FMO DATABASE

FMODB ID: 1NNMZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1002264.575159
FMO2-HF: Nuclear repulsion	956359.026799
FMO2-HF: Total energy	-45905.54836
FMO2-MP2: Total energy	-46041.718563

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.
-1.964	0.395	-0.013	-1.037	-1.31	0.004

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 : -0.049 / q_NPA : -0.033

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	0.861	0.913	3.813	5.496	7.570	-0.019	-0.988	-1.068	0.004
4	A	3	ILE	0	0.001	0.001	6.485	0.617	0.617	0.000	0.000	0.000	0.000
5	A	4	LEU	0	-0.018	0.005	10.080	0.063	0.063	0.000	0.000	0.000	0.000
6	A	5	LEU	0	-0.014	-0.009	12.913	0.151	0.151	0.000	0.000	0.000	0.000
7	A	6	ALA	0	-0.002	-0.002	16.092	-0.011	-0.011	0.000	0.000	0.000	0.000
8	A	7	GLU	-1	-0.799	-0.912	19.177	-0.297	-0.297	0.000	0.000	0.000	0.000
9	A	8	ASP	-1	-0.906	-0.960	22.022	-0.330	-0.330	0.000	0.000	0.000	0.000
10	A	9	ASP	-1	-0.832	-0.904	24.960	-0.193	-0.193	0.000	0.000	0.000	0.000
11	A	10	LEU	0	0.005	-0.006	23.587	-0.015	-0.015	0.000	0.000	0.000	0.000
12	A	11	HIS	0	-0.012	0.002	22.915	0.000	0.000	0.000	0.000	0.000	0.000
13	A	12	LEU	0	-0.033	-0.014	22.047	0.023	0.023	0.000	0.000	0.000	0.000
14	A	13	GLY	0	0.011	0.003	19.668	-0.012	-0.012	0.000	0.000	0.000	0.000
15	A	14	GLU	-1	-0.944	-0.976	18.450	-0.186	-0.186	0.000	0.000	0.000	0.000
16	A	15	GLY	0	0.022	0.015	18.893	0.038	0.038	0.000	0.000	0.000	0.000
17	A	16	LEU	0	-0.026	-0.028	16.909	0.055	0.055	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.017	0.005	13.384	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	18	GLU	-1	-0.822	-0.892	14.260	0.198	0.198	0.000	0.000	0.000	0.000
20	A	19	ALA	0	-0.056	-0.037	15.665	0.122	0.122	0.000	0.000	0.000	0.000
21	A	20	LEU	0	-0.009	-0.020	11.559	0.132	0.132	0.000	0.000	0.000	0.000
22	A	21	GLN	0	0.004	0.003	10.393	0.267	0.267	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.774	0.883	11.655	-0.063	-0.063	0.000	0.000	0.000	0.000
24	A	23	GLU	-1	-0.848	-0.908	11.408	0.828	0.828	0.000	0.000	0.000	0.000
25	A	24	GLY	0	-0.033	-0.005	8.484	0.307	0.307	0.000	0.000	0.000	0.000
26	A	25	LEU	0	-0.035	-0.005	6.027	0.594	0.594	0.000	0.000	0.000	0.000
27	A	26	ILE	0	0.003	0.002	3.645	-0.310	-0.025	0.006	-0.049	-0.242	0.000
28	A	27	VAL	0	0.008	0.003	6.480	-0.382	-0.382	0.000	0.000	0.000	0.000
29	A	28	ASN	0	-0.048	-0.011	9.327	-0.237	-0.237	0.000	0.000	0.000	0.000
30	A	29	LEU	0	0.046	0.021	12.168	0.041	0.041	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.038	-0.018	15.940	0.002	0.002	0.000	0.000	0.000	0.000
32	A	31	SER	0	0.074	0.027	18.512	0.024	0.024	0.000	0.000	0.000	0.000
33	A	32	ASP	-1	-0.836	-0.919	21.924	-0.507	-0.507	0.000	0.000	0.000	0.000
34	A	33	GLY	0	0.095	0.034	22.110	-0.065	-0.065	0.000	0.000	0.000	0.000
35	A	34	GLU	-1	-0.937	-0.958	22.531	-0.552	-0.552	0.000	0.000	0.000	0.000
36	A	35	ALA	0	0.030	0.018	19.382	-0.061	-0.061	0.000	0.000	0.000	0.000
37	A	36	ALA	0	-0.002	-0.002	18.142	-0.112	-0.112	0.000	0.000	0.000	0.000
38	A	37	GLN	0	-0.033	-0.049	17.950	-0.055	-0.055	0.000	0.000	0.000	0.000
