FMO DATABASE

FMODB ID: N186Q

Calculation Name: 2CO4-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CO4

Chain ID: A

ChEMBL ID:

UniProt ID: Q8ZRK4

Base Structure: X-ray

Registration Date: 2023-03-13

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	123
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-917334.437269
FMO2-HF: Nuclear repulsion	872360.29252
FMO2-HF: Total energy	-44974.144749
FMO2-MP2: Total energy	-45107.593449

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:ASP)

Summations of interaction energy for fragment #1(A:22: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.
-28.094	-22.692	3.63	-4.093	-4.938	0.007

Interaction energy analysis for fragmet #1(A:22:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.910 / q_NPA : -0.957

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	THR	0	-0.007	-0.001	3.576	1.685	5.457	0.054	-1.828	-1.998	0.007
4	A	25	VAL	0	0.031	0.011	5.755	-5.621	-5.622	-0.001	-0.002	0.004	0.000
5	A	26	SER	0	-0.052	-0.022	8.809	-0.983	-0.983	0.000	0.000	0.000	0.000
6	A	27	LEU	0	0.016	0.006	12.142	-0.617	-0.617	0.000	0.000	0.000	0.000
7	A	28	ILE	0	-0.019	-0.014	15.329	-0.448	-0.448	0.000	0.000	0.000	0.000
8	A	29	PRO	0	0.010	0.006	18.429	-0.566	-0.566	0.000	0.000	0.000	0.000
9	A	30	VAL	0	-0.019	0.004	21.896	-0.040	-0.040	0.000	0.000	0.000	0.000
10	A	31	SER	0	0.013	0.009	24.759	-0.224	-0.224	0.000	0.000	0.000	0.000
11	A	32	GLY	0	-0.013	-0.020	27.398	-0.167	-0.167	0.000	0.000	0.000	0.000
12	A	33	LEU	0	0.000	0.012	26.861	-0.382	-0.382	0.000	0.000	0.000	0.000
13	A	34	LYS	1	0.921	0.956	31.188	-8.856	-8.856	0.000	0.000	0.000	0.000
14	A	35	ALA	0	0.024	0.020	34.728	0.054	0.054	0.000	0.000	0.000	0.000
15	A	36	GLY	0	0.024	0.018	36.312	-0.177	-0.177	0.000	0.000	0.000	0.000
16	A	37	LYS	1	0.920	0.960	37.276	-7.600	-7.600	0.000	0.000	0.000	0.000
17	A	38	ASN	0	-0.028	-0.017	33.401	0.216	0.216	0.000	0.000	0.000	0.000
18	A	39	ALA	0	0.005	0.000	34.234	-0.175	-0.175	0.000	0.000	0.000	0.000
19	A	40	PRO	0	0.019	-0.012	33.749	0.198	0.198	0.000	0.000	0.000	0.000
20	A	41	SER	0	-0.004	0.006	29.388	0.116	0.116	0.000	0.000	0.000	0.000
21	A	42	ALA	0	-0.008	0.014	29.461	0.261	0.261	0.000	0.000	0.000	0.000
22	A	43	LYS	1	0.892	0.929	24.747	-12.221	-12.221	0.000	0.000	0.000	0.000
23	A	44	ILE	0	-0.001	-0.016	23.906	-0.277	-0.277	0.000	0.000	0.000	0.000
24	A	45	ALA	0	0.011	0.008	19.926	0.154	0.154	0.000	0.000	0.000	0.000
