FMO DATABASE

FMODB ID: G55J1

Calculation Name: 5UIC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5UIC

Chain ID: A

ChEMBL ID:

UniProt ID: A0Q7W8

Base Structure: X-ray

Registration Date: 2023-09-21

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	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	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1004856.32403
FMO2-HF: Nuclear repulsion	958950.272899
FMO2-HF: Total energy	-45906.051131
FMO2-MP2: Total energy	-46042.186982

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:ASN)

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

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.
-1.257	1.052	0.012	-1.026	-1.294	0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.037 / q_NPA : -0.029

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	ARG	1	0.846	0.913	3.650	4.862	6.890	0.002	-0.981	-1.048	0.002
4	A	3	ILE	0	-0.004	-0.001	6.395	0.520	0.520	0.000	0.000	0.000	0.000
5	A	4	LEU	0	-0.022	-0.004	9.789	0.021	0.021	0.000	0.000	0.000	0.000
6	A	5	LEU	0	-0.005	-0.006	13.211	0.132	0.132	0.000	0.000	0.000	0.000
7	A	6	ALA	0	-0.004	-0.008	16.157	-0.043	-0.043	0.000	0.000	0.000	0.000
8	A	7	GLU	-1	-0.790	-0.900	19.494	-0.221	-0.221	0.000	0.000	0.000	0.000
9	A	8	ASP	-1	-0.892	-0.962	22.071	-0.288	-0.288	0.000	0.000	0.000	0.000
10	A	9	ASP	-1	-0.828	-0.900	25.106	-0.135	-0.135	0.000	0.000	0.000	0.000
11	A	10	LEU	0	-0.004	-0.014	23.588	-0.009	-0.009	0.000	0.000	0.000	0.000
12	A	11	HIS	0	-0.025	0.006	23.200	0.011	0.011	0.000	0.000	0.000	0.000
13	A	12	LEU	0	-0.017	-0.011	21.878	0.024	0.024	0.000	0.000	0.000	0.000
14	A	13	GLY	0	0.011	0.000	19.816	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	14	GLU	-1	-0.944	-0.975	18.525	-0.133	-0.133	0.000	0.000	0.000	0.000
16	A	15	GLY	0	0.010	0.004	18.856	0.036	0.036	0.000	0.000	0.000	0.000
17	A	16	LEU	0	-0.031	-0.033	16.843	0.060	0.060	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.007	0.007	13.497	0.009	0.009	0.000	0.000	0.000	0.000
19	A	18	GLU	-1	-0.806	-0.879	14.187	0.308	0.308	0.000	0.000	0.000	0.000
20	A	19	ALA	0	-0.021	-0.016	15.527	0.111	0.111	0.000	0.000	0.000	0.000
21	A	20	LEU	0	-0.022	-0.019	11.480	0.125	0.125	0.000	0.000	0.000	0.000
22	A	21	GLN	0	-0.019	-0.006	10.440	0.273	0.273	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.765	0.870	11.454	-0.069	-0.069	0.000	0.000	0.000	0.000
24	A	23	GLU	-1	-0.841	-0.900	11.755	0.917	0.917	0.000	0.000	0.000	0.000
25	A	24	GLY	0	-0.029	-0.006	8.803	0.314	0.314	0.000	0.000	0.000	0.000
26	A	25	LEU	0	-0.048	-0.016	6.276	0.614	0.614	0.000	0.000	0.000	0.000
27	A	26	ILE	0	0.004	0.001	3.541	-0.429	-0.148	0.010	-0.045	-0.246	0.000
28	A	27	VAL	0	0.010	0.008	6.547	-0.513	-0.513	0.000	0.000	0.000	0.000
29	A	28	ASN	0	-0.027	-0.007	9.854	-0.206	-0.206	0.000	0.000	0.000	0.000
30	A	29	LEU	0	0.026	0.013	12.551	0.040	0.040	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.033	-0.006	16.358	-0.007	-0.007	0.000	0.000	0.000	0.000
32	A	31	SER	0	0.069	0.026	19.213	0.021	0.021	0.000	0.000	0.000	0.000
33	A	32	ASP	-1	-0.813	-0.911	22.471	-0.461	-0.461	0.000	0.000	0.000	0.000
34	A	33	GLY	0	0.086	0.021	22.523	-0.057	-0.057	0.000	0.000	0.000	0.000
