FMO DATABASE

FMODB ID: 1NV5Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1094320.230495
FMO2-HF: Nuclear repulsion	1043456.623502
FMO2-HF: Total energy	-50863.606993
FMO2-MP2: Total energy	-51010.356117

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.
-5.399	-2.709	0.721	-1.435	-1.975	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 : 0.013 / q_NPA : -0.005

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	109	MET	0	0.040	0.011	3.804	-0.898	0.436	-0.004	-0.591	-0.740	0.001
4	A	110	LEU	0	-0.024	-0.002	2.502	-2.500	-1.402	0.724	-0.767	-1.054	0.002
5	A	111	GLN	0	0.034	0.009	3.843	-1.206	-0.948	0.001	-0.077	-0.181	0.000
6	A	112	GLU	-1	-0.941	-0.975	5.518	0.104	0.104	0.000	0.000	0.000	0.000
7	A	113	GLY	0	-0.024	-0.009	7.550	-0.025	-0.025	0.000	0.000	0.000	0.000
8	A	114	GLU	-1	-0.729	-0.816	7.084	-0.257	-0.257	0.000	0.000	0.000	0.000
9	A	115	PHE	0	0.031	0.017	9.441	0.012	0.012	0.000	0.000	0.000	0.000
10	A	116	LEU	0	-0.015	0.004	11.999	-0.012	-0.012	0.000	0.000	0.000	0.000
11	A	117	LEU	0	-0.044	-0.032	9.854	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	118	GLN	0	-0.003	-0.010	14.114	-0.033	-0.033	0.000	0.000	0.000	0.000
13	A	119	ALA	0	-0.049	-0.007	17.037	-0.011	-0.011	0.000	0.000	0.000	0.000
14	A	120	LEU	0	-0.060	-0.019	14.892	0.000	0.000	0.000	0.000	0.000	0.000
15	A	121	ASN	0	0.013	0.007	18.879	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	122	GLY	0	0.046	0.020	19.694	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	123	PHE	0	-0.042	-0.007	15.193	0.006	0.006	0.000	0.000	0.000	0.000
18	A	124	VAL	0	-0.001	0.001	11.524	0.010	0.010	0.000	0.000	0.000	0.000
19	A	125	LEU	0	0.005	-0.002	13.130	-0.036	-0.036	0.000	0.000	0.000	0.000
20	A	126	VAL	0	-0.039	-0.021	10.752	0.031	0.031	0.000	0.000	0.000	0.000
21	A	127	VAL	0	-0.012	0.006	13.295	-0.031	-0.031	0.000	0.000	0.000	0.000
22	A	128	THR	0	-0.033	-0.044	14.173	0.016	0.016	0.000	0.000	0.000	0.000
23	A	129	ALA	0	0.033	0.010	16.717	0.001	0.001	0.000	0.000	0.000	0.000
24	A	130	ASP	-1	-0.822	-0.871	18.128	-0.094	-0.094	0.000	0.000	0.000	0.000
25	A	131	ALA	0	-0.018	-0.010	19.883	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	132	LEU	0	-0.012	0.003	15.978	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	133	VAL	0	-0.014	-0.007	12.489	0.016	0.016	0.000	0.000	0.000	0.000
28	A	134	PHE	0	-0.029	-0.019	8.251	-0.037	-0.037	0.000	0.000	0.000	0.000
29	A	135	TYR	0	-0.044	-0.074	6.465	0.037	0.037	0.000	0.000	0.000	0.000
30	A	136	ALA	0	0.052	0.023	9.564	0.054	0.054	0.000	0.000	0.000	0.000
31	A	137	SER	0	0.024	0.027	9.841	-0.063	-0.063	0.000	0.000	0.000	0.000
32	A	138	SER	0	0.019	-0.035	10.094	-0.036	-0.036	0.000	0.000	0.000	0.000
33	A	139	THR	0	0.017	0.016	12.216	0.002	0.002	0.000	0.000	0.000	0.000
34	A	140	ILE	0	-0.053	-0.009	14.328	0.014	0.014	0.000	0.000	0.000	0.000
35	A	141	GLN	0	0.013	0.021	16.091	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	142	ASP	-1	-0.900	-0.965	18.032	-0.038	-0.038	0.000	0.000	0.000	0.000
37	A	143	TYR	0	-0.067	-0.033	18.541	0.012	0.012	0.000	0.000	0.000	0.000
38	A	144	LEU	0	-0.007	-0.019	19.545	0.003	0.003	0.000	0.000	0.000	0.000
39	A	145	GLY	0	0.037	0.032	20.705	0.000	0.000	0.000	0.000	0.000	0.000
40	A	146	PHE	0	-0.044	-0.028	17.791	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	147	GLN	0	0.035	0.009	15.133	-0.022	-0.022	0.000	0.000	0.000	0.000
