FMO DATABASE

FMODB ID: NN24Q

Calculation Name: 2C0D-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2C0D

Chain ID: A

ChEMBL ID:

UniProt ID: Q8I5Q6

Base Structure: X-ray

Registration Date: 2023-09-22

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	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	168
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1778111.657809
FMO2-HF: Nuclear repulsion	1711294.793487
FMO2-HF: Total energy	-66816.864321
FMO2-MP2: Total energy	-67011.840797

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:21:LEU)

Summations of interaction energy for fragment #1(A:21: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.
-12.319	-4.664	10.286	-5.185	-12.757	-0.039

Interaction energy analysis for fragmet #1(A:21:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.006 / q_NPA : 0.004

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	23	THR	0	-0.038	-0.015	3.865	1.390	2.642	-0.010	-0.541	-0.701	0.003
4	A	24	LYS	1	0.862	0.935	2.935	-2.908	-2.042	0.112	-0.233	-0.746	0.000
5	A	25	LYS	1	0.862	0.907	5.003	-0.362	-0.337	-0.001	-0.008	-0.015	0.000
6	A	26	ALA	0	0.016	0.010	4.460	-0.397	-0.220	-0.001	-0.013	-0.163	0.000
7	A	27	TYR	0	-0.038	-0.028	4.171	0.125	0.335	-0.001	-0.018	-0.191	0.000
8	A	28	ASN	0	0.063	0.022	5.641	-0.025	-0.025	0.000	0.000	0.000	0.000
9	A	29	PHE	0	-0.006	-0.007	8.709	-0.003	-0.003	0.000	0.000	0.000	0.000
10	A	30	THR	0	0.030	0.010	11.594	0.028	0.028	0.000	0.000	0.000	0.000
11	A	31	ALA	0	-0.024	-0.005	14.365	-0.003	-0.003	0.000	0.000	0.000	0.000
12	A	32	GLN	0	0.022	0.012	16.308	0.012	0.012	0.000	0.000	0.000	0.000
13	A	33	GLY	0	0.015	0.007	17.956	-0.029	-0.029	0.000	0.000	0.000	0.000
14	A	34	LEU	0	-0.030	0.007	19.534	0.022	0.022	0.000	0.000	0.000	0.000
15	A	35	ASN	0	0.025	-0.021	21.677	-0.008	-0.008	0.000	0.000	0.000	0.000
16	A	36	LYS	1	0.944	0.981	23.274	0.153	0.153	0.000	0.000	0.000	0.000
17	A	37	ASN	0	-0.064	-0.025	25.449	0.010	0.010	0.000	0.000	0.000	0.000
18	A	38	ASN	0	-0.065	-0.042	26.570	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	39	GLU	-1	-0.799	-0.867	26.727	-0.124	-0.124	0.000	0.000	0.000	0.000
20	A	40	ILE	0	-0.029	-0.024	23.461	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	41	ILE	0	-0.019	-0.004	20.947	0.010	0.010	0.000	0.000	0.000	0.000
22	A	42	ASN	0	0.004	-0.009	19.569	-0.024	-0.024	0.000	0.000	0.000	0.000
23	A	43	VAL	0	-0.005	0.001	14.838	0.008	0.008	0.000	0.000	0.000	0.000
24	A	44	ASP	-1	-0.808	-0.885	15.409	-0.325	-0.325	0.000	0.000	0.000	0.000
25	A	45	LEU	0	-0.008	0.013	8.611	0.014	0.014	0.000	0.000	0.000	0.000
26	A	46	SER	0	-0.035	-0.049	13.044	0.021	0.021	0.000	0.000	0.000	0.000
