FMO DATABASE

FMODB ID: R93N8

Calculation Name: 4B93-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4B93

Chain ID: A

ChEMBL ID:

UniProt ID: Q96NW4

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	157
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1618062.998078
FMO2-HF: Nuclear repulsion	1554935.127802
FMO2-HF: Total energy	-63127.870276
FMO2-MP2: Total energy	-63311.26099

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:SER)

Summations of interaction energy for fragment #1(A:0: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.
-9.71	-4.459	1.225	-2.582	-3.893	0.011

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / q_NPA : -0.016

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	ALA	0	0.081	0.050	3.805	-0.083	1.466	-0.012	-0.623	-0.914	0.003
4	A	3	ILE	0	-0.042	-0.012	4.653	1.305	1.411	-0.001	-0.006	-0.099	0.000
5	A	4	LEU	0	-0.038	-0.012	4.992	0.302	0.302	0.000	0.000	0.000	0.000
6	A	5	PHE	0	0.006	-0.024	8.099	0.181	0.181	0.000	0.000	0.000	0.000
7	A	6	ALA	0	-0.006	-0.005	11.838	-0.127	-0.127	0.000	0.000	0.000	0.000
8	A	7	VAL	0	0.000	-0.008	14.863	0.053	0.053	0.000	0.000	0.000	0.000
9	A	8	VAL	0	0.002	0.012	18.576	-0.037	-0.037	0.000	0.000	0.000	0.000
10	A	9	ALA	0	0.018	0.016	21.943	0.021	0.021	0.000	0.000	0.000	0.000
11	A	10	ARG	1	0.871	0.946	24.718	-0.070	-0.070	0.000	0.000	0.000	0.000
12	A	11	GLY	0	-0.007	0.001	28.261	0.007	0.007	0.000	0.000	0.000	0.000
13	A	12	THR	0	0.060	0.013	26.891	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	13	THR	0	-0.028	-0.001	26.944	0.013	0.013	0.000	0.000	0.000	0.000
15	A	14	ILE	0	0.005	0.004	21.032	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	15	LEU	0	-0.001	-0.001	24.196	0.003	0.003	0.000	0.000	0.000	0.000
17	A	16	ALA	0	-0.019	-0.028	20.955	0.006	0.006	0.000	0.000	0.000	0.000
18	A	17	LYS	1	0.936	0.988	17.539	-0.316	-0.316	0.000	0.000	0.000	0.000
19	A	18	HIS	0	0.023	-0.008	10.925	-0.055	-0.055	0.000	0.000	0.000	0.000
20	A	19	ALA	0	0.002	0.030	11.310	-0.060	-0.060	0.000	0.000	0.000	0.000
21	A	20	TRP	0	-0.017	-0.018	2.694	-1.122	0.192	0.501	-0.794	-1.020	-0.005
22	A	21	CYS	0	-0.002	0.008	6.758	0.230	0.230	0.000	0.000	0.000	0.000
23	A	22	GLY	0	0.056	0.057	8.880	-0.231	-0.231	0.000	0.000	0.000	0.000
24	A	23	GLY	0	0.065	0.004	11.160	0.183	0.183	0.000	0.000	0.000	0.000
25	A	24	ASN	0	-0.058	0.003	13.445	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	25	PHE	0	0.037	0.006	9.567	-0.120	-0.120	0.000	0.000	0.000	0.000
27	A	26	LEU	0	0.014	0.005	15.691	-0.063	-0.063	0.000	0.000	0.000	0.000
28	A	27	GLU	-1	-0.857	-0.911	19.230	0.244	0.244	0.000	0.000	0.000	0.000
29	A	28	VAL	0	0.053	0.018	16.344	-0.034	-0.034	0.000	0.000	0.000	0.000
30	A	29	THR	0	-0.024	-0.033	17.301	-0.046	-0.046	0.000	0.000	0.000	0.000
31	A	30	GLU	-1	-0.963	-0.982	19.482	0.109	0.109	0.000	0.000	0.000	0.000
32	A	31	GLN	0	-0.001	0.007	22.448	-0.032	-0.032	0.000	0.000	0.000	0.000
33	A	32	ILE	0	-0.052	-0.022	17.760	-0.023	-0.023	0.000	0.000	0.000	0.000
34	A	33	LEU	0	-0.024	-0.020	22.318	-0.019	-0.019	0.000	0.000	0.000	0.000
