FMO DATABASE

FMODB ID: QLK1Y

Calculation Name: 2E4J-A-Other547

Preferred Name: Prostaglandin-H2 D-isomerase

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2E4J

Chain ID: A

ChEMBL ID: CHEMBL4334

UniProt ID: O09114

Base Structure: SolutionNMR

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	167
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1616037.828603
FMO2-HF: Nuclear repulsion	1551115.913552
FMO2-HF: Total energy	-64921.915051
FMO2-MP2: Total energy	-65112.077203

3D Structure Molmil

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:23:GLY)

Summations of interaction energy for fragment #1(A:23:GLY)

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.
-11.904	-11.021	-0.005	-0.275	-0.602	-0.001

Interaction energy analysis for fragmet #1(A:23:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.871 / q_NPA : 0.921

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	25	GLN	0	-0.009	-0.012	3.844	6.360	7.243	-0.005	-0.275	-0.602	-0.001
4	A	26	GLY	0	0.046	0.026	5.570	-2.753	-2.753	0.000	0.000	0.000	0.000
5	A	27	HIS	0	0.029	0.018	8.486	1.050	1.050	0.000	0.000	0.000	0.000
6	A	28	ASP	-1	-0.846	-0.916	11.668	-19.915	-19.915	0.000	0.000	0.000	0.000
7	A	29	THR	0	-0.067	-0.021	8.856	-0.119	-0.119	0.000	0.000	0.000	0.000
8	A	30	VAL	0	0.030	0.010	12.097	0.676	0.676	0.000	0.000	0.000	0.000
9	A	31	GLN	0	0.017	0.010	14.150	-0.926	-0.926	0.000	0.000	0.000	0.000
10	A	32	PRO	0	-0.040	-0.020	13.528	1.018	1.018	0.000	0.000	0.000	0.000
11	A	33	ASN	0	-0.047	-0.026	16.477	0.840	0.840	0.000	0.000	0.000	0.000
12	A	34	PHE	0	0.051	0.039	20.131	0.367	0.367	0.000	0.000	0.000	0.000
13	A	35	GLN	0	-0.001	-0.014	22.240	0.538	0.538	0.000	0.000	0.000	0.000
14	A	36	GLN	0	0.050	0.012	25.300	0.420	0.420	0.000	0.000	0.000	0.000
15	A	37	ASP	-1	-0.860	-0.928	28.176	-9.691	-9.691	0.000	0.000	0.000	0.000
16	A	38	LYS	1	0.865	0.937	26.993	11.958	11.958	0.000	0.000	0.000	0.000
17	A	39	PHE	0	-0.008	-0.002	24.029	-0.014	-0.014	0.000	0.000	0.000	0.000
18	A	40	LEU	0	-0.005	0.030	29.598	0.104	0.104	0.000	0.000	0.000	0.000
19	A	41	GLY	0	0.017	0.021	32.749	0.149	0.149	0.000	0.000	0.000	0.000
20	A	42	ARG	1	0.879	0.939	34.849	8.256	8.256	0.000	0.000	0.000	0.000
21	A	43	TRP	0	-0.001	0.003	27.637	-0.120	-0.120	0.000	0.000	0.000	0.000
22	A	44	TYR	0	0.014	-0.004	33.624	0.299	0.299	0.000	0.000	0.000	0.000
23	A	45	SER	0	-0.024	-0.024	29.818	-0.309	-0.309	0.000	0.000	0.000	0.000
24	A	46	ALA	0	-0.003	-0.005	30.231	0.365	0.365	0.000	0.000	0.000	0.000
25	A	47	GLY	0	0.034	0.018	27.384	-0.225	-0.225	0.000	0.000	0.000	0.000
