FMO DATABASE

FMODB ID: 982N2

Calculation Name: 1HX5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1HX5

Chain ID: A

ChEMBL ID:

UniProt ID: P9WPE5

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:

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	93
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-595106.916897
FMO2-HF: Nuclear repulsion	560515.89444
FMO2-HF: Total energy	-34591.022457
FMO2-MP2: Total energy	-34694.346818

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:5:ILE)

Summations of interaction energy for fragment #1(A:5:ILE)

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.
-8.173	-3.213	3.229	-1.889	-6.298	-0.006

Interaction energy analysis for fragmet #1(A:5:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.008 / q_NPA : -0.014

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	7	PRO	0	0.005	0.022	3.869	-1.150	0.691	-0.013	-0.726	-1.102	0.003
4	A	8	LEU	0	0.023	0.001	4.978	0.447	0.498	-0.001	-0.004	-0.045	0.000
5	A	9	GLU	-1	-0.796	-0.888	8.206	-0.061	-0.061	0.000	0.000	0.000	0.000
6	A	10	ASP	-1	-0.817	-0.879	11.373	-0.267	-0.267	0.000	0.000	0.000	0.000
7	A	11	LYS	1	0.800	0.903	7.549	0.254	0.254	0.000	0.000	0.000	0.000
8	A	12	ILE	0	0.022	0.011	7.422	0.055	0.055	0.000	0.000	0.000	0.000
9	A	13	LEU	0	-0.037	-0.016	2.372	-1.535	-0.573	1.675	-0.503	-2.135	-0.005
10	A	14	VAL	0	0.039	0.014	5.700	0.184	0.184	0.000	0.000	0.000	0.000
11	A	15	GLN	0	-0.007	-0.004	7.989	-0.351	-0.351	0.000	0.000	0.000	0.000
12	A	16	ALA	0	0.003	-0.006	8.759	0.196	0.196	0.000	0.000	0.000	0.000
13	A	17	ASN	0	-0.049	-0.037	11.190	0.069	0.069	0.000	0.000	0.000	0.000
14	A	18	GLU	-1	-0.843	-0.911	13.160	-0.465	-0.465	0.000	0.000	0.000	0.000
15	A	19	ALA	0	-0.053	-0.023	15.904	0.029	0.029	0.000	0.000	0.000	0.000
16	A	20	GLU	-1	-0.885	-0.942	19.756	-0.281	-0.281	0.000	0.000	0.000	0.000
17	A	21	THR	0	-0.049	-0.036	22.978	0.023	0.023	0.000	0.000	0.000	0.000
18	A	22	THR	0	-0.109	-0.062	24.157	0.025	0.025	0.000	0.000	0.000	0.000
19	A	23	THR	0	0.023	0.029	20.216	-0.019	-0.019	0.000	0.000	0.000	0.000
20	A	24	ALA	0	0.021	-0.002	19.980	0.024	0.024	0.000	0.000	0.000	0.000
21	A	25	SER	0	-0.059	-0.051	21.837	0.026	0.026	0.000	0.000	0.000	0.000
22	A	26	GLY	0	-0.041	-0.013	23.341	0.021	0.021	0.000	0.000	0.000	0.000
23	A	27	LEU	0	-0.039	-0.009	23.669	0.019	0.019	0.000	0.000	0.000	0.000
24	A	28	VAL	0	0.029	0.001	25.649	-0.008	-0.008	0.000	0.000	0.000	0.000
25	A	29	ILE	0	0.029	0.013	21.405	0.012	0.012	0.000	0.000	0.000	0.000
