FMO DATABASE

FMODB ID: 4LN8N

Calculation Name: 1Q67-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

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	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	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1480809.84428
FMO2-HF: Nuclear repulsion	1421009.22345
FMO2-HF: Total energy	-59800.62083
FMO2-MP2: Total energy	-59978.094517

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: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.
-8.748	-3.092	3.033	-3.094	-5.593	-0.005

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 : 0.016 / 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	24	PHE	0	0.069	0.041	2.854	-3.939	-0.220	0.127	-1.867	-1.979	0.004
4	A	25	ASN	0	0.052	0.022	4.767	-0.977	-0.815	-0.001	-0.013	-0.148	0.000
5	A	26	VAL	0	-0.019	-0.008	6.809	-0.332	-0.332	0.000	0.000	0.000	0.000
6	A	27	ILE	0	0.037	0.023	5.954	-0.148	-0.148	0.000	0.000	0.000	0.000
7	A	28	GLY	0	0.026	0.016	8.684	-0.103	-0.103	0.000	0.000	0.000	0.000
8	A	29	ARG	1	0.852	0.935	10.653	-0.451	-0.451	0.000	0.000	0.000	0.000
9	A	30	TYR	0	-0.013	-0.012	11.887	-0.045	-0.045	0.000	0.000	0.000	0.000
10	A	31	ASP	-1	-0.748	-0.826	12.373	0.074	0.074	0.000	0.000	0.000	0.000
11	A	32	PRO	0	0.008	-0.009	12.663	0.050	0.050	0.000	0.000	0.000	0.000
12	A	33	LYS	1	0.922	0.972	14.512	-0.089	-0.089	0.000	0.000	0.000	0.000
13	A	34	ILE	0	-0.032	0.031	6.945	-0.042	-0.042	0.000	0.000	0.000	0.000
14	A	35	LYS	1	0.920	0.961	10.281	-0.067	-0.067	0.000	0.000	0.000	0.000
15	A	36	GLN	0	-0.009	-0.022	6.317	0.149	0.149	0.000	0.000	0.000	0.000
16	A	37	LEU	0	-0.035	-0.005	2.280	-0.842	-0.609	2.580	-0.641	-2.172	-0.005
17	A	38	LEU	0	-0.036	-0.024	5.036	-0.261	-0.151	-0.001	-0.001	-0.107	0.000
18	A	39	PHE	0	0.031	0.008	6.104	-0.111	-0.111	0.000	0.000	0.000	0.000
19	A	40	HIS	0	-0.026	-0.017	2.941	-1.677	-0.245	0.328	-0.572	-1.187	-0.004
20	A	41	THR	0	0.017	0.006	6.463	-0.020	-0.020	0.000	0.000	0.000	0.000
21	A	42	PRO	0	-0.029	-0.038	8.144	0.027	0.027	0.000	0.000	0.000	0.000
22	A	43	HIS	0	0.030	-0.004	9.841	0.075	0.075	0.000	0.000	0.000	0.000
23	A	44	ALA	0	0.040	0.037	13.491	0.010	0.010	0.000	0.000	0.000	0.000
24	A	45	SER	0	-0.010	-0.003	15.433	0.022	0.022	0.000	0.000	0.000	0.000
25	A	46	LEU	0	-0.002	0.009	18.810	0.000	0.000	0.000	0.000	0.000	0.000
26	A	47	TYR	0	0.027	0.013	20.693	0.009	0.009	0.000	0.000	0.000	0.000
27	A	48	LYS	1	0.889	0.926	23.949	0.051	0.051	0.000	0.000	0.000	0.000
28	A	49	TRP	0	-0.006	0.015	26.577	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	50	ASP	-1	-0.868	-0.932	29.487	-0.044	-0.044	0.000	0.000	0.000	0.000
30	A	51	PHE	0	0.033	-0.006	31.208	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	52	LYS	1	0.886	0.957	35.275	0.035	0.035	0.000	0.000	0.000	0.000
32	A	53	LYS	1	0.910	0.938	36.346	0.045	0.045	0.000	0.000	0.000	0.000
