FMO DATABASE

FMODB ID: R9Z68

Calculation Name: 5EQZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5EQZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q9S0B8

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	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	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1123194.303241
FMO2-HF: Nuclear repulsion	1069490.659227
FMO2-HF: Total energy	-53703.644014
FMO2-MP2: Total energy	-53862.548754

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:20:HIS)

Summations of interaction energy for fragment #1(A:20:HIS)

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.
-11.658	-8.44	9.93	-4.731	-8.417	-0.022

Interaction energy analysis for fragmet #1(A:20:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.031 / q_NPA : -0.037

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	22	HIS	0	0.033	0.015	2.020	-8.665	-7.471	9.685	-4.083	-6.796	-0.028
4	A	23	TYR	0	0.025	0.007	4.908	0.290	0.645	-0.001	-0.024	-0.330	0.000
5	A	24	VAL	0	-0.001	-0.002	7.505	-0.031	-0.031	0.000	0.000	0.000	0.000
6	A	25	GLU	-1	-0.831	-0.928	9.216	-0.449	-0.449	0.000	0.000	0.000	0.000
7	A	26	GLU	-1	-0.801	-0.902	10.699	0.007	0.007	0.000	0.000	0.000	0.000
8	A	27	LYS	1	0.833	0.914	3.944	0.427	0.537	-0.001	-0.011	-0.099	0.000
9	A	28	LYS	1	0.889	0.956	10.804	0.673	0.673	0.000	0.000	0.000	0.000
10	A	29	GLU	-1	-0.927	-0.956	13.754	0.045	0.045	0.000	0.000	0.000	0.000
11	A	30	ILE	0	-0.036	-0.023	11.889	0.032	0.032	0.000	0.000	0.000	0.000
12	A	31	ASP	-1	-0.861	-0.930	13.108	-0.244	-0.244	0.000	0.000	0.000	0.000
13	A	32	SER	0	-0.026	-0.009	15.715	0.012	0.012	0.000	0.000	0.000	0.000
14	A	33	LEU	0	0.038	0.022	18.682	0.014	0.014	0.000	0.000	0.000	0.000
15	A	34	MET	0	-0.032	-0.013	17.398	0.021	0.021	0.000	0.000	0.000	0.000
16	A	35	GLU	-1	-0.933	-0.973	19.052	-0.105	-0.105	0.000	0.000	0.000	0.000
17	A	36	ASP	-1	-0.950	-0.963	21.520	-0.041	-0.041	0.000	0.000	0.000	0.000
18	A	37	VAL	0	-0.065	-0.043	22.489	0.010	0.010	0.000	0.000	0.000	0.000
19	A	38	LEU	0	-0.018	-0.020	20.590	0.010	0.010	0.000	0.000	0.000	0.000
20	A	39	ALA	0	-0.026	0.000	24.663	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	40	LEU	0	-0.096	-0.028	26.995	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	41	VAL	0	0.015	-0.006	29.609	0.002	0.002	0.000	0.000	0.000	0.000
23	A	42	ASN	0	0.056	0.005	32.829	0.006	0.006	0.000	0.000	0.000	0.000
24	A	43	ASP	-1	-0.912	-0.943	35.871	0.004	0.004	0.000	0.000	0.000	0.000
25	A	44	SER	0	-0.036	-0.003	33.037	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	45	SER	0	0.021	0.000	35.077	0.007	0.007	0.000	0.000	0.000	0.000
27	A	46	GLY	0	0.105	0.034	34.558	0.003	0.003	0.000	0.000	0.000	0.000
28	A	47	GLY	0	-0.009	-0.011	34.157	0.006	0.006	0.000	0.000	0.000	0.000
