FMO DATABASE

FMODB ID: 59L3Z

Calculation Name: 3G7G-A-Xray312

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3G7G

Chain ID: A

ChEMBL ID:

UniProt ID: Q97DZ9

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	152
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1435285.292077
FMO2-HF: Nuclear repulsion	1374982.622913
FMO2-HF: Total energy	-60302.669164
FMO2-MP2: Total energy	-60477.731378

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:7:ACE )

Summations of interaction energy for fragment #1(A:7:ACE )

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.
1.358	1.982	-0.005	-0.294	-0.325	0

Interaction energy analysis for fragmet #1(A:7:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.020 / q_NPA : -0.022

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].
3	A	9	MET	0	-0.034	-0.002	3.858	1.426	2.033	-0.005	-0.290	-0.312
4	A	10	ASN	0	0.020	0.012	4.710	-0.048	-0.031	0.000	-0.004	-0.013
5	A	11	TYR	0	-0.018	-0.017	8.489	0.055	0.055	0.000	0.000	0.000
6	A	12	GLU	-1	-0.863	-0.928	12.256	0.000	0.000	0.000	0.000	0.000
7	A	13	GLU	-1	-0.969	-0.984	15.370	-0.114	-0.114	0.000	0.000	0.000
8	A	14	VAL	0	-0.048	-0.015	18.743	0.020	0.020	0.000	0.000	0.000
9	A	15	PHE	0	-0.017	-0.029	21.192	0.012	0.012	0.000	0.000	0.000
10	A	16	SER	0	0.004	0.004	24.050	-0.015	-0.015	0.000	0.000	0.000
11	A	17	ILE	0	-0.042	-0.028	26.633	0.009	0.009	0.000	0.000	0.000
12	A	18	THR	0	-0.036	-0.001	29.903	-0.007	-0.007	0.000	0.000	0.000
13	A	19	ILE	0	-0.010	-0.010	31.985	0.005	0.005	0.000	0.000	0.000
14	A	20	THR	0	0.027	0.024	34.983	-0.001	-0.001	0.000	0.000	0.000
15	A	21	VAL	0	-0.025	-0.021	36.888	0.001	0.001	0.000	0.000	0.000
16	A	22	ASP	-1	-0.843	-0.910	39.699	-0.034	-0.034	0.000	0.000	0.000
17	A	23	LYS	1	0.897	0.942	42.133	0.032	0.032	0.000	0.000	0.000
18	A	24	PRO	0	0.003	-0.015	41.554	0.001	0.001	0.000	0.000	0.000
19	A	25	ILE	0	-0.034	-0.004	43.316	0.002	0.002	0.000	0.000	0.000
20	A	26	LEU	0	-0.025	-0.023	44.354	-0.002	-0.002	0.000	0.000	0.000
21	A	27	ILE	0	-0.050	-0.010	43.922	0.002	0.002	0.000	0.000	0.000
22	A	28	GLY	0	0.012	-0.006	45.199	0.002	0.002	0.000	0.000	0.000
23	A	29	GLN	0	0.024	0.008	44.351	-0.003	-0.003	0.000	0.000	0.000
24	A	30	ASP	-1	-0.833	-0.900	44.662	-0.044	-0.044	0.000	0.000	0.000
25	A	31	ASP	-1	-0.862	-0.938	44.105	-0.051	-0.051	0.000	0.000	0.000
26	A	32	ILE	0	-0.055	-0.019	42.086	-0.002	-0.002	0.000	0.000	0.000
27	A	33	VAL	0	-0.091	-0.054	40.438	-0.004	-0.004	0.000	0.000	0.000
28	A	34	GLY	0	0.054	0.036	39.562	-0.004	-0.004	0.000	0.000	0.000
29	A	35	ARG	1	0.915	0.948	40.523	0.052	0.052	0.000	0.000	0.000
30	A	36	ARG	1	0.921	0.973	36.705	0.052	0.052	0.000	0.000	0.000
31	A	37	GLN	0	0.005	-0.020	38.547	0.005	0.005	0.000	0.000	0.000