27	A	47	SER	0	-0.045	-0.034	13.995	0.040	0.040	0.000	0.000	0.000	0.000
28	A	48	PHE	0	0.050	0.019	14.540	0.029	0.029	0.000	0.000	0.000	0.000
29	A	49	ILE	0	-0.007	0.004	12.235	0.011	0.011	0.000	0.000	0.000	0.000
30	A	50	GLY	0	-0.048	-0.029	15.647	0.024	0.024	0.000	0.000	0.000	0.000
31	A	51	GLN	0	-0.118	-0.057	17.768	0.034	0.034	0.000	0.000	0.000	0.000
32	A	52	LYS	1	0.840	0.912	17.211	0.224	0.224	0.000	0.000	0.000	0.000
33	A	53	TYR	0	-0.059	-0.045	13.566	-0.019	-0.019	0.000	0.000	0.000	0.000
34	A	54	CYS	0	-0.029	0.004	11.395	0.022	0.022	0.000	0.000	0.000	0.000
35	A	55	CYS	0	-0.003	-0.004	11.403	-0.047	-0.047	0.000	0.000	0.000	0.000
36	A	56	LEU	0	-0.018	0.007	6.552	0.047	0.047	0.000	0.000	0.000	0.000
37	A	57	LEU	0	0.023	-0.001	9.715	-0.059	-0.059	0.000	0.000	0.000	0.000
38	A	58	PHE	0	0.041	0.015	6.457	0.035	0.035	0.000	0.000	0.000	0.000
39	A	59	TYR	0	-0.010	-0.001	11.271	0.042	0.042	0.000	0.000	0.000	0.000
40	A	60	PRO	0	0.022	0.029	14.248	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	61	LEU	0	0.041	0.003	16.588	0.017	0.017	0.000	0.000	0.000	0.000
42	A	62	ASN	0	-0.029	-0.010	19.425	0.028	0.028	0.000	0.000	0.000	0.000
43	A	63	TYR	0	0.040	0.008	21.253	0.001	0.001	0.000	0.000	0.000	0.000
44	A	64	THR	0	-0.004	-0.001	22.722	0.006	0.006	0.000	0.000	0.000	0.000
45	A	65	PHE	0	0.039	0.008	19.187	0.004	0.004	0.000	0.000	0.000	0.000
46	A	66	VAL	0	-0.027	0.030	20.299	-0.013	-0.013	0.000	0.000	0.000	0.000
47	A	67	CYS	0	-0.013	-0.017	19.944	0.016	0.016	0.000	0.000	0.000	0.000
48	A	68	PRO	0	0.062	0.027	21.199	-0.013	-0.013	0.000	0.000	0.000	0.000
49	A	69	THR	0	0.033	0.007	23.458	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	70	GLU	-1	-0.738	-0.822	16.955	-0.271	-0.271	0.000	0.000	0.000	0.000
51	A	71	ILE	0	0.004	0.008	17.669	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	72	ILE	0	0.003	0.009	20.904	0.004	0.004	0.000	0.000	0.000	0.000
53	A	73	GLU	-1	-0.847	-0.920	22.403	-0.109	-0.109	0.000	0.000	0.000	0.000
54	A	74	PHE	0	0.016	-0.004	15.726	0.004	0.004	0.000	0.000	0.000	0.000
55	A	75	ASN	0	0.040	0.030	21.098	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	76	LYS	1	0.814	0.910	23.421	0.115	0.115	0.000	0.000	0.000	0.000
57	A	77	HIS	1	0.809	0.897	22.618	0.137	0.137	0.000	0.000	0.000	0.000
58	A	78	ILE	0	0.047	0.043	21.292	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	79	LYS	1	1.003	0.983	23.434	0.087	0.087	0.000	0.000	0.000	0.000
60	A	80	ASP	-1	-0.888	-0.941	22.980	-0.105	-0.105	0.000	0.000	0.000	0.000
61	A	81	PHE	0	-0.016	-0.023	16.439	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	82	GLU	-1	-0.922	-0.973	20.876	-0.142	-0.142	0.000	0.000	0.000	0.000
