FMO DATABASE

FMODB ID: 94VL2

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	OptAll
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	-1500574.315665
FMO2-HF: Nuclear repulsion	1439691.430317
FMO2-HF: Total energy	-60882.885348
FMO2-MP2: Total energy	-61060.301415

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.
-7.96	-3.057	0.567	-1.769	-3.702	0.007

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 : 0.054 / 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	-0.863	-0.939	3.803	-3.297	-1.526	0.001	-0.670	-1.102	0.001
4	A	38	LYS	1	0.875	0.952	3.583	-2.411	-1.670	0.014	-0.179	-0.577	0.000
5	A	39	PHE	0	-0.011	-0.017	2.591	-2.209	-0.087	0.554	-0.912	-1.764	0.006
6	A	40	LEU	0	0.009	0.039	7.275	-0.054	-0.054	0.000	0.000	0.000	0.000
7	A	41	GLY	0	0.028	0.020	10.171	0.185	0.185	0.000	0.000	0.000	0.000
8	A	42	ARG	1	0.887	0.937	13.663	-0.427	-0.427	0.000	0.000	0.000	0.000
9	A	43	TRP	0	-0.033	-0.006	9.043	0.111	0.111	0.000	0.000	0.000	0.000
10	A	44	TYR	0	-0.002	-0.010	15.658	-0.078	-0.078	0.000	0.000	0.000	0.000
11	A	45	SER	0	-0.001	-0.003	17.709	0.047	0.047	0.000	0.000	0.000	0.000
12	A	46	ALA	0	0.041	0.009	18.784	-0.034	-0.034	0.000	0.000	0.000	0.000
13	A	47	GLY	0	0.006	0.009	19.710	-0.020	-0.020	0.000	0.000	0.000	0.000
14	A	48	LEU	0	-0.048	-0.022	19.974	0.010	0.010	0.000	0.000	0.000	0.000
15	A	49	ALA	0	0.054	0.026	21.973	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	50	SER	0	-0.022	-0.030	22.704	-0.012	-0.012	0.000	0.000	0.000	0.000
17	A	51	ASN	0	0.072	0.040	25.213	0.003	0.003	0.000	0.000	0.000	0.000
18	A	52	SER	0	-0.025	-0.009	27.176	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	53	SER	0	0.055	0.017	29.025	0.007	0.007	0.000	0.000	0.000	0.000
20	A	54	TRP	0	-0.035	0.000	26.019	0.005	0.005	0.000	0.000	0.000	0.000
21	A	55	PHE	0	0.027	0.008	25.852	0.005	0.005	0.000	0.000	0.000	0.000
22	A	56	ARG	1	0.883	0.910	28.783	-0.028	-0.028	0.000	0.000	0.000	0.000
23	A	57	GLU	-1	-0.926	-0.962	31.841	0.029	0.029	0.000	0.000	0.000	0.000
24	A	58	LYS	1	0.864	0.929	30.288	-0.043	-0.043	0.000	0.000	0.000	0.000
25	A	59	LYS	1	0.811	0.902	28.897	-0.092	-0.092	0.000	0.000	0.000	0.000
26	A	60	ALA	0	0.008	0.012	30.331	0.009	0.009	0.000	0.000	0.000	0.000
27	A	61	VAL	0	-0.039	-0.020	32.219	0.001	0.001	0.000	0.000	0.000	0.000
28	A	62	LEU	0	-0.064	-0.016	26.085	0.000	0.000	0.000	0.000	0.000	0.000
29	A	63	TYR	0	0.039	0.012	27.544	0.004	0.004	0.000	0.000	0.000	0.000
30	A	64	MET	0	-0.072	-0.015	21.723	0.007	0.007	0.000	0.000	0.000	0.000
31	A	65	ALA	0	-0.009	-0.006	21.922	-0.021	-0.021	0.000	0.000	0.000	0.000
32	A	66	LYS	1	0.904	0.964	20.057	-0.152	-0.152	0.000	0.000	0.000	0.000
33	A	67	THR	0	0.010	-0.005	15.490	-0.044	-0.044	0.000	0.000	0.000	0.000
34	A	68	VAL	0	-0.018	-0.004	16.228	0.054	0.054	0.000	0.000	0.000	0.000
35	A	69	VAL	0	-0.012	0.006	10.226	-0.052	-0.052	0.000	0.000	0.000	0.000
36	A	70	ALA	0	0.014	0.005	12.636	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	71	PRO	0	0.087	0.028	9.735	0.016	0.016	0.000	0.000	0.000	0.000
