FMO DATABASE

FMODB ID: 22V8R

Calculation Name: 3UT4-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3UT4

Chain ID: A

ChEMBL ID:

UniProt ID: A3DJ21

Base Structure: X-ray

Registration Date: 2023-06-20

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	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	128
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1235365.212839
FMO2-HF: Nuclear repulsion	1182325.216713
FMO2-HF: Total energy	-53039.996125
FMO2-MP2: Total energy	-53196.749285

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:2:THR)

Summations of interaction energy for fragment #1(A:2:THR)

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.
-10.86	-6.281	3.564	-3.537	-4.608	0.002

Interaction energy analysis for fragmet #1(A:2:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.024 / q_NPA : -0.010

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

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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	4	LEU	0	0.038	0.021	3.061	-4.146	-1.431	0.141	-1.176	-1.680	0.004
4	A	5	ARG	1	0.884	0.924	2.079	-2.720	-1.753	3.415	-2.072	-2.311	0.000
5	A	6	ASP	-1	-0.911	-0.937	3.577	-6.251	-5.428	0.009	-0.287	-0.546	-0.002
6	A	7	LEU	0	0.002	-0.003	5.248	0.739	0.813	-0.001	-0.002	-0.071	0.000
7	A	8	ILE	0	-0.049	0.020	6.089	0.317	0.317	0.000	0.000	0.000	0.000
8	A	9	PRO	0	0.004	0.025	8.916	-0.124	-0.124	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.846	0.891	6.932	1.218	1.218	0.000	0.000	0.000	0.000
10	A	11	HIS	0	0.017	-0.004	11.871	0.108	0.108	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.995	0.997	15.665	0.040	0.040	0.000	0.000	0.000	0.000
12	A	13	PHE	0	-0.036	-0.028	18.463	0.017	0.017	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.820	-0.864	12.652	-0.489	-0.489	0.000	0.000	0.000	0.000
14	A	15	ASN	0	0.073	0.019	15.393	-0.034	-0.034	0.000	0.000	0.000	0.000
15	A	16	SER	0	-0.058	-0.053	13.172	-0.032	-0.032	0.000	0.000	0.000	0.000
16	A	17	THR	0	-0.040	-0.043	10.109	0.000	0.000	0.000	0.000	0.000	0.000
17	A	18	ILE	0	0.027	0.013	12.971	0.028	0.028	0.000	0.000	0.000	0.000
18	A	19	ASP	-1	-0.862	-0.935	15.717	-0.182	-0.182	0.000	0.000	0.000	0.000
19	A	20	GLN	0	-0.067	-0.042	10.882	-0.008	-0.008	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.030	0.018	10.508	0.071	0.071	0.000	0.000	0.000	0.000
21	A	22	CYS	0	-0.058	-0.029	13.486	0.060	0.060	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.873	0.938	15.273	0.155	0.155	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.021	0.020	10.056	0.027	0.027	0.000	0.000	0.000	0.000
24	A	25	ILE	0	0.001	-0.004	14.008	-0.018	-0.018	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.838	-0.923	13.881	0.059	0.059	0.000	0.000	0.000	0.000
26	A	27	ASN	0	0.001	-0.024	13.554	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.896	-0.939	10.110	0.204	0.204	0.000	0.000	0.000	0.000
28	A	29	ILE	0	-0.004	-0.003	8.793	0.033	0.033	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.934	-0.966	10.145	0.103	0.103	0.000	0.000	0.000	0.000
30	A	31	PRO	0	-0.008	-0.006	6.474	-0.021	-0.021	0.000	0.000	0.000	0.000
31	A	32	ILE	0	-0.025	-0.012	6.188	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.000	0.019	8.844	-0.024	-0.024	0.000	0.000	0.000	0.000
33	A	34	PHE	0	0.046	0.012	12.453	-0.014	-0.014	0.000	0.000	0.000	0.000
34	A	35	ASP	-1	-0.841	-0.936	9.088	0.247	0.247	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.029	-0.017	10.925	-0.030	-0.030	0.000	0.000	0.000	0.000
36	A	37	LEU	0	0.037	0.011	13.315	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.945	0.983	13.305	-0.161	-0.161	0.000	0.000	0.000	0.000
38	A	39	TRP	0	-0.036	0.002	12.506	0.009	0.009	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.022	-0.022	17.380	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	41	GLN	0	-0.043	-0.028	18.641	0.002	0.002	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.784	-0.924	21.778	-0.023	-0.023	0.000	0.000	0.000	0.000
42	A	43	TYR	0	0.006	0.004	23.173	-0.012	-0.012	0.000	0.000	0.000	0.000
43	A	44	ASN	0	0.009	-0.008	24.829	-0.008	-0.008	0.000	0.000	0.000	0.000
44	A	45	TRP	0	-0.045	-0.014	18.987	-0.013	-0.013	0.000	0.000	0.000	0.000
45	A	46	PRO	0	-0.038	-0.043	22.378	0.000	0.000	0.000	0.000	0.000	0.000
46	A	47	ILE	0	0.049	0.039	16.209	0.005	0.005	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.027	0.026	19.199	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.806	0.912	20.637	0.080	0.080	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.863	-0.922	19.407	-0.128	-0.128	0.000	0.000	0.000	0.000
50	A	51	ILE	0	-0.054	-0.024	14.766	-0.007	-0.007	0.000	0.000	0.000	0.000
51	A	52	LEU	0	0.000	0.000	18.095	0.013	0.013	0.000	0.000	0.000	0.000
52	A	53	PRO	0	0.027	0.002	21.115	0.011	0.011	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.030	0.021	15.020	0.013	0.013	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.003	-0.013	16.446	0.017	0.017	0.000	0.000	0.000	0.000
55	A	56	VAL	0	-0.008	0.004	18.417	0.014	0.014	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.005	0.004	19.596	0.010	0.010	0.000	0.000	0.000	0.000
57	A	58	HIS	1	0.810	0.896	16.454	0.009	0.009	0.000	0.000	0.000	0.000
58	A	59	GLN	0	0.051	0.019	18.216	0.015	0.015	0.000	0.000	0.000	0.000
59	A	60	SER	0	0.004	-0.015	20.832	0.003	0.003	0.000	0.000	0.000	0.000
60	A	61	ILE	0	0.004	0.025	14.574	0.003	0.003	0.000	0.000	0.000	0.000
