FMO DATABASE

FMODB ID: LN339

Calculation Name: 2PRX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2PRX

Chain ID: A

ChEMBL ID:

UniProt ID: A3QJH3

Base Structure: X-ray

Registration Date: 2023-09-23

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	123
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-979704.88566
FMO2-HF: Nuclear repulsion	932340.793579
FMO2-HF: Total energy	-47364.092081
FMO2-MP2: Total energy	-47499.604153

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:6:PHE)

Summations of interaction energy for fragment #1(A:6:PHE)

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.
-20.189	-6.065	10.235	-8.108	-16.254	-0.005

Interaction energy analysis for fragmet #1(A:6:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.007 / q_NPA : -0.013

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	8	ASP	-1	-0.857	-0.892	2.771	-7.838	-2.615	2.702	-2.883	-5.043	0.009
4	A	9	ALA	0	-0.073	-0.024	2.261	-1.975	-0.681	3.880	-1.662	-3.513	0.007
5	A	10	TYR	0	-0.051	-0.047	2.298	-5.166	-2.990	2.560	-1.545	-3.191	-0.008
6	A	11	PRO	0	0.025	0.012	5.843	0.112	0.112	0.000	0.000	0.000	0.000
7	A	12	ASP	-1	-0.810	-0.905	6.520	0.302	0.302	0.000	0.000	0.000	0.000
8	A	13	ASP	-1	-0.936	-0.955	8.181	0.220	0.220	0.000	0.000	0.000	0.000
9	A	14	LEU	0	-0.092	-0.085	11.344	-0.017	-0.017	0.000	0.000	0.000	0.000
10	A	15	SER	0	0.013	0.023	9.370	-0.051	-0.051	0.000	0.000	0.000	0.000
11	A	16	HIS	0	-0.072	-0.027	10.792	0.012	0.012	0.000	0.000	0.000	0.000
12	A	17	CYS	0	-0.001	0.041	10.586	0.017	0.017	0.000	0.000	0.000	0.000
13	A	18	TYR	0	-0.050	-0.040	12.408	-0.053	-0.053	0.000	0.000	0.000	0.000
14	A	19	GLY	0	0.042	0.023	7.757	-0.057	-0.057	0.000	0.000	0.000	0.000
15	A	30	LEU	0	-0.025	-0.034	7.756	-0.069	-0.069	0.000	0.000	0.000	0.000
16	A	31	LYS	1	0.812	0.902	4.135	0.643	0.821	-0.001	-0.013	-0.164	0.000
17	A	32	SER	0	-0.029	-0.018	3.493	0.010	0.467	0.009	-0.108	-0.358	0.000
18	A	33	TYR	0	0.008	0.004	2.664	-4.638	-1.249	0.964	-1.402	-2.951	-0.013
19	A	34	TRP	0	0.009	0.004	5.026	-0.250	-0.250	0.000	0.000	0.000	0.000
20	A	35	ARG	1	0.912	0.951	6.891	-0.209	-0.209	0.000	0.000	0.000	0.000
21	A	36	GLY	0	0.002	0.004	10.600	-0.048	-0.048	0.000	0.000	0.000	0.000
22	A	37	GLU	-1	-0.916	-0.961	10.895	0.111	0.111	0.000	0.000	0.000	0.000
23	A	38	GLN	0	0.006	0.014	11.325	0.010	0.010	0.000	0.000	0.000	0.000
24	A	39	THR	0	-0.035	-0.022	6.065	-0.026	-0.026	0.000	0.000	0.000	0.000
25	A	40	ILE	0	-0.046	-0.045	7.830	-0.087	-0.087	0.000	0.000	0.000	0.000
26	A	41	ALA	0	0.014	0.000	7.480	0.100	0.100	0.000	0.000	0.000	0.000