25	A	46	LYS	1	0.836	0.934	18.021	-15.581	-15.581	0.000	0.000	0.000	0.000
26	A	47	LEU	0	0.016	0.019	12.492	0.457	0.457	0.000	0.000	0.000	0.000
27	A	48	VAL	0	-0.011	-0.018	12.467	-0.904	-0.904	0.000	0.000	0.000	0.000
28	A	49	VAL	0	0.045	0.035	8.090	1.816	1.816	0.000	0.000	0.000	0.000
29	A	50	ASN	0	0.019	0.007	8.598	-3.718	-3.718	0.000	0.000	0.000	0.000
30	A	51	SER	0	0.023	-0.011	3.083	4.575	5.212	0.006	-0.359	-0.284	0.001
31	A	52	THR	0	0.006	0.009	4.728	-3.565	-3.392	-0.001	-0.013	-0.159	0.000
32	A	53	THR	0	-0.036	-0.018	1.950	-7.396	-7.076	3.149	-1.673	-1.796	0.000
33	A	54	LEU	0	-0.017	0.000	2.749	-4.171	-3.670	0.423	-0.218	-0.705	-0.001
34	A	55	LYS	1	0.975	0.969	5.550	-22.152	-22.152	0.000	0.000	0.000	0.000
35	A	56	GLU	-1	-0.793	-0.881	8.758	17.754	17.754	0.000	0.000	0.000	0.000
36	A	57	PHE	0	-0.032	-0.015	8.128	2.930	2.930	0.000	0.000	0.000	0.000
37	A	58	GLY	0	0.050	0.037	9.519	-2.335	-2.335	0.000	0.000	0.000	0.000
38	A	59	VAL	0	-0.049	-0.041	11.165	1.668	1.668	0.000	0.000	0.000	0.000
39	A	60	ARG	1	0.810	0.930	13.786	-16.366	-16.366	0.000	0.000	0.000	0.000
40	A	61	GLY	0	0.001	-0.008	16.207	0.823	0.823	0.000	0.000	0.000	0.000
41	A	62	ILE	0	-0.030	-0.006	16.321	-0.539	-0.539	0.000	0.000	0.000	0.000
42	A	63	SER	0	-0.047	-0.054	19.457	-0.149	-0.149	0.000	0.000	0.000	0.000
43	A	64	ASN	0	0.009	0.003	22.965	0.269	0.269	0.000	0.000	0.000	0.000
44	A	65	ASN	0	-0.062	-0.039	25.890	-0.409	-0.409	0.000	0.000	0.000	0.000
45	A	66	VAL	0	0.031	0.019	22.304	0.109	0.109	0.000	0.000	0.000	0.000
46	A	67	VAL	0	-0.018	-0.018	25.419	-0.338	-0.338	0.000	0.000	0.000	0.000
47	A	68	ASP	-1	-0.794	-0.884	24.045	12.128	12.128	0.000	0.000	0.000	0.000
48	A	69	SER	0	-0.002	-0.008	24.697	0.444	0.444	0.000	0.000	0.000	0.000
49	A	70	THR	0	0.025	-0.001	20.647	0.089	0.089	0.000	0.000	0.000	0.000
50	A	71	GLY	0	0.023	0.013	19.742	0.761	0.761	0.000	0.000	0.000	0.000
51	A	72	THR	0	-0.008	-0.004	19.255	0.706	0.706	0.000	0.000	0.000	0.000
52	A	73	ALA	0	-0.019	-0.015	21.393	-0.096	-0.096	0.000	0.000	0.000	0.000
53	A	74	TRP	0	-0.018	0.006	19.884	0.048	0.048	0.000	0.000	0.000	0.000
54	A	75	ARG	1	0.848	0.920	25.381	-9.946	-9.946	0.000	0.000	0.000	0.000
55	A	76	VAL	0	0.012	0.017	23.764	0.284	0.284	0.000	0.000	0.000	0.000
56	A	77	ALA	0	0.031	0.011	26.998	-0.387	-0.387	0.000	0.000	0.000	0.000
57	A	78	GLY	0	-0.032	-0.018	28.520	0.379	0.379	0.000	0.000	0.000	0.000
58	A	79	LYS	1	0.938	0.947	24.504	-12.389	-12.389	0.000	0.000	0.000	0.000
