FMO DATABASE

FMODB ID: Q1GZY

Calculation Name: 4UF3-A-Xray372

Preferred Name: Bcl-2-like protein 11

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 4UF3

Chain ID: A

ChEMBL ID: CHEMBL5777

UniProt ID: O43521

Base Structure: X-ray

Registration Date: 2023-06-19

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	OptAll
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	136
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1190263.684331
FMO2-HF: Nuclear repulsion	1135016.944627
FMO2-HF: Total energy	-55246.739705
FMO2-MP2: Total energy	-55408.341243

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:3:ALA)

Summations of interaction energy for fragment #1(A:3:ALA)

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.
-2.786	-0.578	0.078	-1.016	-1.269	0.002

Interaction energy analysis for fragmet #1(A:3:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.007 / 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

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	5	ILE	0	0.037	0.006	2.960	-0.819	1.389	0.078	-1.016	-1.269	0.002
4	A	6	GLU	-1	-0.870	-0.937	5.693	-2.453	-2.453	0.000	0.000	0.000	0.000
5	A	7	PHE	0	-0.005	-0.004	8.743	0.441	0.441	0.000	0.000	0.000	0.000
6	A	8	ASP	-1	-0.848	-0.910	7.770	-0.937	-0.937	0.000	0.000	0.000	0.000
7	A	9	GLU	-1	-0.833	-0.922	10.259	-0.546	-0.546	0.000	0.000	0.000	0.000
8	A	10	ILE	0	-0.024	0.002	13.464	0.122	0.122	0.000	0.000	0.000	0.000
9	A	11	VAL	0	0.021	0.008	11.847	0.105	0.105	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.804	0.885	10.244	0.848	0.848	0.000	0.000	0.000	0.000
11	A	13	LYS	1	0.846	0.914	15.942	0.415	0.415	0.000	0.000	0.000	0.000
12	A	14	LEU	0	0.012	-0.001	17.457	0.050	0.050	0.000	0.000	0.000	0.000
13	A	15	LEU	0	0.005	0.002	15.949	0.044	0.044	0.000	0.000	0.000	0.000
14	A	16	ASN	0	-0.046	-0.030	19.188	0.058	0.058	0.000	0.000	0.000	0.000
15	A	17	ILE	0	0.006	0.011	22.019	0.028	0.028	0.000	0.000	0.000	0.000
16	A	18	TYR	0	0.021	0.010	22.456	0.022	0.022	0.000	0.000	0.000	0.000
17	A	19	ILE	0	0.027	0.007	22.695	0.019	0.019	0.000	0.000	0.000	0.000
18	A	20	ASN	0	-0.014	-0.018	25.351	0.026	0.026	0.000	0.000	0.000	0.000
19	A	21	ASP	-1	-0.908	-0.933	27.667	-0.120	-0.120	0.000	0.000	0.000	0.000
20	A	22	ILE	0	-0.009	0.002	26.824	0.013	0.013	0.000	0.000	0.000	0.000
21	A	23	CYS	0	-0.068	-0.027	28.733	0.012	0.012	0.000	0.000	0.000	0.000
22	A	24	THR	0	0.032	0.002	31.460	0.008	0.008	0.000	0.000	0.000	0.000
23	A	25	THR	0	-0.053	-0.037	32.419	0.009	0.009	0.000	0.000	0.000	0.000
24	A	26	GLY	0	-0.052	-0.029	33.711	0.007	0.007	0.000	0.000	0.000	0.000
25	A	27	GLU	-1	-0.899	-0.968	34.260	-0.084	-0.084	0.000	0.000	0.000	0.000
26	A	28	LYS	1	0.930	0.956	36.169	0.101	0.101	0.000	0.000	0.000	0.000
27	A	29	ARG	1	0.896	0.957	33.968	0.074	0.074	0.000	0.000	0.000	0.000
28	A	30	LEU	0	0.005	-0.001	38.619	0.004	0.004	0.000	0.000	0.000	0.000
29	A	31	LEU	0	0.005	0.042	41.737	0.003	0.003	0.000	0.000	0.000	0.000
30	A	32	ASN	0	0.002	-0.025	44.170	0.002	0.002	0.000	0.000	0.000	0.000
31	A	33	ASN	0	0.008	-0.018	47.283	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	34	TYR	0	0.031	0.028	48.868	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	35	GLU	-1	-0.766	-0.860	46.230	-0.051	-0.051	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.817	0.913	42.762	0.052	0.052	0.000	0.000	0.000	0.000
35	A	37	SER	0	-0.054	-0.032	45.914	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	38	ILE	0	0.046	0.016	48.729	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	39	LEU	0	0.017	0.009	40.822	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	40	ASP	-1	-0.826	-0.894	44.782	-0.071	-0.071	0.000	0.000	0.000	0.000
39	A	41	ARG	1	0.824	0.903	45.863	0.049	0.049	0.000	0.000	0.000	0.000