33	A	54	ASP	-1	-0.924	-0.945	35.492	-0.060	-0.060	0.000	0.000	0.000	0.000
34	A	55	GLU	-1	-0.931	-0.966	32.982	-0.069	-0.069	0.000	0.000	0.000	0.000
35	A	56	TRP	0	-0.022	-0.011	26.048	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	57	ASN	0	-0.003	0.005	29.372	0.001	0.001	0.000	0.000	0.000	0.000
37	A	58	LYS	1	0.802	0.890	21.125	0.135	0.135	0.000	0.000	0.000	0.000
38	A	59	LEU	0	-0.028	-0.018	23.225	0.010	0.010	0.000	0.000	0.000	0.000
39	A	60	GLU	-1	-0.925	-0.964	23.286	-0.058	-0.058	0.000	0.000	0.000	0.000
40	A	61	TYR	0	0.026	0.020	18.178	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	62	GLN	0	-0.050	-0.050	17.274	0.001	0.001	0.000	0.000	0.000	0.000
42	A	63	GLY	0	-0.027	0.000	13.849	0.026	0.026	0.000	0.000	0.000	0.000
43	A	64	VAL	0	-0.006	0.011	7.135	-0.050	-0.050	0.000	0.000	0.000	0.000
44	A	65	LEU	0	0.008	0.022	10.114	0.111	0.111	0.000	0.000	0.000	0.000
45	A	66	ALA	0	-0.001	-0.007	7.042	-0.163	-0.163	0.000	0.000	0.000	0.000
46	A	67	ILE	0	0.014	0.015	8.199	0.136	0.136	0.000	0.000	0.000	0.000
47	A	68	TYR	0	-0.076	-0.090	8.030	-0.088	-0.088	0.000	0.000	0.000	0.000
48	A	69	LEU	0	0.040	0.030	9.343	0.023	0.023	0.000	0.000	0.000	0.000
49	A	70	ARG	1	0.797	0.865	10.921	0.003	0.003	0.000	0.000	0.000	0.000
50	A	71	ASP	-1	-0.960	-0.989	13.640	0.131	0.131	0.000	0.000	0.000	0.000
51	A	72	VAL	0	-0.009	-0.009	15.685	0.008	0.008	0.000	0.000	0.000	0.000
52	A	73	SER	0	-0.066	-0.023	19.198	-0.018	-0.018	0.000	0.000	0.000	0.000
53	A	135	LYS	1	0.990	0.978	25.740	-0.018	-0.018	0.000	0.000	0.000	0.000
54	A	136	ASP	-1	-0.885	-0.939	20.614	0.045	0.045	0.000	0.000	0.000	0.000
55	A	137	ILE	0	0.055	0.014	22.552	0.000	0.000	0.000	0.000	0.000	0.000
56	A	138	TYR	0	-0.005	0.014	18.585	-0.012	-0.012	0.000	0.000	0.000	0.000
57	A	139	ASN	0	0.016	0.021	17.378	0.010	0.010	0.000	0.000	0.000	0.000
58	A	140	TYR	0	0.055	0.026	13.016	0.015	0.015	0.000	0.000	0.000	0.000
59	A	141	GLY	0	0.014	0.019	13.200	0.019	0.019	0.000	0.000	0.000	0.000
60	A	142	LEU	0	0.005	0.016	12.537	-0.046	-0.046	0.000	0.000	0.000	0.000
61	A	143	ILE	0	-0.015	-0.011	10.246	0.047	0.047	0.000	0.000	0.000	0.000
62	A	144	ILE	0	0.003	-0.006	11.850	-0.083	-0.083	0.000	0.000	0.000	0.000
63	A	145	LEU	0	0.002	0.002	9.288	0.060	0.060	0.000	0.000	0.000	0.000
64	A	146	ASN	0	0.014	-0.010	12.944	-0.096	-0.096	0.000	0.000	0.000	0.000
65	A	147	ARG	1	0.854	0.938	8.960	0.620	0.620	0.000	0.000	0.000	0.000
66	A	148	ILE	0	-0.021	-0.014	14.519	0.022	0.022	0.000	0.000	0.000	0.000
67	A	149	ASN	0	0.050	0.047	17.635	0.020	0.020	0.000	0.000	0.000	0.000
68	A	150	PRO	0	0.007	-0.026	17.243	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	151	ASP	-1	-0.915	-0.914	17.735	-0.015	-0.015	0.000	0.000	0.000	0.000
70	A	152	ASN	0	0.005	-0.021	14.483	-0.047	-0.047	0.000	0.000	0.000	0.000
71	A	153	PHE	0	0.005	0.013	16.132	0.018	0.018	0.000	0.000	0.000	0.000
