FMO DATABASE

FMODB ID: JQ2Z9

Calculation Name: 3AHP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3AHP

Chain ID: A

ChEMBL ID:

UniProt ID: E7FH74

Base Structure: X-ray

Registration Date: 2023-09-22

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	106
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-771587.071276
FMO2-HF: Nuclear repulsion	728989.957555
FMO2-HF: Total energy	-42597.113721
FMO2-MP2: Total energy	-42716.666088

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:3:LYS)

Summations of interaction energy for fragment #1(A:3:LYS)

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.
-113.161	-111.332	-0.018	-0.778	-1.033	0.003

Interaction energy analysis for fragmet #1(A:3:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.959 / q_NPA : 0.967

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	5	GLU	-1	-0.770	-0.865	3.823	-28.255	-26.534	-0.017	-0.770	-0.934	0.003
4	A	6	GLN	0	-0.060	-0.040	6.898	1.548	1.548	0.000	0.000	0.000	0.000
5	A	7	LEU	0	0.005	0.000	5.511	-3.916	-3.916	0.000	0.000	0.000	0.000
6	A	8	LEU	0	-0.027	-0.017	9.392	2.944	2.944	0.000	0.000	0.000	0.000
7	A	9	ILE	0	-0.004	-0.005	10.882	-1.730	-1.730	0.000	0.000	0.000	0.000
8	A	10	PHE	0	-0.013	-0.011	12.991	1.887	1.887	0.000	0.000	0.000	0.000
9	A	11	THR	0	-0.012	-0.033	15.579	-0.423	-0.423	0.000	0.000	0.000	0.000
10	A	12	THR	0	0.037	0.012	18.175	0.551	0.551	0.000	0.000	0.000	0.000
11	A	13	CYS	0	-0.052	0.005	21.770	-0.080	-0.080	0.000	0.000	0.000	0.000
12	A	14	PRO	0	0.067	0.033	24.754	0.153	0.153	0.000	0.000	0.000	0.000
13	A	15	ASP	-1	-0.815	-0.899	28.107	-9.909	-9.909	0.000	0.000	0.000	0.000
14	A	16	ALA	0	0.043	-0.008	28.711	-0.361	-0.361	0.000	0.000	0.000	0.000
15	A	17	ASP	-1	-0.912	-0.943	29.578	-9.636	-9.636	0.000	0.000	0.000	0.000
16	A	18	ILE	0	-0.083	-0.065	25.622	-0.163	-0.163	0.000	0.000	0.000	0.000
17	A	19	ALA	0	0.046	0.020	25.164	-0.401	-0.401	0.000	0.000	0.000	0.000
18	A	20	CYS	0	0.038	-0.001	25.393	-0.371	-0.371	0.000	0.000	0.000	0.000
19	A	21	ARG	1	0.894	0.972	27.476	10.189	10.189	0.000	0.000	0.000	0.000
20	A	22	ILE	0	0.022	0.010	21.935	-0.132	-0.132	0.000	0.000	0.000	0.000
21	A	23	ALA	0	0.010	-0.007	22.729	-0.562	-0.562	0.000	0.000	0.000	0.000
22	A	24	THR	0	-0.039	-0.032	23.813	-0.185	-0.185	0.000	0.000	0.000	0.000
23	A	25	ALA	0	0.029	0.025	24.376	-0.054	-0.054	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.004	0.006	17.695	-0.292	-0.292	0.000	0.000	0.000	0.000
25	A	27	VAL	0	-0.031	-0.025	20.872	-0.513	-0.513	0.000	0.000	0.000	0.000
26	A	28	GLU	-1	-0.961	-0.972	22.871	-10.919	-10.919	0.000	0.000	0.000	0.000
27	A	29	ALA	0	-0.087	-0.037	21.755	0.166	0.166	0.000	0.000	0.000	0.000
28	A	30	LYS	1	0.883	0.936	20.845	12.259	12.259	0.000	0.000	0.000	0.000
29	A	31	LEU	0	0.007	0.019	16.635	-0.685	-0.685	0.000	0.000	0.000	0.000
