FMO DATABASE

FMODB ID: VQQ91

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1002035.102454
FMO2-HF: Nuclear repulsion	956130.399175
FMO2-HF: Total energy	-45904.703279
FMO2-MP2: Total energy	-46040.92031

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.
-2.256	0.358	-0.017	-1.148	-1.448	0.005

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 : -0.053 / q_NPA : -0.036

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	0.859	0.916	3.813	4.986	7.305	-0.020	-1.108	-1.190	0.005
4	A	3	ILE	0	-0.006	-0.003	6.485	0.427	0.427	0.000	0.000	0.000	0.000
5	A	4	LEU	0	-0.006	0.008	9.863	0.160	0.160	0.000	0.000	0.000	0.000
6	A	5	LEU	0	-0.023	-0.016	13.000	0.098	0.098	0.000	0.000	0.000	0.000
7	A	6	ALA	0	0.005	0.000	15.897	0.008	0.008	0.000	0.000	0.000	0.000
8	A	7	GLU	-1	-0.826	-0.942	19.234	-0.243	-0.243	0.000	0.000	0.000	0.000
9	A	8	ASP	-1	-0.915	-0.960	21.833	-0.230	-0.230	0.000	0.000	0.000	0.000
10	A	9	ASP	-1	-0.901	-0.940	24.871	-0.074	-0.074	0.000	0.000	0.000	0.000
11	A	10	LEU	0	0.001	-0.013	23.434	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	11	HIS	0	0.013	0.008	22.754	0.023	0.023	0.000	0.000	0.000	0.000
13	A	12	LEU	0	-0.035	-0.005	21.747	0.033	0.033	0.000	0.000	0.000	0.000
14	A	13	GLY	0	0.011	0.002	19.484	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	14	GLU	-1	-0.939	-0.971	18.277	0.101	0.101	0.000	0.000	0.000	0.000
16	A	15	GLY	0	0.025	0.015	18.734	0.062	0.062	0.000	0.000	0.000	0.000
17	A	16	LEU	0	-0.021	-0.029	16.641	0.062	0.062	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.028	0.003	13.343	0.021	0.021	0.000	0.000	0.000	0.000
19	A	18	GLU	-1	-0.920	-0.957	14.100	0.488	0.488	0.000	0.000	0.000	0.000
20	A	19	ALA	0	-0.076	-0.049	15.512	0.147	0.147	0.000	0.000	0.000	0.000
21	A	20	LEU	0	-0.008	-0.020	11.409	0.124	0.124	0.000	0.000	0.000	0.000
22	A	21	GLN	0	0.020	0.007	10.298	0.198	0.198	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.877	0.953	11.508	-0.285	-0.285	0.000	0.000	0.000	0.000
24	A	23	GLU	-1	-0.951	-0.978	11.418	0.864	0.864	0.000	0.000	0.000	0.000
25	A	24	GLY	0	-0.037	-0.007	8.486	0.172	0.172	0.000	0.000	0.000	0.000
26	A	25	LEU	0	-0.044	-0.012	6.101	1.147	1.147	0.000	0.000	0.000	0.000
27	A	26	ILE	0	0.006	0.007	3.680	-0.126	0.169	0.003	-0.040	-0.258	0.000
28	A	27	VAL	0	0.017	0.003	6.318	-0.700	-0.700	0.000	0.000	0.000	0.000
29	A	28	ASN	0	-0.062	0.003	9.338	-0.231	-0.231	0.000	0.000	0.000	0.000
30	A	29	LEU	0	0.052	0.024	12.233	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.051	-0.023	15.978	0.007	0.007	0.000	0.000	0.000	0.000
32	A	31	SER	0	0.063	0.020	18.651	0.023	0.023	0.000	0.000	0.000	0.000
33	A	32	ASP	-1	-0.790	-0.889	22.074	-0.400	-0.400	0.000	0.000	0.000	0.000
34	A	33	GLY	0	0.084	0.026	22.240	-0.060	-0.060	0.000	0.000	0.000	0.000
35	A	34	GLU	-1	-1.028	-1.001	22.426	-0.465	-0.465	0.000	0.000	0.000	0.000
36	A	35	ALA	0	0.034	0.016	19.450	-0.064	-0.064	0.000	0.000	0.000	0.000
37	A	36	ALA	0	-0.008	-0.004	18.147	-0.109	-0.109	0.000	0.000	0.000	0.000
38	A	37	GLN	0	-0.007	-0.020	17.799	-0.061	-0.061	0.000	0.000	0.000	0.000
