FMO DATABASE

FMODB ID: 858RY

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	OptAll
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	-696058.151229
FMO2-HF: Nuclear repulsion	656020.976086
FMO2-HF: Total energy	-40037.175142
FMO2-MP2: Total energy	-40153.313216

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.
17.262	21.148	0.416	-2.04	-2.259	-0.012

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 : 0.943 / q_NPA : 0.963

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	0.036	0.020	2.878	-18.588	-14.844	0.418	-2.036	-2.125	-0.012
4	A	10	THR	0	-0.011	-0.022	5.020	2.745	2.802	-0.001	-0.001	-0.054	0.000
5	A	11	MET	0	0.059	0.025	7.612	1.835	1.835	0.000	0.000	0.000	0.000
6	A	12	GLU	-1	-0.751	-0.854	6.483	-33.459	-33.459	0.000	0.000	0.000	0.000
7	A	13	ILE	0	0.005	0.005	4.762	1.922	2.007	-0.001	-0.003	-0.080	0.000
8	A	14	MET	0	-0.022	-0.015	8.912	2.456	2.456	0.000	0.000	0.000	0.000
9	A	15	PHE	0	0.034	0.027	12.066	1.637	1.637	0.000	0.000	0.000	0.000
10	A	16	ASP	-1	-0.766	-0.853	9.392	-22.591	-22.591	0.000	0.000	0.000	0.000
11	A	17	ILE	0	-0.043	-0.024	11.888	1.341	1.341	0.000	0.000	0.000	0.000
12	A	18	LEU	0	-0.009	-0.008	14.624	1.207	1.207	0.000	0.000	0.000	0.000
13	A	19	ARG	1	0.837	0.911	12.199	19.721	19.721	0.000	0.000	0.000	0.000
14	A	20	ASN	0	-0.069	-0.033	14.977	1.418	1.418	0.000	0.000	0.000	0.000
15	A	21	CYS	0	-0.139	-0.048	18.606	0.112	0.112	0.000	0.000	0.000	0.000
16	A	22	GLU	-1	-0.751	-0.830	20.954	-11.410	-11.410	0.000	0.000	0.000	0.000
17	A	23	PRO	0	0.005	0.004	23.733	0.042	0.042	0.000	0.000	0.000	0.000
18	A	24	LYS	1	0.852	0.886	25.154	10.383	10.383	0.000	0.000	0.000	0.000
19	A	26	GLY	0	0.092	0.049	22.798	0.192	0.192	0.000	0.000	0.000	0.000
20	A	27	ILE	0	0.011	-0.006	17.122	-0.452	-0.452	0.000	0.000	0.000	0.000
21	A	28	THR	0	0.032	0.010	18.527	-0.847	-0.847	0.000	0.000	0.000	0.000
22	A	29	ARG	1	0.862	0.915	18.962	12.487	12.487	0.000	0.000	0.000	0.000
23	A	30	VAL	0	0.015	0.013	14.848	-0.471	-0.471	0.000	0.000	0.000	0.000
24	A	31	ILE	0	-0.026	-0.011	14.466	-0.952	-0.952	0.000	0.000	0.000	0.000
25	A	32	TYR	0	0.012	0.003	13.768	-1.254	-1.254	0.000	0.000	0.000	0.000
26	A	33	GLY	0	0.039	0.039	14.467	-0.373	-0.373	0.000	0.000	0.000	0.000
27	A	34	ALA	0	0.001	0.000	11.873	-0.262	-0.262	0.000	0.000	0.000	0.000
28	A	35	GLY	0	0.056	0.040	10.169	-2.270	-2.270	0.000	0.000	0.000	0.000
29	A	36	ILE	0	-0.065	-0.032	8.187	-3.023	-3.023	0.000	0.000	0.000	0.000
30	A	37	ASN	0	0.074	0.031	9.531	3.165	3.165	0.000	0.000	0.000	0.000