61	A	62	ALA	0	0.015	0.010	16.688	0.006	0.006	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.024	0.005	18.152	0.001	0.001	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.035	0.024	18.782	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	65	HIS	0	0.044	0.014	14.209	0.000	0.000	0.000	0.000	0.000	0.000
65	A	66	ILE	0	0.029	0.007	18.716	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.026	-0.013	21.661	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	68	THR	0	0.006	0.007	19.594	0.001	0.001	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.041	-0.017	18.771	0.000	0.000	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.045	-0.028	22.580	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	71	GLN	0	-0.047	-0.029	25.237	0.002	0.002	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.025	0.043	24.489	0.003	0.003	0.000	0.000	0.000	0.000
72	A	73	ASN	0	-0.055	-0.034	25.449	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.865	-0.925	23.025	0.029	0.029	0.000	0.000	0.000	0.000
74	A	75	ILE	0	0.039	0.007	25.891	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	76	MET	0	0.057	0.043	26.036	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	77	TRP	0	-0.008	-0.001	17.708	0.003	0.003	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.865	0.909	24.254	-0.037	-0.037	0.000	0.000	0.000	0.000
78	A	79	TYR	0	0.039	0.017	26.275	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	80	TRP	0	-0.005	-0.006	24.822	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	81	VAL	0	0.007	0.011	22.167	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	82	ILE	0	0.017	0.006	24.914	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.914	0.963	28.399	0.009	0.009	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.033	-0.025	25.046	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	85	MET	0	0.003	-0.001	20.760	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.002	0.021	26.231	0.002	0.002	0.000	0.000	0.000	0.000
86	A	87	PRO	0	-0.060	-0.023	29.060	0.002	0.002	0.000	0.000	0.000	0.000
87	A	88	TYR	0	-0.017	-0.004	27.088	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.018	0.017	24.790	0.001	0.001	0.000	0.000	0.000	0.000
89	A	90	ILE	0	0.015	0.005	26.159	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	91	TYR	0	0.015	-0.010	29.303	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.029	0.004	28.011	0.000	0.000	0.000	0.000	0.000	0.000
92	A	93	ASN	0	0.030	-0.009	24.199	0.007	0.007	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.900	0.949	27.311	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	95	GLN	0	-0.034	-0.014	30.175	0.001	0.001	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.030	0.000	25.204	0.001	0.001	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.031	0.015	26.422	0.002	0.002	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.863	0.942	29.067	-0.023	-0.023	0.000	0.000	0.000	0.000
98	A	99	SER	0	0.044	0.009	31.503	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.796	-0.880	27.797	0.040	0.040	0.000	0.000	0.000	0.000
100	A	101	LEU	0	0.014	0.019	31.190	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.856	-0.925	33.314	0.022	0.022	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.854	0.918	29.932	-0.038	-0.038	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.006	-0.013	30.034	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	105	SER	0	-0.067	-0.036	34.663	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.033	-0.034	37.887	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.081	-0.021	33.741	0.001	0.001	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.910	-0.953	38.507	0.017	0.017	0.000	0.000	0.000	0.000
108	A	109	ILE	0	-0.071	-0.039	39.621	0.001	0.001	0.000	0.000	0.000	0.000
109	A	110	ILE	0	0.000	0.023	37.358	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	111	ASN	0	0.013	-0.003	34.799	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.902	-0.981	37.934	0.006	0.006	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.813	-0.885	34.158	0.009	0.009	0.000	0.000	0.000	0.000
113	A	114	ILE	0	-0.083	-0.049	32.962	0.000	0.000	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.946	0.971	35.526	-0.007	-0.007	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.922	-0.960	34.116	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	117	ILE	0	0.003	0.007	30.600	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	118	VAL	0	-0.007	0.009	33.860	0.000	0.000	0.000	0.000	0.000	0.000
118	A	119	ASN	0	-0.009	-0.037	36.972	0.001	0.001	0.000	0.000	0.000	0.000
119	A	120	LEU	0	-0.011	0.025	31.571	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	121	SER	0	-0.007	-0.010	33.831	0.000	0.000	0.000	0.000	0.000	0.000
121	A	122	LYS	1	0.898	0.956	35.489	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	123	ASP	-1	-0.934	-0.952	38.065	0.001	0.001	0.000	0.000	0.000	0.000
123	A	124	TYR	0	-0.014	-0.028	31.567	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	125	LEU	0	-0.047	-0.023	36.308	0.000	0.000	0.000	0.000	0.000	0.000
125	A	126	HIS	0	-0.069	-0.052	37.929	0.000	0.000	0.000	0.000	0.000	0.000
126	A	127	PHE	0	-0.050	-0.002	37.538	0.000	0.000	0.000	0.000	0.000	0.000
127	A	128	TYR	0	0.014	0.011	35.025	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	129	TYR	0	-0.062	-0.034	31.903	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:THR)