FMO DATABASE

FMODB ID: NN9KQ

Calculation Name: 3CG0-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CG0

Chain ID: A

ChEMBL ID:

UniProt ID: Q311G8

Base Structure: X-ray

Registration Date: 2023-09-21

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-878933.942459
FMO2-HF: Nuclear repulsion	830931.608877
FMO2-HF: Total energy	-48002.333582
FMO2-MP2: Total energy	-48141.0673

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:6:ASP)

Summations of interaction energy for fragment #1(A:6: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.
96.521	97.99	-0.006	-0.575	-0.888	0.003

Interaction energy analysis for fragmet #1(A:6:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.966 / q_NPA : -0.992

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

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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	8	PRO	0	-0.009	0.004	3.859	-1.917	-0.448	-0.006	-0.575	-0.888	0.003
4	A	9	GLY	0	0.045	0.020	6.329	-1.438	-1.438	0.000	0.000	0.000	0.000
5	A	10	VAL	0	-0.044	-0.027	8.494	-1.919	-1.919	0.000	0.000	0.000	0.000
6	A	11	LEU	0	-0.017	0.001	12.141	-0.121	-0.121	0.000	0.000	0.000	0.000
7	A	12	ILE	0	-0.010	-0.014	15.457	-0.445	-0.445	0.000	0.000	0.000	0.000
8	A	13	VAL	0	-0.013	-0.007	18.709	-0.196	-0.196	0.000	0.000	0.000	0.000
9	A	14	GLU	-1	-0.851	-0.939	22.325	11.174	11.174	0.000	0.000	0.000	0.000
10	A	15	ASP	-1	-0.787	-0.856	24.693	9.642	9.642	0.000	0.000	0.000	0.000
11	A	16	GLY	0	0.006	-0.003	27.767	-0.246	-0.246	0.000	0.000	0.000	0.000
12	A	17	ARG	1	0.929	0.945	26.683	-9.478	-9.478	0.000	0.000	0.000	0.000
13	A	18	LEU	0	0.007	0.010	25.761	0.307	0.307	0.000	0.000	0.000	0.000
14	A	19	ALA	0	0.046	0.042	24.826	0.316	0.316	0.000	0.000	0.000	0.000
15	A	20	ALA	0	0.044	0.022	22.154	0.557	0.557	0.000	0.000	0.000	0.000
16	A	21	ALA	0	-0.016	-0.009	20.846	0.672	0.672	0.000	0.000	0.000	0.000
17	A	22	THR	0	-0.059	-0.043	20.651	0.454	0.454	0.000	0.000	0.000	0.000
18	A	23	LEU	0	0.025	0.009	18.784	0.506	0.506	0.000	0.000	0.000	0.000
19	A	24	ARG	1	0.827	0.915	13.756	-17.991	-17.991	0.000	0.000	0.000	0.000
20	A	25	ILE	0	0.024	0.011	15.688	0.889	0.889	0.000	0.000	0.000	0.000
21	A	26	GLN	0	-0.027	-0.013	16.279	0.659	0.659	0.000	0.000	0.000	0.000
22	A	27	LEU	0	0.018	0.005	12.869	0.625	0.625	0.000	0.000	0.000	0.000
23	A	28	GLU	-1	-0.800	-0.889	11.370	20.543	20.543	0.000	0.000	0.000	0.000
24	A	29	SER	0	-0.099	-0.064	11.416	0.857	0.857	0.000	0.000	0.000	0.000
