FMO DATABASE

FMODB ID: V5MQ1

Calculation Name: 4IQH-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4IQH

Chain ID: A

ChEMBL ID:

UniProt ID: O75923

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:

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	128
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1058661.403839
FMO2-HF: Nuclear repulsion	1009581.575305
FMO2-HF: Total energy	-49079.828534
FMO2-MP2: Total energy	-49223.963533

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:-1:ILE)

Summations of interaction energy for fragment #1(A:-1: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.
-2.452	0.78	3.843	-2.603	-4.472	0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.037 / q_NPA : 0.020

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	1	HIS	1	0.862	0.919	2.671	-2.571	0.594	3.844	-2.595	-4.414	0.009
4	A	2	MET	0	0.004	0.005	4.771	-0.107	-0.040	-0.001	-0.008	-0.058	0.000
5	A	3	LEU	0	-0.001	0.013	8.412	0.116	0.116	0.000	0.000	0.000	0.000
6	A	4	ALA	0	0.038	0.018	11.799	-0.023	-0.023	0.000	0.000	0.000	0.000
7	A	5	CYS	0	-0.047	-0.026	13.632	0.038	0.038	0.000	0.000	0.000	0.000
8	A	6	LEU	0	0.039	0.027	17.378	-0.005	-0.005	0.000	0.000	0.000	0.000
9	A	7	LEU	0	0.000	-0.012	19.753	0.009	0.009	0.000	0.000	0.000	0.000
10	A	8	VAL	0	0.019	0.007	23.143	0.005	0.005	0.000	0.000	0.000	0.000
11	A	9	ARG	1	0.952	0.971	25.584	0.057	0.057	0.000	0.000	0.000	0.000
12	A	10	ALA	0	-0.016	0.003	28.860	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	11	SER	0	-0.021	-0.016	31.415	0.005	0.005	0.000	0.000	0.000	0.000
14	A	12	ASN	0	-0.054	-0.043	34.650	0.000	0.000	0.000	0.000	0.000	0.000
15	A	13	LEU	0	-0.005	0.010	33.794	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	14	PRO	0	0.058	0.039	37.749	0.003	0.003	0.000	0.000	0.000	0.000
17	A	15	SER	0	0.017	-0.012	40.442	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	16	ALA	0	-0.021	-0.017	43.108	0.002	0.002	0.000	0.000	0.000	0.000
19	A	17	LYS	1	0.854	0.895	45.603	0.040	0.040	0.000	0.000	0.000	0.000
20	A	18	LYS	1	0.970	0.968	46.050	0.039	0.039	0.000	0.000	0.000	0.000
21	A	19	ASP	-1	-0.804	-0.843	47.662	-0.036	-0.036	0.000	0.000	0.000	0.000
22	A	20	ARG	1	0.786	0.871	44.274	0.049	0.049	0.000	0.000	0.000	0.000
23	A	21	ARG	1	0.828	0.884	40.820	0.049	0.049	0.000	0.000	0.000	0.000
24	A	22	SER	0	0.013	0.013	38.860	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	23	ASP	-1	-0.746	-0.858	37.194	-0.055	-0.055	0.000	0.000	0.000	0.000
26	A	24	PRO	0	0.026	0.021	33.630	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	25	VAL	0	-0.039	-0.021	29.781	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	26	ALA	0	0.040	0.029	27.259	0.001	0.001	0.000	0.000	0.000	0.000
29	A	27	SER	0	-0.070	-0.043	25.664	-0.008	-0.008	0.000	0.000	0.000	0.000
30	A	28	LEU	0	0.026	0.013	21.044	0.008	0.008	0.000	0.000	0.000	0.000
31	A	29	THR	0	-0.032	-0.026	21.405	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	30	PHE	0	0.086	0.039	13.742	0.012	0.012	0.000	0.000	0.000	0.000
33	A	31	ARG	1	0.873	0.928	13.189	0.341	0.341	0.000	0.000	0.000	0.000
34	A	32	GLY	0	0.032	0.015	19.039	-0.016	-0.016	0.000	0.000	0.000	0.000
35	A	33	VAL	0	-0.023	0.002	16.942	0.006	0.006	0.000	0.000	0.000	0.000
36	A	34	LYS	1	0.936	0.966	19.938	0.157	0.157	0.000	0.000	0.000	0.000
37	A	35	LYS	1	0.889	0.964	15.943	0.382	0.382	0.000	0.000	0.000	0.000
38	A	36	ARG	1	0.912	0.943	22.109	0.153	0.153	0.000	0.000	0.000	0.000
