FMO DATABASE

FMODB ID: 5N98Z

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1482742.268985
FMO2-HF: Nuclear repulsion	1422940.430324
FMO2-HF: Total energy	-59801.838661
FMO2-MP2: Total energy	-59979.26748

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.
-8.41	-2.457	2.323	-3.06	-5.215	-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 : 0.009 / q_NPA : -0.010

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	0.041	0.027	2.958	-3.752	-0.073	0.047	-1.882	-1.844	0.003
4	A	25	ASN	0	0.056	0.022	4.897	-0.739	-0.594	-0.001	-0.009	-0.135	0.000
5	A	26	VAL	0	-0.016	-0.007	6.959	-0.298	-0.298	0.000	0.000	0.000	0.000
6	A	27	ILE	0	0.037	0.021	5.971	-0.154	-0.154	0.000	0.000	0.000	0.000
7	A	28	GLY	0	0.027	0.019	8.891	-0.098	-0.098	0.000	0.000	0.000	0.000
8	A	29	ARG	1	0.846	0.935	10.846	-0.448	-0.448	0.000	0.000	0.000	0.000
9	A	30	TYR	0	-0.004	-0.006	12.141	-0.034	-0.034	0.000	0.000	0.000	0.000
10	A	31	ASP	-1	-0.744	-0.824	12.635	0.074	0.074	0.000	0.000	0.000	0.000
11	A	32	PRO	0	0.015	-0.006	12.837	0.047	0.047	0.000	0.000	0.000	0.000
12	A	33	LYS	1	0.851	0.928	14.754	-0.082	-0.082	0.000	0.000	0.000	0.000
13	A	34	ILE	0	-0.045	0.022	7.124	-0.042	-0.042	0.000	0.000	0.000	0.000
14	A	35	LYS	1	0.886	0.945	10.608	-0.026	-0.026	0.000	0.000	0.000	0.000
15	A	36	GLN	0	-0.019	-0.027	6.649	0.146	0.146	0.000	0.000	0.000	0.000
16	A	37	LEU	0	-0.033	-0.004	2.220	-0.894	-0.411	1.834	-0.553	-1.764	-0.004
17	A	38	LEU	0	-0.044	-0.027	5.062	-0.279	-0.168	-0.001	-0.001	-0.108	0.000
18	A	39	PHE	0	0.034	0.011	6.157	-0.119	-0.119	0.000	0.000	0.000	0.000
19	A	40	HIS	0	-0.021	-0.018	2.786	-1.728	-0.193	0.444	-0.615	-1.364	-0.004
20	A	41	THR	0	0.021	0.007	6.574	-0.026	-0.026	0.000	0.000	0.000	0.000
21	A	42	PRO	0	-0.028	-0.026	8.271	0.026	0.026	0.000	0.000	0.000	0.000
22	A	43	HIS	0	0.051	0.004	9.826	0.071	0.071	0.000	0.000	0.000	0.000
23	A	44	ALA	0	0.043	0.039	13.481	0.009	0.009	0.000	0.000	0.000	0.000
24	A	45	SER	0	-0.016	-0.008	15.437	0.022	0.022	0.000	0.000	0.000	0.000
25	A	46	LEU	0	0.001	0.012	18.813	0.000	0.000	0.000	0.000	0.000	0.000
26	A	47	TYR	0	0.013	0.010	20.705	0.015	0.015	0.000	0.000	0.000	0.000
27	A	48	LYS	1	0.854	0.904	24.161	0.050	0.050	0.000	0.000	0.000	0.000
28	A	49	TRP	0	-0.013	0.013	26.784	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	50	ASP	-1	-0.871	-0.930	29.690	-0.042	-0.042	0.000	0.000	0.000	0.000
30	A	51	PHE	0	0.031	-0.009	31.612	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	52	LYS	1	0.886	0.959	35.492	0.034	0.034	0.000	0.000	0.000	0.000
32	A	53	LYS	1	0.865	0.925	36.480	0.051	0.051	0.000	0.000	0.000	0.000
33	A	54	ASP	-1	-0.906	-0.942	35.574	-0.059	-0.059	0.000	0.000	0.000	0.000
34	A	55	GLU	-1	-0.910	-0.961	33.255	-0.063	-0.063	0.000	0.000	0.000	0.000