32	A	38	LEU	0	-0.017	-0.006	39.712	-0.003	-0.003	0.000	0.000	0.000
33	A	39	ILE	0	0.019	0.014	37.759	0.002	0.002	0.000	0.000	0.000
34	A	40	PRO	0	0.043	0.019	38.937	-0.001	-0.001	0.000	0.000	0.000
35	A	41	ILE	0	-0.019	-0.001	35.043	-0.002	-0.002	0.000	0.000	0.000
36	A	42	ILE	0	-0.009	-0.001	39.041	0.003	0.003	0.000	0.000	0.000
37	A	43	SER	0	-0.044	-0.027	39.458	0.003	0.003	0.000	0.000	0.000
38	A	44	GLY	0	0.098	0.026	35.462	-0.004	-0.004	0.000	0.000	0.000
39	A	45	LYS	1	0.913	0.974	33.708	0.038	0.038	0.000	0.000	0.000
40	A	46	VAL	0	-0.002	0.003	29.267	-0.005	-0.005	0.000	0.000	0.000
41	A	47	SER	0	-0.051	-0.026	29.324	0.005	0.005	0.000	0.000	0.000
42	A	48	GLY	0	0.144	0.063	25.897	-0.009	-0.009	0.000	0.000	0.000
43	A	49	ASN	0	-0.028	-0.008	23.802	0.011	0.011	0.000	0.000	0.000
44	A	50	ASN	0	-0.018	-0.006	25.433	0.001	0.001	0.000	0.000	0.000
45	A	51	PHE	0	0.018	0.004	26.153	0.002	0.002	0.000	0.000	0.000
46	A	52	ASN	0	0.028	0.005	28.349	-0.010	-0.010	0.000	0.000	0.000
47	A	53	GLY	0	0.051	0.019	31.675	0.004	0.004	0.000	0.000	0.000
48	A	54	LYS	1	0.883	0.957	34.231	0.021	0.021	0.000	0.000	0.000
49	A	55	VAL	0	0.025	0.018	33.873	0.000	0.000	0.000	0.000	0.000
50	A	56	LEU	0	-0.089	-0.044	36.167	0.003	0.003	0.000	0.000	0.000
51	A	57	PRO	0	0.021	-0.005	38.877	-0.002	-0.002	0.000	0.000	0.000
52	A	58	GLY	0	0.012	0.001	40.315	0.000	0.000	0.000	0.000	0.000
53	A	59	GLY	0	-0.005	0.012	37.574	-0.001	-0.001	0.000	0.000	0.000
54	A	60	ILE	0	-0.010	-0.001	37.308	0.001	0.001	0.000	0.000	0.000
55	A	61	ASP	-1	-0.793	-0.916	33.474	-0.073	-0.073	0.000	0.000	0.000
56	A	62	SER	0	-0.024	-0.012	35.580	0.002	0.002	0.000	0.000	0.000
57	A	63	GLN	0	-0.054	-0.038	34.396	-0.003	-0.003	0.000	0.000	0.000
58	A	64	ILE	0	-0.019	-0.018	35.335	0.005	0.005	0.000	0.000	0.000
59	A	65	VAL	0	-0.002	0.007	35.474	-0.006	-0.006	0.000	0.000	0.000
60	A	66	ARG	1	0.842	0.917	34.470	0.075	0.075	0.000	0.000	0.000
61	A	67	PRO	0	0.022	0.013	37.234	-0.001	-0.001	0.000	0.000	0.000
62	A	68	ASP	-1	-0.896	-0.957	33.631	-0.088	-0.088	0.000	0.000	0.000
63	A	69	GLY	0	0.041	0.025	35.692	-0.003	-0.003	0.000	0.000	0.000
64	A	70	LYS	1	0.910	0.973	28.651	0.108	0.108	0.000	0.000	0.000
65	A	71	CYS	0	-0.038	-0.011	32.314	0.008	0.008	0.000	0.000	0.000
66	A	72	GLU	-1	-0.911	-0.957	30.803	-0.092	-0.092	0.000	0.000	0.000
67	A	73	LEU	0	-0.071	-0.046	29.731	0.007	0.007	0.000	0.000	0.000
68	A	74	SER	0	0.015	-0.019	30.190	-0.004	-0.004	0.000	0.000	0.000
69	A	75	ALA	0	0.009	0.019	31.149	0.006	0.006	0.000	0.000	0.000
70	A	76	ARG	1	0.913	0.960	31.782	0.045	0.045	0.000	0.000	0.000
71	A	77	TYR	0	0.014	-0.003	29.695	0.001	0.001	0.000	0.000	0.000
72	A	78	ALA	0	0.033	0.023	33.192	0.000	0.000	0.000	0.000	0.000
