FMO DATABASE

FMODB ID: NN2MQ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-770872.029197
FMO2-HF: Nuclear repulsion	728275.841805
FMO2-HF: Total energy	-42596.187392
FMO2-MP2: Total energy	-42715.766007

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.
-117.458	-116.158	-0.015	-0.432	-0.854	0

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 : 0.949 / q_NPA : 0.946

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].
3	A	5	GLU	-1	-0.824	-0.921	3.803	-27.942	-26.747	-0.014	-0.422	-0.759
4	A	6	GLN	0	-0.059	-0.024	6.898	0.958	0.958	0.000	0.000	0.000
5	A	7	LEU	0	0.008	-0.004	5.048	-4.451	-4.451	0.000	0.000	0.000
6	A	8	LEU	0	-0.031	-0.016	8.954	3.145	3.145	0.000	0.000	0.000
7	A	9	ILE	0	0.002	0.002	10.773	-1.904	-1.904	0.000	0.000	0.000
8	A	10	PHE	0	-0.020	-0.018	12.586	1.864	1.864	0.000	0.000	0.000
9	A	11	THR	0	0.011	-0.023	15.218	-0.453	-0.453	0.000	0.000	0.000
10	A	12	THR	0	0.073	0.051	17.840	0.493	0.493	0.000	0.000	0.000
11	A	13	CYS	0	-0.065	0.009	21.432	-0.173	-0.173	0.000	0.000	0.000
12	A	14	PRO	0	0.049	0.030	24.483	0.151	0.151	0.000	0.000	0.000
13	A	15	ASP	-1	-0.805	-0.912	27.824	-9.933	-9.933	0.000	0.000	0.000
14	A	16	ALA	0	0.020	-0.013	28.453	-0.364	-0.364	0.000	0.000	0.000
15	A	17	ASP	-1	-0.922	-0.945	29.288	-9.674	-9.674	0.000	0.000	0.000
16	A	18	ILE	0	-0.071	-0.047	25.211	-0.192	-0.192	0.000	0.000	0.000
17	A	19	ALA	0	0.051	0.009	24.764	-0.411	-0.411	0.000	0.000	0.000
18	A	20	CYS	0	0.015	-0.002	25.158	-0.402	-0.402	0.000	0.000	0.000
19	A	21	ARG	1	0.949	0.982	27.189	10.289	10.289	0.000	0.000	0.000
20	A	22	ILE	0	0.010	0.008	21.783	-0.121	-0.121	0.000	0.000	0.000
21	A	23	ALA	0	0.009	-0.007	22.413	-0.561	-0.561	0.000	0.000	0.000
22	A	24	THR	0	-0.029	-0.028	23.474	-0.198	-0.198	0.000	0.000	0.000
23	A	25	ALA	0	0.021	0.020	24.377	-0.042	-0.042	0.000	0.000	0.000
24	A	26	LEU	0	-0.007	0.005	18.119	-0.242	-0.242	0.000	0.000	0.000
25	A	27	VAL	0	-0.018	-0.014	20.772	-0.515	-0.515	0.000	0.000	0.000
26	A	28	GLU	-1	-0.956	-0.973	22.765	-10.916	-10.916	0.000	0.000	0.000
27	A	29	ALA	0	-0.098	-0.041	21.638	0.172	0.172	0.000	0.000	0.000
28	A	30	LYS	1	0.886	0.940	20.664	12.245	12.245	0.000	0.000	0.000
29	A	31	LEU	0	0.006	0.018	16.234	-0.670	-0.670	0.000	0.000	0.000
30	A	32	ALA	0	-0.008	-0.011	15.939	-1.460	-1.460	0.000	0.000	0.000
31	A	33	ALA	0	-0.002	0.022	17.298	0.895	0.895	0.000	0.000	0.000
32	A	34	CYS	0	-0.065	-0.049	18.713	1.044	1.044	0.000	0.000	0.000
