FMO DATABASE

FMODB ID: 1643Z

Calculation Name: 3ILC-A-Xray372

Preferred Name: Bcl-2-like protein 1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3ILC

Chain ID: A

ChEMBL ID: CHEMBL3309112

UniProt ID: Q64373

Base Structure: X-ray

Registration Date: 2023-09-26

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	144
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1416422.120659
FMO2-HF: Nuclear repulsion	1358492.923464
FMO2-HF: Total energy	-57929.197196
FMO2-MP2: Total energy	-58098.48464

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:0:HIS)

Summations of interaction energy for fragment #1(A:0:HIS)

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.
-16.093	-17.722	22.524	-7.221	-13.675	0.016

Interaction energy analysis for fragmet #1(A:0:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.031 / q_NPA : 0.012

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	2	SER	0	-0.009	-0.015	2.100	-14.698	-15.403	14.921	-4.781	-9.435	0.022
4	A	3	GLN	0	-0.007	-0.007	1.649	-2.822	-4.053	7.580	-2.645	-3.705	-0.005
5	A	4	SER	0	0.026	0.005	3.316	-0.197	0.110	0.023	0.205	-0.535	-0.001
6	A	5	ASN	0	0.013	-0.005	5.538	-0.334	-0.334	0.000	0.000	0.000	0.000
7	A	6	ARG	1	0.930	0.968	6.318	-0.025	-0.025	0.000	0.000	0.000	0.000
8	A	7	GLU	-1	-0.952	-0.987	6.826	0.394	0.394	0.000	0.000	0.000	0.000
9	A	8	LEU	0	0.020	0.024	9.512	-0.067	-0.067	0.000	0.000	0.000	0.000
10	A	9	VAL	0	-0.046	-0.017	11.028	-0.090	-0.090	0.000	0.000	0.000	0.000
11	A	10	VAL	0	-0.028	-0.009	12.098	-0.047	-0.047	0.000	0.000	0.000	0.000
12	A	11	ASP	-1	-0.819	-0.881	13.510	0.314	0.314	0.000	0.000	0.000	0.000
13	A	12	PHE	0	0.046	0.017	15.306	-0.036	-0.036	0.000	0.000	0.000	0.000
14	A	13	LEU	0	0.007	-0.026	16.353	-0.027	-0.027	0.000	0.000	0.000	0.000
15	A	14	SER	0	-0.004	-0.009	17.399	-0.028	-0.028	0.000	0.000	0.000	0.000
16	A	15	TYR	0	-0.118	-0.090	19.508	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	16	LYS	1	0.797	0.879	21.226	-0.109	-0.109	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.011	-0.011	21.246	-0.012	-0.012	0.000	0.000	0.000	0.000
19	A	18	SER	0	-0.034	-0.008	23.763	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	19	GLN	0	-0.020	-0.006	25.392	-0.020	-0.020	0.000	0.000	0.000	0.000
21	A	20	LYS	1	0.863	0.935	27.162	-0.053	-0.053	0.000	0.000	0.000	0.000
22	A	21	GLY	0	0.023	0.029	28.948	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	22	TYR	0	-0.094	-0.076	26.551	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	23	SER	0	0.000	-0.002	25.887	0.016	0.016	0.000	0.000	0.000	0.000
25	A	24	TRP	0	0.044	0.009	20.825	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	25	SER	0	0.009	0.000	20.773	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	26	GLN	0	-0.058	-0.027	19.984	0.008	0.008	0.000	0.000	0.000	0.000
28	A	27	PHE	0	-0.049	-0.023	15.806	-0.050	-0.050	0.000	0.000	0.000	0.000