35	A	56	TRP	0	0.004	0.005	25.983	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	57	ASN	0	-0.017	-0.007	29.498	0.000	0.000	0.000	0.000	0.000	0.000
37	A	58	LYS	1	0.808	0.896	21.402	0.128	0.128	0.000	0.000	0.000	0.000
38	A	59	LEU	0	-0.013	-0.009	23.247	0.010	0.010	0.000	0.000	0.000	0.000
39	A	60	GLU	-1	-0.925	-0.968	23.287	-0.056	-0.056	0.000	0.000	0.000	0.000
40	A	61	TYR	0	0.016	0.017	18.230	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	62	GLN	0	-0.012	-0.031	17.282	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	63	GLY	0	-0.042	-0.009	13.839	0.025	0.025	0.000	0.000	0.000	0.000
43	A	64	VAL	0	0.001	0.012	7.172	-0.048	-0.048	0.000	0.000	0.000	0.000
44	A	65	LEU	0	0.004	0.020	10.128	0.108	0.108	0.000	0.000	0.000	0.000
45	A	66	ALA	0	0.002	-0.004	7.204	-0.157	-0.157	0.000	0.000	0.000	0.000
46	A	67	ILE	0	0.020	0.015	8.465	0.129	0.129	0.000	0.000	0.000	0.000
47	A	68	TYR	0	-0.069	-0.077	8.161	-0.088	-0.088	0.000	0.000	0.000	0.000
48	A	69	LEU	0	0.034	0.025	9.537	0.019	0.019	0.000	0.000	0.000	0.000
49	A	70	ARG	1	0.776	0.845	11.200	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	71	ASP	-1	-0.836	-0.910	13.930	0.107	0.107	0.000	0.000	0.000	0.000
51	A	72	VAL	0	-0.041	-0.029	15.997	0.007	0.007	0.000	0.000	0.000	0.000
52	A	73	SER	0	-0.062	-0.027	19.493	-0.017	-0.017	0.000	0.000	0.000	0.000
53	A	135	LYS	1	0.987	0.980	26.012	-0.016	-0.016	0.000	0.000	0.000	0.000
54	A	136	ASP	-1	-0.805	-0.888	20.532	0.050	0.050	0.000	0.000	0.000	0.000
55	A	137	ILE	0	0.057	0.022	22.825	0.001	0.001	0.000	0.000	0.000	0.000
56	A	138	TYR	0	-0.006	0.014	18.835	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	139	ASN	0	0.025	0.012	17.584	0.008	0.008	0.000	0.000	0.000	0.000
58	A	140	TYR	0	0.060	0.025	13.083	0.017	0.017	0.000	0.000	0.000	0.000
59	A	141	GLY	0	0.013	0.020	13.399	0.019	0.019	0.000	0.000	0.000	0.000
60	A	142	LEU	0	-0.002	0.011	12.577	-0.045	-0.045	0.000	0.000	0.000	0.000
61	A	143	ILE	0	-0.014	-0.010	10.406	0.045	0.045	0.000	0.000	0.000	0.000
62	A	144	ILE	0	0.010	-0.003	11.912	-0.080	-0.080	0.000	0.000	0.000	0.000
63	A	145	LEU	0	-0.007	-0.003	9.427	0.061	0.061	0.000	0.000	0.000	0.000
64	A	146	ASN	0	0.007	-0.013	12.936	-0.090	-0.090	0.000	0.000	0.000	0.000
65	A	147	ARG	1	0.830	0.927	9.045	0.583	0.583	0.000	0.000	0.000	0.000
66	A	148	ILE	0	-0.022	-0.020	14.522	0.022	0.022	0.000	0.000	0.000	0.000
67	A	149	ASN	0	-0.021	-0.005	17.675	0.011	0.011	0.000	0.000	0.000	0.000
68	A	150	PRO	0	0.029	-0.006	17.244	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	151	ASP	-1	-0.850	-0.880	17.735	-0.011	-0.011	0.000	0.000	0.000	0.000
70	A	152	ASN	0	-0.031	-0.038	13.976	-0.033	-0.033	0.000	0.000	0.000	0.000
71	A	153	PHE	0	0.020	0.021	16.241	0.017	0.017	0.000	0.000	0.000	0.000
72	A	154	SER	0	-0.018	-0.019	15.819	-0.026	-0.026	0.000	0.000	0.000	0.000
73	A	155	MET	0	0.004	0.006	16.362	0.003	0.003	0.000	0.000	0.000	0.000
