FMO DATABASE

FMODB ID: 3J1KL

Calculation Name: 1AU7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1AU7

Chain ID: A

ChEMBL ID:

UniProt ID: P10037

Base Structure: X-ray

Registration Date: 2023-09-24

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	130
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1089312.106603
FMO2-HF: Nuclear repulsion	1035587.81055
FMO2-HF: Total energy	-53724.296053
FMO2-MP2: Total energy	-53879.348567

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:5:GLY)

Summations of interaction energy for fragment #1(A:5:GLY)

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.
1.48	3.298	0.073	-0.734	-1.157	0

Interaction energy analysis for fragmet #1(A:5:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.049 / q_NPA : 0.013

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].
3	A	7	ARG	1	1.085	1.046	3.865	-0.898	0.146	-0.004	-0.508	-0.532
4	A	8	ALA	0	0.053	0.031	2.863	-0.477	0.037	0.075	-0.169	-0.420
5	A	9	LEU	0	-0.064	-0.022	4.766	0.017	0.141	-0.001	-0.019	-0.104
6	A	10	GLU	-1	-0.868	-0.949	6.639	-0.093	-0.093	0.000	0.000	0.000
7	A	11	GLN	0	0.000	-0.004	8.435	0.329	0.329	0.000	0.000	0.000
8	A	12	PHE	0	0.047	0.025	8.733	0.026	0.026	0.000	0.000	0.000
9	A	13	ALA	0	0.019	0.012	10.328	0.080	0.080	0.000	0.000	0.000
10	A	14	ASN	0	-0.088	-0.051	12.573	0.103	0.103	0.000	0.000	0.000
11	A	15	GLU	-1	-0.835	-0.933	13.059	-0.067	-0.067	0.000	0.000	0.000
12	A	16	PHE	0	-0.005	0.004	14.141	0.025	0.025	0.000	0.000	0.000
13	A	17	LYS	1	0.860	0.930	15.809	0.253	0.253	0.000	0.000	0.000
14	A	18	VAL	0	-0.014	-0.008	17.999	0.023	0.023	0.000	0.000	0.000
15	A	19	ARG	1	0.856	0.894	15.929	0.138	0.138	0.000	0.000	0.000
16	A	20	ARG	1	0.830	0.920	19.713	0.174	0.174	0.000	0.000	0.000
17	A	21	ILE	0	-0.057	-0.029	21.533	0.015	0.015	0.000	0.000	0.000
18	A	22	LYS	1	0.937	0.954	23.019	0.073	0.073	0.000	0.000	0.000
19	A	23	LEU	0	0.027	0.034	21.941	0.009	0.009	0.000	0.000	0.000
20	A	24	GLY	0	-0.055	-0.033	25.485	0.008	0.008	0.000	0.000	0.000
21	A	25	TYR	0	0.017	0.030	24.068	-0.001	-0.001	0.000	0.000	0.000
22	A	26	THR	0	-0.052	-0.057	25.193	-0.007	-0.007	0.000	0.000	0.000
23	A	27	GLN	0	-0.008	-0.049	21.567	0.006	0.006	0.000	0.000	0.000
24	A	28	THR	0	-0.007	-0.005	24.136	-0.013	-0.013	0.000	0.000	0.000
25	A	29	ASN	0	0.029	0.031	26.762	-0.002	-0.002	0.000	0.000	0.000