29	A	28	SER	0	0.011	0.017	14.831	0.036	0.036	0.000	0.000	0.000	0.000
30	A	82	PRO	0	0.113	0.050	11.956	0.075	0.075	0.000	0.000	0.000	0.000
31	A	83	MET	0	-0.013	-0.019	8.569	-0.194	-0.194	0.000	0.000	0.000	0.000
32	A	84	ALA	0	-0.019	-0.010	11.303	-0.115	-0.115	0.000	0.000	0.000	0.000
33	A	85	ALA	0	0.054	0.025	14.740	-0.079	-0.079	0.000	0.000	0.000	0.000
34	A	86	VAL	0	0.028	0.024	12.575	-0.063	-0.063	0.000	0.000	0.000	0.000
35	A	87	LYS	1	0.886	0.946	11.340	-0.638	-0.638	0.000	0.000	0.000	0.000
36	A	88	GLN	0	-0.068	-0.039	15.538	-0.059	-0.059	0.000	0.000	0.000	0.000
37	A	89	ALA	0	0.064	0.028	18.434	-0.047	-0.047	0.000	0.000	0.000	0.000
38	A	90	LEU	0	-0.030	-0.010	15.183	-0.053	-0.053	0.000	0.000	0.000	0.000
39	A	91	ARG	1	0.776	0.870	17.780	-0.338	-0.338	0.000	0.000	0.000	0.000
40	A	92	GLU	-1	-0.828	-0.883	20.860	0.270	0.270	0.000	0.000	0.000	0.000
41	A	93	ALA	0	-0.002	0.006	21.516	-0.031	-0.031	0.000	0.000	0.000	0.000
42	A	94	GLY	0	0.005	-0.012	22.376	-0.032	-0.032	0.000	0.000	0.000	0.000
43	A	95	ASP	-1	-0.754	-0.839	23.435	0.121	0.121	0.000	0.000	0.000	0.000
44	A	96	GLU	-1	-0.796	-0.859	26.535	0.115	0.115	0.000	0.000	0.000	0.000
45	A	97	PHE	0	0.016	-0.002	25.696	-0.023	-0.023	0.000	0.000	0.000	0.000
46	A	98	GLU	-1	-0.847	-0.904	24.961	0.051	0.051	0.000	0.000	0.000	0.000
47	A	99	LEU	0	-0.044	-0.027	28.899	-0.015	-0.015	0.000	0.000	0.000	0.000
48	A	100	ARG	1	0.764	0.859	28.541	-0.118	-0.118	0.000	0.000	0.000	0.000
49	A	101	ALA	0	-0.041	-0.024	30.242	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	102	ARG	1	0.914	0.968	31.995	-0.048	-0.048	0.000	0.000	0.000	0.000
51	A	103	ARG	1	0.906	0.991	29.391	0.027	0.027	0.000	0.000	0.000	0.000
52	A	104	ALA	0	0.062	0.025	30.366	0.001	0.001	0.000	0.000	0.000	0.000
53	A	105	PHE	0	-0.004	-0.028	25.477	-0.012	-0.012	0.000	0.000	0.000	0.000
54	A	106	SER	0	0.034	0.007	29.896	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	107	ASP	-1	-0.908	-0.946	31.419	-0.090	-0.090	0.000	0.000	0.000	0.000
56	A	108	LEU	0	0.058	0.027	25.566	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	109	THR	0	0.011	0.002	27.768	-0.024	-0.024	0.000	0.000	0.000	0.000
58	A	110	SER	0	-0.075	-0.020	29.450	-0.016	-0.016	0.000	0.000	0.000	0.000
59	A	111	GLN	0	-0.057	-0.065	28.810	0.004	0.004	0.000	0.000	0.000	0.000
60	A	112	LEU	0	-0.043	-0.017	23.945	-0.019	-0.019	0.000	0.000	0.000	0.000
61	A	113	HIS	1	0.823	0.914	27.979	0.186	0.186	0.000	0.000	0.000	0.000
62	A	114	ILE	0	-0.009	0.007	23.565	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	115	THR	0	0.097	0.032	27.579	0.012	0.012	0.000	0.000	0.000	0.000
64	A	116	PRO	0	-0.002	-0.018	25.968	-0.023	-0.023	0.000	0.000	0.000	0.000
65	A	117	GLY	0	0.021	0.016	26.040	-0.024	-0.024	0.000	0.000	0.000	0.000
66	A	118	THR	0	-0.028	0.001	23.577	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	119	ALA	0	0.048	0.025	21.641	-0.022	-0.022	0.000	0.000	0.000	0.000