59	A	80	ASN	0	-0.059	-0.044	30.553	-0.253	-0.253	0.000	0.000	0.000	0.000
60	A	81	THR	0	-0.071	-0.059	34.081	-0.320	-0.320	0.000	0.000	0.000	0.000
61	A	82	GLY	0	0.027	0.028	33.060	-0.228	-0.228	0.000	0.000	0.000	0.000
62	A	83	LYS	1	0.896	0.949	34.033	-8.173	-8.173	0.000	0.000	0.000	0.000
63	A	84	GLU	-1	-0.759	-0.861	30.876	10.149	10.149	0.000	0.000	0.000	0.000
64	A	85	ILE	0	-0.059	-0.015	28.026	-0.305	-0.305	0.000	0.000	0.000	0.000
65	A	86	GLY	0	-0.013	-0.009	28.967	0.270	0.270	0.000	0.000	0.000	0.000
66	A	87	VAL	0	0.005	0.002	24.021	-0.101	-0.101	0.000	0.000	0.000	0.000
67	A	88	GLY	0	0.077	0.025	23.000	-0.044	-0.044	0.000	0.000	0.000	0.000
68	A	89	LEU	0	-0.009	0.017	17.970	-0.029	-0.029	0.000	0.000	0.000	0.000
69	A	90	SER	0	-0.033	-0.018	22.108	-0.687	-0.687	0.000	0.000	0.000	0.000
70	A	91	SER	0	0.044	-0.001	24.020	0.167	0.167	0.000	0.000	0.000	0.000
71	A	92	ASP	-1	-0.870	-0.916	25.526	11.154	11.154	0.000	0.000	0.000	0.000
72	A	93	SER	0	-0.002	-0.008	20.190	0.471	0.471	0.000	0.000	0.000	0.000
73	A	94	LEU	0	0.013	0.001	20.745	0.400	0.400	0.000	0.000	0.000	0.000
74	A	95	ARG	1	0.850	0.900	22.156	-10.702	-10.702	0.000	0.000	0.000	0.000
75	A	96	ARG	1	0.801	0.889	18.383	-15.914	-15.914	0.000	0.000	0.000	0.000
76	A	97	SER	0	-0.050	-0.002	18.121	0.379	0.379	0.000	0.000	0.000	0.000
77	A	98	ASP	-1	-0.824	-0.914	16.219	16.251	16.251	0.000	0.000	0.000	0.000
78	A	99	SER	0	-0.048	-0.036	17.667	-0.647	-0.647	0.000	0.000	0.000	0.000
79	A	100	THR	0	-0.046	-0.027	18.161	0.386	0.386	0.000	0.000	0.000	0.000
80	A	101	GLU	-1	-0.784	-0.853	15.443	14.799	14.799	0.000	0.000	0.000	0.000
81	A	102	LYS	1	0.899	0.930	17.958	-12.237	-12.237	0.000	0.000	0.000	0.000
82	A	103	TRP	0	0.027	0.025	11.407	0.363	0.363	0.000	0.000	0.000	0.000
83	A	104	ASN	0	-0.004	-0.018	16.643	-0.445	-0.445	0.000	0.000	0.000	0.000
84	A	105	GLY	0	0.010	0.003	19.581	-0.404	-0.404	0.000	0.000	0.000	0.000
85	A	106	VAL	0	-0.025	0.000	18.203	-0.533	-0.533	0.000	0.000	0.000	0.000
86	A	107	ASN	0	-0.053	-0.036	18.379	0.489	0.489	0.000	0.000	0.000	0.000
87	A	108	TRP	0	0.038	0.017	13.338	0.283	0.283	0.000	0.000	0.000	0.000
88	A	109	MET	0	-0.011	0.004	16.631	-0.224	-0.224	0.000	0.000	0.000	0.000
89	A	110	THR	0	-0.004	-0.016	13.281	0.674	0.674	0.000	0.000	0.000	0.000
90	A	111	PHE	0	-0.006	-0.003	13.139	-1.622	-1.622	0.000	0.000	0.000	0.000
91	A	112	ASN	0	-0.008	0.000	12.395	1.877	1.877	0.000	0.000	0.000	0.000
