FMO DATABASE

FMODB ID: YZ3V2

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:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
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	-1058527.436838
FMO2-HF: Nuclear repulsion	1009448.451158
FMO2-HF: Total energy	-49078.98568
FMO2-MP2: Total energy	-49223.011615

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.
5.413	-10.999	28.723	-4.34	-7.972	0.011

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 : 0.015 / q_NPA : -0.010

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	0.844	0.907	2.079	5.465	-11.120	28.725	-4.322	-7.818	0.011
4	A	2	MET	0	0.024	0.020	4.533	0.074	0.163	-0.001	-0.016	-0.073	0.000
5	A	3	LEU	0	0.002	0.013	8.205	0.053	0.053	0.000	0.000	0.000	0.000
6	A	4	ALA	0	0.036	0.018	11.636	0.009	0.009	0.000	0.000	0.000	0.000
7	A	5	CYS	0	-0.054	-0.030	13.490	0.020	0.020	0.000	0.000	0.000	0.000
8	A	6	LEU	0	0.030	0.025	17.252	0.005	0.005	0.000	0.000	0.000	0.000
9	A	7	LEU	0	-0.007	-0.012	19.673	0.003	0.003	0.000	0.000	0.000	0.000
10	A	8	VAL	0	0.013	0.002	23.031	0.006	0.006	0.000	0.000	0.000	0.000
11	A	9	ARG	1	0.965	0.979	25.521	0.042	0.042	0.000	0.000	0.000	0.000
12	A	10	ALA	0	-0.013	0.004	28.767	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	11	SER	0	-0.070	-0.028	31.306	0.003	0.003	0.000	0.000	0.000	0.000
14	A	12	ASN	0	0.027	-0.011	34.564	0.000	0.000	0.000	0.000	0.000	0.000
15	A	13	LEU	0	-0.014	-0.001	33.698	0.000	0.000	0.000	0.000	0.000	0.000
16	A	14	PRO	0	0.049	0.038	37.523	0.002	0.002	0.000	0.000	0.000	0.000
17	A	15	SER	0	0.007	-0.018	40.269	0.000	0.000	0.000	0.000	0.000	0.000
18	A	16	ALA	0	-0.013	-0.012	42.935	0.000	0.000	0.000	0.000	0.000	0.000
19	A	17	LYS	1	0.938	0.964	45.407	0.009	0.009	0.000	0.000	0.000	0.000
20	A	18	LYS	1	0.977	0.967	45.976	0.015	0.015	0.000	0.000	0.000	0.000
21	A	19	ASP	-1	-0.861	-0.893	47.486	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	20	ARG	1	0.770	0.870	44.139	0.010	0.010	0.000	0.000	0.000	0.000
23	A	21	ARG	1	0.811	0.877	40.831	0.006	0.006	0.000	0.000	0.000	0.000
24	A	22	SER	0	0.041	0.028	38.631	0.000	0.000	0.000	0.000	0.000	0.000
25	A	23	ASP	-1	-0.784	-0.878	37.091	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	24	PRO	0	0.020	0.015	33.424	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	25	VAL	0	-0.045	-0.022	29.539	0.001	0.001	0.000	0.000	0.000	0.000
28	A	26	ALA	0	0.048	0.033	26.988	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	27	SER	0	-0.090	-0.058	25.412	0.002	0.002	0.000	0.000	0.000	0.000
30	A	28	LEU	0	0.033	0.014	20.914	0.000	0.000	0.000	0.000	0.000	0.000
31	A	29	THR	0	-0.015	-0.014	21.117	0.001	0.001	0.000	0.000	0.000	0.000
32	A	30	PHE	0	0.060	0.029	13.529	0.001	0.001	0.000	0.000	0.000	0.000
33	A	31	ARG	1	0.897	0.937	12.581	0.189	0.189	0.000	0.000	0.000	0.000
34	A	32	GLY	0	0.032	0.017	18.701	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	33	VAL	0	-0.017	0.004	16.643	0.011	0.011	0.000	0.000	0.000	0.000
36	A	34	LYS	1	0.907	0.948	19.585	0.035	0.035	0.000	0.000	0.000	0.000
37	A	35	LYS	1	0.914	0.973	15.749	0.119	0.119	0.000	0.000	0.000	0.000
38	A	36	ARG	1	0.927	0.955	21.832	0.027	0.027	0.000	0.000	0.000	0.000
39	A	37	THR	0	0.076	0.062	24.394	0.001	0.001	0.000	0.000	0.000	0.000
40	A	38	LYS	1	0.938	0.969	26.039	0.003	0.003	0.000	0.000	0.000	0.000
