FMO DATABASE

FMODB ID: 6618Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1234907.095272
FMO2-HF: Nuclear repulsion	1181866.277592
FMO2-HF: Total energy	-53040.81768
FMO2-MP2: Total energy	-53197.531277

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.
-9.549	-4.792	3.065	-3.283	-4.538	0.007

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 : 0.019 / q_NPA : -0.014

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	0.070	0.030	3.198	-3.282	-0.496	0.156	-1.246	-1.697	0.006
4	A	5	ARG	1	0.898	0.919	2.162	-6.537	-5.012	2.903	-2.045	-2.382	0.001
5	A	6	ASP	-1	-0.878	-0.917	3.565	-2.556	-2.201	0.007	0.012	-0.373	0.000
6	A	7	LEU	0	0.006	-0.010	5.309	0.287	0.378	-0.001	-0.004	-0.086	0.000
7	A	8	ILE	0	-0.050	-0.007	6.104	0.155	0.155	0.000	0.000	0.000	0.000
8	A	9	PRO	0	-0.004	0.016	8.891	-0.169	-0.169	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.827	0.904	6.720	0.876	0.876	0.000	0.000	0.000	0.000
10	A	11	HIS	0	0.016	-0.005	11.768	0.076	0.076	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.937	0.968	15.555	-0.084	-0.084	0.000	0.000	0.000	0.000
12	A	13	PHE	0	-0.034	-0.025	18.404	0.011	0.011	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.819	-0.867	12.669	-0.231	-0.231	0.000	0.000	0.000	0.000
14	A	15	ASN	0	0.039	0.004	15.378	0.000	0.000	0.000	0.000	0.000	0.000
15	A	16	SER	0	-0.053	-0.048	13.251	-0.022	-0.022	0.000	0.000	0.000	0.000
16	A	17	THR	0	-0.018	-0.007	10.176	-0.042	-0.042	0.000	0.000	0.000	0.000
17	A	18	ILE	0	0.006	0.005	12.932	0.073	0.073	0.000	0.000	0.000	0.000
18	A	19	ASP	-1	-0.806	-0.899	15.665	0.001	0.001	0.000	0.000	0.000	0.000
19	A	20	GLN	0	-0.004	-0.013	10.849	0.001	0.001	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.021	0.014	10.281	0.093	0.093	0.000	0.000	0.000	0.000
21	A	22	CYS	0	-0.078	-0.040	13.411	0.055	0.055	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.773	0.880	15.568	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.025	0.019	10.365	0.030	0.030	0.000	0.000	0.000	0.000
24	A	25	ILE	0	-0.011	-0.019	14.597	-0.054	-0.054	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.824	-0.920	14.660	0.423	0.423	0.000	0.000	0.000	0.000
26	A	27	ASN	0	0.007	-0.021	14.301	0.064	0.064	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.887	-0.925	10.840	0.591	0.591	0.000	0.000	0.000	0.000
28	A	29	ILE	0	0.002	-0.002	9.619	0.308	0.308	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.883	-0.932	10.873	0.757	0.757	0.000	0.000	0.000	0.000
30	A	31	PRO	0	0.008	0.005	7.011	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	32	ILE	0	-0.048	-0.029	6.010	0.147	0.147	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.009	0.022	9.044	-0.176	-0.176	0.000	0.000	0.000	0.000
33	A	34	PHE	0	0.061	0.021	12.711	-0.091	-0.091	0.000	0.000	0.000	0.000
34	A	35	ASP	-1	-0.828	-0.904	8.932	1.096	1.096	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.021	-0.009	10.796	-0.114	-0.114	0.000	0.000	0.000	0.000
36	A	37	LEU	0	0.037	0.009	13.273	-0.081	-0.081	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.896	0.948	11.861	-0.699	-0.699	0.000	0.000	0.000	0.000
38	A	39	TRP	0	-0.031	-0.002	12.402	-0.081	-0.081	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.026	-0.021	17.362	-0.038	-0.038	0.000	0.000	0.000	0.000
40	A	41	GLN	0	-0.072	-0.049	18.909	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.770	-0.905	21.767	0.087	0.087	0.000	0.000	0.000	0.000
42	A	43	TYR	0	0.019	0.013	23.159	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	44	ASN	0	-0.038	-0.039	24.806	-0.017	-0.017	0.000	0.000	0.000	0.000
44	A	45	TRP	0	-0.038	-0.014	18.781	-0.022	-0.022	0.000	0.000	0.000	0.000
45	A	46	PRO	0	-0.025	-0.029	22.420	0.007	0.007	0.000	0.000	0.000	0.000
46	A	47	ILE	0	0.036	0.036	16.170	0.001	0.001	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.030	0.024	19.167	0.016	0.016	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.842	0.925	20.608	-0.053	-0.053	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.851	-0.921	19.295	0.044	0.044	0.000	0.000	0.000	0.000
50	A	51	ILE	0	-0.032	-0.019	14.522	0.017	0.017	0.000	0.000	0.000	0.000
51	A	52	LEU	0	0.002	0.007	18.046	0.030	0.030	0.000	0.000	0.000	0.000
52	A	53	PRO	0	0.016	-0.001	20.912	0.013	0.013	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.014	0.013	14.949	0.011	0.011	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.002	-0.015	16.213	0.028	0.028	0.000	0.000	0.000	0.000
55	A	56	VAL	0	-0.003	0.005	18.466	0.005	0.005	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.006	0.008	19.734	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	58	HIS	1	0.825	0.898	16.477	-0.343	-0.343	0.000	0.000	0.000	0.000
58	A	59	GLN	0	0.073	0.030	18.876	0.022	0.022	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.016	-0.019	21.419	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	61	ILE	0	-0.023	0.005	15.217	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	62	ALA	0	0.032	0.020	17.286	0.037	0.037	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.013	0.008	18.727	-0.013	-0.013	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.028	0.018	19.208	-0.016	-0.016	0.000	0.000	0.000	0.000
