FMO DATABASE

FMODB ID: G6LJ1

Calculation Name: 4HW0-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4HW0

Chain ID: A

ChEMBL ID:

UniProt ID: Q97V10

Base Structure: X-ray

Registration Date: 2023-06-21

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	97
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-695324.385864
FMO2-HF: Nuclear repulsion	655287.457106
FMO2-HF: Total energy	-40036.928758
FMO2-MP2: Total energy	-40153.070035

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:7:LYS)

Summations of interaction energy for fragment #1(A:7: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.
22.982	25.964	0.076	-1.437	-1.621	-0.004

Interaction energy analysis for fragmet #1(A:7:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.953 / q_NPA : 0.964

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	9	GLY	0	0.057	0.021	3.163	-12.061	-9.128	0.077	-1.436	-1.574	-0.004
4	A	10	THR	0	0.003	-0.022	5.287	1.350	1.399	-0.001	-0.001	-0.047	0.000
5	A	11	MET	0	0.050	0.021	7.990	1.695	1.695	0.000	0.000	0.000	0.000
6	A	12	GLU	-1	-0.748	-0.858	6.675	-30.513	-30.513	0.000	0.000	0.000	0.000
7	A	13	ILE	0	-0.009	0.012	5.035	1.761	1.761	0.000	0.000	0.000	0.000
8	A	14	MET	0	-0.014	-0.011	8.979	2.346	2.346	0.000	0.000	0.000	0.000
9	A	15	PHE	0	0.026	0.025	12.105	1.612	1.612	0.000	0.000	0.000	0.000
10	A	16	ASP	-1	-0.779	-0.866	9.386	-22.015	-22.015	0.000	0.000	0.000	0.000
11	A	17	ILE	0	-0.030	-0.013	12.111	1.175	1.175	0.000	0.000	0.000	0.000
12	A	18	LEU	0	0.014	0.002	14.689	1.188	1.188	0.000	0.000	0.000	0.000
13	A	19	ARG	1	0.824	0.923	12.329	19.425	19.425	0.000	0.000	0.000	0.000
14	A	20	ASN	0	-0.052	-0.034	15.055	1.322	1.322	0.000	0.000	0.000	0.000
15	A	21	CYS	0	-0.196	-0.066	18.647	0.124	0.124	0.000	0.000	0.000	0.000
16	A	22	GLU	-1	-0.758	-0.840	21.178	-11.337	-11.337	0.000	0.000	0.000	0.000
17	A	23	PRO	0	0.022	0.001	23.912	0.101	0.101	0.000	0.000	0.000	0.000
18	A	24	LYS	1	0.872	0.901	25.116	10.074	10.074	0.000	0.000	0.000	0.000
19	A	26	GLY	0	0.084	0.043	22.766	0.147	0.147	0.000	0.000	0.000	0.000
20	A	27	ILE	0	0.036	0.003	17.029	-0.510	-0.510	0.000	0.000	0.000	0.000
21	A	28	THR	0	0.032	0.019	18.584	-0.804	-0.804	0.000	0.000	0.000	0.000
22	A	29	ARG	1	0.910	0.942	18.711	12.264	12.264	0.000	0.000	0.000	0.000
23	A	30	VAL	0	0.018	0.020	15.082	-0.567	-0.567	0.000	0.000	0.000	0.000
24	A	31	ILE	0	-0.032	-0.016	14.370	-0.992	-0.992	0.000	0.000	0.000	0.000
25	A	32	TYR	0	-0.006	-0.013	13.711	-1.153	-1.153	0.000	0.000	0.000	0.000
26	A	33	GLY	0	0.009	0.020	14.622	-0.272	-0.272	0.000	0.000	0.000	0.000