68	A	120	TYR	0	0.051	0.012	14.402	0.048	0.048	0.000	0.000	0.000	0.000
69	A	121	GLN	0	0.035	0.013	19.076	0.049	0.049	0.000	0.000	0.000	0.000
70	A	122	SER	0	0.007	0.007	20.419	0.022	0.022	0.000	0.000	0.000	0.000
71	A	123	PHE	0	0.010	-0.001	16.948	0.033	0.033	0.000	0.000	0.000	0.000
72	A	124	GLU	-1	-0.876	-0.928	16.774	-0.674	-0.674	0.000	0.000	0.000	0.000
73	A	125	GLN	0	-0.019	-0.016	19.457	0.039	0.039	0.000	0.000	0.000	0.000
74	A	126	VAL	0	0.007	0.013	22.803	0.028	0.028	0.000	0.000	0.000	0.000
75	A	127	VAL	0	0.038	0.025	18.595	0.036	0.036	0.000	0.000	0.000	0.000
76	A	128	ASN	0	0.019	0.019	19.322	0.025	0.025	0.000	0.000	0.000	0.000
77	A	129	GLU	-1	-0.894	-0.918	21.473	-0.159	-0.159	0.000	0.000	0.000	0.000
78	A	130	LEU	0	-0.080	-0.042	21.477	0.028	0.028	0.000	0.000	0.000	0.000
79	A	131	PHE	0	-0.017	-0.015	18.484	0.039	0.039	0.000	0.000	0.000	0.000
80	A	132	ARG	1	0.968	1.000	21.905	0.090	0.090	0.000	0.000	0.000	0.000
81	A	133	ASP	-1	-0.943	-0.959	24.641	-0.073	-0.073	0.000	0.000	0.000	0.000
82	A	134	GLY	0	0.006	-0.001	20.651	0.021	0.021	0.000	0.000	0.000	0.000
83	A	135	VAL	0	-0.032	-0.009	15.911	0.011	0.011	0.000	0.000	0.000	0.000
84	A	136	ASN	0	0.014	0.011	19.139	0.019	0.019	0.000	0.000	0.000	0.000
85	A	137	TRP	0	0.118	0.044	15.486	-0.047	-0.047	0.000	0.000	0.000	0.000
86	A	138	GLY	0	0.032	0.027	20.291	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	139	ARG	1	0.857	0.927	21.037	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	140	ILE	0	0.042	0.028	15.734	-0.039	-0.039	0.000	0.000	0.000	0.000
89	A	141	VAL	0	0.007	0.007	18.685	-0.013	-0.013	0.000	0.000	0.000	0.000
90	A	142	ALA	0	-0.042	-0.013	20.804	-0.021	-0.021	0.000	0.000	0.000	0.000
91	A	143	PHE	0	0.006	-0.002	14.806	-0.039	-0.039	0.000	0.000	0.000	0.000
92	A	144	PHE	0	-0.003	-0.007	13.113	-0.032	-0.032	0.000	0.000	0.000	0.000
93	A	145	SER	0	-0.012	-0.024	18.836	-0.030	-0.030	0.000	0.000	0.000	0.000
94	A	146	PHE	0	-0.006	0.000	21.826	-0.020	-0.020	0.000	0.000	0.000	0.000
95	A	147	GLY	0	0.037	0.002	19.579	-0.025	-0.025	0.000	0.000	0.000	0.000
96	A	148	GLY	0	-0.002	-0.020	20.662	-0.012	-0.012	0.000	0.000	0.000	0.000
97	A	149	ALA	0	0.016	0.009	22.111	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	150	LEU	0	0.026	0.012	21.968	-0.016	-0.016	0.000	0.000	0.000	0.000
99	A	151	CYS	0	-0.097	-0.035	20.752	-0.021	-0.021	0.000	0.000	0.000	0.000
100	A	152	VAL	0	0.032	0.013	23.548	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	153	GLU	-1	-0.866	-0.937	26.853	-0.098	-0.098	0.000	0.000	0.000	0.000
102	A	154	SER	0	-0.073	-0.043	25.355	-0.014	-0.014	0.000	0.000	0.000	0.000
103	A	155	VAL	0	-0.058	-0.041	26.054	-0.007	-0.007	0.000	0.000	0.000	0.000
104	A	156	ASP	-1	-0.784	-0.852	28.618	-0.049	-0.049	0.000	0.000	0.000	0.000
105	A	157	LYS	1	0.788	0.913	29.880	0.148	0.148	0.000	0.000	0.000	0.000
106	A	158	GLU	-1	-0.918	-0.951	31.786	-0.098	-0.098	0.000	0.000	0.000	0.000