38	A	72	SER	0	-0.060	-0.026	11.590	0.031	0.031	0.000	0.000	0.000	0.000
39	A	73	THR	0	0.009	-0.006	13.355	-0.029	-0.029	0.000	0.000	0.000	0.000
40	A	74	GLU	-1	-0.857	-0.918	14.463	-0.192	-0.192	0.000	0.000	0.000	0.000
41	A	75	GLY	0	0.006	0.016	10.405	-0.030	-0.030	0.000	0.000	0.000	0.000
42	A	76	GLY	0	-0.010	0.007	9.167	0.017	0.017	0.000	0.000	0.000	0.000
43	A	77	LEU	0	-0.035	-0.018	7.625	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	78	ASN	0	0.031	0.014	11.901	0.011	0.011	0.000	0.000	0.000	0.000
45	A	79	LEU	0	-0.007	-0.013	12.389	0.029	0.029	0.000	0.000	0.000	0.000
46	A	80	THR	0	0.010	0.005	16.096	-0.024	-0.024	0.000	0.000	0.000	0.000
47	A	81	SER	0	-0.015	-0.021	18.909	0.024	0.024	0.000	0.000	0.000	0.000
48	A	82	THR	0	-0.031	-0.019	20.816	-0.021	-0.021	0.000	0.000	0.000	0.000
49	A	83	PHE	0	-0.034	-0.022	23.890	0.019	0.019	0.000	0.000	0.000	0.000
50	A	84	LEU	0	0.053	0.032	26.118	-0.012	-0.012	0.000	0.000	0.000	0.000
51	A	85	ARG	1	0.809	0.891	29.452	-0.052	-0.052	0.000	0.000	0.000	0.000
52	A	86	LYS	1	0.981	0.964	31.678	-0.047	-0.047	0.000	0.000	0.000	0.000
53	A	87	ASN	0	0.032	0.029	35.332	0.000	0.000	0.000	0.000	0.000	0.000
54	A	88	GLN	0	-0.011	0.007	33.404	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	89	CYS	0	-0.039	-0.021	28.151	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	90	GLU	-1	-0.765	-0.857	29.032	0.048	0.048	0.000	0.000	0.000	0.000
57	A	91	THR	0	-0.003	-0.024	23.713	0.017	0.017	0.000	0.000	0.000	0.000
58	A	92	LYS	1	0.832	0.927	22.214	-0.061	-0.061	0.000	0.000	0.000	0.000
59	A	93	ILE	0	0.033	0.025	20.074	0.015	0.015	0.000	0.000	0.000	0.000
60	A	94	MET	0	-0.013	0.008	18.054	-0.016	-0.016	0.000	0.000	0.000	0.000
61	A	95	VAL	0	0.032	0.013	16.515	0.006	0.006	0.000	0.000	0.000	0.000
62	A	96	LEU	0	-0.030	0.000	11.912	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	97	GLN	0	0.047	0.006	13.109	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	98	PRO	0	0.035	0.016	10.922	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	99	ALA	0	-0.040	-0.026	12.406	0.008	0.008	0.000	0.000	0.000	0.000
66	A	100	GLY	0	0.002	0.004	13.423	-0.025	-0.025	0.000	0.000	0.000	0.000
67	A	101	ALA	0	0.005	0.003	9.134	-0.061	-0.061	0.000	0.000	0.000	0.000
68	A	102	PRO	0	0.031	0.004	4.583	0.073	0.156	-0.001	-0.004	-0.078	0.000
69	A	103	GLY	0	0.008	0.012	6.073	-0.596	-0.596	0.000	0.000	0.000	0.000
70	A	104	HIS	0	-0.012	-0.006	6.731	0.387	0.387	0.000	0.000	0.000	0.000
71	A	105	TYR	0	-0.040	-0.034	6.851	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	106	THR	0	-0.043	-0.017	12.882	0.008	0.008	0.000	0.000	0.000	0.000
73	A	107	TYR	0	0.048	0.020	16.609	0.022	0.022	0.000	0.000	0.000	0.000
74	A	108	SER	0	0.054	0.029	18.708	-0.008	-0.008	0.000	0.000	0.000	0.000
75	A	109	SER	0	0.002	0.017	22.475	0.016	0.016	0.000	0.000	0.000	0.000
