FMO DATABASE

FMODB ID: ZV9NN

Calculation Name: 4G3W-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4G3W

Chain ID: A

ChEMBL ID:

UniProt ID: O66591

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptH
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	139
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1289499.941554
FMO2-HF: Nuclear repulsion	1235975.081097
FMO2-HF: Total energy	-53524.860457
FMO2-MP2: Total energy	-53684.620867

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:ASN)

Summations of interaction energy for fragment #1(A:22:ASN)

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.
-24.07	-16.208	6.515	-5.711	-8.667	0.026

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.078 / q_NPA : 0.023

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	GLU	-1	-0.943	-0.977	2.847	-9.625	-5.504	0.317	-1.885	-2.553	-0.005
4	A	25	THR	0	-0.089	-0.040	2.330	-7.472	-5.040	3.555	-2.424	-3.563	0.015
5	A	26	THR	0	0.026	0.004	2.385	-3.977	-2.753	2.644	-1.384	-2.484	0.016
6	A	27	VAL	0	0.057	0.043	4.737	-1.484	-1.399	-0.001	-0.018	-0.067	0.000
7	A	28	PRO	0	-0.024	-0.017	6.780	-0.273	-0.273	0.000	0.000	0.000	0.000
8	A	29	TYR	0	0.013	0.004	6.182	-0.850	-0.850	0.000	0.000	0.000	0.000
9	A	30	ILE	0	0.056	0.035	9.669	-0.334	-0.334	0.000	0.000	0.000	0.000
10	A	31	PHE	0	-0.014	-0.016	11.555	-0.237	-0.237	0.000	0.000	0.000	0.000
11	A	32	ARG	1	0.907	0.958	9.719	-0.671	-0.671	0.000	0.000	0.000	0.000
12	A	33	LEU	0	0.039	0.021	13.760	-0.129	-0.129	0.000	0.000	0.000	0.000
13	A	34	LEU	0	0.029	0.021	15.634	-0.099	-0.099	0.000	0.000	0.000	0.000
14	A	35	LYS	1	0.912	0.951	17.222	-0.276	-0.276	0.000	0.000	0.000	0.000
15	A	36	LYS	1	0.880	0.942	17.051	-0.478	-0.478	0.000	0.000	0.000	0.000
16	A	37	LEU	0	0.016	0.003	19.627	-0.036	-0.036	0.000	0.000	0.000	0.000
17	A	38	MET	0	0.005	0.016	21.312	0.002	0.002	0.000	0.000	0.000	0.000
18	A	39	GLY	0	0.006	0.018	22.770	-0.025	-0.025	0.000	0.000	0.000	0.000
19	A	40	PHE	0	0.010	0.006	20.010	-0.026	-0.026	0.000	0.000	0.000	0.000
20	A	41	GLU	-1	-0.873	-0.942	20.966	0.117	0.117	0.000	0.000	0.000	0.000
21	A	42	ARG	1	0.827	0.912	18.772	-0.041	-0.041	0.000	0.000	0.000	0.000
22	A	43	LEU	0	0.018	0.027	15.680	-0.017	-0.017	0.000	0.000	0.000	0.000
23	A	44	THR	0	-0.032	-0.022	14.524	-0.095	-0.095	0.000	0.000	0.000	0.000
24	A	45	LEU	0	0.059	0.046	8.535	0.071	0.071	0.000	0.000	0.000	0.000
25	A	46	THR	0	-0.047	-0.021	11.932	-0.163	-0.163	0.000	0.000	0.000	0.000
26	A	47	ILE	0	-0.025	-0.025	8.401	0.140	0.140	0.000	0.000	0.000	0.000
27	A	48	TYR	0	-0.069	-0.054	11.527	-0.136	-0.136	0.000	0.000	0.000	0.000
28	A	49	ASP	-1	-0.883	-0.949	12.245	-0.414	-0.414	0.000	0.000	0.000	0.000
29	A	50	PRO	0	0.022	-0.019	13.315	0.013	0.013	0.000	0.000	0.000	0.000
