042	17.414	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	63	GLY	0	-0.020	-0.010	13.757	0.010	0.010	0.000	0.000	0.000	0.000
43	A	64	VAL	0	0.003	0.021	7.161	-0.031	-0.031	0.000	0.000	0.000	0.000
44	A	65	LEU	0	0.014	0.020	10.064	0.092	0.092	0.000	0.000	0.000	0.000
45	A	66	ALA	0	-0.009	-0.014	6.913	-0.110	-0.110	0.000	0.000	0.000	0.000
46	A	67	ILE	0	0.019	0.010	8.289	0.078	0.078	0.000	0.000	0.000	0.000
47	A	68	TYR	0	-0.065	-0.066	8.232	-0.022	-0.022	0.000	0.000	0.000	0.000
48	A	69	LEU	0	0.038	0.024	9.654	-0.033	-0.033	0.000	0.000	0.000	0.000
49	A	70	ARG	1	0.739	0.823	11.459	-0.079	-0.079	0.000	0.000	0.000	0.000
50	A	71	ASP	-1	-0.783	-0.879	14.299	0.166	0.166	0.000	0.000	0.000	0.000
51	A	72	VAL	0	-0.033	-0.017	16.552	0.001	0.001	0.000	0.000	0.000	0.000
52	A	73	SER	0	-0.100	-0.054	19.876	-0.028	-0.028	0.000	0.000	0.000	0.000
53	A	135	LYS	1	0.986	0.981	26.366	-0.059	-0.059	0.000	0.000	0.000	0.000
54	A	136	ASP	-1	-0.794	-0.879	20.869	0.117	0.117	0.000	0.000	0.000	0.000
55	A	137	ILE	0	0.032	0.009	23.427	0.001	0.001	0.000	0.000	0.000	0.000
56	A	138	TYR	0	-0.005	0.018	18.810	-0.011	-0.011	0.000	0.000	0.000	0.000
57	A	139	ASN	0	0.021	-0.007	17.988	0.010	0.010	0.000	0.000	0.000	0.000
58	A	140	TYR	0	0.059	0.030	13.202	0.023	0.023	0.000	0.000	0.000	0.000
59	A	141	GLY	0	0.015	0.011	13.486	0.004	0.004	0.000	0.000	0.000	0.000
60	A	142	LEU	0	-0.004	0.013	12.420	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	143	ILE	0	-0.006	-0.008	9.988	0.028	0.028	0.000	0.000	0.000	0.000
62	A	144	ILE	0	0.007	-0.002	11.489	-0.060	-0.060	0.000	0.000	0.000	0.000
63	A	145	LEU	0	0.004	0.001	9.261	0.049	0.049	0.000	0.000	0.000	0.000
64	A	146	ASN	0	0.017	0.002	12.898	-0.077	-0.077	0.000	0.000	0.000	0.000
65	A	147	ARG	1	0.826	0.904	8.971	0.500	0.500	0.000	0.000	0.000	0.000
66	A	148	ILE	0	-0.027	-0.008	14.684	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	149	ASN	0	-0.017	-0.020	17.862	0.005	0.005	0.000	0.000	0.000	0.000
68	A	150	PRO	0	0.022	-0.001	17.238	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	151	ASP	-1	-0.847	-0.874	17.397	0.008	0.008	0.000	0.000	0.000	0.000
70	A	152	ASN	0	-0.045	-0.051	13.824	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	153	PHE	0	0.021	0.022	16.009	0.011	0.011	0.000	0.000	0.000	0.000
72	A	154	SER	0	-0.015	-0.017	15.455	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	155	MET	0	-0.002	0.009	16.204	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	156	GLY	0	0.020	0.014	16.645	0.003	0.003	0.000	0.000	0.000	0.000
75	A	157	ILE	0	-0.010	-0.030	15.461	-0.016	-0.016	0.000	0.000	0.000	0.000
76	A	158	VAL	0	-0.015	-0.021	18.939	0.014	0.014	0.000	0.000	0.000	0.000