39	A	38	THR	0	-0.054	-0.028	18.227	-0.051	-0.051	0.000	0.000	0.000	0.000
40	A	39	PHE	0	-0.001	-0.011	14.034	-0.077	-0.077	0.000	0.000	0.000	0.000
41	A	40	ILE	0	0.009	0.021	13.645	-0.249	-0.249	0.000	0.000	0.000	0.000
42	A	41	GLU	-1	-0.842	-0.920	14.737	-0.820	-0.820	0.000	0.000	0.000	0.000
43	A	42	SER	0	-0.071	-0.033	12.827	-0.063	-0.063	0.000	0.000	0.000	0.000
44	A	43	GLY	0	0.000	-0.006	11.707	-0.090	-0.090	0.000	0.000	0.000	0.000
45	A	44	LEU	0	-0.046	-0.013	8.076	-0.415	-0.415	0.000	0.000	0.000	0.000
46	A	45	TYR	0	-0.058	-0.040	7.118	-1.189	-1.189	0.000	0.000	0.000	0.000
47	A	46	ASP	-1	-0.814	-0.900	6.060	-5.752	-5.752	0.000	0.000	0.000	0.000
48	A	47	ILE	0	-0.032	-0.030	9.206	0.590	0.590	0.000	0.000	0.000	0.000
49	A	48	VAL	0	0.007	0.007	11.859	-0.196	-0.196	0.000	0.000	0.000	0.000
50	A	49	VAL	0	-0.019	-0.001	14.728	0.152	0.152	0.000	0.000	0.000	0.000
51	A	50	LEU	0	-0.015	-0.016	17.340	-0.043	-0.043	0.000	0.000	0.000	0.000
52	A	51	ASP	-1	-0.739	-0.857	20.621	-0.276	-0.276	0.000	0.000	0.000	0.000
53	A	52	ILE	0	-0.053	-0.045	23.872	-0.016	-0.016	0.000	0.000	0.000	0.000
54	A	53	GLY	0	-0.062	-0.029	26.940	0.007	0.007	0.000	0.000	0.000	0.000
55	A	54	MET	0	0.001	0.024	22.089	-0.025	-0.025	0.000	0.000	0.000	0.000
56	A	55	PRO	0	0.006	-0.002	26.359	0.015	0.015	0.000	0.000	0.000	0.000
57	A	56	ILE	0	-0.031	-0.011	26.556	-0.032	-0.032	0.000	0.000	0.000	0.000
58	A	57	LYS	1	0.824	0.928	24.442	0.552	0.552	0.000	0.000	0.000	0.000
59	A	58	THR	0	0.034	-0.009	26.536	-0.018	-0.018	0.000	0.000	0.000	0.000
60	A	59	GLY	0	0.034	0.013	24.217	-0.032	-0.032	0.000	0.000	0.000	0.000
61	A	60	LEU	0	0.018	-0.005	24.666	-0.028	-0.028	0.000	0.000	0.000	0.000
62	A	61	GLU	-1	-0.873	-0.906	27.017	-0.373	-0.373	0.000	0.000	0.000	0.000
63	A	62	VAL	0	-0.015	0.000	20.939	-0.019	-0.019	0.000	0.000	0.000	0.000
64	A	63	LEU	0	0.010	0.009	21.907	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	64	ARG	1	0.920	0.944	23.347	0.379	0.379	0.000	0.000	0.000	0.000
66	A	65	ASN	0	-0.038	-0.014	24.114	0.031	0.031	0.000	0.000	0.000	0.000
67	A	66	ILE	0	0.011	0.002	18.549	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	67	ARG	1	0.805	0.901	18.212	0.667	0.667	0.000	0.000	0.000	0.000
69	A	68	ASN	0	-0.033	-0.016	22.677	0.023	0.023	0.000	0.000	0.000	0.000
70	A	69	ARG	1	0.834	0.926	21.022	0.617	0.617	0.000	0.000	0.000	0.000
71	A	70	GLY	0	-0.014	0.006	21.261	-0.028	-0.028	0.000	0.000	0.000	0.000
72	A	71	ILE	0	-0.026	0.003	13.916	-0.043	-0.043	0.000	0.000	0.000	0.000
73	A	72	LYS	1	0.961	0.961	15.998	0.624	0.624	0.000	0.000	0.000	0.000
74	A	73	VAL	0	-0.011	0.014	12.347	0.081	0.081	0.000	0.000	0.000	0.000
75	A	74	PRO	0	0.026	0.014	13.249	0.122	0.122	0.000	0.000	0.000	0.000
76	A	75	ILE	0	-0.023	-0.017	15.407	-0.117	-0.117	0.000	0.000	0.000	0.000
77	A	76	ILE	0	-0.022	-0.006	16.257	0.100	0.100	0.000	0.000	0.000	0.000
78	A	77	LEU	0	-0.004	0.004	19.577	-0.034	-0.034	0.000	0.000	0.000	0.000
79	A	78	LEU	0	-0.022	0.000	20.510	0.052	0.052	0.000	0.000	0.000	0.000
80	A	79	THR	0	0.076	0.029	24.248	-0.009	-0.009	0.000	0.000	0.000	0.000