26	A	30	VAL	0	-0.006	0.013	20.050	-0.001	-0.001	0.000	0.000	0.000
27	A	31	GLY	0	0.011	0.015	23.296	-0.009	-0.009	0.000	0.000	0.000
28	A	32	GLU	-1	-0.802	-0.908	24.632	-0.107	-0.107	0.000	0.000	0.000
29	A	33	ALA	0	-0.001	0.000	24.372	0.004	0.004	0.000	0.000	0.000
30	A	34	LEU	0	-0.029	-0.027	18.898	-0.006	-0.006	0.000	0.000	0.000
31	A	35	ALA	0	-0.012	-0.004	23.419	-0.001	-0.001	0.000	0.000	0.000
32	A	36	ALA	0	-0.011	-0.003	26.760	0.004	0.004	0.000	0.000	0.000
33	A	37	VAL	0	-0.010	0.004	23.620	0.006	0.006	0.000	0.000	0.000
34	A	38	HIS	0	-0.078	-0.046	21.281	-0.022	-0.022	0.000	0.000	0.000
35	A	39	GLY	0	0.041	0.044	23.782	-0.001	-0.001	0.000	0.000	0.000
36	A	40	SER	0	-0.079	-0.052	25.186	0.007	0.007	0.000	0.000	0.000
37	A	41	GLU	-1	-0.942	-0.955	24.931	-0.133	-0.133	0.000	0.000	0.000
38	A	42	PHE	0	-0.036	-0.012	19.850	-0.011	-0.011	0.000	0.000	0.000
39	A	43	SER	0	0.082	0.038	23.962	0.000	0.000	0.000	0.000	0.000
40	A	44	GLN	0	0.085	0.017	23.787	-0.015	-0.015	0.000	0.000	0.000
41	A	45	THR	0	-0.008	-0.006	23.534	-0.012	-0.012	0.000	0.000	0.000
42	A	46	THR	0	-0.049	-0.023	19.409	-0.015	-0.015	0.000	0.000	0.000
43	A	47	ILE	0	0.039	0.029	19.134	-0.036	-0.036	0.000	0.000	0.000
44	A	48	CYS	0	-0.054	-0.015	18.882	-0.023	-0.023	0.000	0.000	0.000
45	A	49	ARG	1	0.980	0.985	18.179	0.194	0.194	0.000	0.000	0.000
46	A	50	PHE	0	0.015	0.008	11.443	-0.028	-0.028	0.000	0.000	0.000
47	A	51	GLU	-1	-0.743	-0.863	14.612	-0.258	-0.258	0.000	0.000	0.000
48	A	52	ASN	0	-0.088	-0.041	16.630	0.033	0.033	0.000	0.000	0.000
49	A	53	LEU	0	0.022	0.009	10.296	0.001	0.001	0.000	0.000	0.000
50	A	54	GLN	0	-0.035	0.008	14.045	0.021	0.021	0.000	0.000	0.000
51	A	55	LEU	0	-0.054	-0.033	13.731	0.029	0.029	0.000	0.000	0.000
52	A	56	SER	0	0.052	0.030	13.589	-0.039	-0.039	0.000	0.000	0.000
53	A	57	PHE	0	0.078	0.025	3.620	-0.033	0.103	0.003	-0.038	-0.101
54	A	58	LYS	1	1.018	1.006	9.074	0.185	0.185	0.000	0.000	0.000
55	A	59	ASN	0	0.030	0.010	10.590	-0.022	-0.022	0.000	0.000	0.000
56	A	60	ALA	0	0.030	0.023	9.913	0.017	0.017	0.000	0.000	0.000
57	A	61	CYS	0	-0.028	-0.017	6.673	-0.160	-0.160	0.000	0.000	0.000
58	A	62	LYS	1	0.958	0.980	9.088	0.373	0.373	0.000	0.000	0.000
59	A	63	LEU	0	0.011	0.001	12.635	0.044	0.044	0.000	0.000	0.000
60	A	64	LYS	1	0.888	0.948	5.744	1.342	1.342	0.000	0.000	0.000
61	A	65	ALA	0	-0.029	-0.007	11.401	0.051	0.051	0.000	0.000	0.000