72	A	154	SER	0	0.000	-0.018	15.719	-0.027	-0.027	0.000	0.000	0.000	0.000
73	A	155	MET	0	-0.028	-0.002	16.277	0.004	0.004	0.000	0.000	0.000	0.000
74	A	156	GLY	0	0.018	0.013	16.700	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	157	ILE	0	-0.010	-0.025	15.006	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	158	VAL	0	-0.023	-0.036	18.734	0.010	0.010	0.000	0.000	0.000	0.000
77	A	159	PRO	0	0.036	0.028	19.635	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	160	ASN	0	0.082	0.022	22.127	0.012	0.012	0.000	0.000	0.000	0.000
79	A	161	SER	0	-0.037	-0.007	24.741	0.007	0.007	0.000	0.000	0.000	0.000
80	A	162	VAL	0	0.013	0.006	22.881	0.007	0.007	0.000	0.000	0.000	0.000
81	A	163	VAL	0	0.012	0.004	25.721	0.006	0.006	0.000	0.000	0.000	0.000
82	A	164	ASN	0	0.007	-0.023	28.061	0.005	0.005	0.000	0.000	0.000	0.000
83	A	165	LYS	1	0.939	0.984	28.296	0.021	0.021	0.000	0.000	0.000	0.000
84	A	166	ARG	1	0.886	0.961	29.645	0.009	0.009	0.000	0.000	0.000	0.000
85	A	167	LYS	1	0.949	0.974	31.546	0.034	0.034	0.000	0.000	0.000	0.000
86	A	168	VAL	0	-0.040	-0.009	34.075	0.001	0.001	0.000	0.000	0.000	0.000
87	A	169	PHE	0	-0.065	-0.046	33.653	0.001	0.001	0.000	0.000	0.000	0.000
88	A	170	ASN	0	-0.030	-0.013	33.357	0.004	0.004	0.000	0.000	0.000	0.000
89	A	171	ALA	0	0.052	0.030	35.636	0.000	0.000	0.000	0.000	0.000	0.000
90	A	172	GLU	-1	-0.943	-0.940	37.904	0.006	0.006	0.000	0.000	0.000	0.000
91	A	173	GLU	-1	-0.870	-0.954	33.032	0.011	0.011	0.000	0.000	0.000	0.000
92	A	174	ASP	-1	-0.919	-0.962	33.382	-0.018	-0.018	0.000	0.000	0.000	0.000
93	A	175	THR	0	0.004	-0.025	35.283	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	176	LEU	0	-0.036	-0.013	37.222	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	177	ASN	0	-0.053	-0.024	30.867	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	178	PRO	0	0.035	0.024	33.316	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	179	LEU	0	-0.034	-0.009	28.085	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	180	GLU	-1	-0.926	-0.959	30.102	-0.042	-0.042	0.000	0.000	0.000	0.000
99	A	181	CYS	0	-0.062	-0.036	27.350	0.000	0.000	0.000	0.000	0.000	0.000
100	A	182	MET	0	-0.001	0.022	20.350	0.003	0.003	0.000	0.000	0.000	0.000
101	A	183	GLY	0	-0.010	-0.002	24.375	0.001	0.001	0.000	0.000	0.000	0.000
102	A	184	VAL	0	-0.003	-0.007	19.545	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	185	GLU	-1	-0.945	-0.970	22.758	-0.098	-0.098	0.000	0.000	0.000	0.000
104	A	186	VAL	0	0.007	0.006	21.051	-0.011	-0.011	0.000	0.000	0.000	0.000
105	A	187	LYS	1	0.949	0.985	23.719	0.104	0.104	0.000	0.000	0.000	0.000
106	A	188	ASP	-1	-0.894	-0.938	25.859	-0.118	-0.118	0.000	0.000	0.000	0.000
107	A	189	GLU	-1	-0.921	-0.993	23.118	-0.175	-0.175	0.000	0.000	0.000	0.000
108	A	190	LEU	0	-0.060	-0.026	21.622	-0.022	-0.022	0.000	0.000	0.000	0.000
109	A	191	VAL	0	-0.009	0.005	17.373	0.007	0.007	0.000	0.000	0.000	0.000
