FMO DATABASE

FMODB ID: 39Q4L

Calculation Name: 3HBW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3HBW

Chain ID: A

ChEMBL ID:

UniProt ID: Q92913

Base Structure: X-ray

Registration Date: 2023-06-21

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	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1499353.390545
FMO2-HF: Nuclear repulsion	1439746.495992
FMO2-HF: Total energy	-59606.894553
FMO2-MP2: Total energy	-59781.313798

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:64:PRO)

Summations of interaction energy for fragment #1(A:64:PRO)

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.
-5.704	-12.223	24.048	-8.25	-9.28	-0.023

Interaction energy analysis for fragmet #1(A:64:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.016 / q_NPA : -0.034

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	66	LEU	0	0.037	0.042	3.809	-3.222	-0.030	-0.028	-1.611	-1.554	-0.001
4	A	67	LYS	1	0.949	0.967	6.044	-1.229	-1.229	0.000	0.000	0.000	0.000
5	A	68	GLY	0	0.026	0.000	9.729	-0.012	-0.012	0.000	0.000	0.000	0.000
6	A	69	ILE	0	-0.071	-0.034	11.606	-0.070	-0.070	0.000	0.000	0.000	0.000
7	A	70	VAL	0	0.041	0.034	14.845	-0.007	-0.007	0.000	0.000	0.000	0.000
8	A	71	THR	0	0.000	-0.025	16.526	-0.022	-0.022	0.000	0.000	0.000	0.000
9	A	72	LYS	1	0.947	0.993	19.766	-0.131	-0.131	0.000	0.000	0.000	0.000
10	A	73	LEU	0	-0.008	-0.006	20.062	0.009	0.009	0.000	0.000	0.000	0.000
11	A	74	TYR	0	0.030	0.017	24.084	-0.013	-0.013	0.000	0.000	0.000	0.000
12	A	75	SER	0	0.045	0.035	27.833	0.000	0.000	0.000	0.000	0.000	0.000
13	A	76	ARG	1	0.757	0.833	29.483	-0.088	-0.088	0.000	0.000	0.000	0.000
14	A	77	GLN	0	-0.124	-0.079	32.229	-0.008	-0.008	0.000	0.000	0.000	0.000
15	A	78	GLY	0	-0.003	0.009	33.272	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	79	TYR	0	-0.003	0.023	31.648	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	80	HIS	0	0.017	0.026	27.290	0.013	0.013	0.000	0.000	0.000	0.000
18	A	81	LEU	0	-0.018	-0.010	22.363	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	82	GLN	0	-0.023	-0.037	24.817	0.012	0.012	0.000	0.000	0.000	0.000
20	A	83	LEU	0	-0.041	-0.008	19.435	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	84	GLN	0	0.002	-0.004	23.291	0.007	0.007	0.000	0.000	0.000	0.000
22	A	85	ALA	0	-0.005	-0.017	23.857	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	86	ASP	-1	-0.813	-0.865	24.739	0.047	0.047	0.000	0.000	0.000	0.000
24	A	87	GLY	0	0.008	-0.004	23.844	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	88	THR	0	-0.085	-0.066	24.883	0.002	0.002	0.000	0.000	0.000	0.000
26	A	89	ILE	0	-0.061	-0.039	23.356	0.009	0.009	0.000	0.000	0.000	0.000
27	A	90	ASP	-1	-0.857	-0.917	26.616	0.064	0.064	0.000	0.000	0.000	0.000
28	A	91	GLY	0	0.022	0.002	27.942	0.011	0.011	0.000	0.000	0.000	0.000
29	A	92	THR	0	0.048	0.028	29.016	-0.007	-0.007	0.000	0.000	0.000	0.000
30	A	93	LYS	1	0.913	0.934	31.349	-0.054	-0.054	0.000	0.000	0.000	0.000