42	A	148	GLN	0	-0.036	-0.042	7.915	-0.102	-0.102	0.000	0.000	0.000	0.000
43	A	149	SER	0	-0.032	-0.026	11.513	-0.010	-0.010	0.000	0.000	0.000	0.000
44	A	150	ASP	-1	-0.912	-0.950	12.418	-0.225	-0.225	0.000	0.000	0.000	0.000
45	A	151	VAL	0	-0.037	-0.012	14.444	0.026	0.026	0.000	0.000	0.000	0.000
46	A	152	ILE	0	-0.031	-0.017	8.373	0.020	0.020	0.000	0.000	0.000	0.000
47	A	153	HIS	0	-0.034	-0.021	9.504	0.030	0.030	0.000	0.000	0.000	0.000
48	A	154	GLN	0	0.001	0.026	14.197	0.037	0.037	0.000	0.000	0.000	0.000
49	A	155	SER	0	0.020	0.010	17.288	0.009	0.009	0.000	0.000	0.000	0.000
50	A	156	VAL	0	0.050	0.006	18.020	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	157	TYR	0	-0.053	-0.039	20.190	0.006	0.006	0.000	0.000	0.000	0.000
52	A	158	GLU	-1	-0.828	-0.898	22.239	-0.067	-0.067	0.000	0.000	0.000	0.000
53	A	159	LEU	0	-0.036	-0.006	18.068	0.002	0.002	0.000	0.000	0.000	0.000
54	A	160	ILE	0	-0.020	0.007	22.345	0.008	0.008	0.000	0.000	0.000	0.000
55	A	161	HIS	0	0.009	0.006	25.330	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	162	THR	0	-0.009	-0.033	29.044	0.001	0.001	0.000	0.000	0.000	0.000
57	A	163	GLU	-1	-0.908	-0.947	30.997	-0.026	-0.026	0.000	0.000	0.000	0.000
58	A	164	ASP	-1	-0.793	-0.860	28.525	-0.017	-0.017	0.000	0.000	0.000	0.000
59	A	165	ARG	1	0.803	0.901	26.921	0.059	0.059	0.000	0.000	0.000	0.000
60	A	166	ALA	0	0.034	0.022	27.847	0.000	0.000	0.000	0.000	0.000	0.000
61	A	167	GLU	-1	-0.775	-0.854	29.033	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	168	PHE	0	0.028	0.001	19.975	0.003	0.003	0.000	0.000	0.000	0.000
63	A	169	GLN	0	0.056	0.029	25.160	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	170	ARG	1	0.812	0.867	26.507	0.005	0.005	0.000	0.000	0.000	0.000
65	A	171	GLN	0	-0.028	-0.027	25.272	0.008	0.008	0.000	0.000	0.000	0.000
66	A	172	LEU	0	-0.020	0.007	19.931	0.007	0.007	0.000	0.000	0.000	0.000
67	A	173	HIS	0	0.063	0.055	23.309	0.004	0.004	0.000	0.000	0.000	0.000
68	A	174	TRP	0	0.035	-0.007	24.941	0.006	0.006	0.000	0.000	0.000	0.000
69	A	175	ALA	0	-0.042	-0.018	26.334	0.004	0.004	0.000	0.000	0.000	0.000
70	A	176	LEU	0	-0.062	-0.029	28.126	0.000	0.000	0.000	0.000	0.000	0.000
71	A	177	ASN	0	-0.043	-0.036	30.229	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	178	PRO	0	-0.036	-0.025	28.384	0.000	0.000	0.000	0.000	0.000	0.000
73	A	179	ASP	-1	-0.948	-0.941	29.825	-0.028	-0.028	0.000	0.000	0.000	0.000
74	A	206	ASN	0	-0.024	-0.028	33.269	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	207	ALA	0	0.019	0.019	28.463	0.003	0.003	0.000	0.000	0.000	0.000
76	A	208	SER	0	0.007	0.005	26.817	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	209	PHE	0	-0.021	-0.025	21.948	0.009	0.009	0.000	0.000	0.000	0.000
78	A	210	MET	0	0.003	0.019	22.993	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	211	GLU	-1	-0.827	-0.907	23.433	0.069	0.069	0.000	0.000	0.000	0.000
80	A	212	ARG	1	0.804	0.900	22.857	-0.023	-0.023	0.000	0.000	0.000	0.000
81	A	213	CYS	0	0.011	0.001	23.991	0.006	0.006	0.000	0.000	0.000	0.000
82	A	214	PHE	0	-0.031	0.007	22.899	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	215	ARG	1	0.998	1.002	26.312	0.004	0.004	0.000	0.000	0.000	0.000
