FMO DATABASE

FMODB ID: 7262K

Calculation Name: 1A0K-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1A0K

Chain ID: A

ChEMBL ID:

UniProt ID: Q42449

Base Structure: X-ray

Registration Date: 2023-06-22

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1106696.143603
FMO2-HF: Nuclear repulsion	1056806.435817
FMO2-HF: Total energy	-49889.707786
FMO2-MP2: Total energy	-50034.267926

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:SER)

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

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.
-17.69	-17.003	15.245	-7.549	-8.383	0.005

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.018 / q_NPA : 0.009

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	GLN	0	-0.035	-0.049	2.644	-4.916	-0.707	0.807	-2.357	-2.659	0.015
4	A	5	SER	0	0.045	0.034	1.872	-10.973	-15.328	14.422	-4.982	-5.085	-0.010
5	A	6	TYR	0	-0.016	0.004	3.610	-0.773	0.060	0.016	-0.210	-0.639	0.000
6	A	7	VAL	0	-0.015	-0.008	5.424	0.698	0.698	0.000	0.000	0.000	0.000
7	A	8	ASP	-1	-0.848	-0.941	6.804	0.623	0.623	0.000	0.000	0.000	0.000
8	A	9	ASP	-1	-0.886	-0.940	6.110	-1.849	-1.849	0.000	0.000	0.000	0.000
9	A	10	HIS	0	-0.038	-0.019	6.309	0.013	0.013	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.044	-0.017	9.538	0.280	0.280	0.000	0.000	0.000	0.000
11	A	12	MET	0	-0.098	-0.034	11.098	0.159	0.159	0.000	0.000	0.000	0.000
12	A	13	CYS	0	-0.010	0.012	12.116	0.096	0.096	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.863	-0.957	13.728	-0.209	-0.209	0.000	0.000	0.000	0.000
14	A	15	VAL	0	-0.070	-0.033	17.252	-0.023	-0.023	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.993	-1.017	19.589	-0.155	-0.155	0.000	0.000	0.000	0.000
16	A	17	GLY	0	0.015	0.014	21.499	0.022	0.022	0.000	0.000	0.000	0.000
17	A	18	ASN	0	-0.019	0.012	21.771	0.035	0.035	0.000	0.000	0.000	0.000
18	A	19	HIS	1	0.902	0.943	16.516	0.126	0.126	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.011	-0.011	14.864	0.040	0.040	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.080	-0.060	17.812	0.023	0.023	0.000	0.000	0.000	0.000
21	A	22	ALA	0	-0.035	-0.029	15.865	0.046	0.046	0.000	0.000	0.000	0.000
22	A	23	ALA	0	0.019	0.008	12.615	-0.054	-0.054	0.000	0.000	0.000	0.000
23	A	24	ALA	0	0.009	-0.002	11.352	0.130	0.130	0.000	0.000	0.000	0.000
24	A	25	ILE	0	0.010	0.025	7.657	-0.152	-0.152	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.008	-0.002	11.089	0.148	0.148	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.091	0.030	13.443	-0.104	-0.104	0.000	0.000	0.000	0.000
27	A	28	GLN	0	-0.053	-0.041	14.230	0.077	0.077	0.000	0.000	0.000	0.000
28	A	29	ASP	-1	-0.897	-0.923	16.172	-0.022	-0.022	0.000	0.000	0.000	0.000
29	A	30	GLY	0	-0.050	-0.042	17.579	0.025	0.025	0.000	0.000	0.000	0.000
30	A	31	SER	0	-0.058	-0.038	14.007	0.025	0.025	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.008	-0.003	10.891	-0.070	-0.070	0.000	0.000	0.000	0.000
32	A	33	TRP	0	-0.051	-0.004	7.748	0.035	0.035	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.020	0.014	6.118	0.374	0.374	0.000	0.000	0.000	0.000
34	A	35	GLN	0	-0.040	-0.021	8.162	-0.336	-0.336	0.000	0.000	0.000	0.000
35	A	36	SER	0	0.050	0.044	10.107	0.161	0.161	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.014	-0.018	12.099	0.009	0.009	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.935	0.964	14.735	-0.025	-0.025	0.000	0.000	0.000	0.000
38	A	39	PHE	0	-0.001	0.009	14.886	-0.042	-0.042	0.000	0.000	0.000	0.000
39	A	40	PRO	0	0.022	0.020	16.953	0.032	0.032	0.000	0.000	0.000	0.000