76	A	110	PRO	0	0.015	0.001	24.129	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	111	HIS	0	-0.036	-0.041	27.024	0.011	0.011	0.000	0.000	0.000	0.000
78	A	112	SER	0	0.015	0.006	26.886	0.000	0.000	0.000	0.000	0.000	0.000
79	A	113	GLY	0	0.001	0.022	28.106	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	114	SER	0	-0.013	-0.013	26.128	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	115	ILE	0	0.021	0.014	21.345	0.007	0.007	0.000	0.000	0.000	0.000
82	A	116	HIS	0	-0.045	-0.035	19.539	0.008	0.008	0.000	0.000	0.000	0.000
83	A	117	SER	0	-0.015	-0.015	16.353	-0.020	-0.020	0.000	0.000	0.000	0.000
84	A	118	VAL	0	-0.024	-0.019	12.936	0.024	0.024	0.000	0.000	0.000	0.000
85	A	119	SER	0	-0.012	-0.002	10.963	-0.069	-0.069	0.000	0.000	0.000	0.000
86	A	120	VAL	0	0.013	-0.005	6.439	0.163	0.163	0.000	0.000	0.000	0.000
87	A	121	VAL	0	-0.048	-0.007	8.714	-0.243	-0.243	0.000	0.000	0.000	0.000
88	A	122	GLU	-1	-0.779	-0.862	8.139	0.534	0.534	0.000	0.000	0.000	0.000
89	A	123	ALA	0	-0.026	-0.017	6.330	-0.045	-0.045	0.000	0.000	0.000	0.000
90	A	124	ASN	0	0.010	0.015	6.969	1.118	1.118	0.000	0.000	0.000	0.000
91	A	125	TYR	0	-0.001	-0.020	5.101	-0.679	-0.493	-0.001	-0.004	-0.181	0.000
92	A	126	ASP	-1	-0.812	-0.887	7.370	1.134	1.134	0.000	0.000	0.000	0.000
93	A	127	GLU	-1	-0.897	-0.929	10.520	0.740	0.740	0.000	0.000	0.000	0.000
94	A	128	TYR	0	-0.060	-0.070	10.822	-0.197	-0.197	0.000	0.000	0.000	0.000
95	A	129	ALA	0	0.040	0.008	9.560	0.405	0.405	0.000	0.000	0.000	0.000
96	A	130	LEU	0	-0.014	0.010	10.763	-0.204	-0.204	0.000	0.000	0.000	0.000
97	A	131	LEU	0	-0.010	-0.006	10.192	-0.039	-0.039	0.000	0.000	0.000	0.000
98	A	132	PHE	0	0.015	-0.001	13.274	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	133	SER	0	-0.001	0.008	15.060	-0.062	-0.062	0.000	0.000	0.000	0.000
100	A	134	ARG	1	0.982	0.993	15.832	0.229	0.229	0.000	0.000	0.000	0.000
101	A	135	GLY	0	0.046	0.020	20.378	-0.016	-0.016	0.000	0.000	0.000	0.000
102	A	136	THR	0	-0.035	-0.024	23.247	0.002	0.002	0.000	0.000	0.000	0.000
103	A	137	LYS	1	0.937	0.981	26.718	0.010	0.010	0.000	0.000	0.000	0.000
104	A	138	GLY	0	0.040	0.023	30.101	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	139	PRO	0	0.015	-0.007	30.836	0.002	0.002	0.000	0.000	0.000	0.000
106	A	140	GLY	0	0.041	0.038	31.104	0.005	0.005	0.000	0.000	0.000	0.000
107	A	141	GLN	0	-0.051	-0.027	31.273	0.010	0.010	0.000	0.000	0.000	0.000
108	A	142	ASP	-1	-0.926	-0.959	26.147	-0.053	-0.053	0.000	0.000	0.000	0.000
109	A	143	PHE	0	-0.089	-0.046	22.999	0.011	0.011	0.000	0.000	0.000	0.000
110	A	144	ARG	1	0.929	0.960	21.753	0.001	0.001	0.000	0.000	0.000	0.000
111	A	145	MET	0	-0.004	0.001	19.746	0.013	0.013	0.000	0.000	0.000	0.000
112	A	146	ALA	0	0.046	0.051	17.864	-0.008	-0.008	0.000	0.000	0.000	0.000
113	A	147	THR	0	-0.040	-0.046	16.522	-0.014	-0.014	0.000	0.000	0.000	0.000
114	A	148	LEU	0	0.014	0.023	14.634	0.031	0.031	0.000	0.000	0.000	0.000
115	A	149	TYR	0	0.019	0.005	13.239	-0.071	-0.071	0.000	0.000	0.000	0.000
116	A	150	SER	0	0.018	-0.002	14.067	0.151	0.151	0.000	0.000	0.000	0.000