74	A	156	GLY	0	0.009	0.011	16.767	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	157	ILE	0	-0.010	-0.031	15.344	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	158	VAL	0	-0.022	-0.035	18.932	0.009	0.009	0.000	0.000	0.000	0.000
77	A	159	PRO	0	0.039	0.029	19.678	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	160	ASN	0	0.074	0.014	22.225	0.013	0.013	0.000	0.000	0.000	0.000
79	A	161	SER	0	-0.035	-0.032	24.869	0.006	0.006	0.000	0.000	0.000	0.000
80	A	162	VAL	0	-0.007	-0.002	23.035	0.008	0.008	0.000	0.000	0.000	0.000
81	A	163	VAL	0	0.004	0.001	25.801	0.006	0.006	0.000	0.000	0.000	0.000
82	A	164	ASN	0	0.028	-0.008	28.207	0.006	0.006	0.000	0.000	0.000	0.000
83	A	165	LYS	1	0.875	0.943	27.071	0.024	0.024	0.000	0.000	0.000	0.000
84	A	166	ARG	1	0.822	0.914	29.899	0.007	0.007	0.000	0.000	0.000	0.000
85	A	167	LYS	1	0.900	0.945	31.732	0.035	0.035	0.000	0.000	0.000	0.000
86	A	168	VAL	0	-0.045	-0.011	34.223	0.001	0.001	0.000	0.000	0.000	0.000
87	A	169	PHE	0	-0.056	-0.038	33.496	0.001	0.001	0.000	0.000	0.000	0.000
88	A	170	ASN	0	-0.046	-0.028	33.713	0.004	0.004	0.000	0.000	0.000	0.000
89	A	171	ALA	0	0.055	0.029	35.848	0.000	0.000	0.000	0.000	0.000	0.000
90	A	172	GLU	-1	-0.941	-0.942	38.101	0.006	0.006	0.000	0.000	0.000	0.000
91	A	173	GLU	-1	-0.814	-0.913	32.922	0.010	0.010	0.000	0.000	0.000	0.000
92	A	174	ASP	-1	-0.867	-0.932	33.056	-0.016	-0.016	0.000	0.000	0.000	0.000
93	A	175	THR	0	-0.002	-0.018	35.497	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	176	LEU	0	-0.045	-0.012	37.594	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	177	ASN	0	-0.059	-0.031	30.749	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	178	PRO	0	0.020	0.018	33.396	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	179	LEU	0	-0.027	0.004	28.251	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	180	GLU	-1	-0.855	-0.913	30.290	-0.045	-0.045	0.000	0.000	0.000	0.000
99	A	181	CYS	0	-0.078	-0.042	27.602	0.001	0.001	0.000	0.000	0.000	0.000
100	A	182	MET	0	0.025	0.038	20.650	0.003	0.003	0.000	0.000	0.000	0.000
101	A	183	GLY	0	0.009	0.007	24.611	0.001	0.001	0.000	0.000	0.000	0.000
102	A	184	VAL	0	-0.005	-0.012	19.592	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	185	GLU	-1	-0.839	-0.907	22.896	-0.096	-0.096	0.000	0.000	0.000	0.000
104	A	186	VAL	0	0.002	0.003	21.039	-0.010	-0.010	0.000	0.000	0.000	0.000
105	A	187	LYS	1	0.837	0.920	23.752	0.105	0.105	0.000	0.000	0.000	0.000
106	A	188	ASP	-1	-0.886	-0.944	25.896	-0.115	-0.115	0.000	0.000	0.000	0.000
107	A	189	GLU	-1	-0.857	-0.918	23.033	-0.190	-0.190	0.000	0.000	0.000	0.000
108	A	190	LEU	0	-0.061	-0.028	21.631	-0.021	-0.021	0.000	0.000	0.000	0.000
109	A	191	VAL	0	-0.007	0.003	17.495	0.007	0.007	0.000	0.000	0.000	0.000