30	A	51	SER	0	-0.028	0.006	15.700	0.027	0.027	0.000	0.000	0.000	0.000
31	A	52	THR	0	-0.044	-0.018	16.311	0.027	0.027	0.000	0.000	0.000	0.000
32	A	53	ASP	-1	-0.843	-0.884	18.193	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	54	GLN	0	-0.023	-0.022	17.427	0.023	0.023	0.000	0.000	0.000	0.000
34	A	55	ILE	0	-0.023	0.001	14.860	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	56	VAL	0	0.040	0.008	12.245	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	57	VAL	0	-0.049	-0.028	11.946	0.066	0.066	0.000	0.000	0.000	0.000
37	A	58	ARG	1	0.883	0.939	4.815	0.303	0.303	0.000	0.000	0.000	0.000
38	A	59	ALA	0	0.071	0.026	7.576	-0.385	-0.385	0.000	0.000	0.000	0.000
39	A	60	THR	0	-0.026	-0.004	9.529	0.193	0.193	0.000	0.000	0.000	0.000
40	A	61	SER	0	0.022	0.016	11.940	0.027	0.027	0.000	0.000	0.000	0.000
41	A	62	SER	0	-0.106	-0.062	14.131	0.006	0.006	0.000	0.000	0.000	0.000
42	A	63	GLY	0	0.030	0.009	13.291	-0.038	-0.038	0.000	0.000	0.000	0.000
43	A	64	LYS	1	0.991	0.995	14.064	0.214	0.214	0.000	0.000	0.000	0.000
44	A	65	PHE	0	0.012	0.011	7.439	0.183	0.183	0.000	0.000	0.000	0.000
45	A	66	PRO	0	0.005	0.015	13.213	-0.101	-0.101	0.000	0.000	0.000	0.000
46	A	67	LYS	1	0.953	0.975	8.968	1.217	1.217	0.000	0.000	0.000	0.000
47	A	68	GLU	-1	-0.899	-0.949	14.623	-0.223	-0.223	0.000	0.000	0.000	0.000
48	A	69	GLY	0	0.037	0.023	15.924	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	70	PHE	0	-0.047	-0.022	17.717	0.013	0.013	0.000	0.000	0.000	0.000
50	A	71	LYS	1	1.056	1.019	19.672	0.107	0.107	0.000	0.000	0.000	0.000
51	A	72	LYS	1	0.991	0.985	21.875	-0.089	-0.089	0.000	0.000	0.000	0.000
52	A	73	GLY	0	-0.048	-0.023	23.790	-0.012	-0.012	0.000	0.000	0.000	0.000
53	A	74	GLU	-1	-0.866	-0.908	23.465	-0.080	-0.080	0.000	0.000	0.000	0.000
54	A	75	GLY	0	0.069	0.022	24.130	0.006	0.006	0.000	0.000	0.000	0.000
55	A	76	ILE	0	0.053	0.021	24.740	0.010	0.010	0.000	0.000	0.000	0.000
56	A	77	THR	0	-0.002	0.007	18.787	0.013	0.013	0.000	0.000	0.000	0.000
57	A	78	GLY	0	0.066	0.029	21.472	0.023	0.023	0.000	0.000	0.000	0.000
58	A	79	LYS	1	0.836	0.916	22.789	-0.043	-0.043	0.000	0.000	0.000	0.000
59	A	80	VAL	0	0.031	0.027	21.255	0.007	0.007	0.000	0.000	0.000	0.000
60	A	81	TRP	0	-0.051	-0.021	19.023	0.016	0.016	0.000	0.000	0.000	0.000
61	A	82	LYS	1	0.868	0.928	21.456	-0.053	-0.053	0.000	0.000	0.000	0.000
62	A	83	HIS	0	0.021	0.003	24.756	0.002	0.002	0.000	0.000	0.000	0.000
63	A	84	GLY	0	-0.006	0.008	23.138	0.008	0.008	0.000	0.000	0.000	0.000
64	A	85	VAL	0	-0.009	0.000	24.191	0.027	0.027	0.000	0.000	0.000	0.000
65	A	86	PRO	0	-0.011	-0.016	24.060	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	87	ILE	0	0.001	0.009	25.168	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	88	VAL	0	-0.001	0.003	26.236	0.011	0.011	0.000	0.000	0.000	0.000