30	A	32	ALA	0	-0.025	-0.017	16.059	-1.451	-1.451	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.012	0.025	17.420	0.880	0.880	0.000	0.000	0.000	0.000
32	A	34	CYS	0	-0.059	-0.045	18.877	1.040	1.040	0.000	0.000	0.000	0.000
33	A	35	VAL	0	0.048	0.024	19.095	-1.038	-1.038	0.000	0.000	0.000	0.000
34	A	36	GLN	0	-0.066	-0.039	20.634	0.404	0.404	0.000	0.000	0.000	0.000
35	A	37	ILE	0	0.046	0.028	22.070	-0.489	-0.489	0.000	0.000	0.000	0.000
36	A	38	GLY	0	-0.045	-0.006	24.541	0.385	0.385	0.000	0.000	0.000	0.000
37	A	39	GLN	0	-0.017	-0.029	25.968	0.407	0.407	0.000	0.000	0.000	0.000
38	A	40	ALA	0	0.020	-0.006	27.834	-0.317	-0.317	0.000	0.000	0.000	0.000
39	A	41	VAL	0	-0.016	0.005	24.435	0.082	0.082	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.821	-0.902	27.903	-9.726	-9.726	0.000	0.000	0.000	0.000
41	A	43	SER	0	-0.024	-0.019	24.997	-0.416	-0.416	0.000	0.000	0.000	0.000
42	A	44	ILE	0	-0.029	-0.026	25.980	0.432	0.432	0.000	0.000	0.000	0.000
43	A	45	TYR	0	-0.032	-0.020	24.763	-0.535	-0.535	0.000	0.000	0.000	0.000
44	A	46	GLN	0	-0.028	-0.013	26.031	0.549	0.549	0.000	0.000	0.000	0.000
45	A	47	TRP	0	-0.029	-0.013	26.664	-0.223	-0.223	0.000	0.000	0.000	0.000
46	A	48	ASP	-1	-0.869	-0.942	28.895	-9.233	-9.233	0.000	0.000	0.000	0.000
47	A	49	ASN	0	-0.047	-0.029	30.469	0.036	0.036	0.000	0.000	0.000	0.000
48	A	50	ASN	0	-0.086	-0.037	31.780	0.448	0.448	0.000	0.000	0.000	0.000
49	A	51	ILE	0	0.033	0.016	30.969	-0.298	-0.298	0.000	0.000	0.000	0.000
50	A	52	CYS	0	-0.038	-0.013	29.575	0.423	0.423	0.000	0.000	0.000	0.000
51	A	53	GLN	0	-0.043	-0.040	30.049	-0.158	-0.158	0.000	0.000	0.000	0.000
52	A	54	SER	0	0.014	0.030	28.122	0.387	0.387	0.000	0.000	0.000	0.000
53	A	55	HIS	0	-0.056	-0.028	29.206	-0.118	-0.118	0.000	0.000	0.000	0.000
54	A	56	GLU	-1	-0.828	-0.889	25.253	-12.354	-12.354	0.000	0.000	0.000	0.000
55	A	57	VAL	0	-0.032	-0.027	25.891	0.175	0.175	0.000	0.000	0.000	0.000
56	A	58	PRO	0	-0.002	0.036	21.960	-0.440	-0.440	0.000	0.000	0.000	0.000
57	A	59	MET	0	0.015	-0.015	20.407	0.468	0.468	0.000	0.000	0.000	0.000
58	A	60	GLN	0	-0.012	-0.001	17.396	-1.115	-1.115	0.000	0.000	0.000	0.000
59	A	61	ILE	0	0.019	0.014	15.436	0.915	0.915	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.870	0.952	14.442	15.631	15.631	0.000	0.000	0.000	0.000
61	A	63	CYS	0	0.051	0.017	11.318	1.236	1.236	0.000	0.000	0.000	0.000
62	A	64	MET	0	0.006	0.053	10.200	-1.813	-1.813	0.000	0.000	0.000	0.000
63	A	65	THR	0	-0.029	-0.051	4.303	0.864	0.972	-0.001	-0.008	-0.099	0.000
64	A	66	THR	0	-0.005	-0.006	7.768	-0.731	-0.731	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.855	-0.928	9.452	-20.314	-20.314	0.000	0.000	0.000	0.000
66	A	68	TYR	0	-0.073	-0.063	9.004	0.080	0.080	0.000	0.000	0.000	0.000
67	A	69	PRO	0	0.018	0.003	10.140	1.367	1.367	0.000	0.000	0.000	0.000
68	A	70	ALA	0	-0.020	0.002	12.601	1.485	1.485	0.000	0.000	0.000	0.000