40	A	41	GLN	0	-0.013	-0.002	18.997	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.009	-0.003	19.253	-0.015	-0.015	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.858	0.922	21.952	0.011	0.011	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.060	0.018	23.796	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	45	GLN	0	0.070	0.019	24.863	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.797	-0.875	24.700	-0.022	-0.022	0.000	0.000	0.000	0.000
46	A	47	ILE	0	0.029	0.016	19.603	-0.016	-0.016	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.841	-0.925	23.179	-0.069	-0.069	0.000	0.000	0.000	0.000
48	A	49	GLY	0	-0.012	0.000	26.054	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.009	-0.010	21.746	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.857	0.932	21.460	0.069	0.069	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.834	0.913	24.673	0.068	0.068	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.847	-0.937	27.258	-0.125	-0.125	0.000	0.000	0.000	0.000
53	A	54	PHE	0	-0.047	-0.029	21.441	-0.007	-0.007	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.900	-0.943	25.437	-0.163	-0.163	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.895	-0.925	28.832	-0.071	-0.071	0.000	0.000	0.000	0.000
56	A	57	PRO	0	0.015	0.001	29.281	0.004	0.004	0.000	0.000	0.000	0.000
57	A	58	GLY	0	-0.024	-0.008	31.242	0.008	0.008	0.000	0.000	0.000	0.000
58	A	59	PHE	0	0.002	0.001	30.621	0.011	0.011	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.028	-0.024	27.561	0.009	0.009	0.000	0.000	0.000	0.000
60	A	61	ALA	0	-0.040	-0.013	32.045	0.005	0.005	0.000	0.000	0.000	0.000
61	A	62	PRO	0	-0.016	-0.001	34.254	0.004	0.004	0.000	0.000	0.000	0.000
62	A	63	THR	0	0.011	0.003	33.427	0.004	0.004	0.000	0.000	0.000	0.000
63	A	64	GLY	0	-0.051	-0.017	32.872	0.007	0.007	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.050	0.035	25.027	0.001	0.001	0.000	0.000	0.000	0.000
65	A	66	PHE	0	-0.017	-0.026	28.389	0.004	0.004	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.011	0.009	21.953	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.055	0.025	24.423	0.004	0.004	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.110	-0.079	24.913	0.008	0.008	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.841	-0.885	27.019	-0.026	-0.026	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.877	0.931	28.519	0.044	0.044	0.000	0.000	0.000	0.000
71	A	72	TYR	0	-0.004	0.000	25.000	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	73	MET	0	-0.051	-0.024	29.762	0.005	0.005	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.049	0.017	29.652	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.029	-0.010	28.931	0.008	0.008	0.000	0.000	0.000	0.000
75	A	76	GLN	0	-0.017	-0.012	29.984	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.011	0.004	26.925	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.947	-0.970	23.848	-0.260	-0.260	0.000	0.000	0.000	0.000
78	A	79	GLN	0	0.006	-0.014	26.083	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.028	0.023	25.706	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	81	ALA	0	-0.006	0.012	22.069	-0.015	-0.015	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.050	-0.036	20.972	-0.033	-0.033	0.000	0.000	0.000	0.000
82	A	83	ILE	0	0.022	0.032	22.785	0.028	0.028	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.806	0.880	23.318	0.230	0.230	0.000	0.000	0.000	0.000
84	A	85	GLY	0	0.040	0.014	25.576	0.016	0.016	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.813	0.908	26.731	0.096	0.096	0.000	0.000	0.000	0.000