26	A	48	LEU	0	-0.012	-0.005	26.655	-0.046	-0.046	0.000	0.000	0.000	0.000
27	A	49	ALA	0	-0.004	0.014	23.486	0.137	0.137	0.000	0.000	0.000	0.000
28	A	50	SER	0	0.016	-0.014	25.592	-0.061	-0.061	0.000	0.000	0.000	0.000
29	A	51	ASN	0	-0.039	0.012	26.273	0.831	0.831	0.000	0.000	0.000	0.000
30	A	52	SER	0	-0.074	-0.042	28.464	0.466	0.466	0.000	0.000	0.000	0.000
31	A	53	SER	0	0.096	0.045	31.723	0.043	0.043	0.000	0.000	0.000	0.000
32	A	54	TRP	0	0.018	0.003	34.961	0.054	0.054	0.000	0.000	0.000	0.000
33	A	55	PHE	0	0.039	0.021	33.614	0.240	0.240	0.000	0.000	0.000	0.000
34	A	56	ARG	1	0.909	0.942	36.247	7.979	7.979	0.000	0.000	0.000	0.000
35	A	57	GLU	-1	-0.878	-0.936	38.224	-7.422	-7.422	0.000	0.000	0.000	0.000
36	A	58	LYS	1	0.904	0.954	37.858	8.549	8.549	0.000	0.000	0.000	0.000
37	A	59	LYS	1	0.978	0.980	36.089	8.606	8.606	0.000	0.000	0.000	0.000
38	A	60	ALA	0	-0.058	-0.023	38.280	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	61	VAL	0	-0.025	-0.009	41.651	0.158	0.158	0.000	0.000	0.000	0.000
40	A	62	LEU	0	-0.029	0.003	35.210	0.016	0.016	0.000	0.000	0.000	0.000
41	A	63	TYR	0	0.044	0.008	38.775	0.079	0.079	0.000	0.000	0.000	0.000
42	A	64	MET	0	-0.027	0.040	37.097	-0.172	-0.172	0.000	0.000	0.000	0.000
43	A	65	CYS	0	-0.019	-0.008	33.588	0.225	0.225	0.000	0.000	0.000	0.000
44	A	66	LYS	1	0.969	0.977	35.290	7.727	7.727	0.000	0.000	0.000	0.000
45	A	67	THR	0	0.008	0.005	31.907	0.141	0.141	0.000	0.000	0.000	0.000
46	A	68	VAL	0	-0.032	-0.021	34.786	-0.071	-0.071	0.000	0.000	0.000	0.000
47	A	69	VAL	0	0.008	0.009	30.579	0.001	0.001	0.000	0.000	0.000	0.000
48	A	70	ALA	0	0.039	0.018	33.694	0.143	0.143	0.000	0.000	0.000	0.000
49	A	71	PRO	0	0.051	0.026	34.583	-0.233	-0.233	0.000	0.000	0.000	0.000
50	A	72	SER	0	-0.022	-0.012	35.416	0.321	0.321	0.000	0.000	0.000	0.000
51	A	73	THR	0	-0.011	-0.003	37.117	0.023	0.023	0.000	0.000	0.000	0.000
52	A	74	GLU	-1	-0.905	-0.957	37.166	-8.544	-8.544	0.000	0.000	0.000	0.000
53	A	75	GLY	0	-0.003	-0.006	34.306	0.018	0.018	0.000	0.000	0.000	0.000
54	A	76	GLY	0	-0.041	-0.005	32.362	-0.382	-0.382	0.000	0.000	0.000	0.000
55	A	77	LEU	0	-0.018	-0.001	29.147	0.129	0.129	0.000	0.000	0.000	0.000
56	A	78	ASN	0	-0.054	-0.048	32.709	0.038	0.038	0.000	0.000	0.000	0.000
57	A	79	LEU	0	0.034	0.007	30.459	-0.066	-0.066	0.000	0.000	0.000	0.000
58	A	80	THR	0	0.022	0.017	34.521	0.183	0.183	0.000	0.000	0.000	0.000
59	A	81	SER	0	0.010	-0.003	34.372	-0.173	-0.173	0.000	0.000	0.000	0.000
60	A	82	THR	0	0.005	0.007	37.043	0.288	0.288	0.000	0.000	0.000	0.000
61	A	83	PHE	0	-0.022	-0.015	37.899	-0.238	-0.238	0.000	0.000	0.000	0.000
62	A	84	LEU	0	-0.031	-0.007	40.157	0.230	0.230	0.000	0.000	0.000	0.000
