FMO DATABASE

FMODB ID: Z6Q5N

Calculation Name: 3IU5-A-Xray372

Preferred Name: Protein polybromo-1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3IU5

Chain ID: A

ChEMBL ID: CHEMBL1795184

UniProt ID: Q86U86

Base Structure: X-ray

Registration Date: 2023-09-20

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	114
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1007644.824164
FMO2-HF: Nuclear repulsion	959097.004449
FMO2-HF: Total energy	-48547.819715
FMO2-MP2: Total energy	-48687.620883

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:41:SER)

Summations of interaction energy for fragment #1(A:41:SER)

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.
-32.274	-31.902	29.809	-14.99	-15.194	-0.052

Interaction energy analysis for fragmet #1(A:41:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.011 / 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	43	THR	0	-0.067	-0.027	2.103	-10.889	-5.849	3.890	-4.696	-4.235	0.043
4	A	44	VAL	0	-0.018	-0.008	2.343	-9.207	-6.701	2.373	-2.100	-2.779	-0.021
5	A	45	ASP	-1	-0.805	-0.908	4.414	-0.368	-0.241	0.000	-0.029	-0.098	0.000
6	A	46	PRO	0	-0.019	-0.020	7.812	-0.033	-0.033	0.000	0.000	0.000	0.000
7	A	47	ILE	0	0.086	0.053	9.781	0.072	0.072	0.000	0.000	0.000	0.000
8	A	48	ALA	0	-0.001	0.015	8.866	0.115	0.115	0.000	0.000	0.000	0.000
9	A	49	VAL	0	-0.001	-0.005	6.019	0.093	0.093	0.000	0.000	0.000	0.000
10	A	50	CYS	0	-0.042	-0.022	9.104	0.150	0.150	0.000	0.000	0.000	0.000
11	A	51	HIS	0	-0.007	-0.016	12.404	0.200	0.200	0.000	0.000	0.000	0.000
12	A	52	GLU	-1	-0.851	-0.914	10.380	-0.362	-0.362	0.000	0.000	0.000	0.000
13	A	53	LEU	0	-0.038	-0.001	9.375	0.116	0.116	0.000	0.000	0.000	0.000
14	A	54	TYR	0	-0.017	-0.013	12.830	0.119	0.119	0.000	0.000	0.000	0.000
15	A	55	ASN	0	-0.008	-0.014	15.354	0.086	0.086	0.000	0.000	0.000	0.000
16	A	56	THR	0	-0.025	-0.019	13.559	0.068	0.068	0.000	0.000	0.000	0.000
17	A	57	ILE	0	-0.056	-0.028	15.989	0.054	0.054	0.000	0.000	0.000	0.000
18	A	58	ARG	1	0.733	0.823	18.559	0.309	0.309	0.000	0.000	0.000	0.000
19	A	59	ASP	-1	-0.774	-0.858	19.470	-0.190	-0.190	0.000	0.000	0.000	0.000
20	A	60	TYR	0	-0.019	0.006	19.113	0.026	0.026	0.000	0.000	0.000	0.000
21	A	61	LYS	1	0.888	0.937	20.984	0.103	0.103	0.000	0.000	0.000	0.000
22	A	62	ASP	-1	-0.778	-0.872	23.306	-0.106	-0.106	0.000	0.000	0.000	0.000
23	A	63	GLU	-1	-0.807	-0.909	25.073	-0.086	-0.086	0.000	0.000	0.000	0.000
24	A	64	GLN	0	-0.109	-0.047	27.153	0.011	0.011	0.000	0.000	0.000	0.000
25	A	65	GLY	0	0.020	0.021	28.060	0.004	0.004	0.000	0.000	0.000	0.000
26	A	66	ARG	1	0.833	0.893	28.517	0.099	0.099	0.000	0.000	0.000	0.000
27	A	67	LEU	0	0.034	0.021	24.384	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	68	LEU	0	0.006	-0.001	23.341	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	69	CYS	0	-0.012	-0.006	22.882	0.003	0.003	0.000	0.000	0.000	0.000
30	A	70	GLU	-1	-0.882	-0.946	24.881	-0.135	-0.135	0.000	0.000	0.000	0.000
31	A	71	LEU	0	-0.072	-0.034	28.300	0.006	0.006	0.000	0.000	0.000	0.000
32	A	72	PHE	0	-0.028	-0.016	25.341	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	73	ILE	0	0.025	0.017	26.884	-0.015	-0.015	0.000	0.000	0.000	0.000
