FMO DATABASE

FMODB ID: NNYZQ

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:

Apendix: None

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	130
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1083535.067997
FMO2-HF: Nuclear repulsion	1029812.810274
FMO2-HF: Total energy	-53722.257723
FMO2-MP2: Total energy	-53877.472235

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.
5.824	8.847	0.062	-1.44	-1.644	0.003

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 : 0.087 / q_NPA : 0.042

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	7	ARG	1	1.037	1.039	3.465	-0.577	1.638	0.002	-1.199	-1.018	0.003
4	A	8	ALA	0	0.040	0.011	2.904	0.566	1.115	0.062	-0.194	-0.417	0.000
5	A	9	LEU	0	-0.085	-0.035	4.539	1.020	1.186	-0.001	-0.032	-0.132	0.000
6	A	10	GLU	-1	-0.891	-0.962	6.324	-0.709	-0.709	0.000	0.000	0.000	0.000
7	A	11	GLN	0	-0.003	-0.011	8.101	0.426	0.426	0.000	0.000	0.000	0.000
8	A	12	PHE	0	0.028	0.026	8.601	0.247	0.247	0.000	0.000	0.000	0.000
9	A	13	ALA	0	0.030	0.020	10.226	0.233	0.233	0.000	0.000	0.000	0.000
10	A	14	ASN	0	-0.069	-0.046	12.422	0.285	0.285	0.000	0.000	0.000	0.000
11	A	15	GLU	-1	-0.872	-0.949	13.255	-0.383	-0.383	0.000	0.000	0.000	0.000
12	A	16	PHE	0	-0.030	-0.005	14.180	0.091	0.091	0.000	0.000	0.000	0.000
13	A	17	LYS	1	0.965	0.981	15.823	0.570	0.570	0.000	0.000	0.000	0.000
14	A	18	VAL	0	-0.030	-0.026	18.141	0.068	0.068	0.000	0.000	0.000	0.000
15	A	19	ARG	1	0.975	0.985	15.956	0.444	0.444	0.000	0.000	0.000	0.000
16	A	20	ARG	1	0.861	0.962	20.013	0.408	0.408	0.000	0.000	0.000	0.000
17	A	21	ILE	0	-0.061	-0.048	21.635	0.039	0.039	0.000	0.000	0.000	0.000
18	A	22	LYS	1	0.894	0.940	23.325	0.293	0.293	0.000	0.000	0.000	0.000
19	A	23	LEU	0	0.028	0.046	21.976	0.019	0.019	0.000	0.000	0.000	0.000
20	A	24	GLY	0	-0.057	-0.024	25.591	0.021	0.021	0.000	0.000	0.000	0.000
21	A	25	TYR	0	0.032	0.037	24.174	0.004	0.004	0.000	0.000	0.000	0.000
22	A	26	THR	0	-0.067	-0.037	25.650	-0.016	-0.016	0.000	0.000	0.000	0.000
23	A	27	GLN	0	-0.006	-0.047	21.686	0.019	0.019	0.000	0.000	0.000	0.000
24	A	28	THR	0	-0.004	-0.009	24.374	-0.014	-0.014	0.000	0.000	0.000	0.000
25	A	29	ASN	0	0.009	0.007	26.904	0.001	0.001	0.000	0.000	0.000	0.000
26	A	30	VAL	0	-0.012	0.011	20.202	0.002	0.002	0.000	0.000	0.000	0.000
27	A	31	GLY	0	-0.009	-0.009	23.354	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	32	GLU	-1	-0.816	-0.908	24.269	-0.184	-0.184	0.000	0.000	0.000	0.000
29	A	33	ALA	0	0.029	0.010	24.777	0.011	0.011	0.000	0.000	0.000	0.000
30	A	34	LEU	0	-0.087	-0.044	19.217	0.000	0.000	0.000	0.000	0.000	0.000
31	A	35	ALA	0	-0.002	0.000	23.371	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	36	ALA	0	-0.031	-0.016	26.335	0.012	0.012	0.000	0.000	0.000	0.000
33	A	37	VAL	0	0.012	0.022	22.739	0.010	0.010	0.000	0.000	0.000	0.000
34	A	38	HIS	0	-0.084	-0.050	20.039	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	39	GLY	0	0.008	0.023	23.652	0.003	0.003	0.000	0.000	0.000	0.000
36	A	40	SER	0	-0.065	-0.035	24.533	0.009	0.009	0.000	0.000	0.000	0.000
37	A	41	GLU	-1	-0.872	-0.936	25.002	-0.201	-0.201	0.000	0.000	0.000	0.000
38	A	42	PHE	0	-0.081	-0.035	19.670	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	43	SER	0	0.060	0.025	23.885	-0.004	-0.004	0.000	0.000	0.000	0.000
40	A	44	GLN	0	0.069	0.016	23.768	-0.013	-0.013	0.000	0.000	0.000	0.000