27	A	34	ALA	0	-0.011	-0.015	11.553	-0.421	-0.421	0.000	0.000	0.000	0.000
28	A	35	GLY	0	0.060	0.044	9.977	-2.032	-2.032	0.000	0.000	0.000	0.000
29	A	36	ILE	0	-0.062	-0.026	8.084	-2.883	-2.883	0.000	0.000	0.000	0.000
30	A	37	ASN	0	0.072	0.033	9.289	3.235	3.235	0.000	0.000	0.000	0.000
31	A	38	TYR	0	0.106	0.029	12.139	-0.333	-0.333	0.000	0.000	0.000	0.000
32	A	39	VAL	0	0.022	0.018	11.876	0.575	0.575	0.000	0.000	0.000	0.000
33	A	40	VAL	0	-0.024	-0.020	7.448	0.000	0.000	0.000	0.000	0.000	0.000
34	A	41	ALA	0	0.040	0.017	10.276	0.433	0.433	0.000	0.000	0.000	0.000
35	A	42	GLN	0	0.026	0.010	13.119	1.527	1.527	0.000	0.000	0.000	0.000
36	A	43	LYS	1	0.962	0.989	8.652	30.283	30.283	0.000	0.000	0.000	0.000
37	A	44	TYR	0	-0.016	-0.025	7.331	-0.672	-0.672	0.000	0.000	0.000	0.000
38	A	45	LEU	0	-0.006	-0.001	13.026	0.876	0.876	0.000	0.000	0.000	0.000
39	A	46	ASP	-1	-0.832	-0.893	16.430	-14.515	-14.515	0.000	0.000	0.000	0.000
40	A	47	GLN	0	0.002	-0.003	12.515	-0.503	-0.503	0.000	0.000	0.000	0.000
41	A	48	LEU	0	0.019	0.004	15.085	0.719	0.719	0.000	0.000	0.000	0.000
42	A	49	VAL	0	0.005	0.004	18.009	0.736	0.736	0.000	0.000	0.000	0.000
43	A	50	LYS	1	0.808	0.907	19.672	15.037	15.037	0.000	0.000	0.000	0.000
44	A	51	VAL	0	-0.037	-0.016	18.493	0.539	0.539	0.000	0.000	0.000	0.000
45	A	52	GLY	0	0.044	0.033	21.294	0.301	0.301	0.000	0.000	0.000	0.000
46	A	53	ALA	0	-0.039	-0.004	19.665	0.395	0.395	0.000	0.000	0.000	0.000
47	A	54	LEU	0	-0.001	-0.012	18.503	0.090	0.090	0.000	0.000	0.000	0.000
48	A	55	ASN	0	0.036	0.026	22.570	-0.041	-0.041	0.000	0.000	0.000	0.000
49	A	56	ILE	0	-0.020	-0.016	22.764	-0.311	-0.311	0.000	0.000	0.000	0.000
50	A	57	LYS	1	0.882	0.928	25.589	10.302	10.302	0.000	0.000	0.000	0.000
51	A	58	THR	0	0.005	-0.002	27.321	-0.531	-0.531	0.000	0.000	0.000	0.000
52	A	59	GLU	-1	-0.821	-0.899	29.531	-9.576	-9.576	0.000	0.000	0.000	0.000
53	A	60	ASN	0	-0.070	-0.044	30.646	-0.060	-0.060	0.000	0.000	0.000	0.000
54	A	61	ASP	-1	-0.869	-0.936	31.058	-9.974	-9.974	0.000	0.000	0.000	0.000
55	A	62	ARG	1	0.915	0.970	26.670	9.823	9.823	0.000	0.000	0.000	0.000
56	A	63	LYS	1	0.943	0.971	21.342	13.811	13.811	0.000	0.000	0.000	0.000
57	A	64	ILE	0	-0.058	-0.034	24.651	-0.303	-0.303	0.000	0.000	0.000	0.000
58	A	65	TYR	0	0.019	-0.005	20.044	0.110	0.110	0.000	0.000	0.000	0.000
59	A	66	GLU	-1	-0.793	-0.871	23.733	-10.166	-10.166	0.000	0.000	0.000	0.000
60	A	67	ILE	0	-0.042	0.001	21.115	-0.162	-0.162	0.000	0.000	0.000	0.000
61	A	68	THR	0	-0.010	-0.023	23.981	0.488	0.488	0.000	0.000	0.000	0.000
62	A	69	GLU	-1	-0.840	-0.935	25.261	-10.831	-10.831	0.000	0.000	0.000	0.000
