FMO DATABASE

FMODB ID: 6N4QZ

Calculation Name: 1C3K-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1C3K

Chain ID: A

ChEMBL ID:

UniProt ID: Q9ZQY5

Base Structure: X-ray

Registration Date: 2023-06-26

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	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	143
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1229027.313578
FMO2-HF: Nuclear repulsion	1176684.358581
FMO2-HF: Total energy	-52342.954997
FMO2-MP2: Total energy	-52498.424321

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:5:ASP)

Summations of interaction energy for fragment #1(A:5:ASP)

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.
-111.051	-111.413	23.14	-13.022	-9.756	0.097

Interaction energy analysis for fragmet #1(A:5:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.834 / q_NPA : -0.912

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	7	ALA	0	-0.011	0.007	3.357	-13.362	-10.287	0.022	-1.618	-1.479	0.006
4	A	8	VAL	0	-0.009	0.002	5.170	-5.952	-5.952	0.000	0.000	0.000	0.000
5	A	9	GLN	0	-0.033	-0.027	6.895	0.201	0.201	0.000	0.000	0.000	0.000
6	A	10	ALA	0	0.013	0.016	9.426	-2.499	-2.499	0.000	0.000	0.000	0.000
7	A	11	GLY	0	0.049	0.029	12.361	0.081	0.081	0.000	0.000	0.000	0.000
8	A	12	PRO	0	-0.084	-0.043	15.316	0.390	0.390	0.000	0.000	0.000	0.000
9	A	13	TRP	0	0.020	-0.007	15.065	-0.593	-0.593	0.000	0.000	0.000	0.000
10	A	14	GLY	0	0.048	-0.002	19.763	0.391	0.391	0.000	0.000	0.000	0.000
11	A	15	GLY	0	-0.008	-0.003	22.501	-0.460	-0.460	0.000	0.000	0.000	0.000
12	A	16	ASN	0	-0.054	-0.033	21.794	1.186	1.186	0.000	0.000	0.000	0.000
13	A	17	GLY	0	0.049	0.043	23.008	-0.113	-0.113	0.000	0.000	0.000	0.000
14	A	18	GLY	0	0.036	0.022	21.690	0.747	0.747	0.000	0.000	0.000	0.000
15	A	19	LYS	1	0.910	0.945	18.556	-14.901	-14.901	0.000	0.000	0.000	0.000
16	A	20	ARG	1	0.886	0.942	12.599	-21.547	-21.547	0.000	0.000	0.000	0.000
17	A	21	TRP	0	-0.021	0.010	10.956	0.845	0.845	0.000	0.000	0.000	0.000
18	A	22	LEU	0	0.015	-0.019	5.298	0.281	0.281	0.000	0.000	0.000	0.000
19	A	23	GLN	0	-0.054	-0.023	7.033	-3.513	-3.513	0.000	0.000	0.000	0.000
20	A	24	THR	0	-0.028	-0.038	1.623	-27.074	-34.495	20.324	-8.346	-4.556	0.078
21	A	25	ALA	0	0.041	0.018	4.576	-5.625	-5.604	-0.001	-0.029	0.009	0.000
22	A	26	HIS	0	-0.033	-0.007	3.134	-5.493	-3.973	0.140	-0.710	-0.950	0.006
23	A	27	GLY	0	-0.007	-0.003	3.374	-10.160	-9.481	0.019	-0.318	-0.381	0.003
24	A	28	GLY	0	-0.032	-0.005	4.764	-6.716	-6.666	-0.001	-0.007	-0.042	0.000
25	A	29	LYS	1	0.760	0.847	7.527	-18.731	-18.731	0.000	0.000	0.000	0.000
26	A	30	ILE	0	-0.001	-0.007	7.399	-0.570	-0.570	0.000	0.000	0.000	0.000
27	A	31	THR	0	0.014	-0.003	10.354	-1.167	-1.167	0.000	0.000	0.000	0.000
28	A	32	SER	0	0.022	0.010	13.810	-2.148	-2.148	0.000	0.000	0.000	0.000