41	A	45	THR	0	0.000	-0.018	23.599	-0.022	-0.022	0.000	0.000	0.000	0.000
42	A	46	THR	0	-0.037	-0.004	19.143	-0.028	-0.028	0.000	0.000	0.000	0.000
43	A	47	ILE	0	0.052	0.034	19.210	-0.058	-0.058	0.000	0.000	0.000	0.000
44	A	48	CYS	0	-0.045	-0.020	19.128	-0.052	-0.052	0.000	0.000	0.000	0.000
45	A	49	ARG	1	0.976	0.975	18.405	0.303	0.303	0.000	0.000	0.000	0.000
46	A	50	PHE	0	0.004	0.009	11.321	-0.055	-0.055	0.000	0.000	0.000	0.000
47	A	51	GLU	-1	-0.742	-0.855	14.695	-0.575	-0.575	0.000	0.000	0.000	0.000
48	A	52	ASN	0	-0.101	-0.052	15.741	-0.029	-0.029	0.000	0.000	0.000	0.000
49	A	53	LEU	0	-0.012	-0.004	10.341	-0.030	-0.030	0.000	0.000	0.000	0.000
50	A	54	GLN	0	-0.040	-0.011	14.180	0.046	0.046	0.000	0.000	0.000	0.000
51	A	55	LEU	0	-0.065	-0.032	14.100	0.079	0.079	0.000	0.000	0.000	0.000
52	A	56	SER	0	0.056	0.036	13.824	-0.074	-0.074	0.000	0.000	0.000	0.000
53	A	57	PHE	0	0.098	0.022	4.067	0.057	0.150	-0.001	-0.015	-0.077	0.000
54	A	58	LYS	1	1.008	1.006	9.322	0.023	0.023	0.000	0.000	0.000	0.000
55	A	59	ASN	0	0.011	0.001	11.214	-0.045	-0.045	0.000	0.000	0.000	0.000
56	A	60	ALA	0	0.035	0.014	10.138	0.027	0.027	0.000	0.000	0.000	0.000
57	A	61	CYS	0	-0.009	-0.006	6.726	-0.336	-0.336	0.000	0.000	0.000	0.000
58	A	62	LYS	1	0.977	0.994	8.892	0.446	0.446	0.000	0.000	0.000	0.000
59	A	63	LEU	0	-0.010	-0.021	12.201	0.045	0.045	0.000	0.000	0.000	0.000
60	A	64	LYS	1	0.978	1.002	5.539	2.788	2.788	0.000	0.000	0.000	0.000
61	A	65	ALA	0	-0.005	0.010	10.884	0.053	0.053	0.000	0.000	0.000	0.000
62	A	66	ILE	0	-0.049	-0.020	11.857	0.087	0.087	0.000	0.000	0.000	0.000
63	A	67	LEU	0	0.006	-0.020	14.310	0.049	0.049	0.000	0.000	0.000	0.000
64	A	68	SER	0	-0.033	-0.017	11.577	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	69	LYS	1	0.944	0.977	13.700	0.340	0.340	0.000	0.000	0.000	0.000
66	A	70	TRP	0	0.024	0.017	16.389	0.012	0.012	0.000	0.000	0.000	0.000
67	A	71	LEU	0	-0.011	-0.018	15.922	0.016	0.016	0.000	0.000	0.000	0.000
68	A	72	GLU	-1	-0.950	-0.975	14.868	-0.345	-0.345	0.000	0.000	0.000	0.000
69	A	73	GLU	-1	-0.931	-0.948	19.086	-0.187	-0.187	0.000	0.000	0.000	0.000
70	A	74	ALA	0	-0.081	-0.033	21.559	0.020	0.020	0.000	0.000	0.000	0.000
71	A	75	GLU	-1	-0.872	-0.944	21.295	-0.258	-0.258	0.000	0.000	0.000	0.000
72	A	76	GLN	0	-0.057	-0.025	24.850	0.004	0.004	0.000	0.000	0.000	0.000
73	A	103	LYS	1	0.967	0.956	32.852	0.150	0.150	0.000	0.000	0.000	0.000
74	A	104	ARG	1	1.002	1.021	28.701	0.198	0.198	0.000	0.000	0.000	0.000
75	A	105	ARG	1	0.949	0.962	27.989	0.206	0.206	0.000	0.000	0.000	0.000
76	A	106	THR	0	0.075	0.057	27.724	-0.011	-0.011	0.000	0.000	0.000	0.000
77	A	107	THR	0	-0.067	-0.030	23.386	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	108	ILE	0	0.026	0.011	26.170	0.000	0.000	0.000	0.000	0.000	0.000
79	A	109	SER	0	0.030	0.009	24.473	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	110	ILE	0	0.031	-0.001	22.921	0.015	0.015	0.000	0.000	0.000	0.000
81	A	111	ALA	0	0.078	0.060	26.042	0.013	0.013	0.000	0.000	0.000	0.000
82	A	112	ALA	0	0.029	0.017	27.749	0.016	0.016	0.000	0.000	0.000	0.000
83	A	113	LYS	1	0.934	0.948	29.350	0.185	0.185	0.000	0.000	0.000	0.000
84	A	114	ASP	-1	-0.893	-0.938	29.196	-0.164	-0.164	0.000	0.000	0.000	0.000
85	A	115	ALA	0	0.014	0.013	32.009	0.012	0.012	0.000	0.000	0.000	0.000
86	A	116	LEU	0	-0.030	-0.020	33.457	0.010	0.010	0.000	0.000	0.000	0.000
87	A	117	GLU	-1	-0.874	-0.961	35.187	-0.106	-0.106	0.000	0.000	0.000	0.000