63	A	85	ARG	1	0.878	0.931	41.700	6.965	6.965	0.000	0.000	0.000	0.000
64	A	86	LYS	1	0.972	0.989	44.279	7.031	7.031	0.000	0.000	0.000	0.000
65	A	87	ASN	0	-0.060	-0.021	47.357	0.053	0.053	0.000	0.000	0.000	0.000
66	A	88	GLN	0	0.007	0.003	47.647	0.236	0.236	0.000	0.000	0.000	0.000
67	A	89	ALA	0	0.026	0.001	44.777	-0.174	-0.174	0.000	0.000	0.000	0.000
68	A	90	GLU	-1	-0.819	-0.894	42.873	-7.004	-7.004	0.000	0.000	0.000	0.000
69	A	91	THR	0	-0.016	-0.008	42.008	-0.190	-0.190	0.000	0.000	0.000	0.000
70	A	92	LYS	1	0.870	0.931	35.788	8.822	8.822	0.000	0.000	0.000	0.000
71	A	93	ILE	0	0.046	0.028	38.326	-0.148	-0.148	0.000	0.000	0.000	0.000
72	A	94	MET	0	-0.043	-0.017	32.312	-0.191	-0.191	0.000	0.000	0.000	0.000
73	A	95	VAL	0	0.013	0.019	34.135	0.080	0.080	0.000	0.000	0.000	0.000
74	A	96	LEU	0	-0.005	-0.004	27.529	-0.200	-0.200	0.000	0.000	0.000	0.000
75	A	97	GLN	0	0.063	0.021	30.391	-0.075	-0.075	0.000	0.000	0.000	0.000
76	A	98	PRO	0	-0.026	-0.009	26.754	-0.421	-0.421	0.000	0.000	0.000	0.000
77	A	99	ALA	0	0.015	-0.003	23.615	0.215	0.215	0.000	0.000	0.000	0.000
78	A	100	GLY	0	0.013	0.009	24.186	-0.028	-0.028	0.000	0.000	0.000	0.000
79	A	101	ALA	0	-0.028	-0.005	19.561	-0.077	-0.077	0.000	0.000	0.000	0.000
80	A	102	PRO	0	-0.008	-0.025	21.006	0.286	0.286	0.000	0.000	0.000	0.000
81	A	103	GLY	0	0.046	0.029	21.357	-0.412	-0.412	0.000	0.000	0.000	0.000
82	A	104	HIS	0	-0.008	-0.001	17.737	0.059	0.059	0.000	0.000	0.000	0.000
83	A	105	TYR	0	0.053	0.018	22.044	0.356	0.356	0.000	0.000	0.000	0.000
84	A	106	THR	0	-0.015	0.003	24.919	-0.331	-0.331	0.000	0.000	0.000	0.000
85	A	107	TYR	0	-0.010	-0.012	27.283	0.415	0.415	0.000	0.000	0.000	0.000
86	A	108	SER	0	0.019	0.011	29.986	0.095	0.095	0.000	0.000	0.000	0.000
87	A	109	SER	0	-0.023	-0.033	31.705	0.175	0.175	0.000	0.000	0.000	0.000
88	A	110	PRO	0	-0.010	0.004	34.278	0.230	0.230	0.000	0.000	0.000	0.000
89	A	111	HIS	0	0.041	0.018	35.536	-0.021	-0.021	0.000	0.000	0.000	0.000
90	A	112	SER	0	-0.027	-0.013	34.318	-0.028	-0.028	0.000	0.000	0.000	0.000
91	A	113	GLY	0	0.042	0.033	31.568	0.125	0.125	0.000	0.000	0.000	0.000
92	A	114	SER	0	-0.099	-0.036	32.154	0.154	0.154	0.000	0.000	0.000	0.000
93	A	115	ILE	0	0.030	0.016	27.884	0.249	0.249	0.000	0.000	0.000	0.000
94	A	116	HIS	0	-0.002	-0.002	26.706	-0.205	-0.205	0.000	0.000	0.000	0.000
95	A	117	SER	0	0.030	0.015	23.427	0.516	0.516	0.000	0.000	0.000	0.000
96	A	118	VAL	0	-0.028	-0.008	22.837	-0.218	-0.218	0.000	0.000	0.000	0.000
97	A	119	SER	0	0.005	-0.002	18.978	0.052	0.052	0.000	0.000	0.000	0.000
98	A	120	VAL	0	0.013	0.010	20.142	0.107	0.107	0.000	0.000	0.000	0.000