117	A	151	ARG	1	0.829	0.899	9.365	-1.204	-1.204	0.000	0.000	0.000	0.000
118	A	152	THR	0	-0.041	-0.027	15.485	-0.062	-0.062	0.000	0.000	0.000	0.000
119	A	153	GLN	0	0.034	0.009	19.024	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	154	THR	0	0.017	0.017	22.011	-0.035	-0.035	0.000	0.000	0.000	0.000
121	A	155	LEU	0	-0.011	-0.005	17.897	0.051	0.051	0.000	0.000	0.000	0.000
122	A	156	LYS	1	0.926	0.953	16.654	-0.726	-0.726	0.000	0.000	0.000	0.000
123	A	157	ASP	-1	-0.776	-0.883	20.958	0.271	0.271	0.000	0.000	0.000	0.000
124	A	158	GLU	-1	-0.788	-0.903	19.481	0.426	0.426	0.000	0.000	0.000	0.000
125	A	159	LEU	0	-0.066	-0.028	14.872	0.004	0.004	0.000	0.000	0.000	0.000
126	A	160	LYS	1	0.827	0.909	18.491	-0.297	-0.297	0.000	0.000	0.000	0.000
127	A	161	GLU	-1	-0.873	-0.927	21.549	0.214	0.214	0.000	0.000	0.000	0.000
128	A	162	LYS	1	0.836	0.916	13.345	-0.594	-0.594	0.000	0.000	0.000	0.000
129	A	163	PHE	0	-0.018	-0.005	17.207	-0.036	-0.036	0.000	0.000	0.000	0.000
130	A	164	THR	0	-0.010	-0.020	18.834	-0.046	-0.046	0.000	0.000	0.000	0.000
131	A	165	THR	0	-0.022	-0.021	20.060	-0.035	-0.035	0.000	0.000	0.000	0.000
132	A	166	PHE	0	0.006	-0.004	15.718	-0.029	-0.029	0.000	0.000	0.000	0.000
133	A	167	SER	0	0.000	-0.019	18.885	-0.036	-0.036	0.000	0.000	0.000	0.000
134	A	168	LYS	1	0.846	0.908	21.494	-0.131	-0.131	0.000	0.000	0.000	0.000
135	A	169	ALA	0	-0.015	-0.001	20.109	-0.017	-0.017	0.000	0.000	0.000	0.000
136	A	170	GLN	0	-0.049	-0.005	18.242	-0.034	-0.034	0.000	0.000	0.000	0.000
137	A	171	GLY	0	0.007	0.010	21.993	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	172	LEU	0	-0.094	-0.047	22.543	-0.004	-0.004	0.000	0.000	0.000	0.000
139	A	173	THR	0	0.014	-0.024	26.245	0.009	0.009	0.000	0.000	0.000	0.000
140	A	174	GLU	-1	-0.808	-0.909	27.849	0.113	0.113	0.000	0.000	0.000	0.000
141	A	175	GLU	-1	-0.917	-0.939	29.326	0.063	0.063	0.000	0.000	0.000	0.000
142	A	176	ASP	-1	-0.797	-0.847	27.301	0.049	0.049	0.000	0.000	0.000	0.000
143	A	177	ILE	0	0.002	-0.011	24.006	0.006	0.006	0.000	0.000	0.000	0.000
144	A	178	VAL	0	-0.027	-0.008	25.090	-0.009	-0.009	0.000	0.000	0.000	0.000
145	A	179	PHE	0	0.015	0.010	20.993	0.018	0.018	0.000	0.000	0.000	0.000
146	A	180	LEU	0	-0.051	-0.017	21.911	-0.017	-0.017	0.000	0.000	0.000	0.000
147	A	181	PRO	0	0.042	0.027	25.270	0.020	0.020	0.000	0.000	0.000	0.000
148	A	182	GLN	0	0.021	-0.009	25.575	-0.009	-0.009	0.000	0.000	0.000	0.000
149	A	183	PRO	0	-0.066	-0.017	26.798	-0.012	-0.012	0.000	0.000	0.000	0.000
150	A	184	ASP	-1	-0.887	-0.944	29.885	0.122	0.122	0.000	0.000	0.000	0.000
151	A	185	LYS	1	0.886	0.935	31.253	-0.090	-0.090	0.000	0.000	0.000	0.000
152	A	187	ILE	0	-0.061	-0.046	23.463	0.005	0.005	0.000	0.000	0.000	0.000
153	A	188	GLN	0	-0.030	-0.008	25.161	0.018	0.018	0.000	0.000	0.000	0.000
154	A	189	GLU	-1	-0.769	-0.866	26.679	0.183	0.183	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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