35	A	34	ALA	0	-0.013	-0.005	24.487	-0.013	-0.013	0.000	0.000	0.000	0.000
36	A	35	LYS	1	0.810	0.898	25.237	-0.066	-0.066	0.000	0.000	0.000	0.000
37	A	36	ILE	0	-0.067	-0.012	22.676	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	37	PRO	0	-0.004	0.004	27.192	0.004	0.004	0.000	0.000	0.000	0.000
39	A	38	SER	0	0.037	-0.002	29.373	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	39	GLU	-1	-0.905	-0.951	31.520	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	40	ASN	0	-0.006	-0.006	29.828	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	41	ASN	0	-0.049	-0.011	26.701	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	42	LYS	1	0.872	0.926	23.198	0.131	0.131	0.000	0.000	0.000	0.000
44	A	43	LEU	0	-0.064	-0.020	22.192	0.000	0.000	0.000	0.000	0.000	0.000
45	A	44	THR	0	0.049	0.020	16.811	-0.013	-0.013	0.000	0.000	0.000	0.000
46	A	45	TYR	0	-0.017	-0.027	18.127	0.009	0.009	0.000	0.000	0.000	0.000
47	A	46	SER	0	-0.010	-0.010	16.076	-0.013	-0.013	0.000	0.000	0.000	0.000
48	A	47	HIS	0	-0.015	-0.031	15.456	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	48	GLY	0	0.038	0.032	14.415	0.032	0.032	0.000	0.000	0.000	0.000
50	A	49	ASN	0	-0.071	-0.038	10.393	0.026	0.026	0.000	0.000	0.000	0.000
51	A	50	TYR	0	0.029	0.009	7.721	0.050	0.050	0.000	0.000	0.000	0.000
52	A	51	LEU	0	-0.051	-0.021	11.352	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	52	PHE	0	0.006	-0.009	12.688	0.009	0.009	0.000	0.000	0.000	0.000
54	A	53	HIS	0	0.044	0.029	12.690	0.040	0.040	0.000	0.000	0.000	0.000
55	A	54	TYR	0	-0.008	-0.030	17.207	0.025	0.025	0.000	0.000	0.000	0.000
56	A	55	ILE	0	-0.011	-0.008	20.033	-0.013	-0.013	0.000	0.000	0.000	0.000
57	A	56	CYS	0	-0.046	-0.010	23.008	0.016	0.016	0.000	0.000	0.000	0.000
58	A	57	GLN	0	0.033	0.005	26.169	-0.013	-0.013	0.000	0.000	0.000	0.000
59	A	58	ASP	-1	-0.872	-0.944	28.719	0.001	0.001	0.000	0.000	0.000	0.000
60	A	59	ARG	1	0.876	0.920	30.570	-0.011	-0.011	0.000	0.000	0.000	0.000
61	A	60	ILE	0	-0.065	-0.009	25.467	0.010	0.010	0.000	0.000	0.000	0.000
62	A	61	VAL	0	0.033	0.012	22.057	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	62	TYR	0	0.020	0.006	20.681	0.017	0.017	0.000	0.000	0.000	0.000
64	A	63	LEU	0	0.024	0.000	16.452	-0.025	-0.025	0.000	0.000	0.000	0.000
65	A	64	CYS	0	-0.059	-0.019	12.999	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	65	ILE	0	0.013	0.011	10.555	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	66	THR	0	-0.001	-0.015	8.221	0.080	0.080	0.000	0.000	0.000	0.000
68	A	67	ASP	-1	-0.741	-0.870	3.945	-0.466	-0.288	-0.001	-0.066	-0.111	0.000
69	A	68	ASP	-1	-0.888	-0.942	7.436	-0.465	-0.465	0.000	0.000	0.000	0.000
70	A	69	ASP	-1	-0.909	-0.947	6.820	-2.098	-2.098	0.000	0.000	0.000	0.000
71	A	70	PHE	0	-0.019	0.004	7.854	-0.160	-0.160	0.000	0.000	0.000	0.000
72	A	71	GLU	-1	-0.837	-0.917	9.670	-0.836	-0.836	0.000	0.000	0.000	0.000
73	A	72	ARG	1	0.896	0.903	13.448	0.273	0.273	0.000	0.000	0.000	0.000
74	A	73	SER	0	0.003	0.010	15.763	0.017	0.017	0.000	0.000	0.000	0.000
75	A	74	ARG	1	0.922	0.960	9.706	1.506	1.506	0.000	0.000	0.000	0.000