25	A	30	LEU	0	-0.098	-0.047	12.400	-0.026	-0.026	0.000	0.000	0.000	0.000
26	A	31	GLY	0	-0.024	0.004	8.310	0.812	0.812	0.000	0.000	0.000	0.000
27	A	32	TYR	0	-0.037	-0.020	6.986	3.405	3.405	0.000	0.000	0.000	0.000
28	A	33	ASP	-1	-0.870	-0.937	7.073	28.011	28.011	0.000	0.000	0.000	0.000
29	A	34	VAL	0	-0.052	-0.031	8.998	-1.572	-1.572	0.000	0.000	0.000	0.000
30	A	35	LEU	0	0.016	0.019	8.928	-1.150	-1.150	0.000	0.000	0.000	0.000
31	A	36	GLY	0	-0.007	-0.005	12.930	-0.852	-0.852	0.000	0.000	0.000	0.000
32	A	37	VAL	0	-0.036	-0.026	16.700	0.201	0.201	0.000	0.000	0.000	0.000
33	A	38	PHE	0	-0.022	-0.003	18.349	-0.275	-0.275	0.000	0.000	0.000	0.000
34	A	39	ASP	-1	-0.845	-0.911	22.937	10.879	10.879	0.000	0.000	0.000	0.000
35	A	40	ASN	0	-0.020	-0.021	26.067	-0.242	-0.242	0.000	0.000	0.000	0.000
36	A	41	GLY	0	0.088	0.031	25.335	0.472	0.472	0.000	0.000	0.000	0.000
37	A	42	GLU	-1	-0.845	-0.931	25.255	10.324	10.324	0.000	0.000	0.000	0.000
38	A	43	GLU	-1	-0.824	-0.885	24.079	11.719	11.719	0.000	0.000	0.000	0.000
39	A	44	ALA	0	0.034	0.032	21.195	0.522	0.522	0.000	0.000	0.000	0.000
40	A	45	VAL	0	-0.023	-0.028	20.677	0.571	0.571	0.000	0.000	0.000	0.000
41	A	46	ARG	1	0.774	0.847	22.200	-11.325	-11.325	0.000	0.000	0.000	0.000
42	A	47	CYS	0	-0.035	-0.008	18.960	0.095	0.095	0.000	0.000	0.000	0.000
43	A	48	ALA	0	0.029	0.017	16.940	0.871	0.871	0.000	0.000	0.000	0.000
44	A	49	PRO	0	0.011	-0.005	16.159	1.035	1.035	0.000	0.000	0.000	0.000
45	A	50	ASP	-1	-0.924	-0.960	16.194	16.069	16.069	0.000	0.000	0.000	0.000
46	A	51	LEU	0	-0.065	-0.021	13.764	1.207	1.207	0.000	0.000	0.000	0.000
47	A	52	ARG	1	0.815	0.907	10.455	-21.839	-21.839	0.000	0.000	0.000	0.000
48	A	53	PRO	0	-0.007	-0.003	10.655	1.682	1.682	0.000	0.000	0.000	0.000
49	A	54	ASP	-1	-0.852	-0.908	7.678	29.760	29.760	0.000	0.000	0.000	0.000
50	A	55	ILE	0	-0.075	-0.044	11.062	-1.504	-1.504	0.000	0.000	0.000	0.000
51	A	56	ALA	0	0.010	0.005	14.056	0.317	0.317	0.000	0.000	0.000	0.000
52	A	57	LEU	0	-0.015	-0.004	16.899	-0.608	-0.608	0.000	0.000	0.000	0.000
53	A	58	VAL	0	0.014	-0.007	19.343	-0.053	-0.053	0.000	0.000	0.000	0.000
54	A	59	ASP	-1	-0.832	-0.909	22.844	10.237	10.237	0.000	0.000	0.000	0.000
55	A	60	ILE	0	-0.028	-0.022	26.092	-0.169	-0.169	0.000	0.000	0.000	0.000
56	A	61	MET	0	-0.106	-0.037	29.040	-0.467	-0.467	0.000	0.000	0.000	0.000
57	A	62	LEU	0	0.028	0.015	26.614	-0.153	-0.153	0.000	0.000	0.000	0.000
58	A	63	CYS	0	-0.077	-0.054	29.995	-0.499	-0.499	0.000	0.000	0.000	0.000