39	A	38	THR	0	-0.040	-0.021	17.956	-0.064	-0.064	0.000	0.000	0.000	0.000
40	A	39	PHE	0	0.010	-0.007	13.953	-0.077	-0.077	0.000	0.000	0.000	0.000
41	A	40	ILE	0	-0.003	0.017	13.508	-0.248	-0.248	0.000	0.000	0.000	0.000
42	A	41	GLU	-1	-0.914	-0.965	14.631	-0.868	-0.868	0.000	0.000	0.000	0.000
43	A	42	SER	0	-0.065	-0.032	12.978	-0.058	-0.058	0.000	0.000	0.000	0.000
44	A	43	GLY	0	-0.003	-0.007	11.631	-0.095	-0.095	0.000	0.000	0.000	0.000
45	A	44	LEU	0	-0.053	-0.016	7.981	-0.462	-0.462	0.000	0.000	0.000	0.000
46	A	45	TYR	0	-0.056	-0.050	6.986	-1.139	-1.139	0.000	0.000	0.000	0.000
47	A	46	ASP	-1	-0.819	-0.909	5.887	-6.432	-6.432	0.000	0.000	0.000	0.000
48	A	47	ILE	0	-0.034	-0.029	9.206	0.558	0.558	0.000	0.000	0.000	0.000
49	A	48	VAL	0	0.023	0.012	11.859	-0.127	-0.127	0.000	0.000	0.000	0.000
50	A	49	VAL	0	-0.032	-0.008	14.728	0.124	0.124	0.000	0.000	0.000	0.000
51	A	50	LEU	0	-0.015	-0.022	17.301	-0.022	-0.022	0.000	0.000	0.000	0.000
52	A	51	ASP	-1	-0.745	-0.865	20.520	-0.245	-0.245	0.000	0.000	0.000	0.000
53	A	52	ILE	0	-0.058	-0.046	23.659	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	53	GLY	0	-0.087	-0.045	26.857	0.003	0.003	0.000	0.000	0.000	0.000
55	A	54	MET	0	0.021	0.035	22.355	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	55	PRO	0	0.018	0.002	26.440	0.008	0.008	0.000	0.000	0.000	0.000
57	A	56	ILE	0	-0.019	-0.003	26.554	-0.029	-0.029	0.000	0.000	0.000	0.000
58	A	57	LYS	1	0.870	0.949	24.598	0.493	0.493	0.000	0.000	0.000	0.000
59	A	58	THR	0	0.043	0.009	26.529	-0.016	-0.016	0.000	0.000	0.000	0.000
60	A	59	GLY	0	0.053	0.023	24.115	-0.035	-0.035	0.000	0.000	0.000	0.000
61	A	60	LEU	0	0.012	-0.007	24.525	-0.037	-0.037	0.000	0.000	0.000	0.000
62	A	61	GLU	-1	-0.898	-0.936	26.889	-0.354	-0.354	0.000	0.000	0.000	0.000
63	A	62	VAL	0	-0.014	0.004	20.820	-0.024	-0.024	0.000	0.000	0.000	0.000
64	A	63	LEU	0	0.012	0.011	21.832	-0.045	-0.045	0.000	0.000	0.000	0.000
65	A	64	ARG	1	0.935	0.941	23.225	0.377	0.377	0.000	0.000	0.000	0.000
66	A	65	ASN	0	-0.068	-0.038	23.995	0.018	0.018	0.000	0.000	0.000	0.000
67	A	66	ILE	0	0.013	0.010	18.643	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	67	ARG	1	0.831	0.920	18.164	0.770	0.770	0.000	0.000	0.000	0.000
69	A	68	ASN	0	-0.024	-0.011	22.597	0.009	0.009	0.000	0.000	0.000	0.000
70	A	69	ARG	1	0.867	0.946	20.938	0.605	0.605	0.000	0.000	0.000	0.000
71	A	70	GLY	0	-0.013	0.009	21.213	-0.033	-0.033	0.000	0.000	0.000	0.000
72	A	71	ILE	0	-0.012	0.007	14.201	-0.063	-0.063	0.000	0.000	0.000	0.000
73	A	72	LYS	1	0.947	0.956	15.885	0.826	0.826	0.000	0.000	0.000	0.000
74	A	73	VAL	0	-0.016	0.014	12.400	0.065	0.065	0.000	0.000	0.000	0.000
75	A	74	PRO	0	0.040	0.010	13.208	0.152	0.152	0.000	0.000	0.000	0.000
76	A	75	ILE	0	-0.048	-0.034	15.407	-0.095	-0.095	0.000	0.000	0.000	0.000
77	A	76	ILE	0	-0.018	-0.004	16.225	0.092	0.092	0.000	0.000	0.000	0.000
78	A	77	LEU	0	-0.004	0.003	19.578	-0.013	-0.013	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.007	0.012	20.469	0.047	0.047	0.000	0.000	0.000	0.000