62	A	66	ILE	0	-0.003	0.005	12.193	0.056	0.056	0.000	0.000	0.000
63	A	67	LEU	0	0.007	-0.005	14.286	0.040	0.040	0.000	0.000	0.000
64	A	68	SER	0	-0.029	-0.024	11.547	0.018	0.018	0.000	0.000	0.000
65	A	69	LYS	1	0.799	0.902	13.642	0.226	0.226	0.000	0.000	0.000
66	A	70	TRP	0	0.012	0.000	16.329	0.022	0.022	0.000	0.000	0.000
67	A	71	LEU	0	-0.036	-0.030	15.563	0.019	0.019	0.000	0.000	0.000
68	A	72	GLU	-1	-0.862	-0.923	15.674	-0.136	-0.136	0.000	0.000	0.000
69	A	73	GLU	-1	-0.785	-0.865	19.183	-0.148	-0.148	0.000	0.000	0.000
70	A	74	ALA	0	-0.052	-0.018	21.561	0.013	0.013	0.000	0.000	0.000
71	A	75	GLU	-1	-0.848	-0.915	20.897	-0.086	-0.086	0.000	0.000	0.000
72	A	76	GLN	0	-0.082	-0.034	24.271	0.013	0.013	0.000	0.000	0.000
73	A	103	LYS	1	0.998	0.994	32.479	0.062	0.062	0.000	0.000	0.000
74	A	104	ARG	1	0.881	0.936	27.599	0.068	0.068	0.000	0.000	0.000
75	A	105	ARG	1	0.968	0.983	28.485	0.084	0.084	0.000	0.000	0.000
76	A	106	THR	0	0.072	0.045	27.679	-0.004	-0.004	0.000	0.000	0.000
77	A	107	THR	0	-0.062	-0.033	23.373	-0.004	-0.004	0.000	0.000	0.000
78	A	108	ILE	0	0.011	0.015	26.061	0.003	0.003	0.000	0.000	0.000
79	A	109	SER	0	0.039	0.022	24.447	-0.007	-0.007	0.000	0.000	0.000
80	A	110	ILE	0	0.058	0.016	23.271	0.003	0.003	0.000	0.000	0.000
81	A	111	ALA	0	0.069	0.033	26.224	0.004	0.004	0.000	0.000	0.000
82	A	112	ALA	0	0.042	0.029	28.062	0.004	0.004	0.000	0.000	0.000
83	A	113	LYS	1	0.810	0.891	29.542	0.040	0.040	0.000	0.000	0.000
84	A	114	ASP	-1	-0.846	-0.923	30.128	-0.032	-0.032	0.000	0.000	0.000
85	A	115	ALA	0	-0.005	0.008	32.234	0.003	0.003	0.000	0.000	0.000
86	A	116	LEU	0	-0.024	-0.017	32.723	0.001	0.001	0.000	0.000	0.000
87	A	117	GLU	-1	-0.839	-0.922	35.217	-0.033	-0.033	0.000	0.000	0.000
88	A	118	ARG	1	0.940	0.990	34.947	0.008	0.008	0.000	0.000	0.000
89	A	119	HIS	0	0.033	0.005	37.477	0.002	0.002	0.000	0.000	0.000
90	A	120	PHE	0	-0.101	-0.050	39.640	0.000	0.000	0.000	0.000	0.000
91	A	121	GLY	0	-0.023	-0.011	41.020	0.000	0.000	0.000	0.000	0.000
92	A	122	GLU	-1	-0.919	-0.959	41.611	-0.006	-0.006	0.000	0.000	0.000
93	A	123	HIS	0	0.008	-0.007	44.048	0.000	0.000	0.000	0.000	0.000
94	A	124	SER	0	0.068	0.050	44.202	-0.001	-0.001	0.000	0.000	0.000
95	A	125	LYS	1	0.872	0.932	44.960	0.013	0.013	0.000	0.000	0.000
96	A	126	PRO	0	0.062	0.049	42.568	0.001	0.001	0.000	0.000	0.000