88	A	118	ARG	1	0.954	1.010	35.175	0.106	0.106	0.000	0.000	0.000	0.000
89	A	119	HIS	0	0.031	-0.005	37.043	0.008	0.008	0.000	0.000	0.000	0.000
90	A	120	PHE	0	-0.102	-0.050	39.628	0.005	0.005	0.000	0.000	0.000	0.000
91	A	121	GLY	0	-0.005	-0.008	41.123	0.004	0.004	0.000	0.000	0.000	0.000
92	A	122	GLU	-1	-0.937	-0.952	41.952	-0.080	-0.080	0.000	0.000	0.000	0.000
93	A	123	HIS	0	-0.005	-0.009	44.275	0.005	0.005	0.000	0.000	0.000	0.000
94	A	124	SER	0	0.046	0.040	44.489	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	125	LYS	1	0.872	0.923	44.858	0.066	0.066	0.000	0.000	0.000	0.000
96	A	126	PRO	0	0.058	0.033	42.465	0.004	0.004	0.000	0.000	0.000	0.000
97	A	127	SER	0	0.017	0.021	45.534	0.000	0.000	0.000	0.000	0.000	0.000
98	A	128	SER	0	-0.001	-0.025	45.232	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	129	GLN	0	0.067	0.036	44.458	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	130	GLU	-1	-0.836	-0.944	43.310	-0.082	-0.082	0.000	0.000	0.000	0.000
101	A	131	ILE	0	-0.058	-0.028	39.853	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	132	MET	0	-0.033	-0.027	39.299	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	133	ARG	1	1.021	1.028	39.223	0.079	0.079	0.000	0.000	0.000	0.000
104	A	134	MET	0	0.005	0.007	36.849	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	135	ALA	0	-0.071	-0.023	34.942	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	136	GLU	-1	-0.890	-0.956	33.919	-0.101	-0.101	0.000	0.000	0.000	0.000
107	A	137	GLU	-1	-0.973	-0.985	33.590	-0.122	-0.122	0.000	0.000	0.000	0.000
108	A	138	LEU	0	-0.066	-0.028	30.780	-0.009	-0.009	0.000	0.000	0.000	0.000
109	A	139	ASN	0	-0.034	-0.001	27.549	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	140	LEU	0	-0.060	-0.027	29.072	-0.016	-0.016	0.000	0.000	0.000	0.000
111	A	141	GLU	-1	-0.853	-0.930	31.769	-0.135	-0.135	0.000	0.000	0.000	0.000
112	A	142	LYS	1	0.970	0.978	34.536	0.093	0.093	0.000	0.000	0.000	0.000
113	A	143	GLU	-1	-0.858	-0.927	37.107	-0.109	-0.109	0.000	0.000	0.000	0.000
114	A	144	VAL	0	-0.006	-0.009	31.901	0.000	0.000	0.000	0.000	0.000	0.000
115	A	145	VAL	0	0.056	0.030	35.310	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	146	ARG	1	0.880	0.934	36.979	0.107	0.107	0.000	0.000	0.000	0.000
117	A	147	VAL	0	0.005	0.003	37.432	0.004	0.004	0.000	0.000	0.000	0.000
118	A	148	TRP	0	0.011	0.010	33.570	0.001	0.001	0.000	0.000	0.000	0.000
119	A	149	PHE	0	0.085	0.023	37.333	0.002	0.002	0.000	0.000	0.000	0.000
120	A	150	CYS	0	-0.120	-0.069	40.610	0.005	0.005	0.000	0.000	0.000	0.000
121	A	151	ASN	0	-0.048	-0.034	38.650	0.004	0.004	0.000	0.000	0.000	0.000
122	A	152	ARG	1	0.766	0.919	37.906	0.113	0.113	0.000	0.000	0.000	0.000
123	A	153	ARG	1	0.964	0.990	40.553	0.095	0.095	0.000	0.000	0.000	0.000
124	A	154	GLN	0	-0.037	-0.025	43.132	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	155	ARG	1	0.914	0.937	35.167	0.141	0.141	0.000	0.000	0.000	0.000
126	A	156	GLU	-1	-0.837	-0.912	43.051	-0.091	-0.091	0.000	0.000	0.000	0.000
127	A	157	LYS	1	0.904	0.967	45.583	0.083	0.083	0.000	0.000	0.000	0.000
128	A	158	ARG	1	0.873	0.945	39.978	0.113	0.113	0.000	0.000	0.000	0.000
129	A	159	VAL	0	0.058	0.036	47.277	0.001	0.001	0.000	0.000	0.000	0.000
130	A	160	LYS	1	0.975	0.991	42.929	0.082	0.082	0.000	0.000	0.000	0.000

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