63	A	83	ASN	0	-0.050	-0.021	23.218	0.008	0.008	0.000	0.000	0.000	0.000
64	A	84	LYS	1	0.826	0.908	19.777	0.118	0.118	0.000	0.000	0.000	0.000
65	A	85	ASN	0	-0.038	-0.026	19.728	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	86	VAL	0	-0.006	-0.010	15.058	-0.020	-0.020	0.000	0.000	0.000	0.000
67	A	87	GLU	-1	-0.888	-0.928	15.766	-0.215	-0.215	0.000	0.000	0.000	0.000
68	A	88	LEU	0	-0.047	-0.018	14.749	-0.048	-0.048	0.000	0.000	0.000	0.000
69	A	89	LEU	0	0.007	-0.003	12.566	0.021	0.021	0.000	0.000	0.000	0.000
70	A	90	GLY	0	0.028	0.021	13.119	-0.045	-0.045	0.000	0.000	0.000	0.000
71	A	91	ILE	0	-0.034	-0.010	9.363	0.010	0.010	0.000	0.000	0.000	0.000
72	A	92	SER	0	0.020	-0.018	13.174	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	93	VAL	0	-0.004	0.005	13.563	0.000	0.000	0.000	0.000	0.000	0.000
74	A	94	ASP	-1	-0.880	-0.900	15.717	-0.233	-0.233	0.000	0.000	0.000	0.000
75	A	95	SER	0	0.016	0.003	19.264	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	96	VAL	0	0.123	0.043	21.540	0.001	0.001	0.000	0.000	0.000	0.000
77	A	97	TYR	0	-0.014	0.005	23.001	0.008	0.008	0.000	0.000	0.000	0.000
78	A	98	SER	0	0.028	0.009	22.588	0.009	0.009	0.000	0.000	0.000	0.000
79	A	99	HIS	0	0.002	-0.003	17.883	0.018	0.018	0.000	0.000	0.000	0.000
80	A	100	LEU	0	0.016	0.005	23.128	0.006	0.006	0.000	0.000	0.000	0.000
81	A	101	ALA	0	-0.021	-0.016	26.486	0.009	0.009	0.000	0.000	0.000	0.000
82	A	102	TRP	0	0.005	-0.017	19.961	0.003	0.003	0.000	0.000	0.000	0.000
83	A	103	LYS	1	0.853	0.933	23.834	0.172	0.172	0.000	0.000	0.000	0.000
84	A	104	ASN	0	-0.048	-0.019	27.083	0.009	0.009	0.000	0.000	0.000	0.000
85	A	105	MET	0	-0.053	0.009	28.637	0.008	0.008	0.000	0.000	0.000	0.000
86	A	106	PRO	0	0.008	0.004	30.803	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	107	ILE	0	0.060	0.020	29.096	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	108	GLU	-1	-0.823	-0.902	31.115	-0.085	-0.085	0.000	0.000	0.000	0.000
89	A	109	LYS	1	0.789	0.874	32.700	0.083	0.083	0.000	0.000	0.000	0.000
90	A	110	GLY	0	0.028	0.025	28.614	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	111	GLY	0	0.000	-0.002	26.937	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	112	ILE	0	-0.063	-0.035	22.372	0.000	0.000	0.000	0.000	0.000	0.000
93	A	113	GLY	0	0.044	0.029	26.212	0.001	0.001	0.000	0.000	0.000	0.000
94	A	114	ASN	0	0.011	-0.013	26.789	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	115	VAL	0	-0.012	0.003	22.066	0.004	0.004	0.000	0.000	0.000	0.000
96	A	116	GLU	-1	-0.898	-0.974	24.681	-0.128	-0.128	0.000	0.000	0.000	0.000
97	A	117	PHE	0	-0.015	-0.024	17.301	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	118	THR	0	-0.005	0.003	18.014	0.014	0.014	0.000	0.000	0.000	0.000
