FMO DATABASE

FMODB ID: LN9G9

Calculation Name: 3CPT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3CPT

Chain ID: A

ChEMBL ID:

UniProt ID: Q9JHS3

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	119
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-963372.788036
FMO2-HF: Nuclear repulsion	918402.593242
FMO2-HF: Total energy	-44970.194795
FMO2-MP2: Total energy	-45104.651516

3D Structure Molmil

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:ASP)

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

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.
-196.556	-194.184	16.677	-10.613	-8.437	0.115

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.831 / q_NPA : -0.920

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	LEU	0	0.070	0.030	3.550	-5.266	-2.958	0.004	-1.021	-1.291	0.005
4	A	6	LYS	1	0.893	0.939	1.681	-131.324	-131.745	16.672	-9.381	-6.870	0.109
5	A	7	ARG	1	0.979	0.984	3.795	-38.331	-37.846	0.001	-0.211	-0.276	0.001
6	A	8	PHE	0	0.006	0.004	5.679	-4.709	-4.709	0.000	0.000	0.000	0.000
7	A	9	LEU	0	0.044	0.012	7.669	-3.064	-3.064	0.000	0.000	0.000	0.000
8	A	10	TYR	0	-0.013	0.001	8.010	-2.501	-2.501	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.893	0.935	9.681	-23.478	-23.478	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.879	0.921	11.702	-18.923	-18.923	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.047	0.013	12.291	-1.461	-1.461	0.000	0.000	0.000	0.000
12	A	14	PRO	0	-0.010	-0.014	14.712	-1.019	-1.019	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.089	-0.047	17.170	-0.958	-0.958	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.017	-0.008	19.186	-0.803	-0.803	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.898	-0.947	20.615	12.050	12.050	0.000	0.000	0.000	0.000
16	A	18	GLY	0	0.013	0.002	22.250	-0.304	-0.304	0.000	0.000	0.000	0.000
17	A	19	LEU	0	-0.044	-0.004	16.416	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	20	HIS	0	0.020	-0.005	17.547	0.827	0.827	0.000	0.000	0.000	0.000
19	A	21	ALA	0	-0.004	-0.015	14.001	1.242	1.242	0.000	0.000	0.000	0.000
20	A	22	ILE	0	0.000	0.017	11.845	-1.366	-1.366	0.000	0.000	0.000	0.000
21	A	23	VAL	0	-0.025	-0.024	11.633	2.478	2.478	0.000	0.000	0.000	0.000
22	A	24	VAL	0	0.026	0.027	10.494	-1.876	-1.876	0.000	0.000	0.000	0.000
23	A	25	SER	0	-0.010	-0.012	11.558	1.926	1.926	0.000	0.000	0.000	0.000
24	A	26	ASP	-1	-0.743	-0.866	14.126	17.248	17.248	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.894	0.918	16.620	-12.641	-12.641	0.000	0.000	0.000	0.000
26	A	28	ASP	-1	-0.876	-0.921	19.261	13.561	13.561	0.000	0.000	0.000	0.000
27	A	29	GLY	0	-0.082	-0.032	17.785	-0.099	-0.099	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.017	-0.028	13.985	1.129	1.129	0.000	0.000	0.000	0.000
29	A	31	PRO	0	-0.079	-0.034	10.791	0.031	0.031	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.023	0.009	7.944	1.063	1.063	0.000	0.000	0.000	0.000
31	A	33	ILE	0	-0.001	-0.007	5.480	5.338	5.338	0.000	0.000	0.000	0.000
32	A	34	LYS	1	0.873	0.935	7.749	-27.737	-27.737	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.058	-0.017	7.008	3.948	3.948	0.000	0.000	0.000	0.000
