FMO DATABASE

FMODB ID: R8448

Calculation Name: 4U4I-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4U4I

Chain ID: A

ChEMBL ID:

UniProt ID: G5CS11

Base Structure: X-ray

Registration Date: 2023-09-23

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	124
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1074162.922475
FMO2-HF: Nuclear repulsion	1023962.616499
FMO2-HF: Total energy	-50200.305976
FMO2-MP2: Total energy	-50342.688634

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:9:PHE)

Summations of interaction energy for fragment #1(A:9:PHE)

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.
-7.126	-1.386	4.109	-2.48	-7.369	0.017

Interaction energy analysis for fragmet #1(A:9:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.010 / q_NPA : -0.012

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	11	ASN	0	-0.018	-0.023	3.865	-0.458	0.866	-0.016	-0.559	-0.749	0.002
4	A	12	VAL	0	0.003	0.001	2.734	-0.400	0.289	0.787	-0.323	-1.153	-0.001
5	A	13	VAL	0	0.021	0.025	5.251	0.065	0.101	-0.001	-0.003	-0.032	0.000
6	A	14	THR	0	0.036	0.012	8.631	-0.008	-0.008	0.000	0.000	0.000	0.000
7	A	15	ALA	0	-0.036	-0.018	10.635	0.061	0.061	0.000	0.000	0.000	0.000
8	A	16	ILE	0	0.013	0.008	14.290	-0.036	-0.036	0.000	0.000	0.000	0.000
9	A	17	CYS	0	-0.068	-0.016	17.267	0.034	0.034	0.000	0.000	0.000	0.000
10	A	18	GLN	0	0.032	0.015	20.362	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	19	LEU	0	-0.012	-0.010	22.408	0.012	0.012	0.000	0.000	0.000	0.000
12	A	20	ASP	-1	-0.760	-0.841	25.847	-0.111	-0.111	0.000	0.000	0.000	0.000
13	A	21	LYS	1	0.840	0.915	28.875	0.105	0.105	0.000	0.000	0.000	0.000
14	A	22	PRO	0	0.018	0.001	30.313	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	23	HIS	0	0.047	0.031	32.286	0.002	0.002	0.000	0.000	0.000	0.000
16	A	24	ASP	-1	-0.802	-0.885	28.157	-0.141	-0.141	0.000	0.000	0.000	0.000
17	A	25	TYR	0	0.002	-0.006	27.747	0.002	0.002	0.000	0.000	0.000	0.000
18	A	26	GLY	0	-0.001	0.020	24.616	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	27	TYR	0	-0.039	-0.037	17.499	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	28	ALA	0	0.026	0.020	17.578	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	29	ILE	0	-0.010	-0.014	11.973	0.017	0.017	0.000	0.000	0.000	0.000
22	A	30	PHE	0	0.016	0.007	12.343	0.009	0.009	0.000	0.000	0.000	0.000
23	A	31	THR	0	-0.009	-0.030	6.197	-0.019	-0.019	0.000	0.000	0.000	0.000
24	A	32	GLN	0	0.023	0.002	7.952	0.102	0.102	0.000	0.000	0.000	0.000
25	A	33	LEU	0	0.020	0.014	2.565	-1.644	-0.091	0.924	-0.577	-1.901	0.006
26	A	34	PRO	0	-0.018	-0.013	2.666	-3.421	-1.283	2.415	-1.018	-3.534	0.010
27	A	35	ASP	-1	-0.838	-0.904	5.475	-0.685	-0.685	0.000	0.000	0.000	0.000
28	A	36	CYS	0	-0.100	-0.074	7.011	-0.337	-0.337	0.000	0.000	0.000	0.000
29	A	37	THR	0	-0.034	-0.017	7.763	0.160	0.160	0.000	0.000	0.000	0.000
30	A	38	GLU	-1	-0.788	-0.876	7.610	-0.978	-0.978	0.000	0.000	0.000	0.000
31	A	39	ILE	0	-0.004	-0.020	9.620	0.034	0.034	0.000	0.000	0.000	0.000
32	A	40	GLN	0	-0.021	-0.004	10.287	0.084	0.084	0.000	0.000	0.000	0.000
33	A	41	PHE	0	0.027	-0.002	14.353	0.026	0.026	0.000	0.000	0.000	0.000
34	A	42	HIS	1	0.824	0.898	15.059	0.336	0.336	0.000	0.000	0.000	0.000
35	A	43	LEU	0	0.013	0.023	20.168	0.014	0.014	0.000	0.000	0.000	0.000
36	A	44	LYS	1	0.866	0.907	23.558	0.141	0.141	0.000	0.000	0.000	0.000