73	A	79	ILE	0	-0.013	0.002	29.428	-0.001	-0.001	0.000	0.000	0.000
74	A	80	ARG	1	0.863	0.934	33.927	0.018	0.018	0.000	0.000	0.000
75	A	81	LEU	0	-0.010	-0.011	29.514	-0.002	-0.002	0.000	0.000	0.000
76	A	82	ASP	-1	-0.880	-0.945	33.914	-0.010	-0.010	0.000	0.000	0.000
77	A	83	ASP	-1	-0.827	-0.878	32.758	-0.003	-0.003	0.000	0.000	0.000
78	A	84	GLY	0	0.003	-0.001	35.940	0.002	0.002	0.000	0.000	0.000
79	A	85	ALA	0	-0.040	-0.015	32.576	0.000	0.000	0.000	0.000	0.000
80	A	86	ALA	0	-0.026	-0.018	34.169	-0.002	-0.002	0.000	0.000	0.000
81	A	87	ILE	0	-0.022	-0.016	27.943	0.002	0.002	0.000	0.000	0.000
82	A	88	TYR	0	0.022	0.019	31.281	-0.003	-0.003	0.000	0.000	0.000
83	A	89	ILE	0	-0.011	-0.016	27.515	-0.002	-0.002	0.000	0.000	0.000
84	A	90	GLU	-1	-0.790	-0.903	28.600	-0.057	-0.057	0.000	0.000	0.000
85	A	91	ASN	0	0.018	0.042	25.842	-0.013	-0.013	0.000	0.000	0.000
86	A	92	ASN	0	0.066	0.074	26.397	0.008	0.008	0.000	0.000	0.000
87	A	93	GLY	0	0.009	-0.022	25.571	-0.013	-0.013	0.000	0.000	0.000
88	A	94	ILE	0	-0.057	-0.013	24.663	0.009	0.009	0.000	0.000	0.000
89	A	95	ARG	1	0.913	0.955	27.286	0.080	0.080	0.000	0.000	0.000
90	A	96	THR	0	-0.017	-0.002	27.788	0.006	0.006	0.000	0.000	0.000
91	A	97	VAL	0	0.037	0.018	30.028	-0.004	-0.004	0.000	0.000	0.000
92	A	98	PRO	0	0.030	0.012	30.450	0.000	0.000	0.000	0.000	0.000
93	A	99	ASP	-1	-0.897	-0.953	32.448	-0.077	-0.077	0.000	0.000	0.000
94	A	100	GLU	-1	-0.932	-0.964	35.175	-0.082	-0.082	0.000	0.000	0.000
95	A	101	TYR	0	0.011	-0.008	34.068	0.005	0.005	0.000	0.000	0.000
96	A	102	ILE	0	0.000	0.000	34.822	0.002	0.002	0.000	0.000	0.000
97	A	103	GLU	-1	-0.915	-0.973	37.951	-0.055	-0.055	0.000	0.000	0.000
98	A	104	ALA	0	0.050	0.043	39.652	0.002	0.002	0.000	0.000	0.000
99	A	105	VAL	0	-0.072	-0.034	35.741	0.002	0.002	0.000	0.000	0.000
100	A	106	LYS	1	0.859	0.941	39.167	0.063	0.063	0.000	0.000	0.000
101	A	107	SER	0	-0.025	-0.002	41.956	0.002	0.002	0.000	0.000	0.000
102	A	108	GLY	0	-0.085	-0.024	41.622	0.002	0.002	0.000	0.000	0.000
103	A	109	GLU	-1	-0.929	-0.977	42.541	-0.051	-0.051	0.000	0.000	0.000
104	A	110	PHE	0	-0.048	-0.041	38.411	-0.003	-0.003	0.000	0.000	0.000
105	A	111	VAL	0	0.011	0.013	34.981	-0.001	-0.001	0.000	0.000	0.000
106	A	112	ASP	-1	-0.836	-0.907	34.093	-0.086	-0.086	0.000	0.000	0.000
107	A	113	PRO	0	-0.053	-0.015	32.478	-0.005	-0.005	0.000	0.000	0.000
108	A	114	ASN	0	-0.020	-0.026	29.593	-0.011	-0.011	0.000	0.000	0.000
109	A	115	ALA	0	-0.014	0.015	29.366	-0.009	-0.009	0.000	0.000	0.000
110	A	116	TYR	0	-0.043	-0.023	29.636	-0.003	-0.003	0.000	0.000	0.000
111	A	117	TYR	0	0.015	0.031	21.278	-0.018	-0.018	0.000	0.000	0.000
112	A	118	PHE	0	-0.006	-0.024	25.589	0.012	0.012	0.000	0.000	0.000
113	A	119	ARG	1	0.907	0.963	20.358	0.192	0.192	0.000	0.000	0.000