110	A	192	ILE	0	-0.029	-0.025	20.602	0.001	0.001	0.000	0.000	0.000	0.000
111	A	193	ILE	0	0.012	-0.001	17.970	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	194	LYS	1	0.830	0.940	22.628	0.066	0.066	0.000	0.000	0.000	0.000
113	A	195	ASN	0	0.039	-0.014	23.847	0.000	0.000	0.000	0.000	0.000	0.000
114	A	196	LEU	0	0.017	-0.004	24.718	0.002	0.002	0.000	0.000	0.000	0.000
115	A	197	LYS	1	0.840	0.902	27.267	0.022	0.022	0.000	0.000	0.000	0.000
116	A	198	HIS	0	-0.040	-0.012	29.095	0.000	0.000	0.000	0.000	0.000	0.000
117	A	199	GLU	-1	-0.759	-0.824	26.722	-0.046	-0.046	0.000	0.000	0.000	0.000
118	A	200	VAL	0	0.001	-0.016	26.326	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	201	TYR	0	-0.023	-0.038	22.344	0.004	0.004	0.000	0.000	0.000	0.000
120	A	202	GLY	0	0.053	0.024	22.875	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	203	ILE	0	-0.027	-0.018	16.383	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	204	TRP	0	0.011	0.014	19.084	-0.015	-0.015	0.000	0.000	0.000	0.000
123	A	205	ILE	0	0.043	0.011	13.978	-0.020	-0.020	0.000	0.000	0.000	0.000
124	A	206	HIS	0	0.018	0.014	16.347	0.027	0.027	0.000	0.000	0.000	0.000
125	A	207	THR	0	-0.013	-0.033	12.557	0.036	0.036	0.000	0.000	0.000	0.000
126	A	208	VAL	0	0.023	0.016	15.681	-0.012	-0.012	0.000	0.000	0.000	0.000
127	A	209	SER	0	0.014	0.015	13.842	0.022	0.022	0.000	0.000	0.000	0.000
128	A	210	ASP	-1	-0.782	-0.883	11.409	-0.594	-0.594	0.000	0.000	0.000	0.000
129	A	211	ARG	1	0.771	0.893	13.460	0.228	0.228	0.000	0.000	0.000	0.000
130	A	212	GLN	0	-0.026	-0.019	16.510	0.018	0.018	0.000	0.000	0.000	0.000
131	A	213	ASN	0	-0.017	-0.010	12.415	-0.022	-0.022	0.000	0.000	0.000	0.000
132	A	214	ILE	0	-0.002	-0.002	12.286	0.009	0.009	0.000	0.000	0.000	0.000
133	A	215	TYR	0	-0.005	0.006	13.958	0.030	0.030	0.000	0.000	0.000	0.000
134	A	216	GLU	-1	-0.848	-0.924	16.345	-0.233	-0.233	0.000	0.000	0.000	0.000
135	A	217	LEU	0	-0.020	-0.001	10.650	0.018	0.018	0.000	0.000	0.000	0.000
136	A	218	ILE	0	0.009	-0.008	14.844	0.028	0.028	0.000	0.000	0.000	0.000
137	A	219	LYS	1	0.948	0.992	16.833	0.145	0.145	0.000	0.000	0.000	0.000
138	A	220	TYR	0	0.001	0.001	15.792	0.016	0.016	0.000	0.000	0.000	0.000
139	A	221	LEU	0	-0.031	-0.028	13.466	0.018	0.018	0.000	0.000	0.000	0.000
140	A	222	LEU	0	-0.044	-0.015	17.888	0.021	0.021	0.000	0.000	0.000	0.000
141	A	223	GLU	-1	-0.933	-0.982	21.354	-0.083	-0.083	0.000	0.000	0.000	0.000
142	A	224	ASN	0	-0.086	-0.031	20.146	0.012	0.012	0.000	0.000	0.000	0.000
143	A	225	GLU	-1	-0.822	-0.888	22.066	-0.025	-0.025	0.000	0.000	0.000	0.000
144	A	226	PRO	0	-0.045	-0.037	19.372	-0.006	-0.006	0.000	0.000	0.000	0.000
145	A	227	LYS	1	0.793	0.891	15.560	-0.075	-0.075	0.000	0.000	0.000	0.000
146	A	228	ASP	-1	-0.843	-0.898	14.179	-0.041	-0.041	0.000	0.000	0.000	0.000

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