33	A	35	VAL	0	0.047	0.025	18.680	-1.061	-1.061	0.000	0.000	0.000
34	A	36	GLN	0	-0.086	-0.042	20.205	0.590	0.590	0.000	0.000	0.000
35	A	37	ILE	0	0.043	0.029	21.640	-0.501	-0.501	0.000	0.000	0.000
36	A	38	GLY	0	-0.042	-0.006	24.120	0.388	0.388	0.000	0.000	0.000
37	A	39	GLN	0	-0.022	-0.032	25.528	0.438	0.438	0.000	0.000	0.000
38	A	40	ALA	0	0.012	-0.006	27.411	-0.322	-0.322	0.000	0.000	0.000
39	A	41	VAL	0	-0.014	0.006	24.212	0.104	0.104	0.000	0.000	0.000
40	A	42	GLU	-1	-0.837	-0.914	27.497	-9.675	-9.675	0.000	0.000	0.000
41	A	43	SER	0	-0.014	-0.003	24.158	-0.406	-0.406	0.000	0.000	0.000
42	A	44	ILE	0	-0.025	-0.021	25.454	0.468	0.468	0.000	0.000	0.000
43	A	45	TYR	0	-0.020	-0.010	24.270	-0.522	-0.522	0.000	0.000	0.000
44	A	46	GLN	0	-0.043	-0.020	25.603	0.774	0.774	0.000	0.000	0.000
45	A	47	TRP	0	-0.016	-0.005	26.304	-0.254	-0.254	0.000	0.000	0.000
46	A	48	ASP	-1	-0.877	-0.947	28.570	-9.349	-9.349	0.000	0.000	0.000
47	A	49	ASN	0	-0.086	-0.043	30.147	0.209	0.209	0.000	0.000	0.000
48	A	50	ASN	0	-0.003	0.003	31.422	0.289	0.289	0.000	0.000	0.000
49	A	51	ILE	0	0.002	-0.007	30.594	-0.326	-0.326	0.000	0.000	0.000
50	A	52	CYS	0	-0.043	-0.016	29.242	0.401	0.401	0.000	0.000	0.000
51	A	53	GLN	0	-0.040	-0.045	29.588	-0.132	-0.132	0.000	0.000	0.000
52	A	54	SER	0	-0.014	0.008	27.780	0.207	0.207	0.000	0.000	0.000
53	A	55	HIS	0	-0.031	-0.008	28.764	-0.140	-0.140	0.000	0.000	0.000
54	A	56	GLU	-1	-0.877	-0.935	24.404	-12.697	-12.697	0.000	0.000	0.000
55	A	57	VAL	0	-0.036	-0.032	25.746	0.187	0.187	0.000	0.000	0.000
56	A	58	PRO	0	0.000	0.031	21.700	-0.450	-0.450	0.000	0.000	0.000
57	A	59	MET	0	0.007	-0.014	19.950	0.433	0.433	0.000	0.000	0.000
58	A	60	GLN	0	-0.016	-0.013	16.929	-1.066	-1.066	0.000	0.000	0.000
59	A	61	ILE	0	0.026	0.021	14.518	0.972	0.972	0.000	0.000	0.000
60	A	62	LYS	1	0.886	0.955	14.012	15.250	15.250	0.000	0.000	0.000
61	A	63	CYS	0	0.038	0.009	11.297	1.111	1.111	0.000	0.000	0.000
62	A	64	MET	0	0.006	0.055	10.060	-1.795	-1.795	0.000	0.000	0.000
63	A	65	THR	0	-0.011	-0.038	4.267	0.835	0.940	-0.001	-0.010	-0.095
64	A	66	THR	0	-0.018	-0.011	7.638	-0.778	-0.778	0.000	0.000	0.000
65	A	67	ASP	-1	-0.847	-0.924	9.264	-20.390	-20.390	0.000	0.000	0.000
66	A	68	TYR	0	-0.069	-0.047	8.914	0.219	0.219	0.000	0.000	0.000
67	A	69	PRO	0	0.005	-0.006	9.906	1.434	1.434	0.000	0.000	0.000
68	A	70	ALA	0	-0.013	0.010	12.675	1.456	1.456	0.000	0.000	0.000
69	A	71	ILE	0	0.021	-0.002	13.530	1.169	1.169	0.000	0.000	0.000
70	A	72	GLU	-1	-0.880	-0.936	12.175	-23.048	-23.048	0.000	0.000	0.000