97	A	127	SER	0	-0.036	-0.056	45.799	-0.001	-0.001	0.000	0.000	0.000
98	A	128	SER	0	0.006	-0.012	45.298	-0.001	-0.001	0.000	0.000	0.000
99	A	129	GLN	0	0.083	0.036	44.387	0.000	0.000	0.000	0.000	0.000
100	A	130	GLU	-1	-0.780	-0.845	43.241	-0.008	-0.008	0.000	0.000	0.000
101	A	131	ILE	0	-0.012	-0.018	40.433	-0.001	-0.001	0.000	0.000	0.000
102	A	132	MET	0	-0.065	-0.024	39.515	-0.003	-0.003	0.000	0.000	0.000
103	A	133	ARG	1	0.984	1.006	38.848	0.003	0.003	0.000	0.000	0.000
104	A	134	MET	0	-0.012	-0.009	37.305	0.001	0.001	0.000	0.000	0.000
105	A	135	ALA	0	-0.054	-0.021	35.072	-0.002	-0.002	0.000	0.000	0.000
106	A	136	GLU	-1	-0.859	-0.945	33.917	-0.002	-0.002	0.000	0.000	0.000
107	A	137	GLU	-1	-0.960	-0.981	33.682	-0.002	-0.002	0.000	0.000	0.000
108	A	138	LEU	0	-0.051	-0.025	31.095	0.000	0.000	0.000	0.000	0.000
109	A	139	ASN	0	-0.050	-0.019	28.692	0.000	0.000	0.000	0.000	0.000
110	A	140	LEU	0	-0.061	-0.020	29.276	-0.007	-0.007	0.000	0.000	0.000
111	A	141	GLU	-1	-0.846	-0.931	31.793	-0.021	-0.021	0.000	0.000	0.000
112	A	142	LYS	1	0.926	0.948	34.380	0.013	0.013	0.000	0.000	0.000
113	A	143	GLU	-1	-0.768	-0.843	37.438	-0.029	-0.029	0.000	0.000	0.000
114	A	144	VAL	0	-0.024	-0.011	31.923	-0.002	-0.002	0.000	0.000	0.000
115	A	145	VAL	0	0.049	0.034	35.348	-0.002	-0.002	0.000	0.000	0.000
116	A	146	ARG	1	0.828	0.872	37.000	0.027	0.027	0.000	0.000	0.000
117	A	147	VAL	0	-0.001	0.000	37.468	0.000	0.000	0.000	0.000	0.000
118	A	148	TRP	0	-0.004	0.003	33.846	-0.001	-0.001	0.000	0.000	0.000
119	A	149	PHE	0	0.069	0.018	37.378	-0.001	-0.001	0.000	0.000	0.000
120	A	150	CYS	0	-0.101	-0.053	40.538	0.001	0.001	0.000	0.000	0.000
121	A	151	ASN	0	-0.021	-0.014	38.348	-0.001	-0.001	0.000	0.000	0.000
122	A	152	ARG	1	0.776	0.867	37.897	0.029	0.029	0.000	0.000	0.000
123	A	153	ARG	1	0.903	0.956	40.314	0.023	0.023	0.000	0.000	0.000
124	A	154	GLN	0	-0.025	-0.004	42.784	-0.001	-0.001	0.000	0.000	0.000
125	A	155	ARG	1	0.870	0.920	34.932	0.047	0.047	0.000	0.000	0.000
126	A	156	GLU	-1	-0.773	-0.875	42.587	-0.026	-0.026	0.000	0.000	0.000
127	A	157	LYS	1	0.917	0.974	45.200	0.026	0.026	0.000	0.000	0.000
128	A	158	ARG	1	0.859	0.928	40.579	0.041	0.041	0.000	0.000	0.000
129	A	159	VAL	0	0.059	0.032	47.529	0.001	0.001	0.000	0.000	0.000
130	A	160	LYS	1	0.959	0.989	42.677	0.033	0.033	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:GLY)