99	A	121	VAL	0	-0.043	-0.010	15.446	-0.614	-0.614	0.000	0.000	0.000	0.000
100	A	122	GLU	-1	-0.891	-0.967	15.352	-21.467	-21.467	0.000	0.000	0.000	0.000
101	A	123	ALA	0	0.004	0.001	18.571	0.830	0.830	0.000	0.000	0.000	0.000
102	A	124	ASN	0	0.010	0.025	21.210	-1.103	-1.103	0.000	0.000	0.000	0.000
103	A	125	TYR	0	-0.026	-0.003	22.584	0.550	0.550	0.000	0.000	0.000	0.000
104	A	126	ASP	-1	-0.963	-0.997	24.366	-10.924	-10.924	0.000	0.000	0.000	0.000
105	A	127	GLU	-1	-0.916	-0.962	26.431	-10.491	-10.491	0.000	0.000	0.000	0.000
106	A	128	TYR	0	-0.043	-0.057	24.684	-0.550	-0.550	0.000	0.000	0.000	0.000
107	A	129	ALA	0	0.040	0.035	23.786	-0.584	-0.584	0.000	0.000	0.000	0.000
108	A	130	LEU	0	0.015	0.003	19.501	0.461	0.461	0.000	0.000	0.000	0.000
109	A	131	LEU	0	-0.012	-0.005	20.918	-0.379	-0.379	0.000	0.000	0.000	0.000
110	A	132	PHE	0	0.039	0.021	15.474	0.192	0.192	0.000	0.000	0.000	0.000
111	A	133	SER	0	-0.076	-0.049	20.216	0.580	0.580	0.000	0.000	0.000	0.000
112	A	134	ARG	1	0.874	0.910	15.263	18.333	18.333	0.000	0.000	0.000	0.000
113	A	135	GLY	0	0.007	-0.004	22.444	0.488	0.488	0.000	0.000	0.000	0.000
114	A	136	THR	0	-0.002	-0.008	25.179	-0.203	-0.203	0.000	0.000	0.000	0.000
115	A	137	LYS	1	0.937	0.971	27.209	10.329	10.329	0.000	0.000	0.000	0.000
116	A	138	GLY	0	0.027	0.004	31.006	0.048	0.048	0.000	0.000	0.000	0.000
117	A	139	PRO	0	-0.002	-0.019	31.183	-0.174	-0.174	0.000	0.000	0.000	0.000
118	A	140	GLY	0	0.044	0.022	27.570	-0.293	-0.293	0.000	0.000	0.000	0.000
119	A	141	GLN	0	-0.087	-0.028	27.497	0.195	0.195	0.000	0.000	0.000	0.000
120	A	142	ASP	-1	-0.918	-0.955	21.590	-14.622	-14.622	0.000	0.000	0.000	0.000
121	A	143	PHE	0	-0.033	-0.007	24.215	0.072	0.072	0.000	0.000	0.000	0.000
122	A	144	ARG	1	0.971	0.986	15.886	17.639	17.639	0.000	0.000	0.000	0.000
123	A	145	MET	0	0.008	0.007	22.233	0.430	0.430	0.000	0.000	0.000	0.000
124	A	146	ALA	0	-0.013	0.017	21.286	-0.616	-0.616	0.000	0.000	0.000	0.000
125	A	147	THR	0	-0.005	-0.013	23.094	0.600	0.600	0.000	0.000	0.000	0.000
126	A	148	LEU	0	0.004	0.019	23.977	-0.604	-0.604	0.000	0.000	0.000	0.000
127	A	149	TYR	0	-0.033	-0.003	25.878	0.547	0.547	0.000	0.000	0.000	0.000
128	A	150	SER	0	-0.002	-0.009	27.809	-0.376	-0.376	0.000	0.000	0.000	0.000
129	A	151	ARG	1	0.924	0.948	30.007	10.279	10.279	0.000	0.000	0.000	0.000
130	A	152	THR	0	0.061	0.028	31.896	0.163	0.163	0.000	0.000	0.000	0.000
131	A	153	GLN	0	0.003	-0.014	34.402	0.208	0.208	0.000	0.000	0.000	0.000
132	A	154	THR	0	-0.004	0.003	34.937	0.222	0.222	0.000	0.000	0.000	0.000
133	A	155	LEU	0	0.004	0.014	31.058	-0.148	-0.148	0.000	0.000	0.000	0.000
