FMO DATABASE

FMODB ID: 2JL6R

Calculation Name: 4O6K-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4O6K

Chain ID: A

ChEMBL ID:

UniProt ID: Q5TLE4

Base Structure: X-ray

Registration Date: 2023-06-22

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	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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1414954.698301
FMO2-HF: Nuclear repulsion	1355270.666265
FMO2-HF: Total energy	-59684.032036
FMO2-MP2: Total energy	-59853.343768

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:GLY)

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

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.
-7.685	-4.263	6.646	-5.002	-5.067	-0.032

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.012 / q_NPA : -0.016

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	ARG	1	0.918	0.965	3.796	1.863	2.744	-0.012	-0.375	-0.494	0.002
4	A	4	PRO	0	0.001	0.011	6.656	0.237	0.237	0.000	0.000	0.000	0.000
5	A	5	THR	0	0.092	0.029	7.030	-0.453	-0.453	0.000	0.000	0.000	0.000
6	A	6	PRO	0	-0.012	-0.004	7.564	-0.093	-0.093	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.002	0.004	5.391	0.166	0.166	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.860	-0.924	2.339	-5.785	-4.287	3.511	-2.874	-2.135	-0.027
9	A	9	SER	0	-0.054	-0.018	5.084	0.562	0.604	-0.001	-0.002	-0.039	0.000
10	A	10	SER	0	0.025	0.019	8.774	-0.085	-0.085	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.019	0.006	10.178	0.033	0.033	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.012	-0.032	10.144	-0.015	-0.015	0.000	0.000	0.000	0.000
13	A	13	TRP	0	0.014	0.004	6.284	0.311	0.311	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.027	-0.009	11.700	0.086	0.086	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.888	-0.937	14.980	-0.377	-0.377	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.020	-0.015	12.223	0.053	0.053	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.034	-0.018	15.500	0.040	0.040	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.004	-0.004	17.047	0.049	0.049	0.000	0.000	0.000	0.000
19	A	19	MET	0	-0.037	-0.025	19.154	0.019	0.019	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.035	-0.020	18.384	0.022	0.022	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.946	-0.968	20.811	-0.230	-0.230	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.053	-0.023	23.031	0.032	0.032	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.007	-0.003	23.821	0.016	0.016	0.000	0.000	0.000	0.000
24	A	24	ARG	1	0.929	0.961	23.229	0.258	0.258	0.000	0.000	0.000	0.000
25	A	25	ASN	0	-0.089	-0.018	26.288	0.017	0.017	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.843	-0.923	28.879	-0.164	-0.164	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.953	-0.980	30.989	-0.142	-0.142	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.847	-0.927	27.291	-0.225	-0.225	0.000	0.000	0.000	0.000
29	A	29	HIS	0	-0.102	-0.048	29.018	0.012	0.012	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.847	-0.925	23.582	-0.251	-0.251	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.095	-0.038	26.736	0.018	0.018	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.876	0.913	17.638	0.360	0.360	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.046	-0.044	23.644	0.022	0.022	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.073	-0.036	16.944	0.011	0.011	0.000	0.000	0.000	0.000
35	A	35	PRO	0	-0.037	-0.009	20.034	0.019	0.019	0.000	0.000	0.000	0.000
36	A	36	TYR	0	-0.008	-0.012	17.520	-0.035	-0.035	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.028	0.005	14.533	0.037	0.037	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.001	0.005	15.120	-0.043	-0.043	0.000	0.000	0.000	0.000
39	A	39	HIS	0	0.053	0.011	10.925	-0.027	-0.027	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.896	-0.953	12.835	-0.042	-0.042	0.000	0.000	0.000	0.000