34	A	74	ARG	1	0.912	0.945	28.286	0.150	0.150	0.000	0.000	0.000	0.000
35	A	75	ALA	0	0.019	0.030	30.316	0.005	0.005	0.000	0.000	0.000	0.000
36	A	76	PRO	0	0.027	0.016	31.889	0.010	0.010	0.000	0.000	0.000	0.000
37	A	77	LYS	1	0.964	0.993	35.446	0.112	0.112	0.000	0.000	0.000	0.000
38	A	78	ARG	1	0.959	0.964	34.681	0.168	0.168	0.000	0.000	0.000	0.000
39	A	79	ARG	1	0.915	0.955	39.004	0.118	0.118	0.000	0.000	0.000	0.000
40	A	80	ASN	0	-0.065	-0.041	40.890	0.002	0.002	0.000	0.000	0.000	0.000
41	A	81	GLN	0	0.031	0.013	38.485	0.003	0.003	0.000	0.000	0.000	0.000
42	A	82	PRO	0	0.059	0.027	39.853	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	83	ASP	-1	-0.816	-0.899	40.846	-0.104	-0.104	0.000	0.000	0.000	0.000
44	A	84	TYR	0	-0.026	-0.032	30.901	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	85	TYR	0	-0.101	-0.091	34.184	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	86	GLU	-1	-0.930	-0.937	37.832	-0.107	-0.107	0.000	0.000	0.000	0.000
47	A	87	VAL	0	-0.059	-0.029	35.048	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	88	VAL	0	-0.036	0.008	31.413	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	89	SER	0	0.025	0.005	32.644	0.004	0.004	0.000	0.000	0.000	0.000
50	A	90	GLN	0	-0.017	-0.012	28.643	0.016	0.016	0.000	0.000	0.000	0.000
51	A	91	PRO	0	-0.008	0.013	29.192	-0.014	-0.014	0.000	0.000	0.000	0.000
52	A	92	ILE	0	-0.001	0.001	23.443	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	93	ASP	-1	-0.794	-0.900	26.442	-0.212	-0.212	0.000	0.000	0.000	0.000
54	A	94	LEU	0	0.057	0.015	21.779	-0.020	-0.020	0.000	0.000	0.000	0.000
55	A	95	MET	0	-0.070	-0.022	24.483	-0.008	-0.008	0.000	0.000	0.000	0.000
56	A	96	LYS	1	0.853	0.928	25.761	0.272	0.272	0.000	0.000	0.000	0.000
57	A	97	ILE	0	0.062	0.026	19.762	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	98	GLN	0	0.018	0.008	21.600	-0.022	-0.022	0.000	0.000	0.000	0.000
59	A	99	GLN	0	-0.019	-0.003	22.933	-0.009	-0.009	0.000	0.000	0.000	0.000
60	A	100	LYS	1	0.836	0.902	21.326	0.425	0.425	0.000	0.000	0.000	0.000
61	A	101	LEU	0	-0.002	0.007	16.468	-0.012	-0.012	0.000	0.000	0.000	0.000
62	A	102	LYS	1	0.877	0.933	20.025	0.240	0.240	0.000	0.000	0.000	0.000
63	A	103	MET	0	-0.109	-0.034	22.555	0.021	0.021	0.000	0.000	0.000	0.000
64	A	104	GLU	-1	-0.930	-0.960	19.158	-0.359	-0.359	0.000	0.000	0.000	0.000
65	A	105	GLU	-1	-0.889	-0.957	19.275	-0.362	-0.362	0.000	0.000	0.000	0.000
66	A	106	TYR	0	-0.116	-0.095	15.414	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	107	ASP	-1	-0.864	-0.936	14.195	-0.701	-0.701	0.000	0.000	0.000	0.000
68	A	108	ASP	-1	-0.763	-0.880	12.792	-1.061	-1.061	0.000	0.000	0.000	0.000
69	A	109	VAL	0	0.026	0.002	8.191	0.082	0.082	0.000	0.000	0.000	0.000
70	A	110	ASN	0	-0.109	-0.067	11.627	0.108	0.108	0.000	0.000	0.000	0.000
71	A	111	LEU	0	0.043	0.033	14.207	0.105	0.105	0.000	0.000	0.000	0.000
72	A	112	LEU	0	0.008	0.023	13.343	0.074	0.074	0.000	0.000	0.000	0.000
73	A	113	THR	0	-0.063	-0.039	13.175	0.039	0.039	0.000	0.000	0.000	0.000
74	A	114	ALA	0	0.007	0.011	15.602	0.072	0.072	0.000	0.000	0.000	0.000