134	A	156	LYS	0	-0.003	0.005	28.536	0.184	0.184	0.000	0.000	0.000	0.000
135	A	157	ASP	-1	-0.856	-0.937	28.102	-11.051	-11.051	0.000	0.000	0.000	0.000
136	A	158	GLU	-1	-0.872	-0.932	23.716	-12.462	-12.462	0.000	0.000	0.000	0.000
137	A	159	LEU	0	-0.037	-0.009	23.138	-0.724	-0.724	0.000	0.000	0.000	0.000
138	A	160	LYS	1	0.913	0.966	24.117	11.028	11.028	0.000	0.000	0.000	0.000
139	A	161	GLU	-1	-0.887	-0.941	20.990	-15.136	-15.136	0.000	0.000	0.000	0.000
140	A	162	LYS	1	0.954	0.999	15.596	18.856	18.856	0.000	0.000	0.000	0.000
141	A	163	PHE	0	0.011	-0.010	18.891	-0.936	-0.936	0.000	0.000	0.000	0.000
142	A	164	THR	0	-0.036	-0.030	20.483	-0.132	-0.132	0.000	0.000	0.000	0.000
143	A	165	THR	0	-0.050	-0.034	16.557	-0.179	-0.179	0.000	0.000	0.000	0.000
144	A	166	PHE	0	-0.014	-0.008	15.200	-0.845	-0.845	0.000	0.000	0.000	0.000
145	A	167	SER	0	-0.012	-0.002	16.371	-0.757	-0.757	0.000	0.000	0.000	0.000
146	A	168	LYS	1	0.844	0.909	18.591	14.362	14.362	0.000	0.000	0.000	0.000
147	A	169	ALA	0	-0.013	-0.001	14.399	0.115	0.115	0.000	0.000	0.000	0.000
148	A	170	GLN	0	-0.048	-0.028	11.767	-0.465	-0.465	0.000	0.000	0.000	0.000
149	A	171	GLY	0	-0.028	0.007	14.991	0.281	0.281	0.000	0.000	0.000	0.000
150	A	172	LEU	0	-0.003	0.007	17.940	0.754	0.754	0.000	0.000	0.000	0.000
151	A	173	THR	0	-0.025	-0.050	21.311	-0.358	-0.358	0.000	0.000	0.000	0.000
152	A	174	GLU	-1	-0.852	-0.914	24.252	-11.580	-11.580	0.000	0.000	0.000	0.000
153	A	175	GLU	-1	-0.948	-0.965	27.296	-10.172	-10.172	0.000	0.000	0.000	0.000
154	A	176	ASP	-1	-0.813	-0.920	24.644	-12.655	-12.655	0.000	0.000	0.000	0.000
155	A	177	ILE	0	-0.047	-0.014	23.983	-0.409	-0.409	0.000	0.000	0.000	0.000
156	A	178	VAL	0	-0.038	-0.017	27.911	0.550	0.550	0.000	0.000	0.000	0.000
157	A	179	PHE	0	0.012	-0.003	27.034	-0.268	-0.268	0.000	0.000	0.000	0.000
158	A	180	LEU	0	-0.032	-0.021	31.593	0.331	0.331	0.000	0.000	0.000	0.000
159	A	181	PRO	0	-0.017	-0.014	34.424	-0.123	-0.123	0.000	0.000	0.000	0.000
160	A	182	GLN	0	0.032	0.023	36.614	-0.101	-0.101	0.000	0.000	0.000	0.000
161	A	183	PRO	0	-0.036	-0.050	37.077	0.144	0.144	0.000	0.000	0.000	0.000
162	A	184	ASP	-1	-0.783	-0.891	39.896	-7.278	-7.278	0.000	0.000	0.000	0.000
163	A	185	LYS	1	0.869	0.915	43.100	6.492	6.492	0.000	0.000	0.000	0.000
164	A	186	ALA	0	0.004	0.002	45.698	-0.024	-0.024	0.000	0.000	0.000	0.000
165	A	187	ILE	0	-0.018	0.004	46.726	-0.008	-0.008	0.000	0.000	0.000	0.000
166	A	188	GLN	0	-0.083	-0.061	45.369	-0.224	-0.224	0.000	0.000	0.000	0.000
167	A	189	GLU	-2	-1.866	-1.907	49.651	-12.172	-12.172	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:23:GLY)