FMO DATABASE

FMODB ID: ZYZ3N

Calculation Name: 4B0E-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4B0E

Chain ID: A

ChEMBL ID:

UniProt ID: P26949

Base Structure: X-ray

Registration Date: 2023-03-14

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	OptAll
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	95
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-713699.449241
FMO2-HF: Nuclear repulsion	675897.372898
FMO2-HF: Total energy	-37802.076343
FMO2-MP2: Total energy	-37913.958759

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:28:LEU)

Summations of interaction energy for fragment #1(A:28:LEU)

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.
-7.592	-1.635	1.224	-2.947	-4.233	-0.008

Interaction energy analysis for fragmet #1(A:28:LEU)

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 : -0.005

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	30	GLY	0	0.025	0.027	2.936	-4.082	-1.702	0.219	-1.274	-1.325	-0.008
4	A	31	ASN	0	0.009	0.008	5.686	0.539	0.539	0.000	0.000	0.000	0.000
5	A	32	TYR	0	-0.007	-0.020	2.622	-0.984	0.845	0.294	-0.840	-1.282	-0.006
6	A	33	PHE	0	-0.013	0.007	9.292	0.224	0.224	0.000	0.000	0.000	0.000
7	A	34	VAL	0	0.005	0.003	10.381	-0.015	-0.015	0.000	0.000	0.000	0.000
8	A	35	ASN	0	-0.018	-0.030	13.211	0.039	0.039	0.000	0.000	0.000	0.000
9	A	36	VAL	0	0.015	0.018	15.912	0.030	0.030	0.000	0.000	0.000	0.000
10	A	37	PHE	0	-0.005	-0.024	17.573	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	38	VAL	0	0.075	0.042	19.657	0.019	0.019	0.000	0.000	0.000	0.000
12	A	39	ASN	0	0.001	-0.002	22.504	0.000	0.000	0.000	0.000	0.000	0.000
13	A	40	GLY	0	0.013	0.012	23.152	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	41	ARG	1	0.894	0.950	24.356	-0.028	-0.028	0.000	0.000	0.000	0.000
15	A	42	LYS	1	0.863	0.926	19.995	0.140	0.140	0.000	0.000	0.000	0.000
16	A	43	VAL	0	-0.038	-0.026	21.433	0.000	0.000	0.000	0.000	0.000	0.000
17	A	44	ASP	-1	-0.759	-0.872	19.323	-0.179	-0.179	0.000	0.000	0.000	0.000
18	A	45	SER	0	-0.089	-0.039	17.745	0.024	0.024	0.000	0.000	0.000	0.000
19	A	46	GLY	0	0.026	0.028	16.474	0.011	0.011	0.000	0.000	0.000	0.000
20	A	47	ASN	0	-0.038	-0.019	12.521	0.057	0.057	0.000	0.000	0.000	0.000
21	A	48	ILE	0	-0.019	0.003	11.865	0.081	0.081	0.000	0.000	0.000	0.000
22	A	49	ASP	-1	-0.895	-0.953	9.304	-1.142	-1.142	0.000	0.000	0.000	0.000
23	A	50	PHE	0	-0.002	-0.002	6.602	0.337	0.337	0.000	0.000	0.000	0.000
24	A	51	ARG	1	0.885	0.925	6.742	-0.738	-0.738	0.000	0.000	0.000	0.000
25	A	52	LEU	0	-0.012	-0.014	4.181	0.193	0.375	-0.001	-0.016	-0.165	0.000
26	A	53	GLU	-1	-0.803	-0.871	7.705	0.045	0.045	0.000	0.000	0.000	0.000
27	A	54	LYS	1	0.826	0.891	11.356	-0.668	-0.668	0.000	0.000	0.000	0.000
28	A	55	HIS	0	0.081	0.031	13.417	-0.095	-0.095	0.000	0.000	0.000	0.000
29	A	56	ASN	0	-0.026	-0.022	16.063	0.026	0.026	0.000	0.000	0.000	0.000
30	A	57	GLY	0	-0.002	0.006	16.927	-0.015	-0.015	0.000	0.000	0.000	0.000
31	A	58	LYS	1	0.901	0.945	13.624	-0.543	-0.543	0.000	0.000	0.000	0.000
32	A	59	GLU	-1	-0.786	-0.876	8.285	1.019	1.019	0.000	0.000	0.000	0.000
33	A	60	LEU	0	-0.044	-0.005	8.405	0.141	0.141	0.000	0.000	0.000	0.000
34	A	61	LEU	0	-0.009	-0.004	2.602	-2.116	-0.904	0.704	-0.727	-1.189	0.007
35	A	62	TRP	0	0.042	0.009	7.253	-0.339	-0.339	0.000	0.000	0.000	0.000
36	A	63	PRO	0	0.010	0.006	10.451	-0.129	-0.129	0.000	0.000	0.000	0.000
37	A	64	CYS	0	-0.094	-0.052	11.885	0.028	0.028	0.000	0.000	0.000	0.000
38	A	65	LEU	0	-0.026	-0.023	14.471	-0.054	-0.054	0.000	0.000	0.000	0.000
39	A	66	SER	0	0.073	0.022	17.395	0.031	0.031	0.000	0.000	0.000	0.000
40	A	67	SER	0	0.011	-0.030	20.883	0.005	0.005	0.000	0.000	0.000	0.000
41	A	68	LEU	0	0.016	0.025	24.086	0.006	0.006	0.000	0.000	0.000	0.000
42	A	69	GLN	0	0.013	0.028	16.574	0.004	0.004	0.000	0.000	0.000	0.000
43	A	70	LEU	0	0.041	0.021	20.074	0.006	0.006	0.000	0.000	0.000	0.000