34	A	36	ALA	0	0.023	-0.005	9.601	-2.572	-2.572	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.013	0.013	12.601	0.703	0.703	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.901	-0.953	15.034	16.779	16.779	0.000	0.000	0.000	0.000
37	A	39	ASN	0	-0.011	-0.007	17.791	-1.530	-1.530	0.000	0.000	0.000	0.000
38	A	40	ALA	0	-0.060	-0.022	17.149	-0.754	-0.754	0.000	0.000	0.000	0.000
39	A	41	PRO	0	0.012	0.004	19.128	0.037	0.037	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.793	-0.893	18.569	16.739	16.739	0.000	0.000	0.000	0.000
41	A	43	HIS	0	-0.041	-0.033	19.588	0.792	0.792	0.000	0.000	0.000	0.000
42	A	44	ALA	0	-0.015	-0.011	20.775	0.028	0.028	0.000	0.000	0.000	0.000
43	A	45	LEU	0	0.022	0.010	14.737	0.628	0.628	0.000	0.000	0.000	0.000
44	A	46	ARG	1	0.840	0.917	16.784	-14.095	-14.095	0.000	0.000	0.000	0.000
45	A	47	PRO	0	0.047	0.031	16.813	-0.526	-0.526	0.000	0.000	0.000	0.000
46	A	48	GLY	0	0.066	0.055	19.068	-0.482	-0.482	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.008	0.011	21.547	-0.613	-0.613	0.000	0.000	0.000	0.000
48	A	50	LEU	0	0.019	-0.005	16.971	-0.459	-0.459	0.000	0.000	0.000	0.000
49	A	51	SER	0	0.041	0.002	20.959	-0.564	-0.564	0.000	0.000	0.000	0.000
50	A	52	THR	0	-0.028	-0.013	22.286	-0.727	-0.727	0.000	0.000	0.000	0.000
51	A	53	PHE	0	-0.012	-0.006	22.964	-0.575	-0.575	0.000	0.000	0.000	0.000
52	A	54	ALA	0	0.044	0.029	22.423	-0.435	-0.435	0.000	0.000	0.000	0.000
53	A	55	LEU	0	0.002	0.007	24.584	-0.425	-0.425	0.000	0.000	0.000	0.000
54	A	56	ALA	0	0.003	0.001	27.360	-0.478	-0.478	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.033	-0.033	26.621	-0.342	-0.342	0.000	0.000	0.000	0.000
56	A	58	ASP	-1	-0.886	-0.913	27.513	10.469	10.469	0.000	0.000	0.000	0.000
57	A	59	GLN	0	0.038	-0.005	29.479	-0.291	-0.291	0.000	0.000	0.000	0.000
58	A	60	GLY	0	0.031	0.020	32.201	-0.337	-0.337	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.040	-0.038	31.958	-0.135	-0.135	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.808	0.909	31.001	-10.143	-10.143	0.000	0.000	0.000	0.000
61	A	63	LEU	0	-0.037	-0.020	35.633	-0.265	-0.265	0.000	0.000	0.000	0.000
62	A	64	GLY	0	0.011	0.017	37.282	-0.259	-0.259	0.000	0.000	0.000	0.000
63	A	65	LEU	0	-0.065	-0.011	33.705	-0.044	-0.044	0.000	0.000	0.000	0.000
64	A	66	SER	0	0.062	0.026	33.983	0.001	0.001	0.000	0.000	0.000	0.000
65	A	67	LYS	1	0.933	0.967	26.048	-11.036	-11.036	0.000	0.000	0.000	0.000
66	A	68	ASN	0	0.013	-0.001	27.016	0.328	0.328	0.000	0.000	0.000	0.000
67	A	69	LYS	1	0.962	0.979	25.949	-9.985	-9.985	0.000	0.000	0.000	0.000
68	A	70	SER	0	0.053	0.017	24.425	0.563	0.563	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.010	0.014	25.085	-0.610	-0.610	0.000	0.000	0.000	0.000
70	A	72	ILE	0	0.015	0.008	25.225	0.580	0.580	0.000	0.000	0.000	0.000
71	A	73	CYS	0	-0.073	-0.016	26.375	-0.562	-0.562	0.000	0.000	0.000	0.000
72	A	74	TYR	0	0.048	0.000	27.011	0.404	0.404	0.000	0.000	0.000	0.000
73	A	75	TYR	0	-0.003	-0.011	26.632	-0.220	-0.220	0.000	0.000	0.000	0.000
74	A	76	ASN	0	0.026	0.004	29.938	-0.183	-0.183	0.000	0.000	0.000	0.000
75	A	77	THR	0	0.013	0.005	28.090	-0.050	-0.050	0.000	0.000	0.000	0.000
76	A	78	TYR	0	0.001	0.012	23.810	0.381	0.381	0.000	0.000	0.000	0.000
77	A	79	GLN	0	0.007	0.013	24.067	-0.538	-0.538	0.000	0.000	0.000	0.000
