FMO DATABASE

FMODB ID: 85YZY

Calculation Name: 3RHE-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3RHE

Chain ID: A

ChEMBL ID:

UniProt ID: Q5ZTJ2

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1000569.100791
FMO2-HF: Nuclear repulsion	952249.991361
FMO2-HF: Total energy	-48319.10943
FMO2-MP2: Total energy	-48458.206113

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:PRO)

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

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.
-6.578	-0.375	2.706	-3.64	-5.269	-0.019

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.082 / q_NPA : 0.029

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	LEU	0	-0.034	-0.006	3.766	-1.450	0.679	-0.021	-1.034	-1.073	0.001
4	A	8	VAL	0	0.020	0.025	6.392	0.013	0.013	0.000	0.000	0.000	0.000
5	A	9	LEU	0	0.012	0.011	9.913	0.102	0.102	0.000	0.000	0.000	0.000
6	A	10	PHE	0	-0.013	-0.007	12.419	0.012	0.012	0.000	0.000	0.000	0.000
7	A	11	TYR	0	-0.011	-0.059	15.862	0.028	0.028	0.000	0.000	0.000	0.000
8	A	12	VAL	0	-0.042	-0.019	18.734	0.016	0.016	0.000	0.000	0.000	0.000
9	A	13	LYS	1	0.997	0.993	21.203	0.061	0.061	0.000	0.000	0.000	0.000
10	A	14	ASN	0	0.024	0.012	24.103	0.009	0.009	0.000	0.000	0.000	0.000
11	A	15	PRO	0	0.092	0.046	19.589	0.004	0.004	0.000	0.000	0.000	0.000
12	A	16	ALA	0	0.034	0.029	21.270	0.010	0.010	0.000	0.000	0.000	0.000
13	A	17	LYS	1	0.939	0.950	23.754	0.017	0.017	0.000	0.000	0.000	0.000
14	A	18	SER	0	0.001	-0.003	20.144	0.004	0.004	0.000	0.000	0.000	0.000
15	A	19	GLH	0	-0.015	-0.011	18.882	0.010	0.010	0.000	0.000	0.000	0.000
16	A	20	GLU	-1	-0.878	-0.932	20.305	0.054	0.054	0.000	0.000	0.000	0.000
17	A	21	PHE	0	-0.053	-0.015	20.983	0.005	0.005	0.000	0.000	0.000	0.000
18	A	22	TYR	0	0.051	0.004	17.463	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	23	LYS	1	0.935	1.001	19.377	-0.070	-0.070	0.000	0.000	0.000	0.000
20	A	24	ASN	0	-0.069	-0.044	20.444	0.014	0.014	0.000	0.000	0.000	0.000
21	A	25	LEU	0	-0.049	-0.010	18.814	0.001	0.001	0.000	0.000	0.000	0.000
22	A	26	LEU	0	-0.042	-0.042	15.073	0.000	0.000	0.000	0.000	0.000	0.000
23	A	27	ASP	-1	-0.928	-0.944	19.063	0.076	0.076	0.000	0.000	0.000	0.000
24	A	28	THR	0	-0.065	-0.029	15.845	0.026	0.026	0.000	0.000	0.000	0.000
25	A	29	GLN	0	0.017	-0.013	18.300	-0.021	-0.021	0.000	0.000	0.000	0.000
26	A	30	PRO	0	-0.036	-0.002	15.093	0.025	0.025	0.000	0.000	0.000	0.000
27	A	31	ILE	0	-0.043	-0.036	9.936	0.019	0.019	0.000	0.000	0.000	0.000
28	A	32	GLU	-1	-0.894	-0.955	13.509	0.115	0.115	0.000	0.000	0.000	0.000
29	A	33	SER	0	-0.038	-0.018	15.459	-0.030	-0.030	0.000	0.000	0.000	0.000
30	A	34	SER	0	0.038	0.026	17.811	0.000	0.000	0.000	0.000	0.000	0.000
31	A	35	PRO	0	-0.018	-0.024	20.101	-0.008	-0.008	0.000	0.000	0.000	0.000
32	A	36	THR	0	0.059	0.024	18.075	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	37	PHE	0	-0.031	-0.014	10.789	-0.033	-0.033	0.000	0.000	0.000	0.000
34	A	38	ALA	0	0.041	0.028	15.788	0.028	0.028	0.000	0.000	0.000	0.000
35	A	39	MET	0	-0.010	0.007	8.865	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	40	PHE	0	0.003	-0.006	11.880	0.059	0.059	0.000	0.000	0.000	0.000