68	A	89	ILE	0	-0.021	-0.013	27.777	-0.015	-0.015	0.000	0.000	0.000	0.000
69	A	90	PRO	0	0.024	0.000	30.001	0.006	0.006	0.000	0.000	0.000	0.000
70	A	91	ASP	-1	-0.835	-0.936	32.361	0.073	0.073	0.000	0.000	0.000	0.000
71	A	92	ILE	0	-0.025	-0.008	26.767	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	93	SER	0	-0.128	-0.068	30.972	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	94	GLN	0	-0.009	-0.004	34.069	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	95	GLU	-1	-0.860	-0.924	31.500	0.063	0.063	0.000	0.000	0.000	0.000
75	A	96	PRO	0	0.017	0.011	32.056	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	97	GLU	-1	-0.916	-0.958	30.227	0.047	0.047	0.000	0.000	0.000	0.000
77	A	98	PHE	0	-0.085	-0.046	24.965	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	99	LEU	0	0.040	0.014	25.045	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	100	ASN	0	-0.033	0.001	25.115	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	101	LYS	1	0.895	0.951	20.918	0.114	0.114	0.000	0.000	0.000	0.000
81	A	102	VAL	0	0.012	0.002	17.152	-0.029	-0.029	0.000	0.000	0.000	0.000
82	A	103	TRP	0	-0.065	-0.048	16.713	-0.051	-0.051	0.000	0.000	0.000	0.000
83	A	104	LYS	1	0.901	0.973	21.604	0.208	0.208	0.000	0.000	0.000	0.000
84	A	105	ARG	1	0.852	0.920	22.261	-0.050	-0.050	0.000	0.000	0.000	0.000
85	A	106	LYS	1	1.013	0.981	26.881	0.052	0.052	0.000	0.000	0.000	0.000
86	A	107	LYS	1	0.982	0.993	30.503	0.032	0.032	0.000	0.000	0.000	0.000
87	A	108	SER	0	-0.020	-0.005	28.869	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	109	LYS	1	0.799	0.874	27.293	-0.101	-0.101	0.000	0.000	0.000	0.000
89	A	110	LYS	1	0.947	0.983	31.641	-0.074	-0.074	0.000	0.000	0.000	0.000
90	A	111	LYS	1	1.034	1.015	33.331	-0.081	-0.081	0.000	0.000	0.000	0.000
91	A	112	ILE	0	-0.031	0.003	27.157	0.011	0.011	0.000	0.000	0.000	0.000
92	A	113	ALA	0	0.084	0.059	28.646	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	114	PHE	0	-0.034	-0.032	21.593	0.008	0.008	0.000	0.000	0.000	0.000
94	A	115	ILE	0	0.030	0.021	23.144	0.000	0.000	0.000	0.000	0.000	0.000
95	A	116	ALA	0	-0.008	-0.004	20.999	0.016	0.016	0.000	0.000	0.000	0.000
96	A	117	VAL	0	0.005	-0.006	18.674	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	118	PRO	0	0.018	0.002	18.898	0.011	0.011	0.000	0.000	0.000	0.000
98	A	119	ILE	0	-0.015	0.003	12.778	0.049	0.049	0.000	0.000	0.000	0.000
99	A	120	LYS	1	0.951	0.957	16.497	-0.429	-0.429	0.000	0.000	0.000	0.000
100	A	121	SER	0	0.059	0.020	13.833	0.048	0.048	0.000	0.000	0.000	0.000
101	A	122	GLY	0	0.038	0.035	16.673	-0.059	-0.059	0.000	0.000	0.000	0.000
102	A	123	GLY	0	-0.016	-0.008	18.816	-0.053	-0.053	0.000	0.000	0.000	0.000
103	A	124	LYS	1	0.936	0.971	19.294	-0.242	-0.242	0.000	0.000	0.000	0.000