31	A	38	TYR	0	0.094	0.028	12.318	-0.459	-0.459	0.000	0.000	0.000	0.000
32	A	39	VAL	0	0.031	0.020	12.296	0.520	0.520	0.000	0.000	0.000	0.000
33	A	40	VAL	0	-0.010	-0.006	7.665	-0.145	-0.145	0.000	0.000	0.000	0.000
34	A	41	ALA	0	0.034	0.009	10.451	0.182	0.182	0.000	0.000	0.000	0.000
35	A	42	GLN	0	0.030	0.018	13.225	1.359	1.359	0.000	0.000	0.000	0.000
36	A	43	LYS	1	0.932	0.979	8.404	31.637	31.637	0.000	0.000	0.000	0.000
37	A	44	TYR	0	-0.004	-0.022	7.241	-0.670	-0.670	0.000	0.000	0.000	0.000
38	A	45	LEU	0	0.005	0.009	12.694	0.800	0.800	0.000	0.000	0.000	0.000
39	A	46	ASP	-1	-0.836	-0.892	16.272	-14.765	-14.765	0.000	0.000	0.000	0.000
40	A	47	GLN	0	0.003	-0.010	12.108	-0.922	-0.922	0.000	0.000	0.000	0.000
41	A	48	LEU	0	0.022	0.002	14.859	0.625	0.625	0.000	0.000	0.000	0.000
42	A	49	VAL	0	0.004	0.011	17.573	0.761	0.761	0.000	0.000	0.000	0.000
43	A	50	LYS	1	0.798	0.890	19.160	15.297	15.297	0.000	0.000	0.000	0.000
44	A	51	VAL	0	-0.011	0.003	17.739	0.490	0.490	0.000	0.000	0.000	0.000
45	A	52	GLY	0	0.032	0.022	20.734	0.444	0.444	0.000	0.000	0.000	0.000
46	A	53	ALA	0	-0.029	0.005	19.310	0.408	0.408	0.000	0.000	0.000	0.000
47	A	54	LEU	0	-0.015	-0.013	18.379	0.102	0.102	0.000	0.000	0.000	0.000
48	A	55	ASN	0	0.041	0.021	22.280	-0.020	-0.020	0.000	0.000	0.000	0.000
49	A	56	ILE	0	-0.031	-0.030	22.387	-0.451	-0.451	0.000	0.000	0.000	0.000
50	A	57	LYS	1	0.868	0.921	25.307	10.407	10.407	0.000	0.000	0.000	0.000
51	A	58	THR	0	0.018	0.006	26.893	-0.566	-0.566	0.000	0.000	0.000	0.000
52	A	59	GLU	-1	-0.834	-0.905	29.265	-9.752	-9.752	0.000	0.000	0.000	0.000
53	A	60	ASN	0	-0.052	-0.038	30.529	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	61	ASP	-1	-0.863	-0.928	31.024	-9.923	-9.923	0.000	0.000	0.000	0.000
55	A	62	ARG	1	0.914	0.961	26.438	9.967	9.967	0.000	0.000	0.000	0.000
56	A	63	LYS	1	0.914	0.957	21.062	13.996	13.996	0.000	0.000	0.000	0.000
57	A	64	ILE	0	-0.044	-0.025	24.202	-0.376	-0.376	0.000	0.000	0.000	0.000
58	A	65	TYR	0	0.021	-0.005	19.663	0.086	0.086	0.000	0.000	0.000	0.000
59	A	66	GLU	-1	-0.787	-0.875	23.810	-10.171	-10.171	0.000	0.000	0.000	0.000
60	A	67	ILE	0	-0.052	0.003	21.023	-0.175	-0.175	0.000	0.000	0.000	0.000
61	A	68	THR	0	-0.001	-0.016	23.980	0.448	0.448	0.000	0.000	0.000	0.000
62	A	69	GLU	-1	-0.842	-0.934	24.994	-11.090	-11.090	0.000	0.000	0.000	0.000
63	A	70	LYS	1	0.871	0.934	22.293	12.970	12.970	0.000	0.000	0.000	0.000
64	A	71	GLY	0	0.064	0.020	20.968	-0.623	-0.623	0.000	0.000	0.000	0.000