92	A	113	SER	0	-0.049	-0.032	7.509	0.162	0.162	0.000	0.000	0.000	0.000
93	A	114	ASN	0	-0.076	-0.041	8.834	0.313	0.313	0.000	0.000	0.000	0.000
94	A	115	ASP	-1	-0.741	-0.827	11.660	15.523	15.523	0.000	0.000	0.000	0.000
95	A	116	THR	0	-0.087	-0.051	13.994	0.750	0.750	0.000	0.000	0.000	0.000
96	A	117	LEU	0	0.022	0.012	15.611	-0.921	-0.921	0.000	0.000	0.000	0.000
97	A	118	ASP	-1	-0.854	-0.927	18.400	14.033	14.033	0.000	0.000	0.000	0.000
98	A	119	ILE	0	0.017	0.019	18.107	-0.160	-0.160	0.000	0.000	0.000	0.000
99	A	120	VAL	0	-0.005	-0.015	22.162	-0.301	-0.301	0.000	0.000	0.000	0.000
100	A	121	LEU	0	-0.001	0.006	25.952	0.076	0.076	0.000	0.000	0.000	0.000
101	A	122	THR	0	-0.009	-0.005	26.901	-0.317	-0.317	0.000	0.000	0.000	0.000
102	A	123	GLY	0	0.025	0.018	29.621	-0.258	-0.258	0.000	0.000	0.000	0.000
103	A	124	PRO	0	0.007	-0.009	32.983	0.023	0.023	0.000	0.000	0.000	0.000
104	A	125	ALA	0	-0.013	-0.005	35.154	0.126	0.126	0.000	0.000	0.000	0.000
105	A	126	GLN	0	0.016	0.010	30.631	-0.230	-0.230	0.000	0.000	0.000	0.000
106	A	127	ASN	0	-0.036	-0.031	35.858	0.087	0.087	0.000	0.000	0.000	0.000
107	A	128	VAL	0	0.042	0.038	32.200	-0.017	-0.017	0.000	0.000	0.000	0.000
108	A	129	THR	0	0.004	-0.001	35.396	-0.250	-0.250	0.000	0.000	0.000	0.000
109	A	130	ALA	0	0.035	0.016	34.475	0.290	0.290	0.000	0.000	0.000	0.000
110	A	131	ASP	-1	-0.684	-0.803	32.087	9.587	9.587	0.000	0.000	0.000	0.000
111	A	132	THR	0	-0.061	-0.027	26.572	0.253	0.253	0.000	0.000	0.000	0.000
112	A	133	TYR	0	-0.005	-0.022	26.997	-0.184	-0.184	0.000	0.000	0.000	0.000
113	A	134	PRO	0	-0.043	-0.002	22.649	0.366	0.366	0.000	0.000	0.000	0.000
114	A	135	ILE	0	0.020	-0.004	19.112	-0.355	-0.355	0.000	0.000	0.000	0.000
115	A	136	THR	0	-0.013	-0.004	16.259	0.312	0.312	0.000	0.000	0.000	0.000
116	A	137	LEU	0	-0.026	-0.013	14.238	-0.844	-0.844	0.000	0.000	0.000	0.000
117	A	138	ASP	-1	-0.848	-0.908	12.144	21.254	21.254	0.000	0.000	0.000	0.000
118	A	139	VAL	0	-0.037	-0.042	8.158	-1.138	-1.138	0.000	0.000	0.000	0.000
119	A	140	VAL	0	-0.024	-0.003	7.406	2.252	2.252	0.000	0.000	0.000	0.000
120	A	141	GLY	0	0.008	0.004	5.237	-0.777	-0.777	0.000	0.000	0.000	0.000
121	A	142	TYR	0	-0.042	-0.040	6.157	-1.230	-1.230	0.000	0.000	0.000	0.000
122	A	143	GLN	0	0.013	-0.009	7.366	0.454	0.454	0.000	0.000	0.000	0.000
123	A	144	PRO	0	-0.024	0.018	10.534	-1.346	-1.346	0.000	0.000	0.000	0.000

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