31	A	94	ASP	-1	-0.874	-0.916	31.537	0.076	0.076	0.000	0.000	0.000	0.000
32	A	95	GLU	-1	-0.844	-0.926	28.635	0.119	0.119	0.000	0.000	0.000	0.000
33	A	96	ASP	-1	-0.906	-0.946	28.187	0.102	0.102	0.000	0.000	0.000	0.000
34	A	97	SER	0	-0.010	0.015	27.676	0.003	0.003	0.000	0.000	0.000	0.000
35	A	98	THR	0	-0.014	-0.030	23.541	0.008	0.008	0.000	0.000	0.000	0.000
36	A	99	TYR	0	-0.013	-0.012	22.692	0.013	0.013	0.000	0.000	0.000	0.000
37	A	100	THR	0	-0.015	-0.002	23.521	0.007	0.007	0.000	0.000	0.000	0.000
38	A	101	LEU	0	-0.054	-0.017	19.597	0.017	0.017	0.000	0.000	0.000	0.000
39	A	102	PHE	0	0.014	-0.003	17.497	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	103	ASN	0	-0.026	-0.004	12.059	0.026	0.026	0.000	0.000	0.000	0.000
41	A	104	LEU	0	-0.005	-0.003	14.065	-0.017	-0.017	0.000	0.000	0.000	0.000
42	A	105	ILE	0	-0.006	-0.011	7.427	0.079	0.079	0.000	0.000	0.000	0.000
43	A	106	PRO	0	0.005	0.012	8.856	-0.129	-0.129	0.000	0.000	0.000	0.000
44	A	107	VAL	0	0.042	0.011	7.341	0.297	0.297	0.000	0.000	0.000	0.000
45	A	108	GLY	0	0.036	0.002	8.953	-0.213	-0.213	0.000	0.000	0.000	0.000
46	A	109	LEU	0	-0.001	-0.005	11.479	0.074	0.074	0.000	0.000	0.000	0.000
47	A	110	ARG	1	0.875	0.929	14.544	-0.341	-0.341	0.000	0.000	0.000	0.000
48	A	111	VAL	0	0.003	0.014	13.156	-0.063	-0.063	0.000	0.000	0.000	0.000
49	A	112	VAL	0	-0.036	-0.015	12.289	0.093	0.093	0.000	0.000	0.000	0.000
50	A	113	ALA	0	0.039	0.038	10.976	-0.082	-0.082	0.000	0.000	0.000	0.000
51	A	114	ILE	0	-0.005	-0.014	12.822	0.059	0.059	0.000	0.000	0.000	0.000
52	A	115	GLN	0	0.013	0.011	11.565	0.017	0.017	0.000	0.000	0.000	0.000
53	A	116	GLY	0	0.083	0.057	15.178	0.023	0.023	0.000	0.000	0.000	0.000
54	A	117	VAL	0	-0.055	-0.032	15.658	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	118	GLN	0	0.029	0.014	16.906	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	119	THR	0	0.060	0.031	19.343	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	120	LYS	1	0.839	0.927	13.376	-0.205	-0.205	0.000	0.000	0.000	0.000
58	A	121	LEU	0	0.053	0.042	14.808	0.002	0.002	0.000	0.000	0.000	0.000
59	A	122	TYR	0	-0.027	-0.028	10.250	0.070	0.070	0.000	0.000	0.000	0.000
60	A	123	LEU	0	0.014	0.019	16.363	-0.026	-0.026	0.000	0.000	0.000	0.000
61	A	124	ALA	0	0.020	0.001	17.760	0.010	0.010	0.000	0.000	0.000	0.000
62	A	125	MET	0	-0.065	-0.011	19.911	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	126	ASN	0	0.074	0.034	22.479	0.000	0.000	0.000	0.000	0.000	0.000
64	A	127	SER	0	0.037	0.007	24.699	0.007	0.007	0.000	0.000	0.000	0.000
65	A	128	GLU	-1	-0.882	-0.929	26.976	0.009	0.009	0.000	0.000	0.000	0.000
66	A	129	GLY	0	-0.032	-0.030	27.530	0.003	0.003	0.000	0.000	0.000	0.000
67	A	130	TYR	0	0.002	-0.002	28.015	0.009	0.009	0.000	0.000	0.000	0.000
68	A	131	LEU	0	-0.015	-0.014	23.948	0.000	0.000	0.000	0.000	0.000	0.000
69	A	132	TYR	0	-0.040	-0.045	21.028	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	133	THR	0	0.036	0.016	20.774	0.011	0.011	0.000	0.000	0.000	0.000