65	A	72	LYS	1	0.843	0.910	20.868	10.769	10.769	0.000	0.000	0.000	0.000
66	A	73	LEU	0	0.005	0.016	22.522	-0.334	-0.334	0.000	0.000	0.000	0.000
67	A	74	LEU	0	-0.012	-0.004	16.756	-0.424	-0.424	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.803	0.861	17.386	13.786	13.786	0.000	0.000	0.000	0.000
69	A	76	THR	0	0.015	-0.007	17.828	-0.635	-0.635	0.000	0.000	0.000	0.000
70	A	77	HIS	0	0.019	0.007	19.327	-0.277	-0.277	0.000	0.000	0.000	0.000
71	A	78	ILE	0	-0.049	-0.026	13.023	-0.630	-0.630	0.000	0.000	0.000	0.000
72	A	79	GLU	-1	-0.811	-0.868	14.837	-15.743	-15.743	0.000	0.000	0.000	0.000
73	A	80	GLU	-1	-0.772	-0.869	15.968	-13.875	-13.875	0.000	0.000	0.000	0.000
74	A	81	PHE	0	-0.008	-0.006	10.782	-0.434	-0.434	0.000	0.000	0.000	0.000
75	A	82	ILE	0	-0.014	-0.007	10.492	-0.701	-0.701	0.000	0.000	0.000	0.000
76	A	83	LYS	1	0.855	0.916	12.760	13.329	13.329	0.000	0.000	0.000	0.000
77	A	84	ILE	0	-0.020	-0.003	15.406	0.352	0.352	0.000	0.000	0.000	0.000
78	A	85	ARG	1	0.759	0.853	6.965	28.342	28.342	0.000	0.000	0.000	0.000
79	A	86	GLU	-1	-0.775	-0.887	9.833	-23.274	-23.274	0.000	0.000	0.000	0.000
80	A	87	ASN	0	-0.046	-0.023	12.801	1.114	1.114	0.000	0.000	0.000	0.000
81	A	88	LEU	0	-0.005	0.005	14.491	0.560	0.560	0.000	0.000	0.000	0.000
82	A	89	TYR	0	-0.045	-0.027	7.200	-0.393	-0.393	0.000	0.000	0.000	0.000
83	A	90	SER	0	0.046	0.013	13.581	0.680	0.680	0.000	0.000	0.000	0.000
84	A	91	ALA	0	-0.024	-0.008	16.404	0.674	0.674	0.000	0.000	0.000	0.000
85	A	92	LYS	1	0.944	0.970	14.174	18.797	18.797	0.000	0.000	0.000	0.000
86	A	93	GLU	-1	-0.953	-0.978	13.402	-16.875	-16.875	0.000	0.000	0.000	0.000
87	A	94	LYS	1	0.823	0.886	17.648	12.298	12.298	0.000	0.000	0.000	0.000
88	A	95	VAL	0	0.002	0.003	20.828	0.509	0.509	0.000	0.000	0.000	0.000
89	A	96	SER	0	0.000	-0.001	19.044	0.301	0.301	0.000	0.000	0.000	0.000
90	A	97	GLU	-1	-0.867	-0.911	21.118	-11.483	-11.483	0.000	0.000	0.000	0.000
91	A	98	LEU	0	0.013	0.004	23.301	0.363	0.363	0.000	0.000	0.000	0.000
92	A	99	LEU	0	-0.081	-0.020	22.487	0.254	0.254	0.000	0.000	0.000	0.000
93	A	100	ARG	1	0.843	0.905	19.660	12.452	12.452	0.000	0.000	0.000	0.000
94	A	101	THR	0	-0.035	-0.050	26.869	0.294	0.294	0.000	0.000	0.000	0.000
95	A	102	ASP	-1	-0.918	-0.958	29.630	-9.122	-9.122	0.000	0.000	0.000	0.000
96	A	103	SER	0	-0.028	-0.006	32.176	0.267	0.267	0.000	0.000	0.000	0.000
97	A	104	GLU	-1	-0.953	-0.931	31.882	-8.776	-8.776	0.000	0.000	0.000	0.000

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