41	A	39	VAL	0	-0.056	-0.023	28.702	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	40	ILE	0	0.010	0.010	30.605	0.003	0.003	0.000	0.000	0.000	0.000
43	A	41	LYS	1	0.908	0.948	33.960	0.005	0.005	0.000	0.000	0.000	0.000
44	A	42	ASN	0	0.002	-0.005	37.673	0.000	0.000	0.000	0.000	0.000	0.000
45	A	43	SER	0	0.021	0.017	36.131	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	44	VAL	0	0.036	0.015	37.709	0.000	0.000	0.000	0.000	0.000	0.000
47	A	45	ASN	0	-0.019	-0.002	35.362	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	46	PRO	0	-0.019	0.011	31.903	0.001	0.001	0.000	0.000	0.000	0.000
49	A	47	VAL	0	0.047	-0.003	29.410	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	48	TRP	0	-0.011	-0.019	26.475	0.001	0.001	0.000	0.000	0.000	0.000
51	A	49	ASN	0	-0.007	0.006	24.564	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	50	GLU	-1	-0.790	-0.896	22.494	-0.026	-0.026	0.000	0.000	0.000	0.000
53	A	51	GLY	0	0.006	0.012	18.274	-0.008	-0.008	0.000	0.000	0.000	0.000
54	A	52	PHE	0	-0.067	-0.043	17.256	0.012	0.012	0.000	0.000	0.000	0.000
55	A	53	GLU	-1	-0.842	-0.929	11.558	-0.229	-0.229	0.000	0.000	0.000	0.000
56	A	54	TRP	0	-0.121	-0.085	12.581	0.044	0.044	0.000	0.000	0.000	0.000
57	A	55	ASP	-1	-0.797	-0.893	8.060	-0.717	-0.717	0.000	0.000	0.000	0.000
58	A	56	LEU	0	-0.027	-0.022	7.662	0.112	0.112	0.000	0.000	0.000	0.000
59	A	57	LYS	1	0.897	0.950	8.798	0.259	0.259	0.000	0.000	0.000	0.000
60	A	58	GLY	0	0.007	0.012	8.081	0.047	0.047	0.000	0.000	0.000	0.000
61	A	59	ILE	0	-0.009	-0.002	9.010	0.079	0.079	0.000	0.000	0.000	0.000
62	A	60	PRO	0	0.007	0.009	10.191	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	61	LEU	0	-0.004	0.016	11.246	0.002	0.002	0.000	0.000	0.000	0.000
64	A	62	ASP	-1	-0.810	-0.914	13.593	-0.102	-0.102	0.000	0.000	0.000	0.000
65	A	63	GLN	0	0.005	-0.019	16.869	0.004	0.004	0.000	0.000	0.000	0.000
66	A	64	GLY	0	-0.005	-0.002	20.050	0.005	0.005	0.000	0.000	0.000	0.000
67	A	65	SER	0	-0.038	0.000	16.928	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	66	GLU	-1	-0.903	-0.957	19.058	-0.070	-0.070	0.000	0.000	0.000	0.000
69	A	67	LEU	0	0.005	0.006	18.436	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	68	HIS	0	-0.091	-0.029	20.980	0.006	0.006	0.000	0.000	0.000	0.000
71	A	69	VAL	0	0.030	0.005	23.496	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	70	VAL	0	-0.054	-0.024	25.795	0.004	0.004	0.000	0.000	0.000	0.000
73	A	71	VAL	0	0.058	0.020	29.130	0.000	0.000	0.000	0.000	0.000	0.000
74	A	72	LYS	1	0.900	0.938	31.372	0.029	0.029	0.000	0.000	0.000	0.000
75	A	73	ASP	-1	-0.775	-0.876	34.159	-0.015	-0.015	0.000	0.000	0.000	0.000
76	A	74	HIS	0	-0.043	-0.029	34.738	0.002	0.002	0.000	0.000	0.000	0.000
77	A	75	GLU	-1	-0.781	-0.890	36.694	-0.009	-0.009	0.000	0.000	0.000	0.000
78	A	76	THR	0	0.035	-0.015	38.863	0.000	0.000	0.000	0.000	0.000	0.000
79	A	77	MET	0	-0.033	-0.002	39.955	0.001	0.001	0.000	0.000	0.000	0.000
80	A	78	GLY	0	0.035	0.037	39.501	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	79	ARG	1	0.863	0.956	38.135	0.010	0.010	0.000	0.000	0.000	0.000
82	A	80	ASN	0	0.042	0.006	33.451	0.001	0.001	0.000	0.000	0.000	0.000
83	A	81	ARG	1	0.901	0.944	37.230	0.016	0.016	0.000	0.000	0.000	0.000
84	A	82	PHE	0	-0.038	-0.007	33.221	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	83	LEU	0	-0.045	-0.015	35.231	0.002	0.002	0.000	0.000	0.000	0.000