29	A	48	LYS	1	0.983	0.995	30.590	0.009	0.009	0.000	0.000	0.000	0.000
30	A	49	PHE	0	0.034	0.020	29.826	0.002	0.002	0.000	0.000	0.000	0.000
31	A	50	LYS	1	0.859	0.913	29.354	-0.053	-0.053	0.000	0.000	0.000	0.000
32	A	51	ASP	-1	-0.851	-0.924	28.812	0.029	0.029	0.000	0.000	0.000	0.000
33	A	52	TYR	0	0.038	0.008	25.276	0.004	0.004	0.000	0.000	0.000	0.000
34	A	53	LYS	1	0.935	0.985	24.812	-0.082	-0.082	0.000	0.000	0.000	0.000
35	A	54	ASP	-1	-0.861	-0.927	25.577	0.100	0.100	0.000	0.000	0.000	0.000
36	A	55	LYS	1	0.928	0.967	22.911	0.005	0.005	0.000	0.000	0.000	0.000
37	A	56	ILE	0	-0.020	-0.004	20.521	0.018	0.018	0.000	0.000	0.000	0.000
38	A	57	ASN	0	-0.061	-0.039	20.938	0.052	0.052	0.000	0.000	0.000	0.000
39	A	58	GLU	-1	-0.941	-0.962	21.893	0.100	0.100	0.000	0.000	0.000	0.000
40	A	59	LEU	0	0.030	0.012	16.283	0.026	0.026	0.000	0.000	0.000	0.000
41	A	60	LYS	1	0.857	0.918	17.667	-0.294	-0.294	0.000	0.000	0.000	0.000
42	A	61	GLU	-1	-0.898	-0.953	18.330	0.312	0.312	0.000	0.000	0.000	0.000
43	A	62	ASN	0	-0.003	-0.016	18.415	0.032	0.032	0.000	0.000	0.000	0.000
44	A	63	LEU	0	-0.038	-0.021	13.018	0.031	0.031	0.000	0.000	0.000	0.000
45	A	64	LYS	1	0.859	0.953	13.837	-0.147	-0.147	0.000	0.000	0.000	0.000
46	A	65	ASP	-1	-0.912	-0.951	14.527	0.545	0.545	0.000	0.000	0.000	0.000
47	A	66	ILE	0	-0.045	-0.007	8.522	0.185	0.185	0.000	0.000	0.000	0.000
48	A	67	GLY	0	-0.008	-0.015	9.219	0.006	0.006	0.000	0.000	0.000	0.000
49	A	68	ASN	0	-0.001	-0.010	3.060	-4.320	-3.040	0.247	-0.560	-0.966	0.006
50	A	69	ALA	0	0.035	0.010	6.008	-1.229	-1.229	0.000	0.000	0.000	0.000
51	A	70	GLU	-1	-0.862	-0.937	4.173	3.901	4.180	0.000	-0.053	-0.226	0.000
52	A	71	LEU	0	-0.009	-0.004	7.006	-0.591	-0.591	0.000	0.000	0.000	0.000
53	A	72	LYS	1	0.922	0.969	8.839	-2.307	-2.307	0.000	0.000	0.000	0.000
54	A	73	GLU	-1	-0.931	-0.952	10.558	0.471	0.471	0.000	0.000	0.000	0.000
55	A	74	LYS	1	0.855	0.928	9.006	-0.105	-0.105	0.000	0.000	0.000	0.000
56	A	75	LEU	0	0.060	0.030	12.641	-0.112	-0.112	0.000	0.000	0.000	0.000
57	A	76	LEU	0	-0.051	-0.007	14.848	-0.081	-0.081	0.000	0.000	0.000	0.000
58	A	77	ASN	0	0.014	-0.002	14.456	-0.054	-0.054	0.000	0.000	0.000	0.000
59	A	78	LEU	0	0.030	0.014	16.820	-0.048	-0.048	0.000	0.000	0.000	0.000
60	A	79	GLN	0	0.004	-0.011	17.908	-0.051	-0.051	0.000	0.000	0.000	0.000
61	A	80	ASN	0	0.002	-0.002	19.914	-0.029	-0.029	0.000	0.000	0.000	0.000
62	A	81	SER	0	0.053	0.029	20.845	-0.032	-0.032	0.000	0.000	0.000	0.000
63	A	82	PHE	0	-0.007	-0.005	22.931	-0.022	-0.022	0.000	0.000	0.000	0.000
64	A	83	GLN	0	-0.012	-0.016	24.860	-0.023	-0.023	0.000	0.000	0.000	0.000
65	A	84	ASP	-1	-0.875	-0.921	25.599	0.127	0.127	0.000	0.000	0.000	0.000
66	A	85	LYS	1	0.833	0.931	26.606	-0.047	-0.047	0.000	0.000	0.000	0.000