40	A	42	ILE	0	0.029	0.026	44.411	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	43	TYR	0	0.019	0.012	37.741	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	44	LYS	1	0.809	0.877	43.989	0.066	0.066	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.017	-0.014	46.678	0.001	0.001	0.000	0.000	0.000	0.000
44	A	46	CYS	0	-0.040	-0.023	43.680	0.000	0.000	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.873	-0.940	41.183	-0.101	-0.101	0.000	0.000	0.000	0.000
46	A	48	TYR	0	-0.074	-0.027	44.549	0.000	0.000	0.000	0.000	0.000	0.000
47	A	49	ILE	0	0.016	0.002	47.795	0.000	0.000	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.797	0.883	39.487	0.107	0.107	0.000	0.000	0.000	0.000
49	A	51	LYS	1	0.930	0.976	44.761	0.082	0.082	0.000	0.000	0.000	0.000
50	A	52	ASN	0	-0.078	-0.043	46.440	0.003	0.003	0.000	0.000	0.000	0.000
51	A	53	TYR	0	0.007	0.014	48.421	0.003	0.003	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.903	-0.932	42.407	-0.104	-0.104	0.000	0.000	0.000	0.000
53	A	55	LEU	0	0.004	-0.010	44.916	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	56	ASP	-1	-0.867	-0.923	46.825	-0.075	-0.075	0.000	0.000	0.000	0.000
55	A	57	PHE	0	0.041	-0.005	43.888	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	58	ASN	0	0.009	0.009	40.775	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	59	SER	0	-0.045	-0.030	42.931	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	60	MET	0	-0.032	-0.015	45.232	0.000	0.000	0.000	0.000	0.000	0.000
59	A	61	TYR	0	-0.010	-0.017	35.052	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	62	ASN	0	-0.016	-0.029	40.430	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	63	GLN	0	-0.050	-0.008	41.411	0.000	0.000	0.000	0.000	0.000	0.000
62	A	64	ILE	0	-0.020	-0.004	39.366	0.000	0.000	0.000	0.000	0.000	0.000
63	A	65	ASN	0	-0.011	-0.006	35.019	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	66	ILE	0	0.003	0.018	36.385	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	67	ASN	0	-0.048	-0.049	33.167	0.004	0.004	0.000	0.000	0.000	0.000
66	A	68	ASP	-1	-0.965	-0.961	36.433	-0.088	-0.088	0.000	0.000	0.000	0.000
67	A	69	ILE	0	0.015	0.018	38.993	0.004	0.004	0.000	0.000	0.000	0.000
68	A	70	THR	0	-0.008	-0.031	38.106	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	71	THR	0	-0.017	-0.043	35.193	0.002	0.002	0.000	0.000	0.000	0.000
70	A	72	SER	0	0.022	0.012	38.468	0.003	0.003	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.851	-0.878	41.981	-0.074	-0.074	0.000	0.000	0.000	0.000
72	A	74	ILE	0	0.000	0.001	37.770	0.002	0.002	0.000	0.000	0.000	0.000
73	A	75	LYS	1	0.798	0.906	40.149	0.079	0.079	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.026	-0.023	43.329	0.003	0.003	0.000	0.000	0.000	0.000
75	A	77	LYS	1	0.872	0.899	45.302	0.069	0.069	0.000	0.000	0.000	0.000
76	A	78	ILE	0	-0.039	-0.009	41.806	0.001	0.001	0.000	0.000	0.000	0.000
77	A	79	ILE	0	-0.033	-0.020	46.167	0.002	0.002	0.000	0.000	0.000	0.000
78	A	80	GLU	-1	-0.804	-0.888	48.622	-0.060	-0.060	0.000	0.000	0.000	0.000
79	A	81	ALA	0	0.002	0.010	50.945	0.003	0.003	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.024	0.001	48.588	0.003	0.003	0.000	0.000	0.000	0.000
81	A	83	LEU	0	-0.081	-0.037	51.931	0.003	0.003	0.000	0.000	0.000	0.000
82	A	84	ILE	0	-0.033	-0.014	54.419	0.002	0.002	0.000	0.000	0.000	0.000
83	A	85	ASP	-1	-0.807	-0.865	56.074	-0.046	-0.046	0.000	0.000	0.000	0.000
84	A	86	SER	0	0.000	-0.004	54.908	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	87	ARG	1	0.862	0.895	55.709	0.047	0.047	0.000	0.000	0.000	0.000
86	A	88	PRO	0	0.024	0.015	54.087	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	89	SER	0	0.039	0.011	53.036	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	90	VAL	0	0.044	0.033	52.322	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	91	LYS	1	0.819	0.930	50.151	0.047	0.047	0.000	0.000	0.000	0.000
