FMO DATABASE

FMODB ID: LZ3Q9

Calculation Name: 2CZU-A-Xray372

Preferred Name: Prostaglandin-H2 D-isomerase

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2CZU

Chain ID: A

ChEMBL ID: CHEMBL4334

UniProt ID: O09114

Base Structure: X-ray

Registration Date: 2023-09-19

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	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	154
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1502226.537795
FMO2-HF: Nuclear repulsion	1441344.281301
FMO2-HF: Total energy	-60882.256494
FMO2-MP2: Total energy	-61059.733923

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:35:GLN)

Summations of interaction energy for fragment #1(A:35:GLN)

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.
-4.838	-0.133	0.646	-1.654	-3.697	0.001

Interaction energy analysis for fragmet #1(A:35:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.052 / q_NPA : 0.008

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	37	ASP	-1	-0.848	-0.937	3.637	-2.727	-0.923	0.005	-0.690	-1.120	0.002
4	A	38	LYS	1	0.857	0.939	2.759	-2.705	-1.302	0.255	-0.528	-1.130	0.000
5	A	39	PHE	0	-0.009	-0.015	2.553	-0.744	0.655	0.387	-0.427	-1.358	-0.001
6	A	40	LEU	0	0.007	0.048	7.105	0.103	0.103	0.000	0.000	0.000	0.000
7	A	41	GLY	0	0.035	0.018	9.675	0.176	0.176	0.000	0.000	0.000	0.000
8	A	42	ARG	1	0.905	0.957	13.000	-0.251	-0.251	0.000	0.000	0.000	0.000
9	A	43	TRP	0	-0.033	-0.005	8.802	0.091	0.091	0.000	0.000	0.000	0.000
10	A	44	TYR	0	0.009	-0.008	15.479	-0.046	-0.046	0.000	0.000	0.000	0.000
11	A	45	SER	0	-0.014	-0.002	17.611	0.022	0.022	0.000	0.000	0.000	0.000
12	A	46	ALA	0	0.038	0.004	18.724	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	47	GLY	0	0.011	0.015	19.549	-0.001	-0.001	0.000	0.000	0.000	0.000
14	A	48	LEU	0	-0.033	-0.022	19.800	-0.015	-0.015	0.000	0.000	0.000	0.000
15	A	49	ALA	0	0.059	0.032	21.628	0.008	0.008	0.000	0.000	0.000	0.000
16	A	50	SER	0	-0.019	-0.032	22.358	-0.022	-0.022	0.000	0.000	0.000	0.000
17	A	51	ASN	0	0.076	0.045	24.754	0.004	0.004	0.000	0.000	0.000	0.000
18	A	52	SER	0	-0.046	-0.021	26.519	0.003	0.003	0.000	0.000	0.000	0.000
19	A	53	SER	0	0.046	0.018	28.413	0.005	0.005	0.000	0.000	0.000	0.000
20	A	54	TRP	0	0.022	0.012	25.536	0.006	0.006	0.000	0.000	0.000	0.000
21	A	55	PHE	0	0.034	0.009	25.614	0.004	0.004	0.000	0.000	0.000	0.000
22	A	56	ARG	1	0.914	0.931	28.641	0.055	0.055	0.000	0.000	0.000	0.000
23	A	57	GLU	-1	-0.949	-0.953	31.848	-0.033	-0.033	0.000	0.000	0.000	0.000
24	A	58	LYS	1	0.838	0.904	30.156	0.047	0.047	0.000	0.000	0.000	0.000
25	A	59	LYS	1	0.860	0.949	29.084	0.001	0.001	0.000	0.000	0.000	0.000
26	A	60	ALA	0	-0.003	0.005	30.134	0.007	0.007	0.000	0.000	0.000	0.000
27	A	61	VAL	0	-0.036	-0.016	31.685	0.005	0.005	0.000	0.000	0.000	0.000
28	A	62	LEU	0	-0.062	-0.012	25.669	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	63	TYR	0	0.040	0.011	27.375	0.008	0.008	0.000	0.000	0.000	0.000
30	A	64	MET	0	-0.062	-0.009	21.518	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	65	ALA	0	-0.002	-0.006	21.517	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	66	LYS	1	0.908	0.967	20.074	-0.045	-0.045	0.000	0.000	0.000	0.000