78	A	80	VAL	0	-0.021	-0.010	21.167	0.709	0.709	0.000	0.000	0.000	0.000
79	A	81	VAL	0	0.007	0.011	21.491	-0.675	-0.675	0.000	0.000	0.000	0.000
80	A	82	GLN	0	-0.028	-0.029	20.111	0.375	0.375	0.000	0.000	0.000	0.000
81	A	83	PHE	0	0.002	-0.009	19.447	-0.955	-0.955	0.000	0.000	0.000	0.000
82	A	84	ASN	0	-0.019	-0.018	19.996	1.017	1.017	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.783	0.867	18.004	-14.712	-14.712	0.000	0.000	0.000	0.000
84	A	86	LEU	0	0.030	0.051	18.717	0.488	0.488	0.000	0.000	0.000	0.000
85	A	87	PRO	0	0.018	-0.012	17.211	-0.393	-0.393	0.000	0.000	0.000	0.000
86	A	88	LEU	0	0.007	0.019	12.963	0.296	0.296	0.000	0.000	0.000	0.000
87	A	89	VAL	0	-0.010	-0.002	16.305	-1.215	-1.215	0.000	0.000	0.000	0.000
88	A	90	VAL	0	0.001	0.012	14.487	1.246	1.246	0.000	0.000	0.000	0.000
89	A	91	SER	0	0.011	0.003	15.980	-1.679	-1.679	0.000	0.000	0.000	0.000
90	A	92	PHE	0	0.014	0.006	16.126	1.378	1.378	0.000	0.000	0.000	0.000
91	A	93	ILE	0	-0.025	-0.011	16.853	-0.982	-0.982	0.000	0.000	0.000	0.000
92	A	94	ALA	0	0.032	0.020	18.924	0.595	0.595	0.000	0.000	0.000	0.000
93	A	95	SER	0	0.049	0.022	21.596	-0.289	-0.289	0.000	0.000	0.000	0.000
94	A	96	SER	0	-0.037	-0.026	24.830	0.078	0.078	0.000	0.000	0.000	0.000
95	A	97	SER	0	0.008	0.002	27.894	-0.066	-0.066	0.000	0.000	0.000	0.000
96	A	98	ALA	0	0.012	0.030	24.057	-0.169	-0.169	0.000	0.000	0.000	0.000
97	A	99	ASN	0	0.045	0.009	26.135	-0.166	-0.166	0.000	0.000	0.000	0.000
98	A	100	THR	0	0.068	0.014	25.369	0.225	0.225	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.009	0.012	25.301	0.320	0.320	0.000	0.000	0.000	0.000
100	A	102	LEU	0	-0.005	-0.008	23.588	0.149	0.149	0.000	0.000	0.000	0.000
101	A	103	ILE	0	0.025	0.018	19.906	0.563	0.563	0.000	0.000	0.000	0.000
102	A	104	VAL	0	-0.001	0.002	21.030	0.485	0.485	0.000	0.000	0.000	0.000
103	A	105	SER	0	-0.043	-0.015	22.632	0.176	0.176	0.000	0.000	0.000	0.000
104	A	106	LEU	0	0.056	0.022	16.132	0.212	0.212	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.820	-0.883	17.768	15.512	15.512	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.889	0.940	18.383	-12.503	-12.503	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.883	-0.925	17.878	15.844	15.844	0.000	0.000	0.000	0.000
108	A	110	LEU	0	-0.010	-0.013	12.846	0.556	0.556	0.000	0.000	0.000	0.000
109	A	111	ALA	0	0.004	0.014	14.598	0.894	0.894	0.000	0.000	0.000	0.000
110	A	112	PRO	0	0.002	0.000	16.019	0.343	0.343	0.000	0.000	0.000	0.000
111	A	113	LEU	0	0.056	0.036	10.591	0.471	0.471	0.000	0.000	0.000	0.000
112	A	114	PHE	0	-0.035	-0.033	11.441	1.105	1.105	0.000	0.000	0.000	0.000
113	A	115	GLU	-1	-0.824	-0.882	13.228	15.476	15.476	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.895	-0.954	11.772	19.544	19.544	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.033	-0.012	7.764	0.741	0.741	0.000	0.000	0.000	0.000
116	A	118	ARG	1	0.737	0.818	11.017	-15.000	-15.000	0.000	0.000	0.000	0.000
117	A	119	GLN	0	-0.089	-0.041	13.690	-1.017	-1.017	0.000	0.000	0.000	0.000
118	A	120	VAL	0	-0.033	0.005	9.748	0.965	0.965	0.000	0.000	0.000	0.000
119	A	121	VAL	0	-0.046	-0.018	12.942	-0.668	-0.668	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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