99	A	119	LEU	0	-0.039	-0.003	17.481	-0.029	-0.029	0.000	0.000	0.000	0.000
100	A	120	VAL	0	0.037	0.000	13.657	0.019	0.019	0.000	0.000	0.000	0.000
101	A	121	SER	0	-0.014	-0.014	15.832	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	122	ASP	-1	-0.776	-0.875	11.341	-0.548	-0.548	0.000	0.000	0.000	0.000
103	A	123	ILE	0	0.017	0.008	14.527	0.002	0.002	0.000	0.000	0.000	0.000
104	A	124	ASN	0	-0.036	-0.034	14.449	-0.013	-0.013	0.000	0.000	0.000	0.000
105	A	125	LYS	1	0.914	0.971	12.525	0.302	0.302	0.000	0.000	0.000	0.000
106	A	126	ASP	-1	-0.783	-0.862	10.616	-0.625	-0.625	0.000	0.000	0.000	0.000
107	A	127	ILE	0	0.001	0.004	7.745	-0.130	-0.130	0.000	0.000	0.000	0.000
108	A	128	SER	0	0.000	-0.050	6.670	-0.204	-0.204	0.000	0.000	0.000	0.000
109	A	129	LYS	1	0.795	0.893	6.404	0.453	0.453	0.000	0.000	0.000	0.000
110	A	130	ASN	0	-0.040	-0.011	5.239	-0.180	-0.096	-0.001	-0.009	-0.074	0.000
111	A	131	TYR	0	-0.042	-0.037	2.133	-3.381	-1.970	3.686	-2.193	-2.905	-0.014
112	A	132	ASN	0	-0.074	-0.034	1.889	0.715	-0.145	3.328	0.208	-2.676	-0.008
113	A	133	VAL	0	0.008	0.003	4.565	0.077	0.152	-0.001	-0.006	-0.068	0.000
114	A	134	LEU	0	-0.028	0.004	7.310	0.115	0.115	0.000	0.000	0.000	0.000
115	A	135	TYR	0	-0.030	-0.021	10.023	0.011	0.011	0.000	0.000	0.000	0.000
116	A	136	ASP	-1	-0.826	-0.915	13.138	-0.185	-0.185	0.000	0.000	0.000	0.000
117	A	137	ASN	0	-0.074	-0.048	13.649	-0.016	-0.016	0.000	0.000	0.000	0.000
118	A	138	SER	0	-0.032	-0.003	14.987	0.015	0.015	0.000	0.000	0.000	0.000
119	A	139	PHE	0	0.014	-0.015	14.999	0.002	0.002	0.000	0.000	0.000	0.000
120	A	140	ALA	0	0.022	0.022	10.903	-0.022	-0.022	0.000	0.000	0.000	0.000
121	A	141	LEU	0	0.042	0.010	9.327	0.058	0.058	0.000	0.000	0.000	0.000
122	A	142	ARG	1	0.786	0.877	10.953	0.194	0.194	0.000	0.000	0.000	0.000
123	A	143	GLY	0	0.004	0.004	7.701	0.011	0.011	0.000	0.000	0.000	0.000
124	A	144	LEU	0	-0.064	-0.034	8.060	0.071	0.071	0.000	0.000	0.000	0.000
125	A	145	PHE	0	0.013	0.002	2.305	-0.986	-0.339	1.599	-0.474	-1.771	0.000
126	A	146	ILE	0	0.005	0.016	7.407	0.130	0.130	0.000	0.000	0.000	0.000
127	A	147	ILE	0	-0.006	0.001	6.619	-0.119	-0.119	0.000	0.000	0.000	0.000
128	A	148	ASP	-1	-0.730	-0.858	9.043	-0.132	-0.132	0.000	0.000	0.000	0.000
129	A	149	LYS	1	0.967	0.981	11.900	0.086	0.086	0.000	0.000	0.000	0.000
130	A	150	ASN	0	0.012	0.017	12.666	0.030	0.030	0.000	0.000	0.000	0.000
131	A	151	GLY	0	0.034	0.029	10.337	0.024	0.024	0.000	0.000	0.000	0.000
132	A	152	CYS	0	-0.065	-0.019	7.557	-0.103	-0.103	0.000	0.000	0.000	0.000
133	A	153	VAL	0	0.039	0.028	2.510	-0.967	0.049	0.437	-0.312	-1.141	0.001