33	A	67	THR	0	0.007	-0.005	15.561	-0.021	-0.021	0.000	0.000	0.000	0.000
34	A	68	VAL	0	-0.022	-0.009	16.207	0.034	0.034	0.000	0.000	0.000	0.000
35	A	69	VAL	0	-0.006	-0.007	10.310	-0.028	-0.028	0.000	0.000	0.000	0.000
36	A	70	ALA	0	0.014	0.010	12.428	0.008	0.008	0.000	0.000	0.000	0.000
37	A	71	PRO	0	0.060	0.022	9.994	-0.013	-0.013	0.000	0.000	0.000	0.000
38	A	72	SER	0	-0.041	0.011	11.877	0.053	0.053	0.000	0.000	0.000	0.000
39	A	73	THR	0	0.018	-0.018	13.637	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	74	GLU	-1	-0.932	-0.959	15.094	-0.258	-0.258	0.000	0.000	0.000	0.000
41	A	75	GLY	0	0.033	0.029	10.978	-0.017	-0.017	0.000	0.000	0.000	0.000
42	A	76	GLY	0	-0.007	-0.013	9.619	-0.031	-0.031	0.000	0.000	0.000	0.000
43	A	77	LEU	0	-0.064	-0.028	7.819	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	78	ASN	0	0.032	0.016	12.168	0.020	0.020	0.000	0.000	0.000	0.000
45	A	79	LEU	0	0.000	-0.010	12.521	0.005	0.005	0.000	0.000	0.000	0.000
46	A	80	THR	0	0.007	0.011	16.251	0.005	0.005	0.000	0.000	0.000	0.000
47	A	81	SER	0	-0.033	-0.033	19.177	0.011	0.011	0.000	0.000	0.000	0.000
48	A	82	THR	0	-0.024	-0.003	21.081	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	83	PHE	0	-0.009	-0.025	24.104	0.009	0.009	0.000	0.000	0.000	0.000
50	A	84	LEU	0	0.047	0.036	26.261	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	85	ARG	1	0.814	0.909	29.781	0.034	0.034	0.000	0.000	0.000	0.000
52	A	86	LYS	1	0.984	0.967	31.394	0.020	0.020	0.000	0.000	0.000	0.000
53	A	87	ASN	0	0.027	0.023	34.754	0.000	0.000	0.000	0.000	0.000	0.000
54	A	88	GLN	0	-0.003	-0.007	33.227	0.002	0.002	0.000	0.000	0.000	0.000
55	A	89	CYS	0	-0.121	-0.060	28.277	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	90	GLU	-1	-0.758	-0.868	28.648	-0.032	-0.032	0.000	0.000	0.000	0.000
57	A	91	THR	0	0.004	-0.017	23.953	0.007	0.007	0.000	0.000	0.000	0.000
58	A	92	LYS	1	0.861	0.941	22.643	0.094	0.094	0.000	0.000	0.000	0.000
59	A	93	ILE	0	0.033	0.015	19.898	0.004	0.004	0.000	0.000	0.000	0.000
60	A	94	MET	0	-0.037	-0.006	18.184	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	95	VAL	0	0.062	0.029	16.728	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	96	LEU	0	-0.037	-0.004	11.769	0.004	0.004	0.000	0.000	0.000	0.000
63	A	97	GLN	0	0.061	0.018	13.397	-0.016	-0.016	0.000	0.000	0.000	0.000
64	A	98	PRO	0	0.031	0.024	11.297	-0.046	-0.046	0.000	0.000	0.000	0.000
65	A	99	ALA	0	-0.036	-0.028	12.018	0.060	0.060	0.000	0.000	0.000	0.000
66	A	100	GLY	0	0.006	0.006	13.110	-0.030	-0.030	0.000	0.000	0.000	0.000
67	A	101	ALA	0	0.013	0.009	8.808	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	102	PRO	0	0.015	-0.002	4.307	-0.013	0.086	-0.001	-0.009	-0.089	0.000
69	A	103	GLY	0	0.017	0.017	5.632	-0.786	-0.786	0.000	0.000	0.000	0.000
70	A	104	HIS	0	-0.009	-0.006	6.325	0.548	0.548	0.000	0.000	0.000	0.000
71	A	105	TYR	0	-0.045	-0.048	6.925	-0.031	-0.031	0.000	0.000	0.000	0.000
72	A	106	THR	0	-0.009	0.001	12.760	0.040	0.040	0.000	0.000	0.000	0.000