76	A	75	ALA	0	0.037	0.027	13.059	0.053	0.053	0.000	0.000	0.000	0.000
77	A	76	PHE	0	0.010	-0.016	14.327	0.080	0.080	0.000	0.000	0.000	0.000
78	A	77	SER	0	0.017	0.025	17.110	0.067	0.067	0.000	0.000	0.000	0.000
79	A	78	PHE	0	0.028	0.010	13.988	0.054	0.054	0.000	0.000	0.000	0.000
80	A	79	LEU	0	-0.003	-0.002	16.269	0.068	0.068	0.000	0.000	0.000	0.000
81	A	80	ASN	0	-0.069	-0.051	18.547	0.066	0.066	0.000	0.000	0.000	0.000
82	A	81	GLU	-1	-0.748	-0.832	19.007	-0.071	-0.071	0.000	0.000	0.000	0.000
83	A	82	VAL	0	-0.044	-0.027	17.238	0.038	0.038	0.000	0.000	0.000	0.000
84	A	83	LYS	1	0.889	0.956	20.335	0.110	0.110	0.000	0.000	0.000	0.000
85	A	84	LYS	1	0.884	0.942	23.523	0.106	0.106	0.000	0.000	0.000	0.000
86	A	85	ARG	1	0.845	0.910	20.776	0.054	0.054	0.000	0.000	0.000	0.000
87	A	86	PHE	0	0.033	0.026	23.584	0.012	0.012	0.000	0.000	0.000	0.000
88	A	87	GLN	0	-0.009	-0.017	25.333	0.001	0.001	0.000	0.000	0.000	0.000
89	A	88	THR	0	-0.050	-0.025	28.094	0.002	0.002	0.000	0.000	0.000	0.000
90	A	89	THR	0	-0.057	-0.029	26.541	0.005	0.005	0.000	0.000	0.000	0.000
91	A	90	TYR	0	-0.094	-0.089	25.168	0.005	0.005	0.000	0.000	0.000	0.000
92	A	91	GLY	0	0.010	0.011	30.381	0.002	0.002	0.000	0.000	0.000	0.000
93	A	92	SER	0	0.037	-0.009	32.144	0.001	0.001	0.000	0.000	0.000	0.000
94	A	93	ARG	1	0.947	0.992	31.415	-0.043	-0.043	0.000	0.000	0.000	0.000
95	A	94	ALA	0	0.040	0.018	29.352	0.006	0.006	0.000	0.000	0.000	0.000
96	A	95	GLN	0	0.001	0.017	31.127	0.008	0.008	0.000	0.000	0.000	0.000
97	A	96	THR	0	-0.025	-0.018	33.878	0.001	0.001	0.000	0.000	0.000	0.000
98	A	97	ALA	0	-0.023	0.019	30.496	0.004	0.004	0.000	0.000	0.000	0.000
99	A	98	LEU	0	0.065	0.026	31.763	0.000	0.000	0.000	0.000	0.000	0.000
100	A	99	PRO	0	0.069	0.013	28.055	0.002	0.002	0.000	0.000	0.000	0.000
101	A	100	TYR	0	-0.043	-0.033	21.674	0.013	0.013	0.000	0.000	0.000	0.000
102	A	101	ALA	0	0.004	0.012	25.913	0.004	0.004	0.000	0.000	0.000	0.000
103	A	102	MET	0	-0.017	0.009	25.093	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	103	ASN	0	0.019	0.012	20.397	0.006	0.006	0.000	0.000	0.000	0.000
105	A	104	SER	0	-0.015	-0.001	21.863	0.017	0.017	0.000	0.000	0.000	0.000
106	A	105	GLU	-1	-0.880	-0.905	23.128	0.090	0.090	0.000	0.000	0.000	0.000
107	A	106	PHE	0	0.022	-0.008	20.789	0.003	0.003	0.000	0.000	0.000	0.000
108	A	107	SER	0	0.003	0.004	17.584	0.000	0.000	0.000	0.000	0.000	0.000
109	A	108	SER	0	0.039	0.021	16.600	0.019	0.019	0.000	0.000	0.000	0.000
110	A	109	VAL	0	-0.010	-0.005	16.958	-0.004	-0.004	0.000	0.000	0.000	0.000
111	A	110	LEU	0	-0.058	-0.032	15.539	-0.024	-0.024	0.000	0.000	0.000	0.000
112	A	111	ALA	0	0.017	0.006	12.712	-0.031	-0.031	0.000	0.000	0.000	0.000
113	A	112	ALA	0	-0.005	0.000	12.300	0.013	0.013	0.000	0.000	0.000	0.000
114	A	113	GLN	0	-0.023	-0.018	13.897	-0.085	-0.085	0.000	0.000	0.000	0.000
115	A	114	LEU	0	0.020	0.020	7.933	-0.088	-0.088	0.000	0.000	0.000	0.000
116	A	115	LYS	1	0.858	0.909	8.765	-0.727	-0.727	0.000	0.000	0.000	0.000
117	A	116	HIS	0	-0.041	-0.021	9.821	-0.152	-0.152	0.000	0.000	0.000	0.000