134	A	154	ARG	1	0.788	0.846	5.536	0.327	0.327	0.000	0.000	0.000	0.000
135	A	155	HIS	0	0.012	0.001	6.894	0.240	0.240	0.000	0.000	0.000	0.000
136	A	156	GLN	0	0.048	0.022	2.630	-5.377	-2.625	1.139	-1.586	-2.306	-0.021
137	A	157	THR	0	-0.040	-0.012	6.017	0.296	0.296	0.000	0.000	0.000	0.000
138	A	158	VAL	0	0.002	-0.011	6.901	-0.144	-0.144	0.000	0.000	0.000	0.000
139	A	159	ASN	0	-0.067	-0.028	9.549	0.080	0.080	0.000	0.000	0.000	0.000
140	A	160	ASP	-1	-0.837	-0.933	13.223	-0.173	-0.173	0.000	0.000	0.000	0.000
141	A	161	LEU	0	-0.001	0.007	14.564	-0.014	-0.014	0.000	0.000	0.000	0.000
142	A	162	PRO	0	-0.004	-0.004	16.631	-0.004	-0.004	0.000	0.000	0.000	0.000
143	A	163	ILE	0	-0.028	0.007	18.032	0.014	0.014	0.000	0.000	0.000	0.000
144	A	164	GLY	0	0.014	0.024	17.345	-0.027	-0.027	0.000	0.000	0.000	0.000
145	A	165	ARG	1	0.763	0.828	11.777	0.397	0.397	0.000	0.000	0.000	0.000
146	A	166	ASN	0	0.044	0.024	17.270	0.009	0.009	0.000	0.000	0.000	0.000
147	A	167	VAL	0	0.040	0.013	18.529	-0.006	-0.006	0.000	0.000	0.000	0.000
148	A	168	GLN	0	0.023	0.000	19.541	-0.003	-0.003	0.000	0.000	0.000	0.000
149	A	169	GLU	-1	-0.810	-0.878	17.485	-0.065	-0.065	0.000	0.000	0.000	0.000
150	A	170	VAL	0	0.006	0.018	14.219	0.000	0.000	0.000	0.000	0.000	0.000
151	A	171	LEU	0	-0.017	-0.009	16.141	-0.004	-0.004	0.000	0.000	0.000	0.000
152	A	172	ARG	1	0.883	0.916	18.829	0.071	0.071	0.000	0.000	0.000	0.000
153	A	173	THR	0	-0.020	-0.014	12.505	0.021	0.021	0.000	0.000	0.000	0.000
154	A	174	ILE	0	-0.011	-0.011	14.607	0.006	0.006	0.000	0.000	0.000	0.000
155	A	175	ASP	-1	-0.831	-0.898	15.967	-0.082	-0.082	0.000	0.000	0.000	0.000
156	A	176	SER	0	-0.025	-0.013	16.408	0.023	0.023	0.000	0.000	0.000	0.000
157	A	177	ILE	0	-0.040	-0.015	11.613	0.018	0.018	0.000	0.000	0.000	0.000
158	A	178	ILE	0	0.010	0.002	15.541	0.016	0.016	0.000	0.000	0.000	0.000
159	A	179	HIS	0	-0.010	-0.005	18.293	0.001	0.001	0.000	0.000	0.000	0.000
160	A	180	VAL	0	-0.007	0.014	15.832	0.014	0.014	0.000	0.000	0.000	0.000
161	A	181	ASP	-1	-0.814	-0.854	15.734	-0.066	-0.066	0.000	0.000	0.000	0.000
162	A	182	THR	0	-0.096	-0.058	18.484	0.006	0.006	0.000	0.000	0.000	0.000
163	A	183	SER	0	-0.031	-0.024	21.869	0.009	0.009	0.000	0.000	0.000	0.000
164	A	184	GLY	0	-0.025	-0.010	20.131	0.008	0.008	0.000	0.000	0.000	0.000
165	A	185	GLU	-1	-0.908	-0.938	21.185	0.073	0.073	0.000	0.000	0.000	0.000
166	A	186	VAL	0	-0.024	-0.023	18.085	0.009	0.009	0.000	0.000	0.000	0.000
167	A	187	CYS	0	-0.082	-0.042	18.915	-0.004	-0.004	0.000	0.000	0.000	0.000
168	A	188	PRO	0	0.032	0.032	19.913	-0.008	-0.008	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:21:LEU)