77	A	159	PRO	0	0.053	0.030	19.762	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	160	ASN	0	0.041	-0.001	22.218	0.010	0.010	0.000	0.000	0.000	0.000
79	A	161	SER	0	-0.018	-0.030	25.018	0.002	0.002	0.000	0.000	0.000	0.000
80	A	162	VAL	0	-0.008	-0.002	23.314	0.003	0.003	0.000	0.000	0.000	0.000
81	A	163	VAL	0	0.009	0.007	25.721	0.002	0.002	0.000	0.000	0.000	0.000
82	A	164	ASN	0	0.021	-0.003	28.219	0.001	0.001	0.000	0.000	0.000	0.000
83	A	165	LYS	1	0.834	0.907	26.806	-0.023	-0.023	0.000	0.000	0.000	0.000
84	A	166	ARG	1	0.818	0.890	29.830	-0.028	-0.028	0.000	0.000	0.000	0.000
85	A	167	LYS	1	0.882	0.934	31.723	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	168	VAL	0	-0.034	0.001	34.284	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	169	PHE	0	-0.043	-0.034	33.433	0.000	0.000	0.000	0.000	0.000	0.000
88	A	170	ASN	0	-0.063	-0.040	33.541	0.004	0.004	0.000	0.000	0.000	0.000
89	A	171	ALA	0	0.041	0.023	35.697	0.001	0.001	0.000	0.000	0.000	0.000
90	A	172	GLU	-1	-0.923	-0.941	37.759	0.025	0.025	0.000	0.000	0.000	0.000
91	A	173	GLU	-1	-0.818	-0.905	32.937	0.040	0.040	0.000	0.000	0.000	0.000
92	A	174	ASP	-1	-0.842	-0.917	32.937	0.017	0.017	0.000	0.000	0.000	0.000
93	A	175	THR	0	-0.036	-0.024	35.687	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	176	LEU	0	-0.031	-0.008	37.939	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	177	ASN	0	-0.042	-0.026	31.034	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	178	PRO	0	0.017	0.024	33.494	0.001	0.001	0.000	0.000	0.000	0.000
97	A	179	LEU	0	-0.037	-0.006	28.094	0.000	0.000	0.000	0.000	0.000	0.000
98	A	180	GLU	-1	-0.844	-0.914	30.063	-0.013	-0.013	0.000	0.000	0.000	0.000
99	A	181	CYS	0	-0.061	-0.028	27.796	0.003	0.003	0.000	0.000	0.000	0.000
100	A	182	MET	0	0.034	0.043	20.597	0.001	0.001	0.000	0.000	0.000	0.000
101	A	183	GLY	0	0.004	0.000	24.666	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	184	VAL	0	-0.010	-0.009	19.800	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	185	GLU	-1	-0.826	-0.898	23.135	-0.057	-0.057	0.000	0.000	0.000	0.000
104	A	186	VAL	0	-0.005	-0.010	20.732	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	187	LYS	1	0.830	0.907	23.459	0.066	0.066	0.000	0.000	0.000	0.000
106	A	188	ASP	-1	-0.877	-0.939	25.480	-0.079	-0.079	0.000	0.000	0.000	0.000
107	A	189	GLU	-1	-0.799	-0.867	23.050	-0.146	-0.146	0.000	0.000	0.000	0.000
108	A	190	LEU	0	-0.057	-0.024	21.550	-0.015	-0.015	0.000	0.000	0.000	0.000
109	A	191	VAL	0	0.006	0.007	17.327	0.005	0.005	0.000	0.000	0.000	0.000
110	A	192	ILE	0	-0.027	-0.014	20.492	0.003	0.003	0.000	0.000	0.000	0.000
111	A	193	ILE	0	-0.002	-0.012	18.044	0.000	0.000	0.000	0.000	0.000	0.000
