FMO DATABASE

FMODB ID: 2271R

Calculation Name: 3UT4-A-Xray320

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: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	130
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1241912.853237
FMO2-HF: Nuclear repulsion	1188701.956163
FMO2-HF: Total energy	-53210.897075
FMO2-MP2: Total energy	-53368.181073

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:1:ACE )

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

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.
1.153	3.057	0.002	-0.87	-1.037	-0.002

Interaction energy analysis for fragmet #1(A:1:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.034 / q_NPA : 0.004

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	3	SER	0	0.035	0.028	3.807	-0.136	1.384	-0.007	-0.763	-0.750	-0.002
4	A	4	LEU	0	0.038	0.024	3.609	-0.269	-0.037	0.009	-0.063	-0.179	0.000
5	A	5	ARG	1	0.896	0.933	4.377	1.513	1.665	0.000	-0.044	-0.108	0.000
6	A	6	ASP	-1	-0.913	-0.938	6.561	-0.549	-0.549	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.002	-0.006	8.545	0.196	0.196	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.046	0.021	8.796	0.107	0.107	0.000	0.000	0.000	0.000
9	A	9	PRO	0	0.002	0.025	11.815	-0.033	-0.033	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.847	0.892	12.122	0.489	0.489	0.000	0.000	0.000	0.000
11	A	11	HIS	0	0.016	-0.004	16.347	0.022	0.022	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.994	0.997	19.960	0.128	0.128	0.000	0.000	0.000	0.000
13	A	13	PHE	0	-0.033	-0.026	22.490	0.016	0.016	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.821	-0.865	16.926	-0.249	-0.249	0.000	0.000	0.000	0.000
15	A	15	ASN	0	0.074	0.018	18.625	-0.022	-0.022	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.060	-0.053	17.211	0.004	0.004	0.000	0.000	0.000	0.000
17	A	17	THR	0	-0.037	-0.043	13.262	0.019	0.019	0.000	0.000	0.000	0.000
18	A	18	ILE	0	0.025	0.012	15.059	0.013	0.013	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.861	-0.935	17.430	-0.045	-0.045	0.000	0.000	0.000	0.000
20	A	20	GLN	0	-0.068	-0.042	12.447	0.003	0.003	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.032	0.018	11.765	0.035	0.035	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.061	-0.029	14.193	0.031	0.031	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.874	0.939	15.483	0.006	0.006	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.023	0.018	10.064	0.023	0.023	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.004	-0.004	13.641	-0.025	-0.025	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.841	-0.924	13.260	0.098	0.098	0.000	0.000	0.000	0.000
27	A	27	ASN	0	0.002	-0.023	12.326	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.897	-0.939	9.005	0.341	0.341	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.005	-0.005	8.119	0.023	0.023	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.930	-0.963	10.039	0.075	0.075	0.000	0.000	0.000	0.000
31	A	31	PRO	0	-0.012	-0.007	5.889	-0.065	-0.065	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.025	-0.012	6.760	-0.232	-0.232	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.002	0.018	9.331	-0.023	-0.023	0.000	0.000	0.000	0.000
34	A	34	PHE	0	0.047	0.012	12.497	-0.014	-0.014	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.839	-0.935	9.866	-0.534	-0.534	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.031	-0.018	12.427	0.012	0.012	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.036	0.010	14.857	0.018	0.018	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.943	0.983	14.651	0.298	0.298	0.000	0.000	0.000	0.000
39	A	39	TRP	0	-0.031	0.004	15.519	0.032	0.032	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.025	-0.023	19.758	0.014	0.014	0.000	0.000	0.000	0.000
41	A	41	GLN	0	-0.043	-0.028	20.337	0.008	0.008	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.785	-0.923	23.778	-0.077	-0.077	0.000	0.000	0.000	0.000
43	A	43	TYR	0	0.007	0.004	25.657	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	44	ASN	0	0.011	-0.008	27.131	0.006	0.006	0.000	0.000	0.000	0.000
45	A	45	TRP	0	-0.045	-0.014	21.612	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	46	PRO	0	-0.042	-0.044	25.614	0.003	0.003	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.053	0.041	19.130	0.008	0.008	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.026	0.025	21.595	0.001	0.001	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.808	0.914	22.970	0.085	0.085	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.863	-0.922	21.343	-0.073	-0.073	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.053	-0.025	16.604	0.001	0.001	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.003	-0.001	19.671	0.009	0.009	0.000	0.000	0.000	0.000
53	A	53	PRO	0	0.029	0.003	22.076	0.010	0.010	0.000	0.000	0.000	0.000
54	A	54	VAL	0	0.027	0.020	15.632	0.014	0.014	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.002	-0.012	16.987	0.015	0.015	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.009	0.004	18.835	0.013	0.013	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.003	0.006	19.702	0.011	0.011	0.000	0.000	0.000	0.000
58	A	58	HIS	1	0.808	0.895	16.311	-0.025	-0.025	0.000	0.000	0.000	0.000
59	A	59	GLN	0	0.049	0.017	17.984	0.007	0.007	0.000	0.000	0.000	0.000