69	A	71	ILE	0	0.017	-0.005	13.072	1.196	1.196	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.874	-0.917	11.754	-23.764	-23.764	0.000	0.000	0.000	0.000
71	A	73	GLN	0	0.020	0.005	14.701	1.531	1.531	0.000	0.000	0.000	0.000
72	A	74	LEU	0	-0.041	-0.006	17.701	1.030	1.030	0.000	0.000	0.000	0.000
73	A	75	VAL	0	0.003	-0.015	17.645	0.866	0.866	0.000	0.000	0.000	0.000
74	A	76	ILE	0	-0.012	-0.018	16.573	0.675	0.675	0.000	0.000	0.000	0.000
75	A	77	THR	0	-0.027	-0.007	19.827	0.691	0.691	0.000	0.000	0.000	0.000
76	A	78	MET	0	-0.095	-0.041	22.658	0.590	0.590	0.000	0.000	0.000	0.000
77	A	79	HIS	0	-0.017	-0.007	21.814	0.805	0.805	0.000	0.000	0.000	0.000
78	A	80	PRO	0	-0.029	-0.012	24.030	0.126	0.126	0.000	0.000	0.000	0.000
79	A	81	TYR	0	-0.103	-0.071	23.691	0.489	0.489	0.000	0.000	0.000	0.000
80	A	82	GLU	-1	-0.907	-0.954	23.594	-12.093	-12.093	0.000	0.000	0.000	0.000
81	A	83	VAL	0	-0.057	-0.032	18.530	-0.581	-0.581	0.000	0.000	0.000	0.000
82	A	84	PRO	0	0.012	0.017	19.157	0.058	0.058	0.000	0.000	0.000	0.000
83	A	85	GLU	-1	-0.891	-0.910	17.140	-17.123	-17.123	0.000	0.000	0.000	0.000
84	A	86	PHE	0	0.019	0.005	12.064	0.221	0.221	0.000	0.000	0.000	0.000
85	A	87	ILE	0	-0.002	0.014	11.415	-1.407	-1.407	0.000	0.000	0.000	0.000
86	A	88	ALA	0	0.024	0.009	7.391	0.549	0.549	0.000	0.000	0.000	0.000
87	A	89	THR	0	-0.008	-0.001	8.322	-1.384	-1.384	0.000	0.000	0.000	0.000
88	A	90	PRO	0	-0.049	-0.018	5.445	-0.623	-0.623	0.000	0.000	0.000	0.000
89	A	91	ILE	0	0.009	0.014	7.326	3.890	3.890	0.000	0.000	0.000	0.000
90	A	92	ILE	0	-0.024	-0.027	6.362	-2.889	-2.889	0.000	0.000	0.000	0.000
91	A	93	GLY	0	0.002	-0.001	8.726	1.244	1.244	0.000	0.000	0.000	0.000
92	A	94	GLY	0	0.024	0.012	12.069	-0.234	-0.234	0.000	0.000	0.000	0.000
93	A	95	PHE	0	0.007	0.001	15.458	0.193	0.193	0.000	0.000	0.000	0.000
94	A	96	GLY	0	0.071	0.033	16.558	-0.285	-0.285	0.000	0.000	0.000	0.000
95	A	97	PRO	0	0.016	-0.001	17.639	-0.461	-0.461	0.000	0.000	0.000	0.000
96	A	98	TYR	0	0.001	0.005	17.360	-0.106	-0.106	0.000	0.000	0.000	0.000
97	A	99	LEU	0	0.009	0.008	12.312	-0.127	-0.127	0.000	0.000	0.000	0.000
98	A	100	GLN	0	-0.071	-0.052	15.463	-1.174	-1.174	0.000	0.000	0.000	0.000
99	A	101	TRP	0	-0.020	0.003	17.455	-0.133	-0.133	0.000	0.000	0.000	0.000
100	A	102	ILE	0	-0.012	-0.025	14.137	0.129	0.129	0.000	0.000	0.000	0.000
101	A	103	LYS	1	0.917	0.913	11.596	21.919	21.919	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.928	-0.944	15.567	-15.061	-15.061	0.000	0.000	0.000	0.000
103	A	105	ASN	0	-0.114	-0.041	18.098	0.528	0.528	0.000	0.000	0.000	0.000
104	A	106	SER	0	0.055	0.037	15.417	0.072	0.072	0.000	0.000	0.000	0.000
105	A	107	PRO	0	-0.034	-0.031	17.621	-0.021	-0.021	0.000	0.000	0.000	0.000
106	A	108	SER	0	-0.023	0.005	15.122	-0.532	-0.532	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LYS)