FMO DATABASE

FMODB ID: VQZV1

Calculation Name: 4M4X-A-Xray372

Preferred Name: Aryl hydrocarbon receptor

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 4M4X

Chain ID: A

ChEMBL ID: CHEMBL6099

UniProt ID: P30561

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	126
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1093367.308204
FMO2-HF: Nuclear repulsion	1042504.18835
FMO2-HF: Total energy	-50863.119854
FMO2-MP2: Total energy	-51009.840054

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:107:GLY)

Summations of interaction energy for fragment #1(A:107:GLY)

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.
-5.718	-2.92	0.564	-1.414	-1.947	0.003

Interaction energy analysis for fragmet #1(A:107:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.010 / q_NPA : -0.003

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	109	MET	0	0.048	0.016	3.804	-1.250	0.100	-0.003	-0.614	-0.732	0.002
4	A	110	LEU	0	-0.028	-0.003	2.617	-2.740	-1.545	0.566	-0.715	-1.046	0.001
5	A	111	GLN	0	0.028	0.004	3.857	-1.008	-0.755	0.001	-0.085	-0.169	0.000
6	A	112	GLU	-1	-0.937	-0.975	5.525	0.184	0.184	0.000	0.000	0.000	0.000
7	A	113	GLY	0	-0.025	-0.007	7.564	-0.033	-0.033	0.000	0.000	0.000	0.000
8	A	114	GLU	-1	-0.751	-0.848	7.107	-0.406	-0.406	0.000	0.000	0.000	0.000
9	A	115	PHE	0	0.027	0.016	9.448	0.010	0.010	0.000	0.000	0.000	0.000
10	A	116	LEU	0	-0.012	0.002	12.189	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	117	LEU	0	-0.043	-0.031	10.006	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	118	GLN	0	-0.010	-0.011	14.120	-0.038	-0.038	0.000	0.000	0.000	0.000
13	A	119	ALA	0	-0.047	-0.007	17.043	-0.006	-0.006	0.000	0.000	0.000	0.000
14	A	120	LEU	0	-0.065	-0.022	14.997	0.002	0.002	0.000	0.000	0.000	0.000
15	A	121	ASN	0	0.003	0.003	18.883	-0.014	-0.014	0.000	0.000	0.000	0.000
16	A	122	GLY	0	0.048	0.001	19.700	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	123	PHE	0	-0.035	-0.002	15.125	0.005	0.005	0.000	0.000	0.000	0.000
18	A	124	VAL	0	-0.001	0.003	11.311	0.011	0.011	0.000	0.000	0.000	0.000
19	A	125	LEU	0	0.000	-0.005	13.129	-0.035	-0.035	0.000	0.000	0.000	0.000
20	A	126	VAL	0	-0.035	-0.017	10.618	0.029	0.029	0.000	0.000	0.000	0.000
21	A	127	VAL	0	-0.018	0.004	13.292	-0.028	-0.028	0.000	0.000	0.000	0.000
22	A	128	THR	0	-0.095	-0.113	14.153	0.014	0.014	0.000	0.000	0.000	0.000
23	A	129	ALA	0	0.046	0.011	16.710	0.004	0.004	0.000	0.000	0.000	0.000
24	A	130	ASP	-1	-0.817	-0.832	18.238	-0.121	-0.121	0.000	0.000	0.000	0.000
25	A	131	ALA	0	-0.031	-0.017	19.922	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	132	LEU	0	0.022	0.018	15.857	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	133	VAL	0	-0.022	-0.010	12.492	0.010	0.010	0.000	0.000	0.000	0.000
28	A	134	PHE	0	-0.035	-0.020	7.867	-0.034	-0.034	0.000	0.000	0.000	0.000
29	A	135	TYR	0	-0.045	-0.069	6.423	0.024	0.024	0.000	0.000	0.000	0.000
30	A	136	ALA	0	0.055	0.023	9.549	0.065	0.065	0.000	0.000	0.000	0.000
31	A	137	SER	0	0.023	0.017	9.844	-0.069	-0.069	0.000	0.000	0.000	0.000
32	A	138	SER	0	0.046	0.009	9.948	-0.012	-0.012	0.000	0.000	0.000	0.000
33	A	139	THR	0	0.038	0.033	12.218	0.005	0.005	0.000	0.000	0.000	0.000
34	A	140	ILE	0	-0.038	-0.004	14.467	0.018	0.018	0.000	0.000	0.000	0.000
35	A	141	GLN	0	0.018	0.021	16.093	0.006	0.006	0.000	0.000	0.000	0.000
36	A	142	ASP	-1	-0.909	-0.958	18.062	-0.056	-0.056	0.000	0.000	0.000	0.000