86	A	84	GLY	0	0.058	0.017	34.241	0.001	0.001	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.948	-0.967	29.946	-0.043	-0.043	0.000	0.000	0.000	0.000
88	A	86	ALA	0	0.055	0.020	27.816	0.001	0.001	0.000	0.000	0.000	0.000
89	A	87	LYS	1	0.904	0.962	25.687	0.052	0.052	0.000	0.000	0.000	0.000
90	A	88	VAL	0	-0.005	-0.007	21.839	0.003	0.003	0.000	0.000	0.000	0.000
91	A	89	PRO	0	0.030	0.021	22.079	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	90	LEU	0	0.041	0.000	16.262	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	91	ARG	1	0.919	0.980	18.034	0.068	0.068	0.000	0.000	0.000	0.000
94	A	92	GLU	-1	-0.921	-0.980	19.094	-0.078	-0.078	0.000	0.000	0.000	0.000
95	A	93	VAL	0	-0.043	-0.012	13.937	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	94	LEU	0	-0.047	-0.029	13.576	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	95	ALA	0	-0.021	0.001	15.930	0.004	0.004	0.000	0.000	0.000	0.000
98	A	96	THR	0	0.010	0.016	17.392	0.001	0.001	0.000	0.000	0.000	0.000
99	A	97	PRO	0	0.034	-0.007	14.507	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	98	SER	0	0.007	0.023	13.978	-0.013	-0.013	0.000	0.000	0.000	0.000
101	A	99	LEU	0	-0.048	-0.010	9.137	-0.014	-0.014	0.000	0.000	0.000	0.000
102	A	100	SER	0	-0.034	-0.046	13.161	-0.016	-0.016	0.000	0.000	0.000	0.000
103	A	101	ALA	0	0.035	0.020	15.833	0.009	0.009	0.000	0.000	0.000	0.000
104	A	102	SER	0	0.005	0.013	19.348	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	103	PHE	0	0.021	0.007	20.171	0.004	0.004	0.000	0.000	0.000	0.000
106	A	104	ASN	0	-0.007	-0.016	24.783	0.001	0.001	0.000	0.000	0.000	0.000
107	A	105	ALA	0	0.018	0.012	27.261	0.001	0.001	0.000	0.000	0.000	0.000
108	A	106	PRO	0	0.026	0.022	29.215	0.002	0.002	0.000	0.000	0.000	0.000
109	A	107	LEU	0	-0.041	-0.016	29.978	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	108	LEU	0	-0.018	0.010	33.022	0.003	0.003	0.000	0.000	0.000	0.000
111	A	109	ASP	-1	-0.738	-0.884	34.648	-0.028	-0.028	0.000	0.000	0.000	0.000
112	A	110	THR	0	-0.033	-0.027	35.587	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	111	LYS	1	0.905	0.941	36.826	0.023	0.023	0.000	0.000	0.000	0.000
114	A	112	LYS	1	0.910	0.956	32.669	0.040	0.040	0.000	0.000	0.000	0.000
115	A	113	GLN	0	0.052	0.037	37.038	0.000	0.000	0.000	0.000	0.000	0.000
116	A	114	PRO	0	-0.023	-0.016	37.193	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	115	THR	0	-0.019	-0.026	36.362	0.002	0.002	0.000	0.000	0.000	0.000
118	A	116	GLY	0	0.003	0.012	38.235	0.002	0.002	0.000	0.000	0.000	0.000
119	A	117	ALA	0	-0.022	0.002	35.235	0.000	0.000	0.000	0.000	0.000	0.000
120	A	118	SER	0	-0.034	-0.014	31.924	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	119	LEU	0	-0.020	-0.018	26.011	0.002	0.002	0.000	0.000	0.000	0.000
122	A	120	VAL	0	0.008	0.009	26.012	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	121	LEU	0	-0.028	-0.026	21.169	0.001	0.001	0.000	0.000	0.000	0.000
124	A	122	GLN	0	0.019	0.021	18.997	0.000	0.000	0.000	0.000	0.000	0.000
125	A	123	VAL	0	0.006	0.006	15.624	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	124	SER	0	0.015	0.008	12.851	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	125	TYR	0	0.003	-0.006	8.756	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	126	THR	0	0.089	0.074	4.766	-0.086	-0.002	-0.001	-0.002	-0.081	0.000

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