71	A	73	GLN	0	0.035	0.010	14.796	1.493	1.493	0.000	0.000	0.000
72	A	74	LEU	0	-0.060	-0.021	17.886	1.041	1.041	0.000	0.000	0.000
73	A	75	VAL	0	0.001	-0.018	17.562	0.894	0.894	0.000	0.000	0.000
74	A	76	ILE	0	0.012	-0.008	16.764	0.704	0.704	0.000	0.000	0.000
75	A	77	THR	0	-0.037	0.001	19.847	0.708	0.708	0.000	0.000	0.000
76	A	78	MET	0	-0.096	-0.043	22.717	0.600	0.600	0.000	0.000	0.000
77	A	79	HIS	0	-0.027	-0.006	21.539	0.861	0.861	0.000	0.000	0.000
78	A	80	PRO	0	-0.019	-0.008	23.963	0.128	0.128	0.000	0.000	0.000
79	A	81	TYR	0	-0.050	-0.034	23.624	0.484	0.484	0.000	0.000	0.000
80	A	82	GLU	-1	-0.908	-0.956	23.521	-12.330	-12.330	0.000	0.000	0.000
81	A	83	VAL	0	-0.044	-0.027	18.634	-0.556	-0.556	0.000	0.000	0.000
82	A	84	PRO	0	-0.007	0.016	18.816	0.085	0.085	0.000	0.000	0.000
83	A	85	GLU	-1	-0.928	-0.954	16.863	-17.314	-17.314	0.000	0.000	0.000
84	A	86	PHE	0	0.017	0.002	12.271	0.157	0.157	0.000	0.000	0.000
85	A	87	ILE	0	-0.013	0.010	11.069	-1.430	-1.430	0.000	0.000	0.000
86	A	88	ALA	0	0.020	0.005	7.102	0.592	0.592	0.000	0.000	0.000
87	A	89	THR	0	0.005	0.007	7.915	-2.672	-2.672	0.000	0.000	0.000
88	A	90	PRO	0	-0.038	-0.012	5.232	-0.979	-0.979	0.000	0.000	0.000
89	A	91	ILE	0	0.002	0.011	6.885	4.316	4.316	0.000	0.000	0.000
90	A	92	ILE	0	-0.027	-0.024	6.643	-2.616	-2.616	0.000	0.000	0.000
91	A	93	GLY	0	-0.004	-0.005	9.025	1.345	1.345	0.000	0.000	0.000
92	A	94	GLY	0	0.027	0.011	12.556	-0.302	-0.302	0.000	0.000	0.000
93	A	95	PHE	0	0.008	0.003	15.727	0.238	0.238	0.000	0.000	0.000
94	A	96	GLY	0	0.074	0.033	16.572	-0.283	-0.283	0.000	0.000	0.000
95	A	97	PRO	0	0.014	-0.003	17.638	-0.465	-0.465	0.000	0.000	0.000
96	A	98	TYR	0	0.007	0.010	17.130	-0.078	-0.078	0.000	0.000	0.000
97	A	99	LEU	0	-0.001	0.002	12.323	-0.148	-0.148	0.000	0.000	0.000
98	A	100	GLN	0	-0.063	-0.055	15.463	-1.071	-1.071	0.000	0.000	0.000
99	A	101	TRP	0	-0.020	-0.002	17.331	-0.135	-0.135	0.000	0.000	0.000
100	A	102	ILE	0	-0.016	-0.022	13.829	0.147	0.147	0.000	0.000	0.000
101	A	103	LYS	1	1.006	0.971	13.006	19.199	19.199	0.000	0.000	0.000
102	A	104	ASP	-1	-0.946	-0.955	15.332	-14.930	-14.930	0.000	0.000	0.000
103	A	105	ASN	0	-0.122	-0.041	17.902	0.564	0.564	0.000	0.000	0.000
104	A	106	SER	0	0.070	0.039	15.209	0.116	0.116	0.000	0.000	0.000
105	A	107	PRO	0	-0.039	-0.031	17.404	0.009	0.009	0.000	0.000	0.000
106	A	108	SER	0	-0.025	0.004	15.102	-0.484	-0.484	0.000	0.000	0.000

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