FMO DATABASE

FMODB ID: G5QN1

Calculation Name: 3DWM-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3DWM

Chain ID: A

ChEMBL ID:

UniProt ID: P9WP33

Base Structure: X-ray

Registration Date: 2023-09-20

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	89
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-547672.436863
FMO2-HF: Nuclear repulsion	515506.890597
FMO2-HF: Total energy	-32165.546266
FMO2-MP2: Total energy	-32260.65257

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:ASN)

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

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.
-32.453	-26.155	7.449	-6.775	-6.973	-0.039

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.001 / q_NPA : 0.003

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	THR	0	-0.029	-0.008	3.924	3.558	5.724	-0.015	-1.061	-1.090	0.004
4	A	5	VAL	0	0.016	0.000	5.919	-1.359	-1.359	0.000	0.000	0.000	0.000
5	A	6	SER	0	-0.035	-0.007	9.269	0.347	0.347	0.000	0.000	0.000	0.000
6	A	7	ILE	0	0.051	0.018	12.152	-0.172	-0.172	0.000	0.000	0.000	0.000
7	A	8	PRO	0	0.045	0.040	14.782	-0.037	-0.037	0.000	0.000	0.000	0.000
8	A	9	THR	0	-0.002	-0.032	18.436	0.051	0.051	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.016	-0.014	20.813	0.051	0.051	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.040	0.011	17.917	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.893	0.954	16.723	-0.564	-0.564	0.000	0.000	0.000	0.000
12	A	13	PRO	0	-0.033	0.008	18.312	0.077	0.077	0.000	0.000	0.000	0.000
13	A	14	HIS	0	-0.010	0.004	17.718	-0.027	-0.027	0.000	0.000	0.000	0.000
14	A	15	THR	0	0.033	0.027	13.448	0.013	0.013	0.000	0.000	0.000	0.000
15	A	16	GLY	0	0.022	0.023	15.305	0.132	0.132	0.000	0.000	0.000	0.000
16	A	17	GLY	0	-0.044	-0.040	17.968	-0.026	-0.026	0.000	0.000	0.000	0.000
17	A	18	GLN	0	-0.057	-0.030	11.663	0.160	0.160	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.925	0.934	14.170	-0.664	-0.664	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.037	-0.018	9.434	-0.113	-0.113	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.010	0.017	8.295	0.011	0.011	0.000	0.000	0.000	0.000
21	A	22	SER	0	0.015	0.016	2.395	-6.964	-5.439	0.719	-0.868	-1.377	0.012
22	A	23	ALA	0	-0.004	-0.005	4.271	-1.574	-1.442	-0.001	-0.017	-0.113	0.000
23	A	24	SER	0	-0.060	-0.029	3.009	-1.326	-0.256	0.093	-0.551	-0.612	-0.003
24	A	25	GLY	0	0.052	0.008	4.396	0.646	0.732	-0.001	-0.013	-0.073	0.000
25	A	26	ASP	-1	-0.867	-0.922	6.750	-1.566	-1.566	0.000	0.000	0.000	0.000
26	A	27	THR	0	-0.030	-0.023	9.027	-0.026	-0.026	0.000	0.000	0.000	0.000
27	A	28	LEU	0	0.064	0.032	10.502	0.110	0.110	0.000	0.000	0.000	0.000
28	A	29	GLY	0	-0.031	-0.029	12.310	0.182	0.182	0.000	0.000	0.000	0.000
29	A	30	ALA	0	-0.042	0.002	10.040	0.134	0.134	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.040	0.028	6.908	0.243	0.243	0.000	0.000	0.000	0.000
31	A	32	ILE	0	-0.030	-0.021	9.352	0.375	0.375	0.000	0.000	0.000	0.000
32	A	33	SER	0	-0.022	-0.021	12.395	0.086	0.086	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.795	-0.895	7.340	2.469	2.469	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.006	-0.013	9.353	0.262	0.262	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.837	-0.912	11.479	0.723	0.723	0.000	0.000	0.000	0.000
36	A	37	ALA	0	-0.035	-0.014	12.473	-0.031	-0.031	0.000	0.000	0.000	0.000
37	A	38	ASN	0	-0.086	-0.041	9.670	0.075	0.075	0.000	0.000	0.000	0.000
38	A	39	TYR	0	-0.051	-0.028	9.693	-0.130	-0.130	0.000	0.000	0.000	0.000
39	A	40	SER	0	0.041	0.032	15.334	-0.134	-0.134	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.022	-0.008	18.472	-0.016	-0.016	0.000	0.000	0.000	0.000
41	A	42	ILE	0	-0.042	-0.026	14.712	-0.093	-0.093	0.000	0.000	0.000	0.000