26	A	30	PRO	0	0.001	0.007	25.032	-0.007	-0.007	0.000	0.000	0.000	0.000
27	A	31	ASP	-1	-0.788	-0.889	22.509	-0.263	-0.263	0.000	0.000	0.000	0.000
28	A	32	THR	0	0.008	-0.018	23.958	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	33	ALA	0	-0.028	0.012	24.671	0.013	0.013	0.000	0.000	0.000	0.000
30	A	34	LYS	1	0.841	0.915	21.572	0.242	0.242	0.000	0.000	0.000	0.000
31	A	35	GLU	-1	-0.812	-0.893	21.687	-0.244	-0.244	0.000	0.000	0.000	0.000
32	A	36	LYS	1	0.819	0.901	18.483	0.243	0.243	0.000	0.000	0.000	0.000
33	A	37	PRO	0	-0.048	-0.007	18.292	-0.040	-0.040	0.000	0.000	0.000	0.000
34	A	38	GLN	0	0.029	0.034	13.946	-0.021	-0.021	0.000	0.000	0.000	0.000
35	A	39	GLU	-1	-0.788	-0.883	17.148	-0.355	-0.355	0.000	0.000	0.000	0.000
36	A	40	GLY	0	0.028	0.024	13.388	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	41	THR	0	-0.010	0.003	11.752	0.098	0.098	0.000	0.000	0.000	0.000
38	A	42	VAL	0	-0.007	0.002	9.931	-0.254	-0.254	0.000	0.000	0.000	0.000
39	A	43	VAL	0	-0.024	-0.018	5.517	0.110	0.110	0.000	0.000	0.000	0.000
40	A	44	ALA	0	-0.009	0.000	4.769	-0.272	-0.171	-0.001	-0.017	-0.082	0.000
41	A	45	VAL	0	0.025	0.011	6.716	-0.081	-0.081	0.000	0.000	0.000	0.000
42	A	46	GLY	0	0.015	0.027	8.620	0.172	0.172	0.000	0.000	0.000	0.000
43	A	47	PRO	0	-0.071	-0.062	9.105	0.022	0.022	0.000	0.000	0.000	0.000
44	A	48	GLY	0	0.062	0.047	12.431	0.010	0.010	0.000	0.000	0.000	0.000
45	A	49	ARG	1	0.842	0.896	14.455	0.093	0.093	0.000	0.000	0.000	0.000
46	A	50	TRP	0	-0.014	0.000	16.806	0.014	0.014	0.000	0.000	0.000	0.000
47	A	51	ASP	-1	-0.815	-0.900	19.576	-0.013	-0.013	0.000	0.000	0.000	0.000
48	A	52	GLU	-1	-0.862	-0.916	22.637	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	53	ASP	-1	-0.939	-0.963	24.609	0.030	0.030	0.000	0.000	0.000	0.000
50	A	54	GLY	0	-0.060	-0.033	23.084	0.010	0.010	0.000	0.000	0.000	0.000
51	A	55	GLU	-1	-0.924	-0.945	23.752	0.055	0.055	0.000	0.000	0.000	0.000
52	A	56	LYS	1	0.765	0.860	22.527	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	57	ARG	1	0.795	0.877	15.196	-0.150	-0.150	0.000	0.000	0.000	0.000
54	A	58	ILE	0	0.007	0.011	19.176	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	59	PRO	0	-0.037	-0.032	17.203	-0.013	-0.013	0.000	0.000	0.000	0.000
56	A	60	LEU	0	0.008	-0.005	12.147	-0.014	-0.014	0.000	0.000	0.000	0.000
57	A	61	ASP	-1	-0.951	-0.965	16.207	-0.176	-0.176	0.000	0.000	0.000	0.000
58	A	62	VAL	0	-0.031	-0.011	13.214	-0.012	-0.012	0.000	0.000	0.000	0.000
59	A	63	ALA	0	-0.036	-0.023	13.621	0.008	0.008	0.000	0.000	0.000	0.000