37	A	41	VAL	0	0.012	0.000	7.926	-0.020	-0.020	0.000	0.000	0.000	0.000
38	A	42	MET	0	-0.008	0.009	9.782	0.004	0.004	0.000	0.000	0.000	0.000
39	A	43	LYS	1	1.002	0.997	10.322	-0.147	-0.147	0.000	0.000	0.000	0.000
40	A	44	THR	0	-0.043	-0.038	11.048	0.049	0.049	0.000	0.000	0.000	0.000
41	A	45	GLY	0	0.025	0.013	7.620	0.007	0.007	0.000	0.000	0.000	0.000
42	A	46	LEU	0	-0.026	0.003	5.995	0.013	0.013	0.000	0.000	0.000	0.000
43	A	47	ARG	1	0.868	0.936	3.058	-0.026	0.882	0.377	-0.351	-0.934	-0.002
44	A	48	LEU	0	0.013	0.005	7.255	-0.192	-0.192	0.000	0.000	0.000	0.000
45	A	49	GLY	0	0.016	0.012	10.516	0.089	0.089	0.000	0.000	0.000	0.000
46	A	50	LEU	0	-0.059	-0.029	12.130	-0.037	-0.037	0.000	0.000	0.000	0.000
47	A	51	TRP	0	0.024	0.003	14.257	0.013	0.013	0.000	0.000	0.000	0.000
48	A	52	ALA	0	0.019	0.002	16.783	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	53	GLN	0	-0.004	0.006	20.233	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	54	GLU	-1	-0.951	-0.991	21.826	-0.076	-0.076	0.000	0.000	0.000	0.000
51	A	55	GLU	-1	-0.955	-0.979	19.462	-0.064	-0.064	0.000	0.000	0.000	0.000
52	A	56	ILE	0	-0.118	-0.029	17.025	-0.016	-0.016	0.000	0.000	0.000	0.000
53	A	57	GLU	-1	-0.867	-0.919	18.376	-0.116	-0.116	0.000	0.000	0.000	0.000
54	A	58	PRO	0	0.063	0.012	17.810	-0.027	-0.027	0.000	0.000	0.000	0.000
55	A	59	LYS	1	0.929	0.968	20.705	0.097	0.097	0.000	0.000	0.000	0.000
56	A	60	ALA	0	0.027	0.032	20.867	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	61	HIS	0	0.031	0.055	22.583	0.023	0.023	0.000	0.000	0.000	0.000
58	A	62	GLN	0	-0.052	-0.070	24.097	0.012	0.012	0.000	0.000	0.000	0.000
59	A	63	THR	0	-0.022	-0.027	23.243	-0.009	-0.009	0.000	0.000	0.000	0.000
60	A	64	GLY	0	0.060	0.052	21.365	0.001	0.001	0.000	0.000	0.000	0.000
61	A	65	GLY	0	0.059	0.029	19.328	-0.020	-0.020	0.000	0.000	0.000	0.000
62	A	66	GLY	0	-0.058	-0.026	20.329	0.005	0.005	0.000	0.000	0.000	0.000
63	A	67	MET	0	-0.048	-0.027	13.251	0.008	0.008	0.000	0.000	0.000	0.000
64	A	68	GLU	-1	-0.695	-0.768	12.422	-0.404	-0.404	0.000	0.000	0.000	0.000
65	A	69	LEU	0	-0.019	0.000	7.831	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	70	SER	0	-0.026	-0.013	7.649	0.017	0.017	0.000	0.000	0.000	0.000
67	A	71	PHE	0	0.007	-0.013	3.649	-0.685	-0.519	0.003	-0.055	-0.114	0.000
68	A	72	GLN	0	0.009	0.013	2.427	-0.211	1.162	0.710	-0.856	-1.227	0.000
69	A	73	VAL	0	-0.025	-0.023	2.418	-3.563	-1.953	1.638	-1.341	-1.908	-0.018
70	A	74	ASN	0	-0.023	-0.029	4.928	0.271	0.288	-0.001	-0.003	-0.013	0.000
71	A	75	SER	0	0.025	-0.003	7.464	0.112	0.112	0.000	0.000	0.000	0.000
72	A	76	ASN	0	0.080	0.012	10.452	-0.098	-0.098	0.000	0.000	0.000	0.000
73	A	77	GLU	-1	-0.838	-0.920	13.040	-0.138	-0.138	0.000	0.000	0.000	0.000
74	A	78	MET	0	-0.048	-0.011	7.819	-0.033	-0.033	0.000	0.000	0.000	0.000
75	A	79	VAL	0	-0.023	-0.013	9.624	-0.083	-0.083	0.000	0.000	0.000	0.000
76	A	80	ASP	-1	-0.814	-0.897	11.123	-0.228	-0.228	0.000	0.000	0.000	0.000
77	A	81	GLU	-1	-0.858	-0.913	12.643	-0.253	-0.253	0.000	0.000	0.000	0.000