35	A	34	GLU	-1	-0.906	-0.940	23.419	-0.496	-0.496	0.000	0.000	0.000	0.000
36	A	35	ALA	0	0.015	0.010	19.562	-0.061	-0.061	0.000	0.000	0.000	0.000
37	A	36	ALA	0	0.004	0.006	18.590	-0.100	-0.100	0.000	0.000	0.000	0.000
38	A	37	GLN	0	-0.026	-0.018	18.484	-0.040	-0.040	0.000	0.000	0.000	0.000
39	A	38	THR	0	-0.031	-0.018	18.177	-0.051	-0.051	0.000	0.000	0.000	0.000
40	A	39	PHE	0	-0.003	-0.014	14.184	-0.084	-0.084	0.000	0.000	0.000	0.000
41	A	40	ILE	0	0.007	0.022	14.105	-0.209	-0.209	0.000	0.000	0.000	0.000
42	A	41	GLU	-1	-0.788	-0.894	15.379	-0.724	-0.724	0.000	0.000	0.000	0.000
43	A	42	SER	0	-0.093	-0.046	13.414	-0.085	-0.085	0.000	0.000	0.000	0.000
44	A	43	GLY	0	0.013	0.000	12.449	-0.098	-0.098	0.000	0.000	0.000	0.000
45	A	44	LEU	0	-0.045	-0.015	8.636	-0.350	-0.350	0.000	0.000	0.000	0.000
46	A	45	TYR	0	-0.057	-0.033	7.761	-0.986	-0.986	0.000	0.000	0.000	0.000
47	A	46	ASP	-1	-0.812	-0.901	6.387	-4.704	-4.704	0.000	0.000	0.000	0.000
48	A	47	ILE	0	-0.040	-0.034	9.442	0.518	0.518	0.000	0.000	0.000	0.000
49	A	48	VAL	0	0.012	0.009	12.072	-0.172	-0.172	0.000	0.000	0.000	0.000
50	A	49	VAL	0	-0.031	-0.007	14.909	0.134	0.134	0.000	0.000	0.000	0.000
51	A	50	LEU	0	0.011	0.002	17.443	-0.034	-0.034	0.000	0.000	0.000	0.000
52	A	51	ASP	-1	-0.766	-0.875	20.691	-0.206	-0.206	0.000	0.000	0.000	0.000
53	A	52	ILE	0	-0.042	-0.043	24.006	-0.023	-0.023	0.000	0.000	0.000	0.000
54	A	53	GLY	0	-0.036	-0.026	27.229	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	54	MET	0	-0.014	0.021	22.500	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	55	PRO	0	0.028	0.016	26.846	0.008	0.008	0.000	0.000	0.000	0.000
57	A	56	ILE	0	-0.046	-0.011	26.605	-0.030	-0.030	0.000	0.000	0.000	0.000
58	A	57	LYS	1	0.770	0.878	24.894	0.484	0.484	0.000	0.000	0.000	0.000
59	A	58	THR	0	0.037	0.012	26.930	-0.017	-0.017	0.000	0.000	0.000	0.000
60	A	59	GLY	0	0.031	0.010	24.644	-0.028	-0.028	0.000	0.000	0.000	0.000
61	A	60	LEU	0	0.012	-0.007	24.982	-0.026	-0.026	0.000	0.000	0.000	0.000
62	A	61	GLU	-1	-0.867	-0.914	27.551	-0.316	-0.316	0.000	0.000	0.000	0.000
63	A	62	VAL	0	-0.005	0.009	21.386	-0.020	-0.020	0.000	0.000	0.000	0.000
64	A	63	LEU	0	0.002	0.006	22.233	-0.041	-0.041	0.000	0.000	0.000	0.000
65	A	64	ARG	1	0.898	0.941	23.804	0.322	0.322	0.000	0.000	0.000	0.000
66	A	65	ASN	0	-0.054	-0.026	24.859	0.030	0.030	0.000	0.000	0.000	0.000
67	A	66	ILE	0	0.021	0.008	18.935	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	67	ARG	1	0.776	0.874	18.404	0.565	0.565	0.000	0.000	0.000	0.000
69	A	68	ASN	0	-0.034	-0.014	23.097	0.014	0.014	0.000	0.000	0.000	0.000
70	A	69	ARG	1	0.796	0.895	21.100	0.570	0.570	0.000	0.000	0.000	0.000
71	A	70	GLY	0	-0.012	0.001	21.425	-0.024	-0.024	0.000	0.000	0.000	0.000
72	A	71	ILE	0	-0.025	0.005	14.047	-0.019	-0.019	0.000	0.000	0.000	0.000
73	A	72	LYS	1	0.902	0.937	16.741	0.553	0.553	0.000	0.000	0.000	0.000
74	A	73	VAL	0	-0.001	0.010	12.756	0.092	0.092	0.000	0.000	0.000	0.000
75	A	74	PRO	0	0.005	0.006	13.361	0.110	0.110	0.000	0.000	0.000	0.000
76	A	75	ILE	0	-0.003	0.003	15.580	-0.094	-0.094	0.000	0.000	0.000	0.000
77	A	76	ILE	0	-0.022	-0.005	16.533	0.082	0.082	0.000	0.000	0.000	0.000
78	A	77	LEU	0	0.006	0.003	19.676	-0.031	-0.031	0.000	0.000	0.000	0.000