67	A	86	LEU	0	-0.037	-0.018	28.904	-0.011	-0.011	0.000	0.000	0.000	0.000
68	A	87	ALA	0	0.012	0.004	30.592	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	88	ALA	0	-0.017	-0.004	31.879	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	89	LYS	1	0.868	0.939	33.243	-0.037	-0.037	0.000	0.000	0.000	0.000
71	A	90	LEU	0	-0.014	-0.021	34.326	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	91	ALA	0	-0.022	-0.004	36.502	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	92	ALA	0	0.006	0.002	37.763	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	93	LEU	0	-0.021	-0.008	38.267	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	94	LYS	1	0.959	0.978	38.978	-0.072	-0.072	0.000	0.000	0.000	0.000
76	A	95	ALA	0	-0.008	0.011	42.351	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	96	ALA	0	0.034	0.019	43.652	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	97	LYS	1	0.834	0.901	45.336	-0.043	-0.043	0.000	0.000	0.000	0.000
79	A	98	ASN	0	0.014	0.013	46.952	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	99	THR	0	-0.019	-0.014	47.609	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	100	ILE	0	-0.041	-0.026	48.512	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	101	GLU	-1	-0.905	-0.965	51.306	0.033	0.033	0.000	0.000	0.000	0.000
83	A	102	ASN	0	0.000	0.001	52.692	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	103	ILE	0	-0.068	-0.019	53.008	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	104	THR	0	0.033	0.012	56.358	0.000	0.000	0.000	0.000	0.000	0.000
86	A	105	ASP	-1	-0.871	-0.918	60.088	0.014	0.014	0.000	0.000	0.000	0.000
87	A	106	LYS	1	0.828	0.912	56.107	-0.022	-0.022	0.000	0.000	0.000	0.000
88	A	107	ASP	-1	-0.845	-0.920	59.936	0.011	0.011	0.000	0.000	0.000	0.000
89	A	108	GLN	0	-0.017	-0.003	61.637	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	109	ASP	-1	-0.883	-0.945	60.532	0.003	0.003	0.000	0.000	0.000	0.000
91	A	110	ILE	0	-0.056	-0.043	57.533	0.000	0.000	0.000	0.000	0.000	0.000
92	A	111	SER	0	0.005	-0.004	56.680	0.000	0.000	0.000	0.000	0.000	0.000
93	A	112	LYS	1	0.910	0.970	55.877	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	113	ARG	1	0.932	0.958	54.485	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	114	LYS	1	0.919	0.982	49.422	-0.014	-0.014	0.000	0.000	0.000	0.000
96	A	115	ILE	0	0.075	0.025	51.028	0.001	0.001	0.000	0.000	0.000	0.000
97	A	116	TRP	0	-0.048	-0.022	49.738	0.000	0.000	0.000	0.000	0.000	0.000
98	A	117	SER	0	-0.078	-0.043	48.425	0.000	0.000	0.000	0.000	0.000	0.000
99	A	118	GLU	-1	-0.854	-0.943	46.618	0.019	0.019	0.000	0.000	0.000	0.000
100	A	119	ALA	0	0.026	0.017	45.353	0.002	0.002	0.000	0.000	0.000	0.000
101	A	120	LYS	1	0.941	0.980	44.424	0.005	0.005	0.000	0.000	0.000	0.000