75	A	115	ASP	-1	-0.741	-0.823	18.958	-0.373	-0.373	0.000	0.000	0.000	0.000
76	A	116	PHE	0	0.020	-0.005	16.309	0.064	0.064	0.000	0.000	0.000	0.000
77	A	117	GLN	0	-0.028	-0.006	19.187	0.048	0.048	0.000	0.000	0.000	0.000
78	A	118	LEU	0	-0.010	0.004	20.687	0.042	0.042	0.000	0.000	0.000	0.000
79	A	119	LEU	0	-0.025	-0.003	22.170	0.033	0.033	0.000	0.000	0.000	0.000
80	A	120	PHE	0	0.023	-0.009	19.086	0.034	0.034	0.000	0.000	0.000	0.000
81	A	121	ASN	0	-0.014	-0.009	24.222	0.024	0.024	0.000	0.000	0.000	0.000
82	A	122	ASN	0	-0.004	0.002	26.019	0.028	0.028	0.000	0.000	0.000	0.000
83	A	123	ALA	0	-0.016	-0.002	27.459	0.019	0.019	0.000	0.000	0.000	0.000
84	A	124	LYS	1	0.850	0.902	25.289	0.248	0.248	0.000	0.000	0.000	0.000
85	A	125	SER	0	-0.004	0.003	29.523	0.010	0.010	0.000	0.000	0.000	0.000
86	A	126	TYR	0	-0.016	0.014	31.958	0.011	0.011	0.000	0.000	0.000	0.000
87	A	127	TYR	0	-0.059	-0.024	32.086	0.011	0.011	0.000	0.000	0.000	0.000
88	A	128	LYS	1	0.937	0.956	33.015	0.124	0.124	0.000	0.000	0.000	0.000
89	A	129	PRO	0	0.048	0.012	32.003	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	130	ASP	-1	-0.801	-0.899	32.488	-0.099	-0.099	0.000	0.000	0.000	0.000
91	A	131	SER	0	-0.057	-0.016	33.099	0.002	0.002	0.000	0.000	0.000	0.000
92	A	132	PRO	0	0.049	0.005	31.745	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	133	GLU	-1	-0.791	-0.896	29.724	-0.147	-0.147	0.000	0.000	0.000	0.000
94	A	134	TYR	0	0.032	0.027	28.287	-0.023	-0.023	0.000	0.000	0.000	0.000
95	A	135	LYS	1	0.810	0.894	27.387	0.095	0.095	0.000	0.000	0.000	0.000
96	A	136	ALA	0	0.002	0.005	25.731	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	137	ALA	0	0.023	0.013	23.913	-0.021	-0.021	0.000	0.000	0.000	0.000
98	A	138	CYS	0	-0.080	-0.031	22.583	-0.031	-0.031	0.000	0.000	0.000	0.000
99	A	139	LYS	1	0.878	0.933	21.504	0.115	0.115	0.000	0.000	0.000	0.000
100	A	140	LEU	0	0.027	0.013	19.748	-0.017	-0.017	0.000	0.000	0.000	0.000
101	A	141	TRP	0	0.012	0.013	16.931	-0.060	-0.060	0.000	0.000	0.000	0.000
102	A	142	ASP	-1	-0.820	-0.897	16.760	-0.367	-0.367	0.000	0.000	0.000	0.000
103	A	143	LEU	0	-0.010	0.003	15.433	-0.042	-0.042	0.000	0.000	0.000	0.000
104	A	144	TYR	0	0.023	0.000	13.072	-0.064	-0.064	0.000	0.000	0.000	0.000
105	A	145	LEU	0	-0.018	-0.005	12.163	-0.155	-0.155	0.000	0.000	0.000	0.000
106	A	146	ARG	1	0.809	0.881	10.964	0.108	0.108	0.000	0.000	0.000	0.000
107	A	147	THR	0	0.003	-0.003	9.927	0.016	0.016	0.000	0.000	0.000	0.000
108	A	148	ARG	1	0.916	0.948	8.057	1.185	1.185	0.000	0.000	0.000	0.000
109	A	149	ASN	0	-0.030	-0.026	6.358	-0.853	-0.853	0.000	0.000	0.000	0.000
110	A	150	GLU	-1	-0.881	-0.917	5.299	-0.189	-0.189	0.000	0.000	0.000	0.000
111	A	151	PHE	0	0.022	0.003	3.941	1.034	1.728	0.006	-0.278	-0.423	-0.001
112	A	152	VAL	0	-0.039	-0.017	1.940	-7.371	-9.576	8.633	-3.482	-2.947	-0.031
113	A	153	GLN	0	-0.089	-0.016	2.685	-1.318	-0.063	0.663	-0.502	-1.416	-0.001
114	A	154	LYS	1	0.983	0.989	1.795	-3.593	-10.638	14.244	-3.903	-3.296	-0.041

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Interactive mode: IFIE and PIEDA for fragment #1(A:41:SER)