29	A	33	ILE	0	-0.061	-0.014	13.826	1.756	1.756	0.000	0.000	0.000	0.000
30	A	34	ILE	0	-0.003	0.007	16.066	-1.213	-1.213	0.000	0.000	0.000	0.000
31	A	35	ILE	0	0.017	0.001	18.343	0.713	0.713	0.000	0.000	0.000	0.000
32	A	36	LYS	1	0.815	0.903	20.779	-13.089	-13.089	0.000	0.000	0.000	0.000
33	A	37	GLY	0	0.025	0.023	24.012	0.066	0.066	0.000	0.000	0.000	0.000
34	A	38	GLY	0	0.020	0.001	25.766	-0.423	-0.423	0.000	0.000	0.000	0.000
35	A	39	THR	0	-0.007	0.010	29.277	-0.027	-0.027	0.000	0.000	0.000	0.000
36	A	40	CYS	0	-0.069	-0.016	25.981	-0.027	-0.027	0.000	0.000	0.000	0.000
37	A	41	ILE	0	-0.010	0.005	20.174	-0.142	-0.142	0.000	0.000	0.000	0.000
38	A	42	PHE	0	0.036	0.004	22.965	0.264	0.264	0.000	0.000	0.000	0.000
39	A	43	SER	0	-0.049	-0.043	20.514	0.287	0.287	0.000	0.000	0.000	0.000
40	A	44	ILE	0	-0.017	-0.002	15.468	-0.349	-0.349	0.000	0.000	0.000	0.000
41	A	45	GLN	0	-0.004	0.013	15.038	-0.750	-0.750	0.000	0.000	0.000	0.000
42	A	46	PHE	0	0.010	-0.006	11.223	-0.041	-0.041	0.000	0.000	0.000	0.000
43	A	47	VAL	0	0.003	0.015	13.196	-0.011	-0.011	0.000	0.000	0.000	0.000
44	A	48	TYR	0	-0.004	0.004	7.850	0.946	0.946	0.000	0.000	0.000	0.000
45	A	49	LYS	1	0.890	0.951	10.481	-20.623	-20.623	0.000	0.000	0.000	0.000
46	A	50	ASP	-1	-0.734	-0.850	8.696	28.384	28.384	0.000	0.000	0.000	0.000
47	A	51	LYS	1	0.943	0.944	8.562	-29.589	-29.589	0.000	0.000	0.000	0.000
48	A	52	ASP	-1	-0.924	-0.951	11.487	20.808	20.808	0.000	0.000	0.000	0.000
49	A	53	ASN	0	-0.079	-0.038	13.285	-1.892	-1.892	0.000	0.000	0.000	0.000
50	A	54	ILE	0	-0.004	0.011	13.726	-1.425	-1.425	0.000	0.000	0.000	0.000
51	A	55	GLU	-1	-0.876	-0.928	13.041	19.462	19.462	0.000	0.000	0.000	0.000
52	A	56	TYR	0	-0.068	-0.048	10.880	-0.749	-0.749	0.000	0.000	0.000	0.000
53	A	57	HIS	0	-0.020	-0.023	12.854	0.306	0.306	0.000	0.000	0.000	0.000
54	A	58	SER	0	-0.024	-0.013	11.361	0.027	0.027	0.000	0.000	0.000	0.000
55	A	59	GLY	0	0.034	0.017	12.944	-1.868	-1.868	0.000	0.000	0.000	0.000
56	A	60	LYS	1	0.875	0.938	14.973	-14.676	-14.676	0.000	0.000	0.000	0.000
57	A	61	PHE	0	0.026	0.012	11.905	0.385	0.385	0.000	0.000	0.000	0.000
58	A	62	GLY	0	0.045	0.043	17.226	-0.314	-0.314	0.000	0.000	0.000	0.000
59	A	63	VAL	0	-0.049	-0.030	20.711	0.385	0.385	0.000	0.000	0.000	0.000
60	A	64	LEU	0	0.023	0.027	23.291	-0.479	-0.479	0.000	0.000	0.000	0.000
61	A	65	GLY	0	0.040	0.015	25.293	0.411	0.411	0.000	0.000	0.000	0.000
62	A	66	ASP	-1	-0.871	-0.919	27.398	10.516	10.516	0.000	0.000	0.000	0.000
63	A	67	LYS	1	0.783	0.863	27.151	-11.148	-11.148	0.000	0.000	0.000	0.000
64	A	68	ALA	0	-0.018	-0.015	23.739	0.286	0.286	0.000	0.000	0.000	0.000
65	A	69	GLU	-1	-0.828	-0.900	23.859	11.638	11.638	0.000	0.000	0.000	0.000
66	A	70	THR	0	0.004	-0.009	19.950	0.715	0.715	0.000	0.000	0.000	0.000
67	A	71	ILE	0	-0.056	-0.014	17.956	-0.726	-0.726	0.000	0.000	0.000	0.000