59	A	64	GLY	0	0.053	0.014	30.606	0.317	0.317	0.000	0.000	0.000	0.000
60	A	65	ALA	0	-0.082	-0.047	32.383	-0.298	-0.298	0.000	0.000	0.000	0.000
61	A	66	LEU	0	-0.057	-0.017	28.035	-0.160	-0.160	0.000	0.000	0.000	0.000
62	A	67	ASP	-1	-0.766	-0.876	30.786	9.649	9.649	0.000	0.000	0.000	0.000
63	A	68	GLY	0	0.046	0.035	27.422	0.324	0.324	0.000	0.000	0.000	0.000
64	A	69	VAL	0	-0.035	-0.033	26.852	0.432	0.432	0.000	0.000	0.000	0.000
65	A	70	GLU	-1	-0.810	-0.892	28.045	9.984	9.984	0.000	0.000	0.000	0.000
66	A	71	THR	0	-0.040	-0.032	23.857	0.266	0.266	0.000	0.000	0.000	0.000
67	A	72	ALA	0	0.003	0.005	23.377	0.468	0.468	0.000	0.000	0.000	0.000
68	A	73	ALA	0	-0.006	0.001	23.660	0.397	0.397	0.000	0.000	0.000	0.000
69	A	74	ARG	1	0.816	0.882	25.251	-9.850	-9.850	0.000	0.000	0.000	0.000
70	A	75	LEU	0	0.014	0.013	19.305	0.267	0.267	0.000	0.000	0.000	0.000
71	A	76	ALA	0	0.008	0.009	20.393	0.531	0.531	0.000	0.000	0.000	0.000
72	A	77	ALA	0	-0.063	-0.035	21.644	0.250	0.250	0.000	0.000	0.000	0.000
73	A	78	GLY	0	-0.025	-0.011	22.929	-0.015	-0.015	0.000	0.000	0.000	0.000
74	A	79	CYS	0	-0.080	-0.047	17.489	0.174	0.174	0.000	0.000	0.000	0.000
75	A	80	ASN	0	-0.025	0.001	16.946	0.267	0.267	0.000	0.000	0.000	0.000
76	A	81	LEU	0	0.028	0.024	14.982	0.625	0.625	0.000	0.000	0.000	0.000
77	A	82	PRO	0	-0.016	-0.003	15.333	-1.085	-1.085	0.000	0.000	0.000	0.000
78	A	83	ILE	0	-0.018	-0.017	17.527	0.385	0.385	0.000	0.000	0.000	0.000
79	A	84	ILE	0	-0.023	-0.008	17.809	-0.308	-0.308	0.000	0.000	0.000	0.000
80	A	85	PHE	0	-0.025	-0.014	21.157	0.057	0.057	0.000	0.000	0.000	0.000
81	A	86	ILE	0	-0.013	0.006	21.656	0.063	0.063	0.000	0.000	0.000	0.000
82	A	87	THR	0	0.030	-0.005	25.078	-0.336	-0.336	0.000	0.000	0.000	0.000
83	A	88	SER	0	-0.019	-0.004	28.825	0.024	0.024	0.000	0.000	0.000	0.000
84	A	89	SER	0	0.053	0.029	31.631	0.019	0.019	0.000	0.000	0.000	0.000
85	A	90	GLN	0	-0.042	-0.011	33.553	-0.132	-0.132	0.000	0.000	0.000	0.000
86	A	91	ASP	-1	-0.832	-0.923	36.180	8.149	8.149	0.000	0.000	0.000	0.000
87	A	92	VAL	0	0.027	-0.004	38.959	-0.142	-0.142	0.000	0.000	0.000	0.000
88	A	93	GLU	-1	-0.898	-0.956	41.270	7.257	7.257	0.000	0.000	0.000	0.000
89	A	94	THR	0	-0.055	-0.031	39.205	-0.079	-0.079	0.000	0.000	0.000	0.000
90	A	95	PHE	0	0.031	0.015	40.917	-0.152	-0.152	0.000	0.000	0.000	0.000
91	A	96	GLN	0	-0.052	-0.011	44.780	-0.349	-0.349	0.000	0.000	0.000	0.000
92	A	97	ARG	1	0.930	0.963	39.722	-7.643	-7.643	0.000	0.000	0.000	0.000
93	A	98	ALA	0	0.031	0.015	44.358	-0.121	-0.121	0.000	0.000	0.000	0.000