71	A	134	SER	0	-0.043	-0.039	16.856	-0.018	-0.018	0.000	0.000	0.000	0.000
72	A	135	GLU	-1	-0.885	-0.942	16.895	0.014	0.014	0.000	0.000	0.000	0.000
73	A	136	LEU	0	-0.017	-0.005	13.865	0.005	0.005	0.000	0.000	0.000	0.000
74	A	137	PHE	0	0.029	0.015	9.049	0.060	0.060	0.000	0.000	0.000	0.000
75	A	138	THR	0	0.102	0.027	12.598	-0.054	-0.054	0.000	0.000	0.000	0.000
76	A	139	PRO	0	0.049	0.005	14.557	0.041	0.041	0.000	0.000	0.000	0.000
77	A	140	GLU	-1	-0.802	-0.851	16.023	0.025	0.025	0.000	0.000	0.000	0.000
78	A	141	CYS	0	-0.036	0.018	14.167	0.015	0.015	0.000	0.000	0.000	0.000
79	A	142	LYS	1	0.849	0.943	10.329	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	143	PHE	0	-0.016	-0.008	15.220	-0.029	-0.029	0.000	0.000	0.000	0.000
81	A	144	LYS	1	0.940	0.969	16.668	-0.074	-0.074	0.000	0.000	0.000	0.000
82	A	145	GLU	-1	-0.819	-0.900	16.774	0.316	0.316	0.000	0.000	0.000	0.000
83	A	146	SER	0	-0.108	-0.075	19.564	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	147	VAL	0	0.055	0.038	22.985	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	148	PHE	0	-0.053	-0.054	25.116	-0.014	-0.014	0.000	0.000	0.000	0.000
86	A	149	GLU	-1	-0.783	-0.871	28.650	0.083	0.083	0.000	0.000	0.000	0.000
87	A	150	ASN	0	-0.012	0.001	29.109	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	151	TYR	0	0.024	0.011	27.907	0.011	0.011	0.000	0.000	0.000	0.000
89	A	152	TYR	0	0.014	0.012	27.131	0.007	0.007	0.000	0.000	0.000	0.000
90	A	153	VAL	0	-0.019	0.005	21.926	0.004	0.004	0.000	0.000	0.000	0.000
91	A	154	THR	0	-0.081	-0.035	23.839	-0.014	-0.014	0.000	0.000	0.000	0.000
92	A	155	TYR	0	0.095	0.039	18.272	0.002	0.002	0.000	0.000	0.000	0.000
93	A	156	SER	0	-0.041	-0.029	21.221	-0.019	-0.019	0.000	0.000	0.000	0.000
94	A	157	SER	0	0.068	0.042	20.514	0.011	0.011	0.000	0.000	0.000	0.000
95	A	158	MET	0	0.008	0.003	16.306	0.007	0.007	0.000	0.000	0.000	0.000
96	A	159	ILE	0	-0.010	-0.001	19.157	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	160	TYR	0	-0.066	-0.035	21.915	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	161	ARG	1	0.841	0.908	22.761	-0.023	-0.023	0.000	0.000	0.000	0.000
99	A	162	GLN	0	-0.061	-0.026	28.032	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	163	GLN	0	0.088	0.036	31.850	0.003	0.003	0.000	0.000	0.000	0.000
101	A	164	GLN	0	0.021	0.022	33.293	0.001	0.001	0.000	0.000	0.000	0.000
102	A	165	SER	0	0.029	0.005	34.774	0.000	0.000	0.000	0.000	0.000	0.000
103	A	166	GLY	0	0.059	0.042	30.795	0.002	0.002	0.000	0.000	0.000	0.000
104	A	167	ARG	1	0.798	0.888	29.556	-0.038	-0.038	0.000	0.000	0.000	0.000
105	A	168	GLY	0	0.027	0.014	26.965	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	169	TRP	0	-0.045	-0.026	26.045	0.000	0.000	0.000	0.000	0.000	0.000
107	A	170	TYR	0	-0.032	-0.037	25.061	0.003	0.003	0.000	0.000	0.000	0.000
108	A	171	LEU	0	0.085	0.060	21.834	-0.009	-0.009	0.000	0.000	0.000	0.000
109	A	172	GLY	0	-0.008	-0.027	25.218	0.004	0.004	0.000	0.000	0.000	0.000