68	A	72	THR	0	0.041	-0.008	18.048	0.704	0.704	0.000	0.000	0.000	0.000
69	A	73	PHE	0	-0.073	-0.027	14.414	-0.624	-0.624	0.000	0.000	0.000	0.000
70	A	74	ALA	0	0.054	0.024	18.376	0.167	0.167	0.000	0.000	0.000	0.000
71	A	75	GLU	-1	-0.862	-0.933	17.935	15.113	15.113	0.000	0.000	0.000	0.000
72	A	76	ASP	-1	-0.853	-0.900	17.032	15.251	15.251	0.000	0.000	0.000	0.000
73	A	77	GLU	-1	-0.786	-0.837	17.485	14.980	14.980	0.000	0.000	0.000	0.000
74	A	78	ASP	-1	-0.852	-0.934	12.146	23.614	23.614	0.000	0.000	0.000	0.000
75	A	79	ILE	0	-0.007	-0.001	11.531	-1.146	-1.146	0.000	0.000	0.000	0.000
76	A	80	THR	0	-0.016	-0.019	12.872	0.994	0.994	0.000	0.000	0.000	0.000
77	A	81	ALA	0	-0.008	-0.012	15.332	-0.195	-0.195	0.000	0.000	0.000	0.000
78	A	82	ILE	0	-0.016	0.019	13.510	0.156	0.156	0.000	0.000	0.000	0.000
79	A	83	SER	0	-0.038	-0.023	16.170	-0.512	-0.512	0.000	0.000	0.000	0.000
80	A	84	GLY	0	0.052	0.015	19.548	0.288	0.288	0.000	0.000	0.000	0.000
81	A	85	THR	0	-0.060	-0.027	22.184	-0.513	-0.513	0.000	0.000	0.000	0.000
82	A	86	PHE	0	0.000	0.005	23.281	0.448	0.448	0.000	0.000	0.000	0.000
83	A	87	GLY	0	0.036	0.015	25.772	-0.443	-0.443	0.000	0.000	0.000	0.000
84	A	88	ALA	0	-0.019	-0.002	28.642	0.291	0.291	0.000	0.000	0.000	0.000
85	A	89	TYR	0	0.052	0.006	28.721	-0.120	-0.120	0.000	0.000	0.000	0.000
86	A	90	TYR	0	-0.008	-0.011	30.990	0.024	0.024	0.000	0.000	0.000	0.000
87	A	91	HIS	0	-0.009	-0.003	33.103	0.210	0.210	0.000	0.000	0.000	0.000
88	A	92	MET	0	0.015	0.029	28.347	0.210	0.210	0.000	0.000	0.000	0.000
89	A	93	THR	0	-0.020	-0.015	26.040	-0.249	-0.249	0.000	0.000	0.000	0.000
90	A	94	VAL	0	-0.008	0.000	24.229	0.448	0.448	0.000	0.000	0.000	0.000
91	A	95	VAL	0	0.029	0.011	19.706	-0.321	-0.321	0.000	0.000	0.000	0.000
92	A	96	THR	0	0.001	-0.001	23.184	-0.066	-0.066	0.000	0.000	0.000	0.000
93	A	97	SER	0	-0.014	-0.027	24.533	-0.216	-0.216	0.000	0.000	0.000	0.000
94	A	98	LEU	0	-0.002	0.004	18.098	0.492	0.492	0.000	0.000	0.000	0.000
95	A	99	THR	0	-0.032	-0.027	20.509	-0.963	-0.963	0.000	0.000	0.000	0.000
96	A	100	PHE	0	0.032	0.026	14.281	0.523	0.523	0.000	0.000	0.000	0.000
97	A	101	GLN	0	-0.026	-0.007	17.517	-1.086	-1.086	0.000	0.000	0.000	0.000
98	A	102	THR	0	0.022	-0.003	16.437	0.945	0.945	0.000	0.000	0.000	0.000
99	A	103	ASN	0	-0.038	-0.032	17.665	-0.483	-0.483	0.000	0.000	0.000	0.000
100	A	104	LYS	1	0.820	0.914	19.475	-14.468	-14.468	0.000	0.000	0.000	0.000
101	A	105	LYS	1	0.884	0.933	21.508	-13.302	-13.302	0.000	0.000	0.000	0.000
102	A	106	VAL	0	0.040	0.026	21.347	0.731	0.731	0.000	0.000	0.000	0.000
103	A	107	TYR	0	-0.058	-0.061	20.187	-0.796	-0.796	0.000	0.000	0.000	0.000
104	A	108	GLY	0	0.048	0.038	21.943	0.678	0.678	0.000	0.000	0.000	0.000
105	A	109	PRO	0	-0.029	-0.011	24.620	-0.322	-0.322	0.000	0.000	0.000	0.000
106	A	110	PHE	0	0.018	0.002	21.631	-0.218	-0.218	0.000	0.000	0.000	0.000