112	A	194	LYS	1	0.820	0.917	22.665	0.023	0.023	0.000	0.000	0.000	0.000
113	A	195	ASN	0	0.031	-0.016	23.708	0.001	0.001	0.000	0.000	0.000	0.000
114	A	196	LEU	0	0.019	-0.004	24.551	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	197	LYS	1	0.841	0.909	27.302	-0.011	-0.011	0.000	0.000	0.000	0.000
116	A	198	HIS	0	-0.012	0.007	29.326	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	199	GLU	-1	-0.757	-0.822	26.295	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	200	VAL	0	0.001	-0.008	26.365	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	201	TYR	0	-0.030	-0.042	22.079	0.002	0.002	0.000	0.000	0.000	0.000
120	A	202	GLY	0	0.055	0.021	22.702	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	203	ILE	0	-0.030	-0.020	16.346	0.000	0.000	0.000	0.000	0.000	0.000
122	A	204	TRP	0	-0.013	0.002	19.094	-0.013	-0.013	0.000	0.000	0.000	0.000
123	A	205	ILE	0	0.026	-0.007	13.717	-0.013	-0.013	0.000	0.000	0.000	0.000
124	A	206	HIS	0	0.019	0.024	16.168	0.020	0.020	0.000	0.000	0.000	0.000
125	A	207	THR	0	-0.031	-0.041	12.337	0.026	0.026	0.000	0.000	0.000	0.000
126	A	208	VAL	0	0.030	0.011	15.294	-0.007	-0.007	0.000	0.000	0.000	0.000
127	A	209	SER	0	0.031	0.007	13.247	0.020	0.020	0.000	0.000	0.000	0.000
128	A	210	ASP	-1	-0.774	-0.845	10.926	-0.428	-0.428	0.000	0.000	0.000	0.000
129	A	211	ARG	1	0.750	0.854	12.839	0.177	0.177	0.000	0.000	0.000	0.000
130	A	212	GLN	0	-0.037	-0.015	16.078	0.020	0.020	0.000	0.000	0.000	0.000
131	A	213	ASN	0	-0.034	-0.040	12.459	-0.017	-0.017	0.000	0.000	0.000	0.000
132	A	214	ILE	0	-0.019	-0.005	12.223	0.010	0.010	0.000	0.000	0.000	0.000
133	A	215	TYR	0	0.007	0.016	13.761	0.028	0.028	0.000	0.000	0.000	0.000
134	A	216	GLU	-1	-0.832	-0.904	16.078	-0.163	-0.163	0.000	0.000	0.000	0.000
135	A	217	LEU	0	-0.016	0.003	10.787	0.018	0.018	0.000	0.000	0.000	0.000
136	A	218	ILE	0	0.008	-0.011	14.906	0.027	0.027	0.000	0.000	0.000	0.000
137	A	219	LYS	1	0.911	0.946	17.057	0.082	0.082	0.000	0.000	0.000	0.000
138	A	220	TYR	0	-0.012	-0.002	15.346	0.011	0.011	0.000	0.000	0.000	0.000
139	A	221	LEU	0	-0.029	-0.021	13.354	0.016	0.016	0.000	0.000	0.000	0.000
140	A	222	LEU	0	-0.053	-0.018	17.691	0.017	0.017	0.000	0.000	0.000	0.000
141	A	223	GLU	-1	-0.894	-0.941	21.403	-0.037	-0.037	0.000	0.000	0.000	0.000
142	A	224	ASN	0	-0.064	-0.027	20.258	0.003	0.003	0.000	0.000	0.000	0.000
143	A	225	GLU	-1	-0.775	-0.851	22.391	0.024	0.024	0.000	0.000	0.000	0.000
144	A	226	PRO	0	-0.073	-0.047	19.497	-0.002	-0.002	0.000	0.000	0.000	0.000
145	A	227	LYS	1	0.810	0.912	16.192	-0.154	-0.154	0.000	0.000	0.000	0.000
146	A	228	ASP	-1	-0.859	-0.908	14.013	0.068	0.068	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:LEU)