84	A	216	CYS	0	-0.046	-0.012	24.846	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	217	ARG	1	0.801	0.878	26.365	0.022	0.022	0.000	0.000	0.000	0.000
86	A	218	LEU	0	0.037	0.008	20.778	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	219	ARG	1	0.957	0.968	23.852	0.069	0.069	0.000	0.000	0.000	0.000
88	A	220	CYS	0	-0.059	-0.028	23.436	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	221	LEU	0	-0.062	-0.036	22.567	0.004	0.004	0.000	0.000	0.000	0.000
90	A	222	LEU	0	0.018	0.011	23.176	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	223	ASP	-1	-0.881	-0.941	27.133	-0.043	-0.043	0.000	0.000	0.000	0.000
92	A	224	ASN	0	-0.080	-0.028	28.501	0.001	0.001	0.000	0.000	0.000	0.000
93	A	225	SER	0	-0.002	-0.015	29.290	0.002	0.002	0.000	0.000	0.000	0.000
94	A	226	SER	0	-0.014	-0.004	31.316	0.000	0.000	0.000	0.000	0.000	0.000
95	A	227	GLY	0	0.026	0.018	29.380	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	228	PHE	0	-0.026	-0.017	27.529	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	229	LEU	0	0.042	0.025	24.467	0.004	0.004	0.000	0.000	0.000	0.000
98	A	230	ALA	0	-0.068	-0.026	26.603	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	231	MET	0	0.000	0.004	21.261	0.000	0.000	0.000	0.000	0.000	0.000
100	A	232	ASN	0	-0.004	-0.015	25.161	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	233	PHE	0	0.042	0.024	18.800	0.002	0.002	0.000	0.000	0.000	0.000
102	A	234	GLN	0	0.021	-0.003	21.265	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	235	GLY	0	0.017	0.003	19.512	0.008	0.008	0.000	0.000	0.000	0.000
104	A	236	ARG	1	0.776	0.883	18.980	-0.099	-0.099	0.000	0.000	0.000	0.000
105	A	237	LEU	0	0.020	0.037	18.770	0.000	0.000	0.000	0.000	0.000	0.000
106	A	238	LYS	1	0.899	0.938	15.002	-0.137	-0.137	0.000	0.000	0.000	0.000
107	A	239	TYR	0	0.029	0.006	17.407	-0.010	-0.010	0.000	0.000	0.000	0.000
108	A	240	LEU	0	-0.010	0.013	10.259	0.026	0.026	0.000	0.000	0.000	0.000
109	A	241	HIS	0	-0.004	-0.016	13.094	-0.016	-0.016	0.000	0.000	0.000	0.000
110	A	242	GLY	0	0.005	0.001	10.205	0.006	0.006	0.000	0.000	0.000	0.000
111	A	243	GLN	0	0.033	0.032	11.202	-0.023	-0.023	0.000	0.000	0.000	0.000
112	A	244	ASN	0	-0.009	0.001	12.568	0.011	0.011	0.000	0.000	0.000	0.000
113	A	253	LEU	0	-0.008	-0.019	19.117	0.004	0.004	0.000	0.000	0.000	0.000
114	A	254	PRO	0	-0.018	0.005	19.004	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	255	PRO	0	0.006	0.005	16.583	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	256	GLN	0	0.027	-0.004	16.511	0.015	0.015	0.000	0.000	0.000	0.000
117	A	257	LEU	0	-0.046	-0.027	17.597	0.008	0.008	0.000	0.000	0.000	0.000
118	A	258	ALA	0	0.039	0.013	15.195	-0.013	-0.013	0.000	0.000	0.000	0.000
119	A	259	LEU	0	-0.010	0.004	17.265	0.019	0.019	0.000	0.000	0.000	0.000
120	A	260	PHE	0	-0.014	-0.011	11.362	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	261	ALA	0	-0.017	-0.026	15.573	0.010	0.010	0.000	0.000	0.000	0.000
122	A	262	ILE	0	0.029	0.021	15.865	0.002	0.002	0.000	0.000	0.000	0.000
123	A	263	ALA	0	-0.003	0.009	18.026	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	264	THR	0	0.006	-0.021	20.142	0.000	0.000	0.000	0.000	0.000	0.000
125	A	265	PRO	0	-0.007	0.004	22.785	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	266	LEU	0	-0.036	-0.016	25.535	0.004	0.004	0.000	0.000	0.000	0.000

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