107	A	111	GLY	0	0.041	0.010	24.762	0.438	0.438	0.000	0.000	0.000	0.000
108	A	112	THR	0	-0.008	-0.015	27.128	-0.446	-0.446	0.000	0.000	0.000	0.000
109	A	113	VAL	0	-0.025	0.006	28.212	0.367	0.367	0.000	0.000	0.000	0.000
110	A	114	ALA	0	0.023	0.008	28.674	-0.441	-0.441	0.000	0.000	0.000	0.000
111	A	115	SER	0	-0.005	-0.018	29.659	0.040	0.040	0.000	0.000	0.000	0.000
112	A	116	SER	0	-0.043	-0.009	27.428	-0.170	-0.170	0.000	0.000	0.000	0.000
113	A	117	SER	0	0.026	0.015	24.949	0.260	0.260	0.000	0.000	0.000	0.000
114	A	118	PHE	0	0.007	0.009	17.543	-0.012	-0.012	0.000	0.000	0.000	0.000
115	A	119	SER	0	0.007	-0.022	19.392	0.139	0.139	0.000	0.000	0.000	0.000
116	A	120	LEU	0	-0.006	0.018	12.071	-0.088	-0.088	0.000	0.000	0.000	0.000
117	A	121	PRO	0	0.037	0.012	15.369	0.844	0.844	0.000	0.000	0.000	0.000
118	A	122	LEU	0	-0.021	-0.004	10.460	0.373	0.373	0.000	0.000	0.000	0.000
119	A	123	THR	0	0.001	0.000	14.788	-0.194	-0.194	0.000	0.000	0.000	0.000
120	A	124	LYS	1	0.899	0.929	13.333	-17.010	-17.010	0.000	0.000	0.000	0.000
121	A	125	GLY	0	0.024	0.031	10.257	0.374	0.374	0.000	0.000	0.000	0.000
122	A	126	LYS	1	0.931	0.965	8.087	-24.682	-24.682	0.000	0.000	0.000	0.000
123	A	127	PHE	0	0.019	0.009	7.239	2.038	2.038	0.000	0.000	0.000	0.000
124	A	128	ALA	0	0.008	0.015	2.431	-1.800	-0.766	1.077	-1.085	-1.025	0.006
125	A	129	GLY	0	0.027	-0.001	4.354	3.856	4.046	-0.001	-0.019	-0.170	0.000
126	A	130	PHE	0	-0.023	0.001	7.028	-3.144	-3.144	0.000	0.000	0.000	0.000
127	A	131	PHE	0	-0.004	0.000	8.906	2.957	2.957	0.000	0.000	0.000	0.000
128	A	132	GLY	0	0.053	0.019	11.078	-1.783	-1.783	0.000	0.000	0.000	0.000
129	A	133	ASN	0	-0.033	-0.002	14.792	1.709	1.709	0.000	0.000	0.000	0.000
130	A	134	SER	0	-0.004	-0.003	17.704	0.125	0.125	0.000	0.000	0.000	0.000
131	A	135	GLY	0	0.036	0.014	19.631	0.230	0.230	0.000	0.000	0.000	0.000
132	A	136	ASP	-1	-0.894	-0.941	22.523	12.323	12.323	0.000	0.000	0.000	0.000
133	A	137	VAL	0	-0.031	-0.007	23.434	-0.066	-0.066	0.000	0.000	0.000	0.000
134	A	138	LEU	0	0.025	0.005	16.965	0.557	0.557	0.000	0.000	0.000	0.000
135	A	139	ASP	-1	-0.839	-0.926	20.825	13.922	13.922	0.000	0.000	0.000	0.000
136	A	140	SER	0	-0.024	-0.021	19.168	-0.155	-0.155	0.000	0.000	0.000	0.000
137	A	141	ILE	0	-0.009	-0.001	14.236	0.841	0.841	0.000	0.000	0.000	0.000
138	A	142	GLY	0	0.037	0.014	13.676	-1.436	-1.436	0.000	0.000	0.000	0.000
139	A	143	GLY	0	-0.006	0.007	10.227	1.038	1.038	0.000	0.000	0.000	0.000
140	A	144	VAL	0	-0.026	-0.001	4.248	-1.135	-0.966	-0.001	-0.034	-0.135	0.000
141	A	145	VAL	0	-0.033	-0.017	6.134	1.118	1.118	0.000	0.000	0.000	0.000
142	A	146	VAL	0	0.054	0.027	2.417	1.544	1.818	1.563	-0.854	-0.984	-0.002
143	A	147	PRO	0	-0.012	-0.005	5.369	-5.098	-5.051	-0.001	-0.002	-0.043	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ASP)