39	A	37	THR	0	0.055	0.055	24.445	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	38	LYS	1	0.923	0.961	26.190	0.100	0.100	0.000	0.000	0.000	0.000
41	A	39	VAL	0	-0.054	-0.029	28.689	0.000	0.000	0.000	0.000	0.000	0.000
42	A	40	ILE	0	0.012	0.016	30.535	0.004	0.004	0.000	0.000	0.000	0.000
43	A	41	LYS	1	0.844	0.903	33.987	0.061	0.061	0.000	0.000	0.000	0.000
44	A	42	ASN	0	0.012	-0.002	37.669	0.002	0.002	0.000	0.000	0.000	0.000
45	A	43	SER	0	0.029	0.018	36.655	0.002	0.002	0.000	0.000	0.000	0.000
46	A	44	VAL	0	0.032	0.017	37.855	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	45	ASN	0	-0.010	0.003	35.459	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	46	PRO	0	-0.008	0.019	32.099	0.003	0.003	0.000	0.000	0.000	0.000
49	A	47	VAL	0	0.048	-0.002	29.375	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	48	TRP	0	-0.009	-0.020	26.555	0.002	0.002	0.000	0.000	0.000	0.000
51	A	49	ASN	0	-0.006	0.003	24.625	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	50	GLU	-1	-0.778	-0.890	22.483	-0.119	-0.119	0.000	0.000	0.000	0.000
53	A	51	GLY	0	0.016	0.016	18.328	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	52	PHE	0	-0.064	-0.038	17.427	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	53	GLU	-1	-0.832	-0.925	11.438	-0.432	-0.432	0.000	0.000	0.000	0.000
56	A	54	TRP	0	-0.111	-0.083	12.817	0.013	0.013	0.000	0.000	0.000	0.000
57	A	55	ASP	-1	-0.803	-0.906	8.372	-1.446	-1.446	0.000	0.000	0.000	0.000
58	A	56	LEU	0	-0.026	-0.022	7.849	0.153	0.153	0.000	0.000	0.000	0.000
59	A	57	LYS	1	0.913	0.971	9.198	0.692	0.692	0.000	0.000	0.000	0.000
60	A	58	GLY	0	0.003	0.008	8.441	0.072	0.072	0.000	0.000	0.000	0.000
61	A	59	ILE	0	-0.016	-0.005	9.383	0.144	0.144	0.000	0.000	0.000	0.000
62	A	60	PRO	0	0.013	0.011	10.126	-0.014	-0.014	0.000	0.000	0.000	0.000
63	A	61	LEU	0	0.000	0.020	11.464	0.011	0.011	0.000	0.000	0.000	0.000
64	A	62	ASP	-1	-0.767	-0.874	13.768	-0.180	-0.180	0.000	0.000	0.000	0.000
65	A	63	GLN	0	0.024	-0.010	16.927	0.006	0.006	0.000	0.000	0.000	0.000
66	A	64	GLY	0	-0.004	-0.001	20.081	0.012	0.012	0.000	0.000	0.000	0.000
67	A	65	SER	0	-0.062	-0.027	17.139	-0.017	-0.017	0.000	0.000	0.000	0.000
68	A	66	GLU	-1	-0.906	-0.963	19.257	-0.129	-0.129	0.000	0.000	0.000	0.000
69	A	67	LEU	0	-0.005	0.002	18.655	-0.021	-0.021	0.000	0.000	0.000	0.000
70	A	68	HIS	0	-0.071	-0.020	21.190	0.011	0.011	0.000	0.000	0.000	0.000
71	A	69	VAL	0	0.031	0.004	23.607	-0.010	-0.010	0.000	0.000	0.000	0.000
72	A	70	VAL	0	-0.065	-0.030	26.006	0.011	0.011	0.000	0.000	0.000	0.000
73	A	71	VAL	0	0.061	0.024	29.357	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	72	LYS	1	0.884	0.934	31.578	0.095	0.095	0.000	0.000	0.000	0.000
75	A	73	ASP	-1	-0.747	-0.844	34.387	-0.060	-0.060	0.000	0.000	0.000	0.000
76	A	74	HIS	0	-0.061	-0.051	35.103	0.001	0.001	0.000	0.000	0.000	0.000
77	A	75	GLU	-1	-0.780	-0.868	36.933	-0.051	-0.051	0.000	0.000	0.000	0.000
78	A	76	THR	0	-0.004	0.000	38.631	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	77	MET	0	0.056	0.018	39.924	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	78	GLY	0	0.063	0.048	39.741	0.002	0.002	0.000	0.000	0.000	0.000
81	A	79	ARG	1	0.793	0.906	38.430	0.057	0.057	0.000	0.000	0.000	0.000
82	A	80	ASN	0	0.067	0.034	33.766	0.006	0.006	0.000	0.000	0.000	0.000
83	A	81	ARG	1	0.882	0.912	37.505	0.057	0.057	0.000	0.000	0.000	0.000