110	A	192	ILE	0	-0.026	-0.027	20.520	0.001	0.001	0.000	0.000	0.000	0.000
111	A	193	ILE	0	0.022	0.006	17.825	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	194	LYS	1	0.932	0.997	22.435	0.075	0.075	0.000	0.000	0.000	0.000
113	A	195	ASN	0	0.053	0.006	23.730	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	196	LEU	0	0.012	-0.008	24.533	0.003	0.003	0.000	0.000	0.000	0.000
115	A	197	LYS	1	0.840	0.912	27.122	0.023	0.023	0.000	0.000	0.000	0.000
116	A	198	HIS	0	-0.021	0.000	28.869	0.000	0.000	0.000	0.000	0.000	0.000
117	A	199	GLU	-1	-0.876	-0.915	26.900	-0.044	-0.044	0.000	0.000	0.000	0.000
118	A	200	VAL	0	0.014	-0.008	26.091	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	201	TYR	0	-0.004	-0.014	22.069	0.005	0.005	0.000	0.000	0.000	0.000
120	A	202	GLY	0	0.048	0.023	22.723	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	203	ILE	0	-0.019	-0.012	16.209	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	204	TRP	0	0.031	0.024	18.926	-0.016	-0.016	0.000	0.000	0.000	0.000
123	A	205	ILE	0	0.050	0.014	14.050	-0.021	-0.021	0.000	0.000	0.000	0.000
124	A	206	HIS	0	0.025	0.014	16.355	0.026	0.026	0.000	0.000	0.000	0.000
125	A	207	THR	0	-0.029	-0.022	12.692	0.042	0.042	0.000	0.000	0.000	0.000
126	A	208	VAL	0	0.042	0.020	15.747	-0.012	-0.012	0.000	0.000	0.000	0.000
127	A	209	SER	0	0.011	0.002	13.856	0.019	0.019	0.000	0.000	0.000	0.000
128	A	210	ASP	-1	-0.790	-0.886	10.997	-0.621	-0.621	0.000	0.000	0.000	0.000
129	A	211	ARG	1	0.817	0.948	13.577	0.237	0.237	0.000	0.000	0.000	0.000
130	A	212	GLN	0	0.025	0.013	16.562	0.007	0.007	0.000	0.000	0.000	0.000
131	A	213	ASN	0	0.028	0.009	12.426	-0.029	-0.029	0.000	0.000	0.000	0.000
132	A	214	ILE	0	0.004	0.000	12.517	0.008	0.008	0.000	0.000	0.000	0.000
133	A	215	TYR	0	-0.017	0.001	13.928	0.030	0.030	0.000	0.000	0.000	0.000
134	A	216	GLU	-1	-0.936	-0.974	16.487	-0.216	-0.216	0.000	0.000	0.000	0.000
135	A	217	LEU	0	-0.023	-0.002	10.585	0.017	0.017	0.000	0.000	0.000	0.000
136	A	218	ILE	0	0.012	-0.006	14.792	0.027	0.027	0.000	0.000	0.000	0.000
137	A	219	LYS	1	0.975	1.000	16.699	0.154	0.154	0.000	0.000	0.000	0.000
138	A	220	TYR	0	-0.004	-0.002	15.876	0.018	0.018	0.000	0.000	0.000	0.000
139	A	221	LEU	0	-0.033	-0.032	13.266	0.017	0.017	0.000	0.000	0.000	0.000
140	A	222	LEU	0	-0.049	-0.018	17.786	0.021	0.021	0.000	0.000	0.000	0.000
141	A	223	GLU	-1	-0.933	-0.973	21.175	-0.086	-0.086	0.000	0.000	0.000	0.000
142	A	224	ASN	0	-0.098	-0.040	20.166	0.012	0.012	0.000	0.000	0.000	0.000
143	A	225	GLU	-1	-0.932	-0.968	22.023	-0.025	-0.025	0.000	0.000	0.000	0.000
144	A	226	PRO	0	-0.049	-0.043	19.261	-0.006	-0.006	0.000	0.000	0.000	0.000
145	A	227	LYS	1	0.859	0.942	14.873	-0.073	-0.073	0.000	0.000	0.000	0.000
146	A	228	ASP	-1	-0.867	-0.921	14.051	-0.047	-0.047	0.000	0.000	0.000	0.000

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