37	A	45	ASN	0	-0.024	-0.036	27.076	0.003	0.003	0.000	0.000	0.000	0.000
38	A	46	LEU	0	0.009	0.021	26.165	0.007	0.007	0.000	0.000	0.000	0.000
39	A	47	PRO	0	0.035	0.008	30.229	0.000	0.000	0.000	0.000	0.000	0.000
40	A	48	PRO	0	0.020	0.007	30.100	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	49	GLY	0	0.012	0.020	29.549	0.006	0.006	0.000	0.000	0.000	0.000
42	A	50	LYS	1	0.800	0.877	26.021	0.093	0.093	0.000	0.000	0.000	0.000
43	A	51	HIS	1	0.791	0.901	26.325	0.113	0.113	0.000	0.000	0.000	0.000
44	A	52	GLY	0	0.095	0.065	25.467	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	53	CYS	0	-0.088	-0.022	20.845	0.000	0.000	0.000	0.000	0.000	0.000
46	A	54	HIS	1	0.772	0.867	22.758	0.101	0.101	0.000	0.000	0.000	0.000
47	A	55	ILE	0	0.055	0.032	19.176	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	56	HIS	1	0.746	0.856	23.226	0.095	0.095	0.000	0.000	0.000	0.000
49	A	57	LYS	1	0.962	0.982	25.469	0.043	0.043	0.000	0.000	0.000	0.000
50	A	58	SER	0	-0.003	0.008	26.572	0.002	0.002	0.000	0.000	0.000	0.000
51	A	59	GLY	0	0.127	0.051	26.614	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	60	ASP	-1	-0.837	-0.891	27.186	-0.065	-0.065	0.000	0.000	0.000	0.000
53	A	61	ARG	1	0.805	0.854	28.191	0.108	0.108	0.000	0.000	0.000	0.000
54	A	62	ARG	1	0.869	0.912	32.543	0.055	0.055	0.000	0.000	0.000	0.000
55	A	63	ASN	0	-0.001	0.013	36.101	0.001	0.001	0.000	0.000	0.000	0.000
56	A	64	GLY	0	0.083	0.037	34.723	0.000	0.000	0.000	0.000	0.000	0.000
57	A	65	CYS	0	-0.035	-0.035	26.836	0.000	0.000	0.000	0.000	0.000	0.000
58	A	66	THR	0	-0.003	0.008	32.175	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	67	SER	0	-0.018	-0.011	33.345	0.002	0.002	0.000	0.000	0.000	0.000
60	A	68	MET	0	-0.033	0.034	26.477	0.001	0.001	0.000	0.000	0.000	0.000
61	A	69	GLY	0	0.006	0.017	29.525	0.001	0.001	0.000	0.000	0.000	0.000
62	A	70	PRO	0	0.021	0.005	30.865	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	71	HIS	0	0.081	0.033	26.857	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	72	PHE	0	-0.053	-0.030	20.712	0.007	0.007	0.000	0.000	0.000	0.000
65	A	73	ASN	0	0.071	0.030	23.953	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	74	PRO	0	-0.006	0.004	22.585	0.004	0.004	0.000	0.000	0.000	0.000
67	A	75	PHE	0	0.032	0.004	19.654	0.005	0.005	0.000	0.000	0.000	0.000
68	A	76	ASN	0	-0.023	0.012	25.444	0.001	0.001	0.000	0.000	0.000	0.000
69	A	89	LEU	0	-0.010	-0.025	19.558	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	90	GLY	0	0.024	0.023	19.976	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	91	ASP	-1	-0.920	-0.963	22.052	-0.109	-0.109	0.000	0.000	0.000	0.000
72	A	92	LEU	0	-0.025	-0.024	17.397	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	93	GLY	0	0.023	0.027	19.508	-0.014	-0.014	0.000	0.000	0.000	0.000
74	A	94	ASN	0	-0.039	-0.028	22.204	0.002	0.002	0.000	0.000	0.000	0.000
75	A	95	ILE	0	0.010	0.017	20.151	-0.009	-0.009	0.000	0.000	0.000	0.000
76	A	96	VAL	0	-0.023	-0.046	22.454	0.018	0.018	0.000	0.000	0.000	0.000
77	A	97	VAL	0	-0.059	0.001	24.007	-0.012	-0.012	0.000	0.000	0.000	0.000
78	A	98	ASN	0	-0.019	-0.019	23.833	0.013	0.013	0.000	0.000	0.000	0.000
79	A	99	ASN	0	0.013	-0.020	27.789	0.006	0.006	0.000	0.000	0.000	0.000
80	A	100	ASN	0	-0.039	-0.029	27.545	0.006	0.006	0.000	0.000	0.000	0.000
81	A	101	GLY	0	0.041	0.028	29.788	0.001	0.001	0.000	0.000	0.000	0.000