37	A	143	TYR	0	-0.072	-0.032	18.508	0.014	0.014	0.000	0.000	0.000	0.000
38	A	144	LEU	0	-0.023	-0.027	19.517	0.005	0.005	0.000	0.000	0.000	0.000
39	A	145	GLY	0	0.042	0.032	20.720	0.002	0.002	0.000	0.000	0.000	0.000
40	A	146	PHE	0	-0.046	-0.025	17.840	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	147	GLN	0	0.020	-0.004	15.117	-0.025	-0.025	0.000	0.000	0.000	0.000
42	A	148	GLN	0	-0.048	-0.056	7.860	-0.059	-0.059	0.000	0.000	0.000	0.000
43	A	149	SER	0	-0.017	-0.022	11.535	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	150	ASP	-1	-0.923	-0.948	12.415	-0.220	-0.220	0.000	0.000	0.000	0.000
45	A	151	VAL	0	-0.039	-0.016	14.109	0.025	0.025	0.000	0.000	0.000	0.000
46	A	152	ILE	0	-0.032	-0.023	8.405	0.014	0.014	0.000	0.000	0.000	0.000
47	A	153	HIS	0	-0.035	-0.020	9.716	0.029	0.029	0.000	0.000	0.000	0.000
48	A	154	GLN	0	0.013	0.030	14.204	0.040	0.040	0.000	0.000	0.000	0.000
49	A	155	SER	0	0.035	0.015	17.282	0.004	0.004	0.000	0.000	0.000	0.000
50	A	156	VAL	0	0.062	0.015	17.975	0.000	0.000	0.000	0.000	0.000	0.000
51	A	157	TYR	0	-0.031	-0.023	20.185	0.008	0.008	0.000	0.000	0.000	0.000
52	A	158	GLU	-1	-0.936	-0.969	21.844	-0.088	-0.088	0.000	0.000	0.000	0.000
53	A	159	LEU	0	-0.040	-0.007	18.091	0.004	0.004	0.000	0.000	0.000	0.000
54	A	160	ILE	0	-0.024	0.010	22.567	0.008	0.008	0.000	0.000	0.000	0.000
55	A	161	HIS	0	0.026	0.020	25.327	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	162	THR	0	0.023	-0.013	29.040	0.000	0.000	0.000	0.000	0.000	0.000
57	A	163	GLU	-1	-0.961	-0.989	30.993	-0.033	-0.033	0.000	0.000	0.000	0.000
58	A	164	ASP	-1	-0.777	-0.852	28.547	-0.034	-0.034	0.000	0.000	0.000	0.000
59	A	165	ARG	1	0.887	0.955	26.893	0.067	0.067	0.000	0.000	0.000	0.000
60	A	166	ALA	0	0.031	0.021	27.842	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	167	GLU	-1	-0.801	-0.901	29.044	-0.022	-0.022	0.000	0.000	0.000	0.000
62	A	168	PHE	0	0.020	-0.001	19.914	0.002	0.002	0.000	0.000	0.000	0.000
63	A	169	GLN	0	0.026	0.008	25.155	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	170	ARG	1	0.837	0.910	26.502	0.020	0.020	0.000	0.000	0.000	0.000
65	A	171	GLN	0	-0.010	-0.014	25.248	0.008	0.008	0.000	0.000	0.000	0.000
66	A	172	LEU	0	-0.007	0.015	19.982	0.005	0.005	0.000	0.000	0.000	0.000
67	A	173	HIS	0	0.075	0.064	23.304	0.002	0.002	0.000	0.000	0.000	0.000
68	A	174	TRP	0	0.025	-0.012	24.880	0.006	0.006	0.000	0.000	0.000	0.000
69	A	175	ALA	0	-0.046	-0.025	26.330	0.004	0.004	0.000	0.000	0.000	0.000
70	A	176	LEU	0	-0.064	-0.030	28.437	0.001	0.001	0.000	0.000	0.000	0.000
71	A	177	ASN	0	-0.037	-0.036	30.236	0.000	0.000	0.000	0.000	0.000	0.000
72	A	178	PRO	0	-0.040	-0.026	28.468	0.000	0.000	0.000	0.000	0.000	0.000
73	A	179	ASP	-1	-0.944	-0.938	29.819	-0.042	-0.042	0.000	0.000	0.000	0.000
74	A	206	ASN	0	-0.005	-0.020	33.206	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	207	ALA	0	0.010	0.019	28.353	0.003	0.003	0.000	0.000	0.000	0.000
76	A	208	SER	0	0.003	0.001	26.833	0.000	0.000	0.000	0.000	0.000	0.000
77	A	209	PHE	0	-0.017	-0.027	21.622	0.007	0.007	0.000	0.000	0.000	0.000
78	A	210	MET	0	0.005	0.020	22.751	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	211	GLU	-1	-0.928	-0.970	23.431	0.028	0.028	0.000	0.000	0.000	0.000
80	A	212	ARG	1	0.803	0.898	22.882	0.006	0.006	0.000	0.000	0.000	0.000
81	A	213	CYS	0	-0.008	-0.005	23.990	0.003	0.003	0.000	0.000	0.000	0.000
82	A	214	PHE	0	-0.013	0.011	23.006	0.000	0.000	0.000	0.000	0.000	0.000