84	A	82	PHE	0	-0.048	-0.012	33.518	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	83	LEU	0	-0.032	-0.007	35.494	0.004	0.004	0.000	0.000	0.000	0.000
86	A	84	GLY	0	0.058	0.020	34.447	0.004	0.004	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.877	-0.922	30.222	-0.109	-0.109	0.000	0.000	0.000	0.000
88	A	86	ALA	0	0.053	0.021	27.983	0.007	0.007	0.000	0.000	0.000	0.000
89	A	87	LYS	1	0.874	0.956	25.881	0.110	0.110	0.000	0.000	0.000	0.000
90	A	88	VAL	0	-0.011	-0.014	22.078	0.009	0.009	0.000	0.000	0.000	0.000
91	A	89	PRO	0	0.033	0.024	22.231	-0.015	-0.015	0.000	0.000	0.000	0.000
92	A	90	LEU	0	0.032	-0.002	16.527	0.002	0.002	0.000	0.000	0.000	0.000
93	A	91	ARG	1	0.901	0.957	18.100	0.096	0.096	0.000	0.000	0.000	0.000
94	A	92	GLU	-1	-0.903	-0.968	19.093	-0.078	-0.078	0.000	0.000	0.000	0.000
95	A	93	VAL	0	-0.049	-0.016	13.905	0.007	0.007	0.000	0.000	0.000	0.000
96	A	94	LEU	0	-0.058	-0.037	13.456	0.001	0.001	0.000	0.000	0.000	0.000
97	A	95	ALA	0	-0.022	0.003	15.873	0.013	0.013	0.000	0.000	0.000	0.000
98	A	96	THR	0	0.007	0.007	17.273	0.016	0.016	0.000	0.000	0.000	0.000
99	A	97	PRO	0	0.050	0.007	14.266	-0.010	-0.010	0.000	0.000	0.000	0.000
100	A	98	SER	0	0.012	0.027	13.717	0.006	0.006	0.000	0.000	0.000	0.000
101	A	99	LEU	0	-0.038	-0.002	9.011	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	100	SER	0	-0.029	-0.051	13.090	-0.032	-0.032	0.000	0.000	0.000	0.000
103	A	101	ALA	0	0.008	0.012	15.756	0.012	0.012	0.000	0.000	0.000	0.000
104	A	102	SER	0	0.015	0.017	19.303	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	103	PHE	0	0.010	0.000	20.016	0.002	0.002	0.000	0.000	0.000	0.000
106	A	104	ASN	0	0.009	-0.008	24.807	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	105	ALA	0	0.014	0.013	27.307	0.003	0.003	0.000	0.000	0.000	0.000
108	A	106	PRO	0	0.031	0.022	29.298	0.000	0.000	0.000	0.000	0.000	0.000
109	A	107	LEU	0	-0.032	-0.009	30.101	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	108	LEU	0	-0.006	0.015	33.179	0.006	0.006	0.000	0.000	0.000	0.000
111	A	109	ASP	-1	-0.732	-0.887	34.846	-0.067	-0.067	0.000	0.000	0.000	0.000
112	A	110	THR	0	-0.043	-0.041	35.804	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	111	LYS	1	0.934	0.958	37.068	0.054	0.054	0.000	0.000	0.000	0.000
114	A	112	LYS	1	0.807	0.909	33.556	0.085	0.085	0.000	0.000	0.000	0.000
115	A	113	GLN	0	0.044	0.029	37.233	0.002	0.002	0.000	0.000	0.000	0.000
116	A	114	PRO	0	-0.002	-0.009	37.357	-0.003	-0.003	0.000	0.000	0.000	0.000
117	A	115	THR	0	-0.034	-0.033	36.525	0.003	0.003	0.000	0.000	0.000	0.000
118	A	116	GLY	0	0.011	0.015	38.371	0.002	0.002	0.000	0.000	0.000	0.000
119	A	117	ALA	0	-0.021	0.009	35.354	0.002	0.002	0.000	0.000	0.000	0.000
120	A	118	SER	0	-0.050	-0.024	32.154	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	119	LEU	0	-0.008	-0.012	26.134	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	120	VAL	0	0.008	0.008	26.115	0.000	0.000	0.000	0.000	0.000	0.000
123	A	121	LEU	0	-0.024	-0.023	21.361	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	122	GLN	0	0.010	0.016	19.014	0.008	0.008	0.000	0.000	0.000	0.000
125	A	123	VAL	0	-0.006	0.002	15.668	-0.016	-0.016	0.000	0.000	0.000	0.000
126	A	124	SER	0	0.030	0.013	12.762	0.014	0.014	0.000	0.000	0.000	0.000
127	A	125	TYR	0	0.004	-0.001	9.155	-0.045	-0.045	0.000	0.000	0.000	0.000
128	A	126	THR	0	0.087	0.067	4.859	-0.136	-0.136	0.000	0.000	0.000	0.000

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