64	A	65	HIS	0	0.001	-0.009	14.652	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	66	ILE	0	0.024	0.006	19.059	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.017	-0.007	21.846	-0.020	-0.020	0.000	0.000	0.000	0.000
67	A	68	THR	0	-0.006	-0.008	19.673	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.022	-0.007	18.673	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.048	-0.025	22.555	-0.020	-0.020	0.000	0.000	0.000	0.000
70	A	71	GLN	0	-0.059	-0.037	25.360	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.019	0.038	24.481	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	73	ASN	0	-0.044	-0.032	25.440	-0.019	-0.019	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.828	-0.901	22.924	0.187	0.187	0.000	0.000	0.000	0.000
74	A	75	ILE	0	0.041	0.005	25.889	0.005	0.005	0.000	0.000	0.000	0.000
75	A	76	MET	0	0.053	0.029	26.388	0.000	0.000	0.000	0.000	0.000	0.000
76	A	77	TRP	0	-0.009	0.000	17.609	0.005	0.005	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.835	0.898	24.238	-0.161	-0.161	0.000	0.000	0.000	0.000
78	A	79	TYR	0	-0.027	-0.041	26.251	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	80	TRP	0	0.001	-0.002	24.829	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	81	VAL	0	0.017	0.015	22.075	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	ILE	0	0.015	0.011	24.875	0.000	0.000	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.873	0.945	28.357	-0.100	-0.100	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.029	-0.021	24.975	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	85	MET	0	0.001	-0.003	20.786	0.004	0.004	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.002	0.015	26.176	0.000	0.000	0.000	0.000	0.000	0.000
86	A	87	PRO	0	-0.044	-0.009	29.151	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	88	TYR	0	-0.035	-0.017	27.205	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.023	0.012	25.077	0.011	0.011	0.000	0.000	0.000	0.000
89	A	90	ILE	0	0.016	0.006	27.403	-0.016	-0.016	0.000	0.000	0.000	0.000
90	A	91	TYR	0	0.024	-0.006	29.951	0.005	0.005	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.023	-0.003	28.851	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	93	ASN	0	0.008	-0.007	24.999	0.008	0.008	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.909	0.943	27.973	-0.104	-0.104	0.000	0.000	0.000	0.000
94	A	95	GLN	0	-0.017	-0.004	30.722	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.031	0.001	25.774	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.019	0.005	26.666	0.003	0.003	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.817	0.915	29.510	-0.111	-0.111	0.000	0.000	0.000	0.000
98	A	99	SER	0	0.039	0.007	31.890	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.794	-0.871	28.052	0.157	0.157	0.000	0.000	0.000	0.000
100	A	101	LEU	0	0.027	0.025	31.416	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.807	-0.894	33.427	0.098	0.098	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.864	0.927	29.955	-0.151	-0.151	0.000	0.000	0.000	0.000
103	A	104	LEU	0	0.013	-0.001	29.969	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	105	SER	0	-0.063	-0.031	34.634	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.027	-0.020	37.851	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.065	-0.014	33.778	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.913	-0.952	38.488	0.068	0.068	0.000	0.000	0.000	0.000
108	A	109	ILE	0	-0.063	-0.038	39.588	0.003	0.003	0.000	0.000	0.000	0.000
109	A	110	ILE	0	-0.002	0.012	37.618	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	111	ASN	0	-0.012	-0.020	34.668	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.797	-0.895	37.932	0.071	0.071	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.823	-0.890	34.175	0.087	0.087	0.000	0.000	0.000	0.000
113	A	114	ILE	0	-0.059	-0.038	33.191	0.006	0.006	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.840	0.900	35.516	-0.064	-0.064	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.834	-0.887	34.201	0.086	0.086	0.000	0.000	0.000	0.000
116	A	117	ILE	0	-0.005	0.003	30.572	0.003	0.003	0.000	0.000	0.000	0.000
117	A	118	VAL	0	0.001	0.022	33.836	0.001	0.001	0.000	0.000	0.000	0.000
118	A	119	ASN	0	-0.007	-0.038	36.946	0.000	0.000	0.000	0.000	0.000	0.000
119	A	120	LEU	0	-0.008	0.025	31.604	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	121	SER	0	-0.007	-0.020	33.934	0.003	0.003	0.000	0.000	0.000	0.000
121	A	122	LYS	1	0.862	0.923	35.450	-0.080	-0.080	0.000	0.000	0.000	0.000
122	A	123	ASP	-1	-0.914	-0.949	38.053	0.076	0.076	0.000	0.000	0.000	0.000
123	A	124	TYR	0	-0.031	-0.045	31.504	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	125	LEU	0	-0.054	-0.024	36.189	0.001	0.001	0.000	0.000	0.000	0.000
125	A	126	HIS	0	-0.071	-0.045	38.060	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	127	PHE	0	-0.040	0.006	37.769	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	128	TYR	0	0.008	0.004	35.149	0.000	0.000	0.000	0.000	0.000	0.000
128	A	129	TYR	0	-0.047	-0.021	32.332	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)