63	A	70	LYS	1	0.867	0.925	22.867	12.748	12.748	0.000	0.000	0.000	0.000
64	A	71	GLY	0	0.058	0.016	21.400	-0.539	-0.539	0.000	0.000	0.000	0.000
65	A	72	LYS	1	0.852	0.922	21.054	10.609	10.609	0.000	0.000	0.000	0.000
66	A	73	LEU	0	0.003	0.016	22.552	-0.336	-0.336	0.000	0.000	0.000	0.000
67	A	74	LEU	0	-0.024	-0.005	17.076	-0.405	-0.405	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.806	0.860	17.686	13.671	13.671	0.000	0.000	0.000	0.000
69	A	76	THR	0	0.008	-0.006	18.120	-0.440	-0.440	0.000	0.000	0.000	0.000
70	A	77	HIS	0	0.025	0.005	19.606	-0.348	-0.348	0.000	0.000	0.000	0.000
71	A	78	ILE	0	-0.060	-0.027	13.103	-0.607	-0.607	0.000	0.000	0.000	0.000
72	A	79	GLU	-1	-0.792	-0.860	14.901	-15.409	-15.409	0.000	0.000	0.000	0.000
73	A	80	GLU	-1	-0.772	-0.868	15.898	-13.705	-13.705	0.000	0.000	0.000	0.000
74	A	81	PHE	0	-0.034	-0.024	10.705	-0.445	-0.445	0.000	0.000	0.000	0.000
75	A	82	ILE	0	-0.011	-0.012	10.560	-0.610	-0.610	0.000	0.000	0.000	0.000
76	A	83	LYS	1	0.867	0.924	12.791	13.050	13.050	0.000	0.000	0.000	0.000
77	A	84	ILE	0	-0.030	-0.019	15.238	0.261	0.261	0.000	0.000	0.000	0.000
78	A	85	ARG	1	0.745	0.852	7.382	27.070	27.070	0.000	0.000	0.000	0.000
79	A	86	GLU	-1	-0.811	-0.911	9.709	-22.915	-22.915	0.000	0.000	0.000	0.000
80	A	87	ASN	0	-0.016	-0.012	13.018	0.576	0.576	0.000	0.000	0.000	0.000
81	A	88	LEU	0	-0.018	0.000	14.758	0.528	0.528	0.000	0.000	0.000	0.000
82	A	89	TYR	0	-0.033	-0.015	7.575	-0.251	-0.251	0.000	0.000	0.000	0.000
83	A	90	SER	0	0.050	0.025	13.913	0.554	0.554	0.000	0.000	0.000	0.000
84	A	91	ALA	0	-0.013	-0.003	16.574	0.621	0.621	0.000	0.000	0.000	0.000
85	A	92	LYS	1	0.935	0.963	14.705	18.168	18.168	0.000	0.000	0.000	0.000
86	A	93	GLU	-1	-0.938	-0.972	13.770	-16.426	-16.426	0.000	0.000	0.000	0.000
87	A	94	LYS	1	0.829	0.901	18.041	12.117	12.117	0.000	0.000	0.000	0.000
88	A	95	VAL	0	0.011	0.007	21.209	0.477	0.477	0.000	0.000	0.000	0.000
89	A	96	SER	0	0.007	0.001	19.383	0.275	0.275	0.000	0.000	0.000	0.000
90	A	97	GLU	-1	-0.868	-0.919	21.473	-11.520	-11.520	0.000	0.000	0.000	0.000
91	A	98	LEU	0	-0.026	-0.015	23.359	0.405	0.405	0.000	0.000	0.000	0.000
92	A	99	LEU	0	-0.103	-0.036	22.876	0.240	0.240	0.000	0.000	0.000	0.000
93	A	100	ARG	1	0.860	0.935	20.006	12.520	12.520	0.000	0.000	0.000	0.000
94	A	101	THR	0	-0.010	-0.036	27.176	0.261	0.261	0.000	0.000	0.000	0.000
95	A	102	ASP	-1	-0.938	-0.964	30.154	-9.172	-9.172	0.000	0.000	0.000	0.000
96	A	103	SER	0	-0.018	-0.002	32.611	0.297	0.297	0.000	0.000	0.000	0.000
97	A	104	GLU	-1	-0.951	-0.950	32.376	-8.664	-8.664	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:LYS)