94	A	99	LYS	1	0.908	0.944	46.301	-6.294	-6.294	0.000	0.000	0.000	0.000
95	A	100	ARG	1	0.938	0.970	48.916	-6.424	-6.424	0.000	0.000	0.000	0.000
96	A	101	VAL	0	-0.012	0.000	46.819	-0.087	-0.087	0.000	0.000	0.000	0.000
97	A	102	ASN	0	-0.071	-0.024	50.249	-0.115	-0.115	0.000	0.000	0.000	0.000
98	A	103	PRO	0	0.008	0.017	48.053	-0.071	-0.071	0.000	0.000	0.000	0.000
99	A	104	PHE	0	0.003	-0.010	50.812	-0.058	-0.058	0.000	0.000	0.000	0.000
100	A	105	GLY	0	0.020	0.010	49.981	-0.083	-0.083	0.000	0.000	0.000	0.000
101	A	106	TYR	0	-0.026	-0.021	44.555	0.125	0.125	0.000	0.000	0.000	0.000
102	A	107	LEU	0	-0.009	-0.008	44.201	-0.089	-0.089	0.000	0.000	0.000	0.000
103	A	108	ALA	0	0.012	0.016	40.263	0.124	0.124	0.000	0.000	0.000	0.000
104	A	109	LYS	1	0.796	0.903	32.559	-9.307	-9.307	0.000	0.000	0.000	0.000
105	A	110	PRO	0	0.044	0.027	36.970	0.053	0.053	0.000	0.000	0.000	0.000
106	A	111	VAL	0	0.005	-0.012	38.745	-0.159	-0.159	0.000	0.000	0.000	0.000
107	A	112	ALA	0	0.038	0.030	42.265	0.017	0.017	0.000	0.000	0.000	0.000
108	A	113	ALA	0	0.052	0.009	44.738	-0.114	-0.114	0.000	0.000	0.000	0.000
109	A	114	ASP	-1	-0.774	-0.875	46.377	6.213	6.213	0.000	0.000	0.000	0.000
110	A	115	THR	0	-0.013	-0.018	47.555	-0.170	-0.170	0.000	0.000	0.000	0.000
111	A	116	LEU	0	-0.001	0.015	44.355	-0.068	-0.068	0.000	0.000	0.000	0.000
112	A	117	HIS	0	-0.047	-0.021	47.921	0.030	0.030	0.000	0.000	0.000	0.000
113	A	118	ARG	1	0.890	0.927	51.048	-6.022	-6.022	0.000	0.000	0.000	0.000
114	A	119	SER	0	-0.032	-0.029	49.701	-0.097	-0.097	0.000	0.000	0.000	0.000
115	A	120	ILE	0	-0.004	0.000	47.801	-0.062	-0.062	0.000	0.000	0.000	0.000
116	A	121	GLU	-1	-0.854	-0.924	52.033	5.480	5.480	0.000	0.000	0.000	0.000
117	A	122	MET	0	-0.001	0.000	54.916	-0.147	-0.147	0.000	0.000	0.000	0.000
118	A	123	ALA	0	-0.003	0.012	53.067	-0.087	-0.087	0.000	0.000	0.000	0.000
119	A	124	ILE	0	-0.023	-0.016	53.587	-0.081	-0.081	0.000	0.000	0.000	0.000
120	A	125	HIS	0	-0.051	-0.057	56.707	-0.153	-0.153	0.000	0.000	0.000	0.000
121	A	126	LYS	1	0.841	0.906	57.367	-5.497	-5.497	0.000	0.000	0.000	0.000
122	A	127	LYS	1	0.916	0.945	56.769	-5.467	-5.467	0.000	0.000	0.000	0.000
123	A	128	LYS	1	0.875	0.941	59.149	-5.243	-5.243	0.000	0.000	0.000	0.000
124	A	129	LEU	0	-0.018	0.007	62.268	-0.078	-0.078	0.000	0.000	0.000	0.000
125	A	130	GLU	-1	-0.822	-0.864	59.698	5.223	5.223	0.000	0.000	0.000	0.000
126	A	131	GLU	-1	-0.995	-0.995	61.020	5.089	5.089	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ASP)