114	A	120	THR	0	-0.006	-0.051	23.099	0.006	0.006	0.000	0.000	0.000
115	A	121	ILE	0	0.025	0.017	19.287	-0.017	-0.017	0.000	0.000	0.000
116	A	122	PRO	0	-0.047	-0.006	21.398	0.013	0.013	0.000	0.000	0.000
117	A	123	THR	0	0.005	0.012	22.722	-0.004	-0.004	0.000	0.000	0.000
118	A	124	PHE	0	-0.018	-0.022	22.417	0.005	0.005	0.000	0.000	0.000
119	A	125	GLU	-1	-0.867	-0.897	26.635	-0.021	-0.021	0.000	0.000	0.000
120	A	126	THR	0	0.019	-0.012	27.358	0.001	0.001	0.000	0.000	0.000
121	A	127	TYR	0	-0.072	-0.081	30.166	0.003	0.003	0.000	0.000	0.000
122	A	128	SER	0	0.014	-0.006	31.107	0.003	0.003	0.000	0.000	0.000
123	A	129	PRO	0	0.042	0.005	28.982	-0.002	-0.002	0.000	0.000	0.000
124	A	130	LYS	1	0.910	0.988	27.439	-0.001	-0.001	0.000	0.000	0.000
125	A	131	TYR	0	0.021	-0.038	26.164	0.000	0.000	0.000	0.000	0.000
126	A	132	LYS	1	0.928	0.971	25.950	-0.002	-0.002	0.000	0.000	0.000
127	A	133	TRP	0	0.060	0.038	19.818	-0.002	-0.002	0.000	0.000	0.000
128	A	134	MET	0	0.002	0.015	20.939	-0.004	-0.004	0.000	0.000	0.000
129	A	135	MET	0	-0.073	-0.018	22.823	-0.007	-0.007	0.000	0.000	0.000
130	A	136	ASN	0	-0.080	-0.038	20.242	0.000	0.000	0.000	0.000	0.000
131	A	137	HIS	0	-0.003	-0.003	15.181	0.022	0.022	0.000	0.000	0.000
132	A	138	ILE	0	0.025	0.022	15.242	-0.001	-0.001	0.000	0.000	0.000
133	A	139	PHE	0	0.027	0.011	16.316	-0.006	-0.006	0.000	0.000	0.000
134	A	140	VAL	0	0.019	0.010	16.326	-0.004	-0.004	0.000	0.000	0.000
135	A	141	CYS	0	-0.062	-0.009	18.996	0.013	0.013	0.000	0.000	0.000
136	A	142	CYS	0	-0.021	-0.008	19.922	-0.016	-0.016	0.000	0.000	0.000
137	A	143	ALA	0	0.041	0.015	22.874	0.013	0.013	0.000	0.000	0.000
138	A	144	SER	0	-0.019	-0.021	26.623	-0.005	-0.005	0.000	0.000	0.000
139	A	145	ARG	1	0.970	0.986	29.315	0.081	0.081	0.000	0.000	0.000
140	A	146	LEU	0	0.004	-0.028	33.067	0.003	0.003	0.000	0.000	0.000
141	A	147	PRO	0	-0.026	-0.019	35.231	0.000	0.000	0.000	0.000	0.000
142	A	148	GLU	-1	-0.909	-0.959	37.880	-0.043	-0.043	0.000	0.000	0.000
143	A	149	ASN	0	-0.038	-0.021	34.948	0.004	0.004	0.000	0.000	0.000
144	A	150	VAL	0	-0.010	0.005	30.586	-0.004	-0.004	0.000	0.000	0.000
145	A	151	LEU	0	-0.027	0.002	27.666	0.004	0.004	0.000	0.000	0.000
146	A	152	LEU	0	-0.018	-0.022	26.703	-0.009	-0.009	0.000	0.000	0.000
147	A	153	LYS	1	0.996	1.002	22.193	0.118	0.118	0.000	0.000	0.000
148	A	154	PHE	0	0.012	-0.003	21.894	-0.014	-0.014	0.000	0.000	0.000
149	A	155	TYR	0	0.014	-0.002	16.326	0.005	0.005	0.000	0.000	0.000
150	A	156	LYS	1	0.881	0.958	14.169	0.016	0.016	0.000	0.000	0.000
151	A	157	ILE	0	-0.024	-0.028	11.118	-0.022	-0.022	0.000	0.000	0.000
152	A	158	SER	-1	-0.950	-0.978	9.330	-0.055	-0.055	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:ACE )