44	A	71	THR	0	0.021	0.009	22.968	0.008	0.008	0.000	0.000	0.000	0.000
45	A	72	LYS	1	0.820	0.904	21.740	0.159	0.159	0.000	0.000	0.000	0.000
46	A	73	TYR	0	-0.010	-0.021	18.000	0.003	0.003	0.000	0.000	0.000	0.000
47	A	74	GLY	0	0.007	0.004	23.512	0.008	0.008	0.000	0.000	0.000	0.000
48	A	75	ILE	0	-0.024	-0.004	22.247	0.008	0.008	0.000	0.000	0.000	0.000
49	A	76	ASP	-1	-0.826	-0.923	26.399	0.003	0.003	0.000	0.000	0.000	0.000
50	A	77	ILE	0	0.044	-0.004	25.632	0.009	0.009	0.000	0.000	0.000	0.000
51	A	78	ASP	-1	-0.876	-0.923	28.259	0.006	0.006	0.000	0.000	0.000	0.000
52	A	79	LYS	1	0.752	0.871	31.458	-0.018	-0.018	0.000	0.000	0.000	0.000
53	A	80	TYR	0	-0.042	-0.025	27.496	0.012	0.012	0.000	0.000	0.000	0.000
54	A	81	PRO	0	0.071	0.039	27.835	0.002	0.002	0.000	0.000	0.000	0.000
55	A	82	ASP	-1	-0.815	-0.901	27.507	0.062	0.062	0.000	0.000	0.000	0.000
56	A	83	LEU	0	-0.007	0.008	22.763	0.007	0.007	0.000	0.000	0.000	0.000
57	A	84	ILE	0	-0.014	-0.010	23.538	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	85	LYS	1	0.783	0.864	25.721	-0.054	-0.054	0.000	0.000	0.000	0.000
59	A	86	SER	0	0.003	0.011	23.878	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	87	GLY	0	-0.007	-0.003	21.615	0.022	0.022	0.000	0.000	0.000	0.000
61	A	88	THR	0	-0.041	-0.009	20.521	-0.025	-0.025	0.000	0.000	0.000	0.000
62	A	89	GLU	-1	-0.814	-0.892	22.541	-0.037	-0.037	0.000	0.000	0.000	0.000
63	A	90	GLN	0	-0.030	-0.014	19.492	0.001	0.001	0.000	0.000	0.000	0.000
64	A	92	VAL	0	0.018	0.019	18.510	0.023	0.023	0.000	0.000	0.000	0.000
65	A	93	ASP	-1	-0.846	-0.928	18.826	0.197	0.197	0.000	0.000	0.000	0.000
66	A	94	LEU	0	-0.051	-0.046	15.786	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	95	LEU	0	-0.031	-0.007	18.086	0.009	0.009	0.000	0.000	0.000	0.000
68	A	96	ALA	0	-0.015	0.012	21.402	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	97	ILE	0	-0.029	-0.004	23.189	-0.019	-0.019	0.000	0.000	0.000	0.000
70	A	98	PRO	0	-0.002	0.004	24.671	0.017	0.017	0.000	0.000	0.000	0.000
71	A	99	HIS	0	-0.028	-0.028	26.003	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	100	SER	0	-0.029	-0.020	22.111	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	101	ASP	-1	-0.904	-0.955	18.843	0.307	0.307	0.000	0.000	0.000	0.000
74	A	102	VAL	0	-0.053	-0.024	13.987	-0.044	-0.044	0.000	0.000	0.000	0.000
75	A	103	GLN	0	0.019	0.007	13.038	0.143	0.143	0.000	0.000	0.000	0.000
76	A	104	PHE	0	0.021	0.016	5.703	-0.093	-0.093	0.000	0.000	0.000	0.000
77	A	105	TYR	0	0.007	0.002	9.588	0.167	0.167	0.000	0.000	0.000	0.000
78	A	106	PHE	0	0.026	0.014	3.426	-0.185	0.169	0.008	-0.090	-0.272	-0.001
79	A	107	ASN	0	0.006	-0.012	8.378	-0.128	-0.128	0.000	0.000	0.000	0.000
80	A	108	GLN	0	-0.013	0.000	10.804	-0.033	-0.033	0.000	0.000	0.000	0.000
81	A	109	GLN	0	-0.014	-0.006	10.278	0.009	0.009	0.000	0.000	0.000	0.000
82	A	110	LYS	1	0.882	0.961	11.758	-0.043	-0.043	0.000	0.000	0.000	0.000
83	A	111	LEU	0	0.026	0.020	12.260	0.068	0.068	0.000	0.000	0.000	0.000
84	A	112	SER	0	-0.029	-0.023	13.810	-0.040	-0.040	0.000	0.000	0.000	0.000
85	A	113	LEU	0	0.001	0.010	16.363	0.047	0.047	0.000	0.000	0.000	0.000
86	A	114	ILE	0	-0.014	-0.017	18.901	-0.026	-0.026	0.000	0.000	0.000	0.000
87	A	115	VAL	0	0.046	0.020	22.055	0.015	0.015	0.000	0.000	0.000	0.000
88	A	116	PRO	0	0.049	0.049	24.952	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	117	PRO	0	0.018	-0.001	28.684	-0.007	-0.007	0.000	0.000	0.000	0.000
90	A	118	GLN	0	0.048	0.016	31.074	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	119	ALA	0	-0.004	0.002	27.321	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	120	LEU	0	-0.051	-0.013	26.820	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	121	LEU	0	0.008	0.013	29.039	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	122	PRO	0	-0.018	-0.010	31.737	0.000	0.000	0.000	0.000	0.000	0.000
95	A	123	ARG	1	0.803	0.900	27.407	0.037	0.037	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:28:LEU)