73	A	107	TYR	0	0.006	-0.009	16.457	0.019	0.019	0.000	0.000	0.000	0.000
74	A	108	SER	0	0.064	0.038	18.448	0.010	0.010	0.000	0.000	0.000	0.000
75	A	109	SER	0	-0.007	0.010	22.138	0.015	0.015	0.000	0.000	0.000	0.000
76	A	110	PRO	0	-0.026	-0.013	23.876	0.007	0.007	0.000	0.000	0.000	0.000
77	A	111	HIS	0	0.027	-0.017	27.027	0.008	0.008	0.000	0.000	0.000	0.000
78	A	112	SER	0	-0.028	0.006	26.604	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	113	GLY	0	-0.001	0.009	27.476	0.003	0.003	0.000	0.000	0.000	0.000
80	A	114	SER	0	-0.008	-0.015	25.961	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	115	ILE	0	0.032	0.016	20.748	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	116	HIS	0	-0.039	-0.026	19.133	0.002	0.002	0.000	0.000	0.000	0.000
83	A	117	SER	0	-0.010	-0.009	16.101	-0.022	-0.022	0.000	0.000	0.000	0.000
84	A	118	VAL	0	-0.026	-0.022	12.366	0.025	0.025	0.000	0.000	0.000	0.000
85	A	119	SER	0	0.030	0.027	10.261	-0.071	-0.071	0.000	0.000	0.000	0.000
86	A	120	VAL	0	-0.018	-0.018	6.464	0.235	0.235	0.000	0.000	0.000	0.000
87	A	121	VAL	0	-0.050	-0.011	7.989	-0.255	-0.255	0.000	0.000	0.000	0.000
88	A	122	GLU	-1	-0.769	-0.851	7.658	0.363	0.363	0.000	0.000	0.000	0.000
89	A	123	ALA	0	-0.024	-0.015	6.376	-0.160	-0.160	0.000	0.000	0.000	0.000
90	A	124	ASN	0	0.019	0.031	6.532	1.287	1.287	0.000	0.000	0.000	0.000
91	A	125	TYR	0	0.018	-0.002	5.045	-0.486	-0.486	0.000	0.000	0.000	0.000
92	A	126	ASP	-1	-0.841	-0.914	7.375	0.947	0.947	0.000	0.000	0.000	0.000
93	A	127	GLU	-1	-0.925	-0.968	10.642	0.625	0.625	0.000	0.000	0.000	0.000
94	A	128	TYR	0	-0.050	-0.069	10.868	-0.160	-0.160	0.000	0.000	0.000	0.000
95	A	129	ALA	0	0.032	0.013	9.480	0.283	0.283	0.000	0.000	0.000	0.000
96	A	130	LEU	0	-0.009	0.008	10.530	-0.100	-0.100	0.000	0.000	0.000	0.000
97	A	131	LEU	0	-0.003	-0.005	10.019	-0.127	-0.127	0.000	0.000	0.000	0.000
98	A	132	PHE	0	0.011	-0.001	13.049	0.070	0.070	0.000	0.000	0.000	0.000
99	A	133	SER	0	0.005	0.007	14.628	-0.077	-0.077	0.000	0.000	0.000	0.000
100	A	134	ARG	1	0.971	0.996	15.216	0.448	0.448	0.000	0.000	0.000	0.000
101	A	135	GLY	0	0.074	0.023	19.842	-0.022	-0.022	0.000	0.000	0.000	0.000
102	A	136	THR	0	-0.044	-0.039	22.768	0.003	0.003	0.000	0.000	0.000	0.000
103	A	137	LYS	1	0.920	0.981	26.131	0.088	0.088	0.000	0.000	0.000	0.000
104	A	138	GLY	0	0.051	0.026	29.215	0.004	0.004	0.000	0.000	0.000	0.000
105	A	139	PRO	0	-0.008	-0.011	30.064	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	140	GLY	0	0.080	0.062	30.237	0.009	0.009	0.000	0.000	0.000	0.000
107	A	141	GLN	0	-0.092	-0.050	30.614	0.006	0.006	0.000	0.000	0.000	0.000
108	A	142	ASP	-1	-0.888	-0.952	25.868	-0.139	-0.139	0.000	0.000	0.000	0.000
109	A	143	PHE	0	-0.093	-0.039	22.388	0.014	0.014	0.000	0.000	0.000	0.000
110	A	144	ARG	1	0.963	0.970	21.186	0.101	0.101	0.000	0.000	0.000	0.000
111	A	145	MET	0	-0.031	-0.011	19.354	0.030	0.030	0.000	0.000	0.000	0.000
112	A	146	ALA	0	0.028	0.035	17.572	-0.037	-0.037	0.000	0.000	0.000	0.000
113	A	147	THR	0	-0.022	-0.029	15.964	0.022	0.022	0.000	0.000	0.000	0.000
114	A	148	LEU	0	0.004	0.018	14.826	-0.009	-0.009	0.000	0.000	0.000	0.000