42	A	43	SER	0	0.035	0.018	17.145	-0.110	-0.110	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.936	-0.970	18.429	0.314	0.314	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.822	0.911	20.962	-0.477	-0.477	0.000	0.000	0.000	0.000
45	A	46	LEU	0	-0.010	-0.003	15.975	-0.037	-0.037	0.000	0.000	0.000	0.000
46	A	47	MET	0	-0.033	0.004	19.764	-0.069	-0.069	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.838	-0.922	22.288	0.077	0.077	0.000	0.000	0.000	0.000
48	A	49	PRO	0	-0.034	-0.003	25.827	0.001	0.001	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.041	-0.009	28.032	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	51	SER	0	-0.075	-0.062	28.423	-0.008	-0.008	0.000	0.000	0.000	0.000
51	A	52	PRO	0	0.064	0.010	25.124	0.000	0.000	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.004	0.014	21.297	-0.022	-0.022	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.850	0.938	21.333	-0.053	-0.053	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.080	0.035	18.143	0.031	0.031	0.000	0.000	0.000	0.000
55	A	56	HIS	0	0.043	0.019	22.268	-0.038	-0.038	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.937	0.954	24.598	-0.051	-0.051	0.000	0.000	0.000	0.000
57	A	58	PHE	0	-0.037	-0.024	26.757	-0.021	-0.021	0.000	0.000	0.000	0.000
58	A	59	VAL	0	0.001	0.031	20.169	0.023	0.023	0.000	0.000	0.000	0.000
59	A	60	ASN	0	0.012	0.012	21.324	-0.040	-0.040	0.000	0.000	0.000	0.000
60	A	61	ILE	0	0.016	-0.013	14.939	0.080	0.080	0.000	0.000	0.000	0.000
61	A	62	TYR	0	-0.044	-0.013	16.631	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	63	VAL	0	0.024	0.006	11.270	0.098	0.098	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.015	-0.003	10.843	0.056	0.056	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.971	-0.980	13.986	-0.683	-0.683	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.810	-0.896	16.897	-0.424	-0.424	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.885	-0.935	17.588	-0.175	-0.175	0.000	0.000	0.000	0.000
67	A	68	VAL	0	0.063	0.026	15.459	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.760	0.875	18.586	0.060	0.060	0.000	0.000	0.000	0.000
69	A	70	PHE	0	-0.064	-0.041	21.443	0.034	0.034	0.000	0.000	0.000	0.000
70	A	71	SER	0	0.027	0.023	18.010	-0.027	-0.027	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.023	0.020	18.754	-0.038	-0.038	0.000	0.000	0.000	0.000
72	A	73	GLY	0	-0.018	-0.015	19.150	0.038	0.038	0.000	0.000	0.000	0.000
73	A	74	LEU	0	0.005	-0.015	16.023	-0.046	-0.046	0.000	0.000	0.000	0.000
74	A	75	ALA	0	-0.025	-0.008	15.162	-0.026	-0.026	0.000	0.000	0.000	0.000
75	A	76	THR	0	-0.021	-0.005	13.890	-0.033	-0.033	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.008	-0.014	12.582	-0.015	-0.015	0.000	0.000	0.000	0.000
77	A	78	ILE	0	-0.058	-0.018	6.571	0.130	0.130	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.031	-0.010	7.874	-0.089	-0.089	0.000	0.000	0.000	0.000
79	A	80	ASP	-1	-0.875	-0.956	1.946	-26.500	-25.643	6.656	-4.191	-3.323	-0.052
80	A	81	GLY	0	-0.041	-0.020	3.975	1.455	1.702	-0.001	-0.066	-0.180	0.000
81	A	82	ASP	-1	-0.821	-0.889	5.293	-1.075	-0.860	-0.001	-0.008	-0.205	0.000
82	A	83	SER	0	-0.072	-0.047	7.037	0.119	0.119	0.000	0.000	0.000	0.000
83	A	84	VAL	0	0.030	0.008	9.050	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.047	-0.030	11.383	0.303	0.303	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.018	0.026	13.937	-0.083	-0.083	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.012	-0.023	16.795	0.058	0.058	0.000	0.000	0.000	0.000
87	A	88	PRO	0	-0.020	-0.004	20.274	-0.026	-0.026	0.000	0.000	0.000	0.000
88	A	89	ALA	0	-0.003	-0.002	23.744	-0.025	-0.025	0.000	0.000	0.000	0.000
89	A	90	VAL	0	-0.031	-0.013	25.932	0.008	0.008	0.000	0.000	0.000	0.000

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