79	A	78	LEU	0	-0.012	0.001	20.653	0.048	0.048	0.000	0.000	0.000	0.000
80	A	79	THR	0	0.085	0.038	24.307	-0.013	-0.013	0.000	0.000	0.000	0.000
81	A	80	ALA	0	0.036	0.021	27.967	0.018	0.018	0.000	0.000	0.000	0.000
82	A	81	ARG	1	0.847	0.913	31.174	0.163	0.163	0.000	0.000	0.000	0.000
83	A	82	ASP	-1	-0.843	-0.909	32.236	-0.081	-0.081	0.000	0.000	0.000	0.000
84	A	83	GLY	0	0.017	0.019	33.832	0.012	0.012	0.000	0.000	0.000	0.000
85	A	84	LEU	0	-0.022	-0.030	33.906	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	85	GLU	-1	-0.924	-0.956	34.548	-0.122	-0.122	0.000	0.000	0.000	0.000
87	A	86	ASP	-1	-0.813	-0.917	32.732	-0.154	-0.154	0.000	0.000	0.000	0.000
88	A	87	ARG	1	0.829	0.904	27.819	0.090	0.090	0.000	0.000	0.000	0.000
89	A	88	ILE	0	0.005	0.006	29.911	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	89	LYS	1	0.799	0.890	31.026	0.194	0.194	0.000	0.000	0.000	0.000
91	A	90	GLY	0	0.051	0.022	28.187	-0.019	-0.019	0.000	0.000	0.000	0.000
92	A	91	LEU	0	0.006	0.009	25.484	-0.028	-0.028	0.000	0.000	0.000	0.000
93	A	92	ASP	-1	-0.835	-0.900	27.126	-0.199	-0.199	0.000	0.000	0.000	0.000
94	A	93	LEU	0	-0.050	-0.038	27.792	0.004	0.004	0.000	0.000	0.000	0.000
95	A	94	GLY	0	-0.019	-0.004	24.872	-0.030	-0.030	0.000	0.000	0.000	0.000
96	A	95	ALA	0	0.000	0.013	22.365	-0.051	-0.051	0.000	0.000	0.000	0.000
97	A	96	ASP	-1	-0.842	-0.923	19.284	-0.456	-0.456	0.000	0.000	0.000	0.000
98	A	97	ASP	-1	-0.837	-0.905	20.653	-0.078	-0.078	0.000	0.000	0.000	0.000
99	A	98	TYR	0	-0.016	-0.018	22.376	-0.041	-0.041	0.000	0.000	0.000	0.000
100	A	99	LEU	0	-0.028	-0.003	22.151	0.035	0.035	0.000	0.000	0.000	0.000
101	A	100	THR	0	-0.027	-0.022	25.305	-0.018	-0.018	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.754	0.876	24.955	0.240	0.240	0.000	0.000	0.000	0.000
103	A	102	PRO	0	-0.009	-0.011	28.567	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	103	PHE	0	0.053	0.006	21.614	0.005	0.005	0.000	0.000	0.000	0.000
105	A	104	GLU	-1	-0.794	-0.887	24.903	0.123	0.123	0.000	0.000	0.000	0.000
106	A	105	LEU	0	0.040	0.016	20.313	0.003	0.003	0.000	0.000	0.000	0.000
107	A	106	LYS	1	0.852	0.902	19.832	-0.165	-0.165	0.000	0.000	0.000	0.000
108	A	107	GLU	-1	-0.830	-0.892	20.057	0.029	0.029	0.000	0.000	0.000	0.000
109	A	108	LEU	0	0.023	0.016	17.761	0.003	0.003	0.000	0.000	0.000	0.000
110	A	109	VAL	0	0.029	0.016	14.775	-0.031	-0.031	0.000	0.000	0.000	0.000
111	A	110	ALA	0	-0.018	-0.007	15.465	0.051	0.051	0.000	0.000	0.000	0.000
112	A	111	ARG	1	0.780	0.860	17.272	0.078	0.078	0.000	0.000	0.000	0.000
113	A	112	ILE	0	0.036	0.022	11.995	-0.023	-0.023	0.000	0.000	0.000	0.000
114	A	113	LYS	1	0.812	0.877	12.062	-0.774	-0.774	0.000	0.000	0.000	0.000
115	A	114	ALA	0	-0.072	-0.038	13.595	0.081	0.081	0.000	0.000	0.000	0.000
116	A	115	ILE	0	0.028	0.004	13.685	0.033	0.033	0.000	0.000	0.000	0.000
117	A	116	SER	0	0.033	0.007	9.590	-0.020	-0.020	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.831	0.931	11.064	-0.241	-0.241	0.000	0.000	0.000	0.000
119	A	118	ARG	1	0.894	0.948	13.693	0.002	0.002	0.000	0.000	0.000	0.000
120	A	119	ILE	0	0.021	0.037	9.177	-0.118	-0.118	0.000	0.000	0.000	0.000

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