110	A	173	LEU	0	0.006	0.032	28.184	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	174	ASN	0	0.015	-0.026	30.883	0.003	0.003	0.000	0.000	0.000	0.000
112	A	175	LYS	1	0.931	0.944	34.622	-0.046	-0.046	0.000	0.000	0.000	0.000
113	A	176	GLU	-1	-0.898	-0.938	36.950	0.046	0.046	0.000	0.000	0.000	0.000
114	A	177	GLY	0	-0.027	-0.005	33.100	0.001	0.001	0.000	0.000	0.000	0.000
115	A	178	GLU	-1	-0.803	-0.885	32.452	0.046	0.046	0.000	0.000	0.000	0.000
116	A	179	ILE	0	-0.016	-0.017	26.059	0.003	0.003	0.000	0.000	0.000	0.000
117	A	180	MET	0	-0.063	-0.020	29.898	-0.005	-0.005	0.000	0.000	0.000	0.000
118	A	181	LYS	1	0.895	0.965	29.280	-0.022	-0.022	0.000	0.000	0.000	0.000
119	A	182	GLY	0	0.113	0.035	27.487	0.002	0.002	0.000	0.000	0.000	0.000
120	A	183	ASN	0	-0.022	-0.012	28.351	0.005	0.005	0.000	0.000	0.000	0.000
121	A	184	HIS	0	-0.038	-0.022	31.135	-0.005	-0.005	0.000	0.000	0.000	0.000
122	A	185	VAL	0	-0.017	0.020	28.906	0.000	0.000	0.000	0.000	0.000	0.000
123	A	186	LYS	1	0.934	0.958	30.529	-0.043	-0.043	0.000	0.000	0.000	0.000
124	A	187	LYS	1	1.016	1.008	27.840	-0.081	-0.081	0.000	0.000	0.000	0.000
125	A	188	ASN	0	0.027	0.029	30.299	0.004	0.004	0.000	0.000	0.000	0.000
126	A	189	LYS	1	0.862	0.919	32.925	-0.060	-0.060	0.000	0.000	0.000	0.000
127	A	190	PRO	0	0.099	0.033	32.291	0.004	0.004	0.000	0.000	0.000	0.000
128	A	191	ALA	0	0.011	0.019	31.797	0.005	0.005	0.000	0.000	0.000	0.000
129	A	192	ALA	0	-0.015	-0.006	28.223	0.004	0.004	0.000	0.000	0.000	0.000
130	A	193	HIS	0	-0.083	-0.019	27.198	0.009	0.009	0.000	0.000	0.000	0.000
131	A	194	PHE	0	0.036	0.019	24.687	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	195	LEU	0	0.031	0.010	26.016	0.007	0.007	0.000	0.000	0.000	0.000
133	A	196	PRO	0	-0.022	-0.009	21.938	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	197	LYS	1	0.814	0.889	23.680	-0.122	-0.122	0.000	0.000	0.000	0.000
135	A	198	PRO	0	-0.021	-0.024	20.241	0.003	0.003	0.000	0.000	0.000	0.000
136	A	199	LEU	0	-0.004	0.015	19.867	-0.016	-0.016	0.000	0.000	0.000	0.000
137	A	200	LYS	1	0.975	0.971	15.984	-0.273	-0.273	0.000	0.000	0.000	0.000
138	A	201	VAL	0	-0.004	0.012	13.844	0.028	0.028	0.000	0.000	0.000	0.000
139	A	202	ALA	0	-0.037	-0.022	11.986	-0.056	-0.056	0.000	0.000	0.000	0.000
140	A	203	MET	0	-0.009	0.007	7.321	0.045	0.045	0.000	0.000	0.000	0.000
141	A	204	TYR	0	-0.026	-0.033	6.217	-0.311	-0.311	0.000	0.000	0.000	0.000
142	A	205	LYS	1	1.016	1.015	2.094	1.459	-0.097	5.380	-1.880	-1.944	0.005
143	A	206	GLU	-1	-0.988	-0.986	1.779	-1.026	-8.716	18.682	-5.563	-5.429	-0.027
144	A	207	PRO	0	-0.028	-0.013	3.047	-0.605	-1.070	0.014	0.804	-0.353	0.000
145	A	208	SER	0	0.005	0.006	6.444	-0.278	-0.278	0.000	0.000	0.000	0.000
146	A	209	LEU	0	-0.054	-0.025	7.915	0.171	0.171	0.000	0.000	0.000	0.000
147	A	210	HIS	0	-0.008	-0.002	10.391	-0.053	-0.053	0.000	0.000	0.000	0.000
148	A	211	ASP	-1	-0.896	-0.955	13.996	-0.159	-0.159	0.000	0.000	0.000	0.000
149	A	212	LEU	0	-0.039	-0.015	17.101	0.011	0.011	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:64:PRO)