60	A	60	SER	0	0.005	-0.014	20.409	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	61	ILE	0	0.005	0.025	14.204	0.001	0.001	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.016	0.009	16.213	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	63	MET	0	-0.028	0.004	17.979	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	64	PRO	0	0.038	0.025	17.725	-0.010	-0.010	0.000	0.000	0.000	0.000
65	A	65	HIS	0	0.043	0.014	13.292	-0.039	-0.039	0.000	0.000	0.000	0.000
66	A	66	ILE	0	0.031	0.007	18.253	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.029	-0.015	21.502	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	68	THR	0	0.007	0.007	18.928	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	69	ILE	0	-0.039	-0.017	19.177	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.048	-0.028	22.591	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	71	GLN	0	-0.046	-0.029	24.332	0.000	0.000	0.000	0.000	0.000	0.000
72	A	72	GLY	0	0.026	0.042	24.560	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	73	ASN	0	-0.054	-0.033	25.408	0.010	0.010	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.864	-0.926	24.489	-0.097	-0.097	0.000	0.000	0.000	0.000
75	A	75	ILE	0	0.037	0.007	26.902	0.002	0.002	0.000	0.000	0.000	0.000
76	A	76	MET	0	0.057	0.043	27.996	0.002	0.002	0.000	0.000	0.000	0.000
77	A	77	TRP	0	-0.007	-0.001	18.453	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.863	0.909	25.646	0.052	0.052	0.000	0.000	0.000	0.000
79	A	79	TYR	0	0.045	0.019	27.109	0.007	0.007	0.000	0.000	0.000	0.000
80	A	80	TRP	0	-0.009	-0.007	26.417	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.007	0.011	23.094	0.004	0.004	0.000	0.000	0.000	0.000
82	A	82	ILE	0	0.016	0.006	25.822	0.007	0.007	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.917	0.964	29.010	0.040	0.040	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.034	-0.024	26.505	0.004	0.004	0.000	0.000	0.000	0.000
85	A	85	MET	0	0.002	-0.002	21.090	0.000	0.000	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.001	0.022	26.661	0.006	0.006	0.000	0.000	0.000	0.000
87	A	87	PRO	0	-0.059	-0.022	29.315	0.005	0.005	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.020	-0.005	27.380	0.003	0.003	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.015	0.018	24.836	0.004	0.004	0.000	0.000	0.000	0.000
90	A	90	ILE	0	0.014	0.004	25.592	0.001	0.001	0.000	0.000	0.000	0.000
91	A	91	TYR	0	0.014	-0.010	28.983	0.000	0.000	0.000	0.000	0.000	0.000
92	A	92	PRO	0	0.028	0.004	27.383	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	93	ASN	0	0.028	-0.010	23.689	0.004	0.004	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.901	0.949	26.894	-0.007	-0.007	0.000	0.000	0.000	0.000
95	A	95	GLN	0	-0.040	-0.017	29.938	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.027	0.001	24.543	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.028	0.014	26.079	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.870	0.945	28.652	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	99	SER	0	0.041	0.008	30.734	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.794	-0.879	27.269	-0.020	-0.020	0.000	0.000	0.000	0.000
101	A	101	LEU	0	0.009	0.018	30.709	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.853	-0.924	33.093	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	103	ARG	1	0.854	0.918	29.429	0.023	0.023	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.005	-0.013	29.961	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	105	SER	0	-0.068	-0.036	34.508	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.033	-0.033	37.598	0.001	0.001	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.080	-0.021	33.732	0.000	0.000	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.910	-0.953	38.430	-0.020	-0.020	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.073	-0.039	39.947	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	110	ILE	0	0.001	0.023	37.873	0.000	0.000	0.000	0.000	0.000	0.000
111	A	111	ASN	0	0.012	-0.003	36.019	0.001	0.001	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.902	-0.980	38.891	-0.035	-0.035	0.000	0.000	0.000	0.000
113	A	113	ASP	-1	-0.812	-0.885	35.636	-0.047	-0.047	0.000	0.000	0.000	0.000
114	A	114	ILE	0	-0.083	-0.050	33.545	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	115	ARG	1	0.947	0.972	36.469	0.029	0.029	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.921	-0.960	35.535	-0.039	-0.039	0.000	0.000	0.000	0.000
117	A	117	ILE	0	0.000	0.006	31.646	0.001	0.001	0.000	0.000	0.000	0.000
118	A	118	VAL	0	-0.006	0.010	34.640	0.003	0.003	0.000	0.000	0.000	0.000
119	A	119	ASN	0	-0.007	-0.037	37.446	0.004	0.004	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.016	0.023	32.522	0.002	0.002	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.005	-0.009	34.049	0.002	0.002	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.897	0.955	35.753	0.019	0.019	0.000	0.000	0.000	0.000
123	A	123	ASP	-1	-0.932	-0.951	38.745	-0.015	-0.015	0.000	0.000	0.000	0.000
124	A	124	TYR	0	-0.016	-0.028	32.193	0.002	0.002	0.000	0.000	0.000	0.000
125	A	125	LEU	0	-0.048	-0.024	36.047	0.003	0.003	0.000	0.000	0.000	0.000
126	A	126	HIS	0	-0.067	-0.050	37.957	0.003	0.003	0.000	0.000	0.000	0.000
127	A	127	PHE	0	-0.049	-0.001	37.818	0.002	0.002	0.000	0.000	0.000	0.000
128	A	128	TYR	0	0.009	0.008	35.078	0.002	0.002	0.000	0.000	0.000	0.000
129	A	129	TYR	0	-0.079	-0.058	31.712	0.002	0.002	0.000	0.000	0.000	0.000
130	A	130	NME	0	0.022	0.025	38.242	0.000	0.000	0.000	0.000	0.000	0.000

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