118	A	117	HIS	0	-0.015	-0.016	11.916	-0.129	-0.129	0.000	0.000	0.000	0.000
119	A	118	SER	0	-0.028	-0.023	6.669	-0.307	-0.307	0.000	0.000	0.000	0.000
120	A	119	GLU	-1	-0.892	-0.918	7.067	-0.137	-0.137	0.000	0.000	0.000	0.000
121	A	120	ASN	0	0.005	0.013	8.586	0.083	0.083	0.000	0.000	0.000	0.000
122	A	128	GLU	-1	-0.930	-0.972	18.284	-0.429	-0.429	0.000	0.000	0.000	0.000
123	A	129	THR	0	-0.045	-0.024	20.588	0.036	0.036	0.000	0.000	0.000	0.000
124	A	130	GLN	0	0.026	0.002	22.896	-0.028	-0.028	0.000	0.000	0.000	0.000
125	A	131	ALA	0	0.003	-0.006	25.387	0.004	0.004	0.000	0.000	0.000	0.000
126	A	132	GLN	0	0.024	-0.007	18.778	-0.026	-0.026	0.000	0.000	0.000	0.000
127	A	133	VAL	0	0.036	0.022	20.727	-0.018	-0.018	0.000	0.000	0.000	0.000
128	A	134	ASP	-1	-0.837	-0.901	22.478	-0.180	-0.180	0.000	0.000	0.000	0.000
129	A	135	GLU	-1	-0.788	-0.875	21.724	-0.142	-0.142	0.000	0.000	0.000	0.000
130	A	136	LEU	0	-0.074	-0.033	19.178	0.013	0.013	0.000	0.000	0.000	0.000
131	A	137	LYS	1	0.834	0.913	23.121	0.180	0.180	0.000	0.000	0.000	0.000
132	A	138	GLY	0	-0.003	-0.008	26.612	0.010	0.010	0.000	0.000	0.000	0.000
133	A	139	ILE	0	-0.025	0.029	21.361	0.014	0.014	0.000	0.000	0.000	0.000
134	A	140	MET	0	-0.015	-0.008	23.224	-0.018	-0.018	0.000	0.000	0.000	0.000
135	A	141	VAL	0	0.047	0.016	19.275	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	142	ARG	1	0.917	0.965	21.386	0.065	0.065	0.000	0.000	0.000	0.000
137	A	143	ASN	0	0.050	0.042	20.859	-0.011	-0.011	0.000	0.000	0.000	0.000
138	A	144	ILE	0	0.004	-0.012	19.709	-0.005	-0.005	0.000	0.000	0.000	0.000
139	A	145	ASP	-1	-0.903	-0.940	22.472	0.076	0.076	0.000	0.000	0.000	0.000
140	A	146	LEU	0	0.008	0.012	19.144	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	147	VAL	0	0.023	0.017	23.239	0.005	0.005	0.000	0.000	0.000	0.000
142	A	148	ALA	0	0.042	0.026	22.929	0.015	0.015	0.000	0.000	0.000	0.000
143	A	149	GLN	0	0.023	-0.006	24.482	-0.016	-0.016	0.000	0.000	0.000	0.000
144	A	150	ARG	1	0.854	0.926	26.130	-0.195	-0.195	0.000	0.000	0.000	0.000
145	A	151	GLY	0	-0.004	0.009	28.122	-0.010	-0.010	0.000	0.000	0.000	0.000
146	A	152	GLU	-1	-0.864	-0.922	24.532	0.158	0.158	0.000	0.000	0.000	0.000
147	A	153	ARG	1	0.808	0.879	18.579	-0.125	-0.125	0.000	0.000	0.000	0.000
148	A	154	LEU	0	-0.016	-0.013	19.456	0.015	0.015	0.000	0.000	0.000	0.000
149	A	155	GLU	-1	-0.831	-0.889	16.398	0.169	0.169	0.000	0.000	0.000	0.000
150	A	156	LEU	0	-0.051	-0.010	11.208	-0.005	-0.005	0.000	0.000	0.000	0.000
151	A	157	LEU	0	-0.018	-0.020	12.978	0.029	0.029	0.000	0.000	0.000	0.000
152	A	158	ILE	0	-0.008	-0.024	6.656	-0.021	-0.021	0.000	0.000	0.000	0.000
153	A	159	ASP	-1	-0.811	-0.900	9.728	1.291	1.291	0.000	0.000	0.000	0.000
154	A	160	LYS	1	0.811	0.880	2.614	-8.743	-6.639	0.738	-1.093	-1.749	0.013
155	A	161	THR	0	-0.081	-0.049	6.345	0.015	0.015	0.000	0.000	0.000	0.000
156	A	162	GLU	-1	-0.945	-0.973	8.922	0.679	0.679	0.000	0.000	0.000	0.000
157	A	163	ASN	0	-0.060	-0.013	8.526	0.150	0.150	0.000	0.000	0.000	0.000

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