FMO DATABASE

FMODB ID: YV182

Calculation Name: 1U61-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1U61

Chain ID: A

ChEMBL ID:

UniProt ID: Q81J58

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:

Apendix: None

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	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1122027.483121
FMO2-HF: Nuclear repulsion	1072063.851917
FMO2-HF: Total energy	-49963.631204
FMO2-MP2: Total energy	-50112.883477

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:ILE)

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

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.
-2.43	1.608	3.02	-1.735	-5.321	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / 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	ALA	0	0.015	-0.006	3.427	-0.460	1.971	0.064	-1.055	-1.439	0.002
4	A	5	LYS	1	0.850	0.918	3.965	1.550	1.732	0.003	-0.018	-0.166	0.000
5	A	6	GLN	0	-0.081	-0.045	6.106	0.532	0.532	0.000	0.000	0.000	0.000
6	A	7	LEU	0	-0.042	0.002	2.634	-0.510	0.189	0.673	-0.218	-1.154	0.000
7	A	8	ASN	0	-0.017	-0.009	5.665	-0.133	-0.133	0.000	0.000	0.000	0.000
8	A	9	SER	0	0.036	-0.019	8.317	-0.016	-0.016	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.016	0.022	10.705	-0.026	-0.026	0.000	0.000	0.000	0.000
10	A	11	ALA	0	-0.014	-0.010	6.047	0.021	0.021	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.018	0.003	5.521	-0.020	-0.020	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.027	0.002	7.326	-0.034	-0.034	0.000	0.000	0.000	0.000
13	A	14	TYR	0	-0.042	-0.018	7.939	0.013	0.013	0.000	0.000	0.000	0.000
14	A	15	MET	0	-0.033	-0.005	5.334	0.068	0.068	0.000	0.000	0.000	0.000
15	A	16	GLY	0	0.045	0.009	7.867	-0.040	-0.040	0.000	0.000	0.000	0.000
16	A	17	ASP	-1	-0.941	-0.973	10.532	0.003	0.003	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.008	0.004	11.097	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.014	0.003	9.511	0.008	0.008	0.000	0.000	0.000	0.000
19	A	20	TYR	0	0.010	-0.013	12.634	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.756	-0.879	15.956	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	22	GLN	0	-0.080	-0.031	12.926	-0.016	-0.016	0.000	0.000	0.000	0.000
22	A	23	TYR	0	-0.019	-0.027	14.620	0.000	0.000	0.000	0.000	0.000	0.000
23	A	24	ILE	0	-0.016	0.008	18.632	0.012	0.012	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.794	0.874	20.017	0.002	0.002	0.000	0.000	0.000	0.000
25	A	26	TYR	0	0.015	0.014	20.529	0.010	0.010	0.000	0.000	0.000	0.000
26	A	27	HIS	0	0.015	-0.006	22.359	0.003	0.003	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.031	-0.023	24.635	0.007	0.007	0.000	0.000	0.000	0.000
28	A	29	LEU	0	-0.058	-0.030	23.779	0.007	0.007	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.043	-0.011	26.019	0.006	0.006	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.828	0.912	28.178	0.060	0.060	0.000	0.000	0.000	0.000
31	A	32	GLY	0	0.021	0.020	30.099	0.004	0.004	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.861	0.911	31.932	0.040	0.040	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.011	0.010	31.424	0.001	0.001	0.000	0.000	0.000	0.000
34	A	35	ARG	1	0.964	0.973	33.509	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.096	0.035	30.633	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	37	ASN	0	-0.008	-0.006	30.449	0.001	0.001	0.000	0.000	0.000	0.000
37	A	38	GLN	0	-0.016	-0.009	32.370	0.002	0.002	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.052	0.032	26.941	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	40	HIS	0	0.067	0.046	24.146	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	41	ARG	1	0.955	0.986	26.803	0.011	0.011	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.001	0.000	28.829	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	43	GLY	0	0.112	0.066	24.542	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.026	-0.025	24.344	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.117	-0.071	25.847	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	46	PHE	0	0.042	0.020	23.004	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	47	VAL	0	0.043	0.017	19.833	-0.013	-0.013	0.000	0.000	0.000	0.000
47	A	48	SER	0	-0.054	-0.016	21.057	0.005	0.005	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.044	0.006	22.065	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.944	0.954	23.082	0.022	0.022	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.006	0.035	24.094	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	52	GLN	0	0.074	0.021	17.652	-0.026	-0.026	0.000	0.000	0.000	0.000
52	A	53	ALA	0	-0.014	-0.001	21.633	-0.014	-0.014	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.845	0.940	23.699	0.076	0.076	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.001	0.008	20.989	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.019	0.002	19.562	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	57	TYR	0	-0.033	-0.029	22.321	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	58	HIS	0	0.075	0.043	25.898	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.029	-0.003	19.811	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.029	-0.007	21.396	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.933	-0.953	24.693	-0.113	-0.113	0.000	0.000	0.000	0.000