90	A	92	LEU	0	0.010	0.018	47.991	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	93	ALA	0	0.010	0.017	47.832	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	94	THR	0	0.013	-0.012	45.972	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	95	LEU	0	-0.005	-0.007	42.777	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	96	SER	0	0.009	-0.021	43.040	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	97	PHE	0	0.006	0.012	42.884	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	98	ILE	0	0.013	0.000	39.484	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	99	SER	0	-0.041	-0.013	38.854	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	100	LEU	0	0.055	0.022	37.988	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	101	ILE	0	-0.017	-0.016	36.416	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	102	ALA	0	-0.038	-0.030	34.495	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	103	GLU	-1	-0.895	-0.929	33.189	-0.130	-0.130	0.000	0.000	0.000	0.000
102	A	104	LYS	1	0.896	0.955	33.204	0.115	0.115	0.000	0.000	0.000	0.000
103	A	105	TRP	0	-0.044	-0.030	31.340	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	106	GLY	0	0.041	0.024	28.981	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.845	-0.901	23.650	-0.327	-0.327	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.852	0.947	25.155	0.148	0.148	0.000	0.000	0.000	0.000
107	A	109	ASN	0	0.025	0.011	24.774	0.011	0.011	0.000	0.000	0.000	0.000
108	A	110	ARG	1	1.040	1.019	26.663	0.154	0.154	0.000	0.000	0.000	0.000
109	A	111	ALA	0	0.027	0.009	28.663	0.011	0.011	0.000	0.000	0.000	0.000
110	A	112	LYS	1	0.839	0.903	29.373	0.144	0.144	0.000	0.000	0.000	0.000
111	A	113	ILE	0	0.024	0.030	31.451	0.007	0.007	0.000	0.000	0.000	0.000
112	A	114	MET	0	-0.004	-0.011	32.942	0.007	0.007	0.000	0.000	0.000	0.000
113	A	115	GLU	-1	-0.793	-0.869	33.221	-0.108	-0.108	0.000	0.000	0.000	0.000
114	A	116	ILE	0	-0.001	0.004	36.177	0.006	0.006	0.000	0.000	0.000	0.000
115	A	117	LEU	0	0.017	0.007	38.131	0.005	0.005	0.000	0.000	0.000	0.000
116	A	118	SER	0	-0.010	-0.033	37.393	0.006	0.006	0.000	0.000	0.000	0.000
117	A	119	ASN	0	-0.035	-0.031	40.085	0.002	0.002	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.776	-0.880	42.980	-0.068	-0.068	0.000	0.000	0.000	0.000
119	A	121	ILE	0	-0.018	0.007	43.218	0.003	0.003	0.000	0.000	0.000	0.000
120	A	122	VAL	0	0.040	0.014	42.321	0.002	0.002	0.000	0.000	0.000	0.000
121	A	123	GLU	-1	-0.894	-0.930	44.934	-0.050	-0.050	0.000	0.000	0.000	0.000
122	A	124	LYS	1	0.892	0.958	47.721	0.051	0.051	0.000	0.000	0.000	0.000
123	A	125	ILE	0	-0.013	-0.016	45.666	0.002	0.002	0.000	0.000	0.000	0.000
124	A	126	SER	0	0.007	-0.006	47.467	0.002	0.002	0.000	0.000	0.000	0.000
125	A	127	ASN	0	-0.064	-0.030	50.143	0.003	0.003	0.000	0.000	0.000	0.000
126	A	128	ASN	0	-0.041	-0.031	53.433	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	129	GLY	0	0.074	0.033	52.452	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	130	LYS	1	0.801	0.892	53.191	0.036	0.036	0.000	0.000	0.000	0.000
129	A	131	ASP	-1	-0.765	-0.876	56.161	-0.039	-0.039	0.000	0.000	0.000	0.000
130	A	132	PHE	0	-0.059	-0.034	48.714	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	133	ILE	0	0.022	0.012	51.308	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	134	ASP	-1	-0.819	-0.896	53.926	-0.040	-0.040	0.000	0.000	0.000	0.000
133	A	135	PHE	0	-0.023	-0.011	53.448	0.000	0.000	0.000	0.000	0.000	0.000
134	A	136	ILE	0	0.008	0.021	50.084	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	137	ASP	-1	-0.837	-0.894	53.416	-0.048	-0.048	0.000	0.000	0.000	0.000
136	A	138	ARG	1	0.799	0.886	55.108	0.046	0.046	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:ALA)