82	A	102	GLU	-1	-0.897	-0.940	24.624	-0.179	-0.179	0.000	0.000	0.000	0.000
83	A	103	CYS	0	-0.061	-0.017	21.558	0.000	0.000	0.000	0.000	0.000	0.000
84	A	104	ASN	0	0.006	0.001	19.593	-0.025	-0.025	0.000	0.000	0.000	0.000
85	A	105	GLU	-1	-0.794	-0.875	17.565	-0.231	-0.231	0.000	0.000	0.000	0.000
86	A	106	ILE	0	-0.002	-0.017	10.895	-0.012	-0.012	0.000	0.000	0.000	0.000
87	A	107	ILE	0	0.018	0.026	13.587	0.007	0.007	0.000	0.000	0.000	0.000
88	A	109	VAL	0	0.011	0.024	11.518	0.020	0.020	0.000	0.000	0.000	0.000
89	A	110	LYS	1	0.838	0.900	9.313	0.123	0.123	0.000	0.000	0.000	0.000
90	A	111	TYR	0	-0.023	-0.024	12.945	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	112	LEU	0	0.057	0.050	14.159	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	113	PRO	0	-0.015	0.020	13.125	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	114	LEU	0	0.051	0.006	10.782	-0.024	-0.024	0.000	0.000	0.000	0.000
94	A	115	THR	0	0.008	0.004	12.384	-0.018	-0.018	0.000	0.000	0.000	0.000
95	A	116	GLY	0	0.037	0.018	14.580	0.028	0.028	0.000	0.000	0.000	0.000
96	A	117	SER	0	-0.012	-0.022	17.265	-0.009	-0.009	0.000	0.000	0.000	0.000
97	A	118	ASN	0	-0.041	-0.018	19.483	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	119	GLN	0	-0.044	-0.001	17.013	0.002	0.002	0.000	0.000	0.000	0.000
99	A	120	ILE	0	0.018	0.000	16.151	0.002	0.002	0.000	0.000	0.000	0.000
100	A	121	ILE	0	-0.013	0.010	14.527	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	122	GLY	0	-0.010	-0.002	18.767	0.015	0.015	0.000	0.000	0.000	0.000
102	A	123	ARG	1	0.801	0.906	21.914	0.077	0.077	0.000	0.000	0.000	0.000
103	A	124	GLY	0	0.018	-0.007	23.290	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	125	LEU	0	0.014	0.011	19.842	0.004	0.004	0.000	0.000	0.000	0.000
105	A	126	VAL	0	-0.068	-0.055	23.398	0.003	0.003	0.000	0.000	0.000	0.000
106	A	127	ILE	0	0.064	0.039	23.078	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	128	HIS	0	-0.061	-0.040	26.718	0.007	0.007	0.000	0.000	0.000	0.000
108	A	129	GLU	-1	-0.888	-0.961	29.771	-0.088	-0.088	0.000	0.000	0.000	0.000
109	A	130	LYS	1	0.879	0.922	32.252	0.067	0.067	0.000	0.000	0.000	0.000
110	A	131	GLU	-1	-0.790	-0.878	28.691	-0.100	-0.100	0.000	0.000	0.000	0.000
111	A	132	ASP	-1	-0.838	-0.907	26.569	-0.089	-0.089	0.000	0.000	0.000	0.000
112	A	133	ASP	-1	-0.977	-0.980	28.568	-0.073	-0.073	0.000	0.000	0.000	0.000
113	A	149	GLY	0	0.062	0.022	32.133	0.001	0.001	0.000	0.000	0.000	0.000
114	A	150	ASP	-1	-0.834	-0.898	33.334	-0.066	-0.066	0.000	0.000	0.000	0.000
115	A	151	ARG	1	0.791	0.883	31.581	0.068	0.068	0.000	0.000	0.000	0.000
116	A	152	ILE	0	0.029	0.026	29.744	0.000	0.000	0.000	0.000	0.000	0.000
117	A	153	ALA	0	0.055	0.039	28.017	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	155	GLY	0	0.092	0.035	24.573	0.001	0.001	0.000	0.000	0.000	0.000
119	A	156	ILE	0	-0.046	-0.022	23.261	0.005	0.005	0.000	0.000	0.000	0.000
120	A	157	ILE	0	0.000	0.016	17.806	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	158	ALA	0	0.010	-0.001	19.203	0.020	0.020	0.000	0.000	0.000	0.000
122	A	159	TYR	0	0.051	0.010	13.738	-0.018	-0.018	0.000	0.000	0.000	0.000
123	A	160	LEU	0	-0.012	0.004	12.544	0.016	0.016	0.000	0.000	0.000	0.000
124	A	161	ASN	0	-0.009	0.006	11.687	0.031	0.031	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:PHE)