78	A	82	ILE	0	-0.024	-0.024	7.746	-0.017	-0.017	0.000	0.000	0.000	0.000
79	A	83	HIS	0	0.018	0.013	12.198	0.019	0.019	0.000	0.000	0.000	0.000
80	A	84	ARG	1	0.897	0.940	14.841	0.218	0.218	0.000	0.000	0.000	0.000
81	A	85	GLN	0	-0.064	-0.041	12.711	-0.035	-0.035	0.000	0.000	0.000	0.000
82	A	86	TRP	0	-0.004	-0.028	9.635	0.013	0.013	0.000	0.000	0.000	0.000
83	A	87	SER	0	-0.002	0.002	15.793	0.025	0.025	0.000	0.000	0.000	0.000
84	A	88	ASP	-1	-0.946	-0.961	19.159	-0.176	-0.176	0.000	0.000	0.000	0.000
85	A	89	LYS	1	0.823	0.912	13.647	0.380	0.380	0.000	0.000	0.000	0.000
86	A	90	GLU	-1	-0.962	-0.971	19.348	-0.153	-0.153	0.000	0.000	0.000	0.000
87	A	91	ILE	0	-0.060	-0.015	14.451	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	92	SER	0	0.018	0.008	18.405	0.006	0.006	0.000	0.000	0.000	0.000
89	A	93	ILE	0	-0.012	-0.011	16.672	-0.033	-0.033	0.000	0.000	0.000	0.000
90	A	94	ILE	0	-0.040	-0.017	18.274	0.028	0.028	0.000	0.000	0.000	0.000
91	A	95	GLN	0	0.004	-0.018	16.829	-0.008	-0.008	0.000	0.000	0.000	0.000
92	A	96	PRO	0	0.030	0.029	17.317	-0.035	-0.035	0.000	0.000	0.000	0.000
93	A	97	PRO	0	0.044	0.015	16.057	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	98	THR	0	-0.038	-0.024	16.485	0.042	0.042	0.000	0.000	0.000	0.000
95	A	99	GLN	0	-0.043	-0.031	16.550	-0.007	-0.007	0.000	0.000	0.000	0.000
96	A	100	MET	0	-0.023	0.012	15.771	0.018	0.018	0.000	0.000	0.000	0.000
97	A	101	ASP	-1	-0.853	-0.926	17.199	-0.049	-0.049	0.000	0.000	0.000	0.000
98	A	102	PHE	0	-0.047	-0.027	11.490	0.025	0.025	0.000	0.000	0.000	0.000
99	A	103	GLY	0	-0.042	-0.032	12.902	0.030	0.030	0.000	0.000	0.000	0.000
100	A	104	TYR	0	-0.097	-0.041	12.798	0.005	0.005	0.000	0.000	0.000	0.000
101	A	105	THR	0	-0.038	-0.039	11.816	-0.069	-0.069	0.000	0.000	0.000	0.000
102	A	106	PHE	0	0.061	0.041	11.901	0.055	0.055	0.000	0.000	0.000	0.000
103	A	107	VAL	0	-0.010	-0.011	12.678	-0.081	-0.081	0.000	0.000	0.000	0.000
104	A	108	GLY	0	0.039	0.024	13.831	0.054	0.054	0.000	0.000	0.000	0.000
105	A	109	VAL	0	-0.023	-0.017	15.404	-0.027	-0.027	0.000	0.000	0.000	0.000
106	A	110	ASP	-1	-0.818	-0.897	15.966	-0.277	-0.277	0.000	0.000	0.000	0.000
107	A	111	PRO	0	-0.014	-0.029	17.748	0.015	0.015	0.000	0.000	0.000	0.000
108	A	112	ASP	-1	-0.969	-0.971	20.152	-0.157	-0.157	0.000	0.000	0.000	0.000
109	A	113	GLU	-1	-0.978	-0.989	20.331	-0.191	-0.191	0.000	0.000	0.000	0.000
110	A	114	HIS	0	-0.096	-0.041	15.871	0.008	0.008	0.000	0.000	0.000	0.000
111	A	115	ARG	1	0.841	0.896	15.103	0.216	0.216	0.000	0.000	0.000	0.000
112	A	116	LEU	0	-0.021	-0.007	11.036	-0.066	-0.066	0.000	0.000	0.000	0.000
113	A	117	ARG	1	0.805	0.847	10.135	0.442	0.442	0.000	0.000	0.000	0.000
114	A	118	ILE	0	0.030	0.039	7.542	-0.300	-0.300	0.000	0.000	0.000	0.000
115	A	119	PHE	0	-0.006	-0.012	5.918	0.231	0.231	0.000	0.000	0.000	0.000
116	A	120	CYS	0	0.003	0.041	7.148	-0.165	-0.165	0.000	0.000	0.000	0.000
117	A	121	LEU	0	-0.042	-0.013	7.946	0.041	0.041	0.000	0.000	0.000	0.000
118	A	122	LYS	1	0.942	0.977	10.344	0.091	0.091	0.000	0.000	0.000	0.000

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