107	A	159	MET	0	-0.086	-0.035	28.050	-0.021	-0.021	0.000	0.000	0.000	0.000
108	A	160	GLN	0	0.072	0.024	25.687	-0.008	-0.008	0.000	0.000	0.000	0.000
109	A	161	VAL	0	-0.017	-0.015	24.345	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	162	LEU	0	-0.015	-0.006	22.591	-0.034	-0.034	0.000	0.000	0.000	0.000
111	A	163	VAL	0	0.030	0.028	20.076	-0.024	-0.024	0.000	0.000	0.000	0.000
112	A	164	SER	0	0.011	-0.003	17.630	-0.009	-0.009	0.000	0.000	0.000	0.000
113	A	165	ARG	1	0.904	0.948	16.666	0.323	0.323	0.000	0.000	0.000	0.000
114	A	166	ILE	0	0.024	0.020	17.290	-0.065	-0.065	0.000	0.000	0.000	0.000
115	A	167	ALA	0	0.049	0.020	14.291	-0.013	-0.013	0.000	0.000	0.000	0.000
116	A	168	SER	0	-0.103	-0.056	12.696	-0.040	-0.040	0.000	0.000	0.000	0.000
117	A	169	TRP	0	0.036	0.013	12.966	-0.084	-0.084	0.000	0.000	0.000	0.000
118	A	170	MET	0	0.022	0.036	14.453	-0.065	-0.065	0.000	0.000	0.000	0.000
119	A	171	ALA	0	0.016	0.011	8.931	0.048	0.048	0.000	0.000	0.000	0.000
120	A	172	THR	0	-0.043	-0.010	9.737	-0.136	-0.136	0.000	0.000	0.000	0.000
121	A	173	TYR	0	-0.004	-0.034	10.588	-0.131	-0.131	0.000	0.000	0.000	0.000
122	A	174	LEU	0	-0.017	0.001	10.116	-0.025	-0.025	0.000	0.000	0.000	0.000
123	A	175	ASN	0	-0.008	-0.028	6.364	1.010	1.010	0.000	0.000	0.000	0.000
124	A	176	ASP	-1	-0.965	-0.962	7.681	-1.640	-1.640	0.000	0.000	0.000	0.000
125	A	177	HIS	1	0.813	0.878	9.868	0.824	0.824	0.000	0.000	0.000	0.000
126	A	178	LEU	0	-0.027	0.001	11.582	0.086	0.086	0.000	0.000	0.000	0.000
127	A	179	GLU	-1	-0.777	-0.896	6.068	2.005	2.005	0.000	0.000	0.000	0.000
128	A	180	PRO	0	0.013	0.014	9.250	0.227	0.227	0.000	0.000	0.000	0.000
129	A	181	TRP	0	0.049	0.018	10.725	0.131	0.131	0.000	0.000	0.000	0.000
130	A	182	ILE	0	-0.001	-0.006	11.242	0.053	0.053	0.000	0.000	0.000	0.000
131	A	183	GLN	0	-0.065	-0.044	7.927	0.150	0.150	0.000	0.000	0.000	0.000
132	A	184	GLU	-1	-0.945	-0.952	11.319	0.222	0.222	0.000	0.000	0.000	0.000
133	A	185	ASN	0	-0.131	-0.068	14.318	-0.029	-0.029	0.000	0.000	0.000	0.000
134	A	186	GLY	0	0.024	0.014	15.122	-0.023	-0.023	0.000	0.000	0.000	0.000
135	A	187	GLY	0	0.025	0.015	12.374	0.151	0.151	0.000	0.000	0.000	0.000
136	A	188	TRP	0	-0.043	-0.065	9.995	-0.326	-0.326	0.000	0.000	0.000	0.000
137	A	189	ASP	-1	-0.882	-0.928	13.723	1.224	1.224	0.000	0.000	0.000	0.000
138	A	190	THR	0	0.047	0.024	15.844	-0.088	-0.088	0.000	0.000	0.000	0.000
139	A	191	PHE	0	-0.057	-0.028	16.544	-0.094	-0.094	0.000	0.000	0.000	0.000
140	A	192	VAL	0	-0.001	-0.026	16.425	-0.071	-0.071	0.000	0.000	0.000	0.000
141	A	193	ASP	-1	-0.889	-0.928	19.151	0.551	0.551	0.000	0.000	0.000	0.000
142	A	194	LEU	0	-0.163	-0.077	21.574	-0.064	-0.064	0.000	0.000	0.000	0.000
143	A	195	TYR	0	-0.070	-0.040	21.421	-0.056	-0.056	0.000	0.000	0.000	0.000
144	A	196	GLY	0	-0.023	0.011	21.396	-0.029	-0.029	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:HIS)