83	A	215	ARG	1	0.998	1.008	26.311	0.019	0.019	0.000	0.000	0.000	0.000
84	A	216	CYS	0	-0.033	-0.014	24.181	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	217	ARG	1	0.797	0.879	26.364	0.035	0.035	0.000	0.000	0.000	0.000
86	A	218	LEU	0	0.041	0.014	20.650	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	219	ARG	1	0.958	0.970	23.911	0.081	0.081	0.000	0.000	0.000	0.000
88	A	220	CYS	0	-0.104	-0.046	23.434	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	221	LEU	0	-0.042	-0.036	22.524	0.006	0.006	0.000	0.000	0.000	0.000
90	A	222	LEU	0	0.030	0.013	23.523	0.000	0.000	0.000	0.000	0.000	0.000
91	A	223	ASP	-1	-0.866	-0.934	27.133	-0.048	-0.048	0.000	0.000	0.000	0.000
92	A	224	ASN	0	-0.071	-0.021	28.496	0.001	0.001	0.000	0.000	0.000	0.000
93	A	225	SER	0	-0.001	-0.013	28.722	0.004	0.004	0.000	0.000	0.000	0.000
94	A	226	SER	0	-0.009	-0.016	31.316	0.000	0.000	0.000	0.000	0.000	0.000
95	A	227	GLY	0	0.003	0.021	29.380	0.000	0.000	0.000	0.000	0.000	0.000
96	A	228	PHE	0	-0.040	-0.025	27.530	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	229	LEU	0	0.055	0.036	24.176	0.005	0.005	0.000	0.000	0.000	0.000
98	A	230	ALA	0	-0.066	-0.028	26.602	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	231	MET	0	-0.009	-0.002	21.261	0.000	0.000	0.000	0.000	0.000	0.000
100	A	232	ASN	0	-0.005	-0.012	25.139	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	233	PHE	0	0.035	0.021	18.931	0.000	0.000	0.000	0.000	0.000	0.000
102	A	234	GLN	0	0.031	0.004	21.278	0.001	0.001	0.000	0.000	0.000	0.000
103	A	235	GLY	0	0.010	-0.003	19.511	0.003	0.003	0.000	0.000	0.000	0.000
104	A	236	ARG	1	0.863	0.944	18.980	-0.055	-0.055	0.000	0.000	0.000	0.000
105	A	237	LEU	0	0.012	0.033	18.767	-0.005	-0.005	0.000	0.000	0.000	0.000
106	A	238	LYS	1	0.899	0.940	15.473	-0.059	-0.059	0.000	0.000	0.000	0.000
107	A	239	TYR	0	0.035	0.007	17.388	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	240	LEU	0	-0.014	0.012	10.321	0.020	0.020	0.000	0.000	0.000	0.000
109	A	241	HIS	0	-0.001	-0.015	13.108	-0.012	-0.012	0.000	0.000	0.000	0.000
110	A	242	GLY	0	0.001	0.000	10.298	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	243	GLN	0	0.031	0.030	11.302	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	244	ASN	0	0.017	0.015	12.684	0.027	0.027	0.000	0.000	0.000	0.000
113	A	253	LEU	0	-0.001	-0.016	19.356	0.005	0.005	0.000	0.000	0.000	0.000
114	A	254	PRO	0	-0.029	0.003	19.114	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	255	PRO	0	0.008	0.006	16.733	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	256	GLN	0	0.043	0.012	16.209	0.018	0.018	0.000	0.000	0.000	0.000
117	A	257	LEU	0	-0.045	-0.030	17.622	0.003	0.003	0.000	0.000	0.000	0.000
118	A	258	ALA	0	0.037	0.016	15.206	-0.012	-0.012	0.000	0.000	0.000	0.000
119	A	259	LEU	0	0.003	0.001	17.260	0.019	0.019	0.000	0.000	0.000	0.000
120	A	260	PHE	0	-0.028	-0.006	11.250	-0.013	-0.013	0.000	0.000	0.000	0.000
121	A	261	ALA	0	-0.020	-0.031	15.582	0.016	0.016	0.000	0.000	0.000	0.000
122	A	262	ILE	0	0.028	0.022	15.865	-0.006	-0.006	0.000	0.000	0.000	0.000
123	A	263	ALA	0	-0.012	0.003	18.027	0.002	0.002	0.000	0.000	0.000	0.000
124	A	264	THR	0	0.018	0.001	20.142	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	265	PRO	0	-0.008	0.006	22.787	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	266	LEU	0	-0.030	-0.016	25.536	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:107:GLY)