115	A	149	TYR	0	0.006	-0.006	13.067	-0.035	-0.035	0.000	0.000	0.000	0.000
116	A	150	SER	0	0.016	-0.014	14.440	0.110	0.110	0.000	0.000	0.000	0.000
117	A	151	ARG	1	0.831	0.913	8.960	-0.601	-0.601	0.000	0.000	0.000	0.000
118	A	152	THR	0	-0.037	-0.018	15.044	-0.042	-0.042	0.000	0.000	0.000	0.000
119	A	153	GLN	0	0.010	-0.010	18.702	-0.019	-0.019	0.000	0.000	0.000	0.000
120	A	154	THR	0	0.003	0.008	21.726	-0.025	-0.025	0.000	0.000	0.000	0.000
121	A	155	LEU	0	0.003	-0.003	18.268	0.035	0.035	0.000	0.000	0.000	0.000
122	A	156	LYS	1	0.921	0.958	17.035	-0.569	-0.569	0.000	0.000	0.000	0.000
123	A	157	ASP	-1	-0.765	-0.873	21.019	0.181	0.181	0.000	0.000	0.000	0.000
124	A	158	GLU	-1	-0.783	-0.898	19.538	0.317	0.317	0.000	0.000	0.000	0.000
125	A	159	LEU	0	-0.063	-0.039	14.803	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	160	LYS	1	0.822	0.903	18.605	-0.201	-0.201	0.000	0.000	0.000	0.000
127	A	161	GLU	-1	-0.882	-0.939	21.440	0.134	0.134	0.000	0.000	0.000	0.000
128	A	162	LYS	1	0.847	0.924	13.027	-0.433	-0.433	0.000	0.000	0.000	0.000
129	A	163	PHE	0	-0.015	0.001	17.298	-0.041	-0.041	0.000	0.000	0.000	0.000
130	A	164	THR	0	0.000	-0.010	18.747	-0.045	-0.045	0.000	0.000	0.000	0.000
131	A	165	THR	0	-0.009	-0.016	19.625	-0.027	-0.027	0.000	0.000	0.000	0.000
132	A	166	PHE	0	-0.005	-0.012	15.413	-0.032	-0.032	0.000	0.000	0.000	0.000
133	A	167	SER	0	-0.002	-0.026	18.478	-0.039	-0.039	0.000	0.000	0.000	0.000
134	A	168	LYS	1	0.849	0.915	21.027	-0.050	-0.050	0.000	0.000	0.000	0.000
135	A	169	ALA	0	-0.066	-0.010	19.757	-0.010	-0.010	0.000	0.000	0.000	0.000
136	A	170	GLN	0	-0.022	-0.010	18.257	-0.035	-0.035	0.000	0.000	0.000	0.000
137	A	171	GLY	0	-0.037	-0.016	21.913	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	172	LEU	0	-0.103	-0.043	22.236	0.000	0.000	0.000	0.000	0.000	0.000
139	A	173	THR	0	0.035	-0.011	25.838	0.011	0.011	0.000	0.000	0.000	0.000
140	A	174	GLU	-1	-0.767	-0.884	27.693	0.039	0.039	0.000	0.000	0.000	0.000
141	A	175	GLU	-1	-0.929	-0.933	28.895	-0.006	-0.006	0.000	0.000	0.000	0.000
142	A	176	ASP	-1	-0.836	-0.900	27.075	-0.036	-0.036	0.000	0.000	0.000	0.000
143	A	177	ILE	0	-0.046	-0.037	23.594	-0.006	-0.006	0.000	0.000	0.000	0.000
144	A	178	VAL	0	-0.034	-0.016	24.952	0.004	0.004	0.000	0.000	0.000	0.000
145	A	179	PHE	0	0.000	0.002	21.209	0.003	0.003	0.000	0.000	0.000	0.000
146	A	180	LEU	0	-0.056	-0.026	21.950	-0.004	-0.004	0.000	0.000	0.000	0.000
147	A	181	PRO	0	0.045	0.039	25.472	0.016	0.016	0.000	0.000	0.000	0.000
148	A	182	GLN	0	0.025	-0.006	25.671	-0.009	-0.009	0.000	0.000	0.000	0.000
149	A	183	PRO	0	-0.076	-0.019	26.468	-0.005	-0.005	0.000	0.000	0.000	0.000
150	A	184	ASP	-1	-0.889	-0.936	29.518	0.058	0.058	0.000	0.000	0.000	0.000
151	A	185	LYS	1	0.927	0.954	31.184	-0.021	-0.021	0.000	0.000	0.000	0.000
152	A	187	ILE	0	-0.019	-0.015	23.357	-0.003	-0.003	0.000	0.000	0.000	0.000
153	A	188	GLN	0	-0.039	-0.008	24.946	0.008	0.008	0.000	0.000	0.000	0.000
154	A	189	GLU	-1	-0.778	-0.874	26.304	0.088	0.088	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:35:GLN)