80	A	79	THR	0	0.048	0.013	24.280	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	80	ALA	0	0.044	0.023	27.964	0.018	0.018	0.000	0.000	0.000	0.000
82	A	81	ARG	1	0.884	0.948	31.162	0.184	0.184	0.000	0.000	0.000	0.000
83	A	82	ASP	-1	-0.906	-0.948	32.374	-0.116	-0.116	0.000	0.000	0.000	0.000
84	A	83	GLY	0	0.063	0.037	34.440	0.011	0.011	0.000	0.000	0.000	0.000
85	A	84	LEU	0	-0.034	-0.038	33.723	-0.015	-0.015	0.000	0.000	0.000	0.000
86	A	85	GLU	-1	-0.941	-0.968	34.448	-0.170	-0.170	0.000	0.000	0.000	0.000
87	A	86	ASP	-1	-0.862	-0.947	32.724	-0.202	-0.202	0.000	0.000	0.000	0.000
88	A	87	ARG	1	0.893	0.948	28.020	0.164	0.164	0.000	0.000	0.000	0.000
89	A	88	ILE	0	0.025	0.020	29.670	-0.023	-0.023	0.000	0.000	0.000	0.000
90	A	89	LYS	1	0.971	1.005	30.912	0.264	0.264	0.000	0.000	0.000	0.000
91	A	90	GLY	0	0.005	-0.009	28.104	-0.022	-0.022	0.000	0.000	0.000	0.000
92	A	91	LEU	0	-0.029	-0.027	25.410	-0.035	-0.035	0.000	0.000	0.000	0.000
93	A	92	ASP	-1	-0.891	-0.948	26.953	-0.304	-0.304	0.000	0.000	0.000	0.000
94	A	93	LEU	0	-0.131	-0.067	27.187	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	94	GLY	0	-0.015	-0.004	24.306	-0.032	-0.032	0.000	0.000	0.000	0.000
96	A	95	ALA	0	-0.038	-0.006	22.129	-0.064	-0.064	0.000	0.000	0.000	0.000
97	A	96	ASP	-1	-0.844	-0.905	19.031	-0.728	-0.728	0.000	0.000	0.000	0.000
98	A	97	ASP	-1	-0.873	-0.939	20.507	-0.237	-0.237	0.000	0.000	0.000	0.000
99	A	98	TYR	0	-0.038	-0.037	22.239	-0.020	-0.020	0.000	0.000	0.000	0.000
100	A	99	LEU	0	-0.009	-0.005	21.644	0.035	0.035	0.000	0.000	0.000	0.000
101	A	100	THR	0	0.000	-0.006	25.065	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.835	0.946	25.387	0.225	0.225	0.000	0.000	0.000	0.000
103	A	102	PRO	0	-0.014	-0.008	28.781	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	103	PHE	0	0.058	0.008	21.624	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	104	GLU	-1	-0.904	-0.950	25.186	0.081	0.081	0.000	0.000	0.000	0.000
106	A	105	LEU	0	0.042	0.011	20.182	-0.008	-0.008	0.000	0.000	0.000	0.000
107	A	106	LYS	1	0.959	0.962	19.806	-0.300	-0.300	0.000	0.000	0.000	0.000
108	A	107	GLU	-1	-0.839	-0.888	19.920	-0.069	-0.069	0.000	0.000	0.000	0.000
109	A	108	LEU	0	0.037	0.019	17.541	-0.020	-0.020	0.000	0.000	0.000	0.000
110	A	109	VAL	0	0.019	0.006	14.635	-0.056	-0.056	0.000	0.000	0.000	0.000
111	A	110	ALA	0	-0.022	-0.010	15.235	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	111	ARG	1	0.821	0.898	16.852	0.148	0.148	0.000	0.000	0.000	0.000
113	A	112	ILE	0	0.051	0.034	11.591	-0.079	-0.079	0.000	0.000	0.000	0.000
114	A	113	LYS	1	0.901	0.949	11.866	-0.653	-0.653	0.000	0.000	0.000	0.000
115	A	114	ALA	0	-0.066	-0.043	13.117	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	115	ILE	0	0.017	0.003	12.917	-0.020	-0.020	0.000	0.000	0.000	0.000
117	A	116	SER	0	0.003	-0.003	8.619	-0.123	-0.123	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.924	0.969	10.546	0.006	0.006	0.000	0.000	0.000	0.000
119	A	118	ARG	1	0.870	0.944	12.941	0.368	0.368	0.000	0.000	0.000	0.000
120	A	119	ILE	0	0.011	0.031	9.461	-0.043	-0.043	0.000	0.000	0.000	0.000

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