86	A	87	LYS	1	0.846	0.913	27.770	0.050	0.050	0.000	0.000	0.000	0.000
87	A	88	GLY	0	0.017	0.021	29.878	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	PRO	0	0.016	0.004	30.223	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	90	GLY	0	0.088	0.049	26.960	-0.007	-0.007	0.000	0.000	0.000	0.000
90	A	91	GLY	0	-0.049	-0.035	25.283	0.005	0.005	0.000	0.000	0.000	0.000
91	A	92	VAL	0	-0.052	-0.012	20.730	0.000	0.000	0.000	0.000	0.000	0.000
92	A	93	THR	0	0.009	-0.002	19.798	0.018	0.018	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.025	-0.018	18.967	-0.019	-0.019	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.872	0.940	16.574	0.463	0.463	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.883	0.954	17.048	0.180	0.180	0.000	0.000	0.000	0.000
96	A	97	THR	0	-0.015	-0.024	13.133	0.005	0.005	0.000	0.000	0.000	0.000
97	A	98	ASN	0	-0.022	-0.021	15.631	0.068	0.068	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.027	-0.013	12.567	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.017	0.001	12.162	0.048	0.048	0.000	0.000	0.000	0.000
100	A	101	LEU	0	0.002	0.010	14.268	0.042	0.042	0.000	0.000	0.000	0.000
101	A	102	VAL	0	0.002	0.008	12.174	-0.010	-0.010	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.013	-0.013	14.513	0.065	0.065	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.035	0.003	15.432	-0.034	-0.034	0.000	0.000	0.000	0.000
104	A	105	PHE	0	0.000	0.004	17.501	0.020	0.020	0.000	0.000	0.000	0.000
105	A	106	TYR	0	0.023	0.004	19.739	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.827	-0.887	22.178	-0.062	-0.062	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.930	-0.957	24.915	-0.088	-0.088	0.000	0.000	0.000	0.000
108	A	109	PRO	0	-0.038	-0.026	26.215	0.010	0.010	0.000	0.000	0.000	0.000
109	A	110	MET	0	-0.021	0.019	18.545	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	111	THR	0	0.002	-0.031	24.641	0.010	0.010	0.000	0.000	0.000	0.000
111	A	112	GLY	0	0.028	0.005	23.869	-0.018	-0.018	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.005	0.003	23.682	-0.019	-0.019	0.000	0.000	0.000	0.000
113	A	114	GLN	0	0.061	0.043	21.357	-0.014	-0.014	0.000	0.000	0.000	0.000
114	A	115	CYS	0	-0.012	0.007	19.362	-0.043	-0.043	0.000	0.000	0.000	0.000
115	A	116	ASN	0	0.036	0.010	18.870	-0.040	-0.040	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.022	0.005	18.384	-0.044	-0.044	0.000	0.000	0.000	0.000
117	A	118	VAL	0	0.005	-0.012	14.508	-0.055	-0.055	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.023	0.012	14.305	-0.118	-0.118	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.801	-0.904	15.067	-0.388	-0.388	0.000	0.000	0.000	0.000
120	A	121	ARG	1	0.906	0.969	12.997	0.714	0.714	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.033	-0.005	8.034	-0.067	-0.067	0.000	0.000	0.000	0.000
122	A	123	GLY	0	0.001	-0.013	11.746	-0.092	-0.092	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.796	-0.910	13.948	-0.472	-0.472	0.000	0.000	0.000	0.000
124	A	125	TYR	0	0.035	0.036	6.885	-0.248	-0.248	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.023	-0.020	7.483	-0.053	-0.053	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.063	-0.029	10.996	0.094	0.094	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-0.948	-0.960	13.732	-0.517	-0.517	0.000	0.000	0.000	0.000
128	A	129	SER	0	-0.115	-0.046	10.197	0.020	0.020	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.939	-0.978	12.138	-0.325	-0.325	0.000	0.000	0.000	0.000
130	A	131	LEU	0	-0.029	0.015	8.225	0.049	0.049	0.000	0.000	0.000	0.000

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