61	A	62	THR	0	-0.043	-0.040	26.915	0.000	0.000	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.008	0.012	25.093	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	64	PHE	0	-0.015	-0.005	21.413	-0.009	-0.009	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.052	-0.025	18.031	-0.026	-0.026	0.000	0.000	0.000	0.000
65	A	66	THR	0	0.051	0.002	17.828	0.003	0.003	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.892	-0.958	18.841	-0.296	-0.296	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.809	-0.871	12.610	-0.794	-0.794	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.705	-0.801	14.530	-0.442	-0.442	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.827	-0.922	15.598	-0.206	-0.206	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.088	-0.045	15.701	0.033	0.033	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.008	0.002	11.006	0.027	0.027	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.008	0.017	13.447	0.044	0.044	0.000	0.000	0.000	0.000
73	A	74	ARG	1	0.929	0.957	16.231	0.265	0.265	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.919	0.956	11.932	0.303	0.303	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.052	0.023	13.335	0.039	0.039	0.000	0.000	0.000	0.000
76	A	77	ARG	1	0.835	0.921	14.221	0.139	0.139	0.000	0.000	0.000	0.000
77	A	78	ASN	0	-0.010	-0.012	16.461	0.029	0.029	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.027	0.018	16.128	0.006	0.006	0.000	0.000	0.000	0.000
79	A	80	ASN	0	0.007	-0.006	16.636	0.018	0.018	0.000	0.000	0.000	0.000
80	A	81	SER	0	0.063	0.046	16.494	0.021	0.021	0.000	0.000	0.000	0.000
81	A	82	GLY	0	-0.042	-0.009	17.918	0.008	0.008	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.032	-0.017	21.208	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.004	-0.007	21.576	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.005	0.009	21.858	0.007	0.007	0.000	0.000	0.000	0.000
85	A	86	LYS	1	1.012	0.998	24.708	-0.041	-0.041	0.000	0.000	0.000	0.000
86	A	87	ASN	0	-0.045	-0.032	28.490	0.000	0.000	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.016	0.004	24.932	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.792	-0.868	27.963	-0.041	-0.041	0.000	0.000	0.000	0.000
89	A	90	VAL	0	0.054	0.022	24.687	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	91	GLN	0	0.036	0.020	24.070	-0.013	-0.013	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.028	-0.037	23.909	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	93	TYR	0	0.009	-0.007	17.627	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.842	0.918	19.777	0.031	0.031	0.000	0.000	0.000	0.000
94	A	95	HIS	0	0.032	0.005	19.184	-0.023	-0.023	0.000	0.000	0.000	0.000
95	A	96	SER	0	-0.037	-0.029	18.767	-0.015	-0.015	0.000	0.000	0.000	0.000
96	A	97	THR	0	-0.030	-0.025	14.464	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.057	-0.017	14.520	-0.027	-0.027	0.000	0.000	0.000	0.000
98	A	99	PHE	0	0.039	0.016	14.909	-0.049	-0.049	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.788	-0.864	13.134	-0.105	-0.105	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.007	-0.003	10.371	-0.042	-0.042	0.000	0.000	0.000	0.000
101	A	102	LEU	0	-0.013	-0.005	10.000	-0.116	-0.116	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.003	0.011	11.471	-0.091	-0.091	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.025	0.012	8.028	-0.059	-0.059	0.000	0.000	0.000	0.000
104	A	105	TYR	0	-0.092	-0.080	6.730	-0.332	-0.332	0.000	0.000	0.000	0.000
105	A	106	HIS	0	0.025	0.001	7.467	-0.398	-0.398	0.000	0.000	0.000	0.000
106	A	107	HIS	0	0.002	0.003	6.128	-0.088	-0.088	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.030	-0.020	2.501	-1.221	-0.538	2.281	-0.438	-2.526	-0.001
108	A	109	LEU	0	-0.053	-0.024	5.155	-0.745	-0.702	-0.001	-0.006	-0.036	0.000
109	A	110	ASN	0	-0.051	-0.016	6.578	0.526	0.526	0.000	0.000	0.000	0.000
110	A	111	ASN	0	0.005	0.015	9.442	0.148	0.148	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.830	0.879	12.401	0.378	0.378	0.000	0.000	0.000	0.000
112	A	113	GLU	-1	-0.921	-0.953	14.287	-0.290	-0.290	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.810	0.863	15.432	0.390	0.390	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.002	-0.006	12.133	0.028	0.028	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.746	-0.840	15.701	-0.219	-0.219	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.887	-0.922	18.844	-0.262	-0.262	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.020	-0.007	16.247	0.033	0.033	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.001	0.001	16.655	0.033	0.033	0.000	0.000	0.000	0.000
119	A	120	TYR	0	-0.047	-0.044	19.585	0.038	0.038	0.000	0.000	0.000	0.000
120	A	121	LYS	1	0.863	0.947	22.644	0.173	0.173	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.004	-0.010	20.904	0.016	0.016	0.000	0.000	0.000	0.000
122	A	123	ILE	0	-0.015	-0.020	21.873	0.018	0.018	0.000	0.000	0.000	0.000
123	A	124	ALA	0	0.000	0.003	24.830	0.013	0.013	0.000	0.000	0.000	0.000
124	A	125	VAL	0	0.057	0.032	26.197	0.010	0.010	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.106	-0.050	23.637	0.012	0.012	0.000	0.000	0.000	0.000
126	A	127	GLU	-1	-0.821	-0.895	27.883	-0.064	-0.064	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-1.025	-0.993	30.681	-0.087	-0.087	0.000	0.000	0.000	0.000

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