81	A	80	ALA	0	0.052	0.029	27.969	0.019	0.019	0.000	0.000	0.000	0.000
82	A	81	ARG	1	0.884	0.952	31.189	0.204	0.204	0.000	0.000	0.000	0.000
83	A	82	ASP	-1	-0.891	-0.943	32.355	-0.119	-0.119	0.000	0.000	0.000	0.000
84	A	83	GLY	0	0.036	0.022	34.440	0.014	0.014	0.000	0.000	0.000	0.000
85	A	84	LEU	0	-0.028	-0.029	33.540	-0.013	-0.013	0.000	0.000	0.000	0.000
86	A	85	GLU	-1	-0.937	-0.967	34.462	-0.153	-0.153	0.000	0.000	0.000	0.000
87	A	86	ASP	-1	-0.855	-0.944	32.524	-0.199	-0.199	0.000	0.000	0.000	0.000
88	A	87	ARG	1	0.815	0.901	27.452	0.146	0.146	0.000	0.000	0.000	0.000
89	A	88	ILE	0	0.021	0.017	29.686	-0.018	-0.018	0.000	0.000	0.000	0.000
90	A	89	LYS	1	0.910	0.977	30.928	0.240	0.240	0.000	0.000	0.000	0.000
91	A	90	GLY	0	0.051	0.011	28.092	-0.022	-0.022	0.000	0.000	0.000	0.000
92	A	91	LEU	0	-0.016	-0.019	25.164	-0.031	-0.031	0.000	0.000	0.000	0.000
93	A	92	ASP	-1	-0.901	-0.953	26.957	-0.238	-0.238	0.000	0.000	0.000	0.000
94	A	93	LEU	0	-0.130	-0.068	27.356	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	94	GLY	0	-0.003	0.003	24.332	-0.031	-0.031	0.000	0.000	0.000	0.000
96	A	95	ALA	0	-0.033	0.001	22.126	-0.054	-0.054	0.000	0.000	0.000	0.000
97	A	96	ASP	-1	-0.847	-0.922	19.104	-0.562	-0.562	0.000	0.000	0.000	0.000
98	A	97	ASP	-1	-0.836	-0.906	20.529	-0.152	-0.152	0.000	0.000	0.000	0.000
99	A	98	TYR	0	-0.024	-0.024	22.263	-0.037	-0.037	0.000	0.000	0.000	0.000
100	A	99	LEU	0	-0.005	0.005	21.694	0.039	0.039	0.000	0.000	0.000	0.000
101	A	100	THR	0	0.031	0.009	25.054	-0.023	-0.023	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.733	0.868	25.085	0.306	0.306	0.000	0.000	0.000	0.000
103	A	102	PRO	0	-0.009	-0.011	28.739	0.001	0.001	0.000	0.000	0.000	0.000
104	A	103	PHE	0	0.060	0.009	21.530	0.006	0.006	0.000	0.000	0.000	0.000
105	A	104	GLU	-1	-0.909	-0.951	25.039	0.041	0.041	0.000	0.000	0.000	0.000
106	A	105	LEU	0	0.034	0.004	20.126	0.003	0.003	0.000	0.000	0.000	0.000
107	A	106	LYS	1	0.965	0.968	19.777	-0.184	-0.184	0.000	0.000	0.000	0.000
108	A	107	GLU	-1	-0.815	-0.883	19.903	-0.044	-0.044	0.000	0.000	0.000	0.000
109	A	108	LEU	0	0.035	0.017	17.526	0.001	0.001	0.000	0.000	0.000	0.000
110	A	109	VAL	0	0.013	0.004	14.518	-0.042	-0.042	0.000	0.000	0.000	0.000
111	A	110	ALA	0	-0.016	-0.005	15.231	0.034	0.034	0.000	0.000	0.000	0.000
112	A	111	ARG	1	0.772	0.854	16.877	0.144	0.144	0.000	0.000	0.000	0.000
113	A	112	ILE	0	0.042	0.029	11.662	-0.040	-0.040	0.000	0.000	0.000	0.000
114	A	113	LYS	1	0.817	0.885	11.747	-0.674	-0.674	0.000	0.000	0.000	0.000
115	A	114	ALA	0	-0.074	-0.043	13.148	0.075	0.075	0.000	0.000	0.000	0.000
116	A	115	ILE	0	0.020	-0.001	13.131	0.024	0.024	0.000	0.000	0.000	0.000
117	A	116	SER	0	0.025	0.006	9.042	-0.011	-0.011	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.877	0.950	10.642	-0.178	-0.178	0.000	0.000	0.000	0.000
119	A	118	ARG	1	0.880	0.946	13.038	0.104	0.104	0.000	0.000	0.000	0.000
120	A	119	ILE	0	0.016	0.033	9.214	-0.077	-0.077	0.000	0.000	0.000	0.000

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