60	A	64	GLU	-1	-0.933	-0.980	8.483	-0.497	-0.497	0.000	0.000	0.000	0.000
61	A	65	GLY	0	-0.026	-0.014	11.886	0.113	0.113	0.000	0.000	0.000	0.000
62	A	66	ASP	-1	-0.846	-0.911	14.003	-0.336	-0.336	0.000	0.000	0.000	0.000
63	A	67	THR	0	-0.061	-0.020	14.366	-0.105	-0.105	0.000	0.000	0.000	0.000
64	A	68	VAL	0	0.036	0.000	13.217	0.059	0.059	0.000	0.000	0.000	0.000
65	A	69	ILE	0	0.004	0.002	16.461	-0.028	-0.028	0.000	0.000	0.000	0.000
66	A	70	TYR	0	-0.029	-0.036	12.762	-0.031	-0.031	0.000	0.000	0.000	0.000
67	A	71	SER	0	-0.007	0.000	16.621	0.040	0.040	0.000	0.000	0.000	0.000
68	A	72	LYS	1	0.788	0.876	13.318	0.606	0.606	0.000	0.000	0.000	0.000
69	A	73	TYR	0	-0.051	-0.045	14.838	0.000	0.000	0.000	0.000	0.000	0.000
70	A	74	GLY	0	-0.015	-0.004	14.834	-0.024	-0.024	0.000	0.000	0.000	0.000
71	A	75	GLY	0	-0.019	0.005	10.937	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	76	THR	0	-0.061	-0.032	7.524	0.119	0.119	0.000	0.000	0.000	0.000
73	A	77	GLU	-1	-0.828	-0.919	7.310	-1.081	-1.081	0.000	0.000	0.000	0.000
74	A	78	ILE	0	-0.030	-0.022	2.302	-0.699	-0.251	1.257	-0.300	-1.405	-0.003
75	A	79	LYS	1	0.824	0.897	5.295	0.390	0.390	0.000	0.000	0.000	0.000
76	A	80	TYR	0	-0.040	-0.024	3.327	-0.744	0.030	0.053	-0.194	-0.633	-0.001
77	A	81	ASN	0	-0.056	-0.039	5.359	0.070	0.085	-0.001	0.000	-0.013	0.000
78	A	82	GLY	0	-0.016	-0.007	8.151	0.137	0.137	0.000	0.000	0.000	0.000
79	A	83	GLU	-1	-0.806	-0.874	7.661	-0.779	-0.779	0.000	0.000	0.000	0.000
80	A	84	GLU	-1	-0.846	-0.906	8.066	-0.824	-0.824	0.000	0.000	0.000	0.000
81	A	85	TYR	0	-0.039	-0.028	4.601	-0.556	-0.283	0.000	-0.029	-0.244	0.000
82	A	86	LEU	0	0.019	0.010	6.599	0.202	0.202	0.000	0.000	0.000	0.000
83	A	87	ILE	0	-0.025	-0.001	2.865	-0.724	-0.229	0.260	-0.116	-0.639	0.000
84	A	88	LEU	0	0.025	0.015	6.471	0.249	0.249	0.000	0.000	0.000	0.000
85	A	89	SER	0	-0.077	-0.071	9.529	-0.017	-0.017	0.000	0.000	0.000	0.000
86	A	90	ALA	0	0.047	0.010	12.125	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	91	ARG	1	0.791	0.871	14.190	0.238	0.238	0.000	0.000	0.000	0.000
88	A	92	ASP	-1	-0.817	-0.873	13.991	-0.387	-0.387	0.000	0.000	0.000	0.000
89	A	93	VAL	0	-0.001	-0.004	13.666	-0.022	-0.022	0.000	0.000	0.000	0.000
90	A	94	LEU	0	-0.061	-0.039	16.290	0.055	0.055	0.000	0.000	0.000	0.000
91	A	95	ALA	0	-0.027	-0.015	19.290	0.037	0.037	0.000	0.000	0.000	0.000
92	A	96	VAL	0	0.049	0.034	17.688	-0.046	-0.046	0.000	0.000	0.000	0.000
93	A	97	VAL	0	-0.053	-0.011	20.153	0.032	0.032	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ILE)