102	A	121	LEU	0	-0.022	-0.009	42.221	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	122	VAL	0	-0.021	0.000	40.074	0.001	0.001	0.000	0.000	0.000	0.000
104	A	123	GLY	0	0.000	-0.005	40.111	0.003	0.003	0.000	0.000	0.000	0.000
105	A	124	VAL	0	-0.076	-0.021	41.089	0.000	0.000	0.000	0.000	0.000	0.000
106	A	125	THR	0	0.000	-0.001	44.410	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	126	VAL	0	0.002	0.006	47.206	0.001	0.001	0.000	0.000	0.000	0.000
108	A	127	PRO	0	-0.019	-0.013	50.735	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	128	LEU	0	0.059	0.014	53.867	0.002	0.002	0.000	0.000	0.000	0.000
110	A	129	LEU	0	-0.021	-0.020	55.753	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	130	GLY	0	0.049	0.008	59.185	0.001	0.001	0.000	0.000	0.000	0.000
112	A	131	SER	0	0.003	0.020	61.144	0.000	0.000	0.000	0.000	0.000	0.000
113	A	132	ASN	0	0.045	-0.011	64.277	0.000	0.000	0.000	0.000	0.000	0.000
114	A	133	THR	0	-0.041	-0.012	65.200	0.000	0.000	0.000	0.000	0.000	0.000
115	A	134	SER	0	0.001	0.002	65.475	0.001	0.001	0.000	0.000	0.000	0.000
116	A	135	GLY	0	0.127	0.066	63.950	0.000	0.000	0.000	0.000	0.000	0.000
117	A	136	ASN	0	-0.036	-0.028	61.161	0.001	0.001	0.000	0.000	0.000	0.000
118	A	137	GLY	0	0.005	-0.006	58.963	0.000	0.000	0.000	0.000	0.000	0.000
119	A	138	ASP	-1	-0.839	-0.928	57.859	0.018	0.018	0.000	0.000	0.000	0.000
120	A	139	LYS	1	0.921	0.974	57.970	-0.010	-0.010	0.000	0.000	0.000	0.000
121	A	140	MET	0	-0.085	-0.027	54.427	0.000	0.000	0.000	0.000	0.000	0.000
122	A	141	SER	0	-0.006	0.006	53.695	0.001	0.001	0.000	0.000	0.000	0.000
123	A	142	LYS	1	0.870	0.929	52.877	-0.025	-0.025	0.000	0.000	0.000	0.000
124	A	143	ASN	0	-0.008	-0.016	51.658	0.003	0.003	0.000	0.000	0.000	0.000
125	A	144	ALA	0	0.029	0.007	49.387	0.001	0.001	0.000	0.000	0.000	0.000
126	A	145	VAL	0	0.037	0.017	48.201	0.002	0.002	0.000	0.000	0.000	0.000
127	A	146	GLU	-1	-0.840	-0.896	48.265	0.029	0.029	0.000	0.000	0.000	0.000
128	A	147	GLN	0	-0.074	-0.046	46.025	0.002	0.002	0.000	0.000	0.000	0.000
129	A	148	ILE	0	0.005	0.000	43.425	0.002	0.002	0.000	0.000	0.000	0.000
130	A	149	ASP	-1	-0.802	-0.881	43.300	0.043	0.043	0.000	0.000	0.000	0.000
131	A	150	LYS	1	0.902	0.969	41.595	-0.036	-0.036	0.000	0.000	0.000	0.000
132	A	151	VAL	0	-0.029	-0.028	38.764	0.003	0.003	0.000	0.000	0.000	0.000
133	A	152	ILE	0	0.035	0.015	39.049	0.004	0.004	0.000	0.000	0.000	0.000
134	A	153	LYS	1	0.966	0.984	39.180	-0.049	-0.049	0.000	0.000	0.000	0.000
135	A	154	PHE	0	-0.097	-0.057	35.446	0.003	0.003	0.000	0.000	0.000	0.000
136	A	155	LEU	0	-0.036	-0.015	33.716	0.003	0.003	0.000	0.000	0.000	0.000
137	A	156	GLU	-1	-0.929	-0.966	34.481	0.082	0.082	0.000	0.000	0.000	0.000
138	A	157	GLU	-1	-1.057	-1.008	34.296	0.068	0.068	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:20:HIS)