104	A	125	VAL	0	-0.005	-0.006	18.341	0.060	0.060	0.000	0.000	0.000	0.000
105	A	126	ILE	0	0.007	0.022	12.483	-0.061	-0.061	0.000	0.000	0.000	0.000
106	A	127	GLY	0	0.035	0.000	13.886	-0.047	-0.047	0.000	0.000	0.000	0.000
107	A	128	VAL	0	-0.044	-0.006	14.760	0.027	0.027	0.000	0.000	0.000	0.000
108	A	129	LEU	0	0.018	0.021	14.294	-0.011	-0.011	0.000	0.000	0.000	0.000
109	A	130	SER	0	-0.033	-0.007	16.305	-0.055	-0.055	0.000	0.000	0.000	0.000
110	A	131	ALA	0	0.020	0.000	17.978	0.035	0.035	0.000	0.000	0.000	0.000
111	A	132	ASP	-1	-0.737	-0.855	20.574	0.086	0.086	0.000	0.000	0.000	0.000
112	A	133	LYS	1	0.938	0.959	23.598	-0.216	-0.216	0.000	0.000	0.000	0.000
113	A	134	GLU	-1	-0.865	-0.926	26.337	0.109	0.109	0.000	0.000	0.000	0.000
114	A	135	ILE	0	-0.047	-0.014	29.648	0.016	0.016	0.000	0.000	0.000	0.000
115	A	136	ASN	0	0.004	0.000	31.301	-0.027	-0.027	0.000	0.000	0.000	0.000
116	A	137	GLU	-1	-0.932	-0.967	33.401	0.131	0.131	0.000	0.000	0.000	0.000
117	A	138	LYS	1	0.928	0.954	35.542	-0.145	-0.145	0.000	0.000	0.000	0.000
118	A	139	ASP	-1	-0.843	-0.905	30.472	0.258	0.258	0.000	0.000	0.000	0.000
119	A	140	SER	0	0.052	0.020	31.628	-0.014	-0.014	0.000	0.000	0.000	0.000
120	A	141	LEU	0	0.030	-0.015	28.936	0.021	0.021	0.000	0.000	0.000	0.000
121	A	142	ASP	-1	-0.840	-0.881	28.524	0.272	0.272	0.000	0.000	0.000	0.000
122	A	143	GLU	-1	-0.891	-0.950	28.590	0.286	0.286	0.000	0.000	0.000	0.000
123	A	144	TYR	0	-0.048	-0.023	24.387	0.044	0.044	0.000	0.000	0.000	0.000
124	A	145	THR	0	-0.019	-0.038	23.949	0.043	0.043	0.000	0.000	0.000	0.000
125	A	146	ARG	1	0.895	0.944	23.769	-0.271	-0.271	0.000	0.000	0.000	0.000
126	A	147	PHE	0	0.048	0.025	19.601	0.050	0.050	0.000	0.000	0.000	0.000
127	A	148	LEU	0	0.035	0.002	18.372	0.082	0.082	0.000	0.000	0.000	0.000
128	A	149	SER	0	-0.007	-0.004	18.936	0.061	0.061	0.000	0.000	0.000	0.000
129	A	150	MET	0	-0.010	0.007	19.631	0.042	0.042	0.000	0.000	0.000	0.000
130	A	151	ILE	0	-0.018	-0.015	14.541	0.109	0.109	0.000	0.000	0.000	0.000
131	A	152	ALA	0	-0.026	-0.027	14.840	0.151	0.151	0.000	0.000	0.000	0.000
132	A	153	THR	0	-0.029	-0.011	14.885	0.081	0.081	0.000	0.000	0.000	0.000
133	A	154	LEU	0	-0.021	-0.008	12.090	0.060	0.060	0.000	0.000	0.000	0.000
134	A	155	ILE	0	-0.029	-0.011	9.817	0.284	0.284	0.000	0.000	0.000	0.000
135	A	156	ALA	0	-0.006	-0.021	10.325	0.251	0.251	0.000	0.000	0.000	0.000
136	A	157	ASN	0	-0.004	0.003	12.034	-0.107	-0.107	0.000	0.000	0.000	0.000
137	A	158	SER	0	-0.003	-0.008	6.464	0.093	0.093	0.000	0.000	0.000	0.000
138	A	159	PHE	0	-0.098	-0.015	7.812	0.192	0.192	0.000	0.000	0.000	0.000
139	A	160	SER	0	0.019	0.009	9.429	-0.358	-0.358	0.000	0.000	0.000	0.000

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