41	A	41	MET	0	-0.008	-0.002	15.234	0.006	0.006	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.058	0.004	10.028	0.002	0.002	0.000	0.000	0.000	0.000
43	A	43	GLN	0	-0.015	-0.003	8.605	0.090	0.090	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.973	-0.965	12.327	-0.066	-0.066	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.877	-0.953	14.095	-0.049	-0.049	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.074	-0.028	15.247	-0.027	-0.027	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.017	-0.049	13.081	-0.036	-0.036	0.000	0.000	0.000	0.000
48	A	48	CYS	0	-0.120	-0.023	7.730	0.482	0.482	0.000	0.000	0.000	0.000
49	A	49	CYS	0	-0.055	-0.029	12.706	-0.014	-0.014	0.000	0.000	0.000	0.000
50	A	50	ILE	0	-0.033	-0.012	16.119	0.021	0.021	0.000	0.000	0.000	0.000
51	A	51	ASN	0	0.020	-0.010	13.668	0.039	0.039	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.050	0.033	14.489	-0.012	-0.012	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.931	0.971	15.889	0.278	0.278	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.026	-0.019	18.071	0.041	0.041	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.014	0.017	13.809	0.027	0.027	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.933	0.977	17.751	0.291	0.291	0.000	0.000	0.000	0.000
57	A	57	TYR	0	-0.049	-0.038	20.534	0.036	0.036	0.000	0.000	0.000	0.000
58	A	58	TYR	0	0.021	-0.029	19.392	0.022	0.022	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.028	-0.006	19.071	0.018	0.018	0.000	0.000	0.000	0.000
60	A	60	ASN	0	-0.081	-0.044	21.654	0.024	0.024	0.000	0.000	0.000	0.000
61	A	61	HIS	0	-0.001	0.012	24.805	0.021	0.021	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.013	0.016	22.686	0.010	0.010	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.019	-0.029	18.894	0.007	0.007	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.926	-0.946	23.473	-0.193	-0.193	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.006	-0.025	26.602	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.890	-0.932	29.465	-0.145	-0.145	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.861	-0.916	32.829	-0.138	-0.138	0.000	0.000	0.000	0.000
68	A	68	HIS	0	0.031	0.016	31.566	-0.015	-0.015	0.000	0.000	0.000	0.000
69	A	69	THR	0	0.003	-0.018	27.785	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.931	-0.969	27.593	-0.222	-0.222	0.000	0.000	0.000	0.000
71	A	71	MET	0	-0.095	-0.037	28.580	0.000	0.000	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.816	0.917	28.066	0.194	0.194	0.000	0.000	0.000	0.000
73	A	73	TYR	0	-0.042	-0.055	23.932	-0.015	-0.015	0.000	0.000	0.000	0.000
74	A	74	PRO	0	0.052	0.029	25.349	-0.010	-0.010	0.000	0.000	0.000	0.000
75	A	75	MET	0	0.005	0.010	20.084	0.009	0.009	0.000	0.000	0.000	0.000
76	A	76	ILE	0	0.015	0.010	20.833	-0.037	-0.037	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.950	0.986	21.656	0.205	0.205	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.017	-0.015	17.814	0.021	0.021	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.036	0.017	16.334	-0.034	-0.034	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.928	0.979	17.112	0.217	0.217	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.915	-0.962	19.000	-0.270	-0.270	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.038	-0.020	15.422	0.003	0.003	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.010	-0.011	13.629	-0.063	-0.063	0.000	0.000	0.000	0.000
84	A	84	HIS	0	0.009	0.005	15.515	-0.029	-0.029	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.924	0.961	15.278	0.358	0.358	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.018	0.016	10.988	0.022	0.022	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.874	-0.950	13.338	-0.341	-0.341	0.000	0.000	0.000	0.000
88	A	88	GLN	0	-0.051	-0.029	16.067	0.075	0.075	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.954	-0.965	11.697	-0.389	-0.389	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.026	-0.030	10.591	0.054	0.054	0.000	0.000	0.000	0.000
91	A	91	GLN	0	-0.015	-0.014	14.425	0.052	0.052	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.049	-0.017	17.235	0.055	0.055	0.000	0.000	0.000	0.000
93	A	93	HIS	0	-0.012	-0.005	13.657	0.059	0.059	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.962	0.974	18.325	0.042	0.042	0.000	0.000	0.000	0.000
95	A	96	HIS	0	-0.012	0.004	21.338	0.020	0.020	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.801	-0.875	21.952	-0.198	-0.198	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.034	0.000	19.572	0.009	0.009	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.035	-0.043	23.050	-0.018	-0.018	0.000	0.000	0.000	0.000
99	A	100	SER	0	0.031	0.010	25.568	0.003	0.003	0.000	0.000	0.000	0.000
100	A	101	HIS	0	0.085	0.029	21.872	0.005	0.005	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.020	-0.029	24.863	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	103	LEU	0	0.051	0.027	19.875	0.007	0.007	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.002	0.018	21.048	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.805	0.905	23.256	0.162	0.162	0.000	0.000	0.000	0.000
105	A	106	GLN	0	-0.041	-0.007	24.755	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	107	PHE	0	0.064	0.045	22.604	0.009	0.009	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.937	0.977	24.741	0.225	0.225	0.000	0.000	0.000	0.000
108	A	109	ARG	1	0.920	0.971	27.334	0.164	0.164	0.000	0.000	0.000	0.000
109	A	110	ASN	0	0.042	0.003	26.352	0.024	0.024	0.000	0.000	0.000	0.000
110	A	111	TYR	0	0.016	0.014	26.482	0.003	0.003	0.000	0.000	0.000	0.000
111	A	112	HIS	0	0.015	0.000	28.489	0.002	0.002	0.000	0.000	0.000	0.000
112	A	113	ALA	0	-0.030	-0.027	31.876	0.009	0.009	0.000	0.000	0.000	0.000
113	A	114	SER	0	0.000	0.003	30.070	0.011	0.011	0.000	0.000	0.000	0.000
114	A	115	ALA	0	0.016	-0.007	31.746	0.004	0.004	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.113	-0.040	33.322	0.008	0.008	0.000	0.000	0.000	0.000
116	A	117	MET	0	-0.045	-0.015	35.631	0.006	0.006	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.801	-0.911	34.924	-0.139	-0.139	0.000	0.000	0.000	0.000
118	A	119	LEU	0	0.023	0.017	32.335	-0.011	-0.011	0.000	0.000	0.000	0.000
119	A	120	ALA	0	0.007	0.003	31.587	-0.014	-0.014	0.000	0.000	0.000	0.000
120	A	121	ALA	0	0.039	0.024	30.711	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.013	0.000	29.557	-0.015	-0.015	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.794	0.879	26.545	0.202	0.202	0.000	0.000	0.000	0.000
123	A	124	ASN	0	0.073	0.043	25.776	-0.035	-0.035	0.000	0.000	0.000	0.000
124	A	125	LYS	1	0.850	0.957	25.191	0.210	0.210	0.000	0.000	0.000	0.000
125	A	126	ALA	0	0.012	0.001	23.181	-0.026	-0.026	0.000	0.000	0.000	0.000
126	A	127	ILE	0	0.007	0.013	21.356	-0.050	-0.050	0.000	0.000	0.000	0.000
127	A	128	GLY	0	0.033	0.035	20.321	-0.045	-0.045	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.745	-0.851	19.203	-0.366	-0.366	0.000	0.000	0.000	0.000
129	A	130	THR	0	-0.026	-0.045	15.864	-0.048	-0.048	0.000	0.000	0.000	0.000
130	A	131	ASN	0	0.029	0.005	13.025	-0.233	-0.233	0.000	0.000	0.000	0.000
131	A	132	THR	0	0.019	0.013	12.949	-0.141	-0.141	0.000	0.000	0.000	0.000
132	A	133	LEU	0	-0.022	0.004	13.029	-0.077	-0.077	0.000	0.000	0.000	0.000
133	A	134	TYR	0	0.006	-0.017	8.678	-0.062	-0.062	0.000	0.000	0.000	0.000
134	A	135	HIS	0	0.001	0.002	8.316	-0.336	-0.336	0.000	0.000	0.000	0.000
135	A	136	TYR	0	0.022	0.020	8.375	-0.161	-0.161	0.000	0.000	0.000	0.000
136	A	137	LEU	0	-0.006	0.004	9.501	0.024	0.024	0.000	0.000	0.000	0.000
137	A	138	PHE	0	-0.046	-0.015	2.521	-2.034	-1.384	3.112	-1.568	-2.195	-0.007
138	A	139	GLU	-1	-0.872	-0.939	4.510	-2.126	-2.174	-0.001	-0.030	0.079	0.000
139	A	140	SER	0	-0.018	-0.016	6.096	0.560	0.560	0.000	0.000	0.000	0.000
140	A	142	THR	0	0.071	0.038	3.189	-0.444	-0.045	0.037	-0.153	-0.283	0.000
141	A	143	PRO	0	-0.067	-0.024	5.699	0.317	0.317	0.000	0.000	0.000	0.000

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