27	A	42	HIS	1	0.880	0.918	9.239	-0.189	-0.189	0.000	0.000	0.000	0.000
28	A	43	PHE	0	0.022	0.013	11.073	-0.026	-0.026	0.000	0.000	0.000	0.000
29	A	44	MET	0	0.027	0.040	13.704	0.005	0.005	0.000	0.000	0.000	0.000
30	A	45	PRO	0	-0.014	-0.006	16.912	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	46	LYS	1	0.972	0.996	18.174	-0.043	-0.043	0.000	0.000	0.000	0.000
32	A	47	PRO	0	0.049	0.014	21.338	0.009	0.009	0.000	0.000	0.000	0.000
33	A	48	PHE	0	0.046	0.013	22.218	0.000	0.000	0.000	0.000	0.000	0.000
34	A	49	HIS	0	-0.009	0.018	19.618	-0.005	-0.005	0.000	0.000	0.000	0.000
35	A	50	THR	0	-0.015	-0.023	23.621	0.011	0.011	0.000	0.000	0.000	0.000
36	A	51	ALA	0	-0.001	0.016	26.383	0.005	0.005	0.000	0.000	0.000	0.000
37	A	52	ILE	0	0.004	0.002	27.865	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	53	PRO	0	0.023	-0.020	29.782	0.004	0.004	0.000	0.000	0.000	0.000
39	A	54	GLY	0	0.038	0.029	29.747	0.000	0.000	0.000	0.000	0.000	0.000
40	A	55	PHE	0	0.008	0.004	26.640	0.002	0.002	0.000	0.000	0.000	0.000
41	A	56	VAL	0	-0.003	-0.009	20.497	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	57	TYR	0	-0.033	-0.005	22.327	0.010	0.010	0.000	0.000	0.000	0.000
43	A	58	GLY	0	0.095	0.031	21.762	0.015	0.015	0.000	0.000	0.000	0.000
44	A	59	GLY	0	0.024	0.000	21.090	0.019	0.019	0.000	0.000	0.000	0.000
45	A	60	LEU	0	0.017	0.048	16.652	0.022	0.022	0.000	0.000	0.000	0.000
46	A	61	ILE	0	0.000	0.003	16.849	0.039	0.039	0.000	0.000	0.000	0.000
47	A	62	ALA	0	0.001	-0.009	16.607	0.043	0.043	0.000	0.000	0.000	0.000
48	A	63	SER	0	-0.035	-0.045	15.507	0.031	0.031	0.000	0.000	0.000	0.000
49	A	64	LEU	0	-0.007	-0.005	12.351	0.080	0.080	0.000	0.000	0.000	0.000
50	A	65	ILE	0	0.028	-0.002	11.581	0.151	0.151	0.000	0.000	0.000	0.000
51	A	66	ASP	-1	-0.858	-0.914	11.756	0.633	0.633	0.000	0.000	0.000	0.000
52	A	67	CYS	0	0.031	0.010	8.889	0.098	0.098	0.000	0.000	0.000	0.000
53	A	68	HIS	0	0.020	0.018	7.362	0.912	0.912	0.000	0.000	0.000	0.000
54	A	69	GLY	0	0.019	0.031	7.140	0.388	0.388	0.000	0.000	0.000	0.000
55	A	70	THR	0	0.021	0.000	7.123	-0.168	-0.168	0.000	0.000	0.000	0.000
56	A	71	GLY	0	-0.030	-0.006	4.066	-0.280	-0.048	0.008	-0.108	-0.132	0.001
57	A	72	SER	0	-0.027	-0.052	3.720	-1.346	-0.921	0.013	-0.148	-0.290	-0.001
58	A	73	ALA	0	-0.025	0.000	5.706	-0.562	-0.562	0.000	0.000	0.000	0.000
59	A	74	SER	0	-0.062	-0.098	4.131	-0.280	-0.190	-0.001	-0.012	-0.078	0.000
60	A	75	ALA	0	-0.024	-0.001	2.676	-1.166	-0.538	0.102	-0.215	-0.515	0.000
61	A	76	ALA	0	0.002	-0.004	4.546	0.189	0.221	-0.001	-0.012	-0.019	0.000
62	A	77	ALA	0	-0.066	-0.028	8.061	0.026	0.026	0.000	0.000	0.000	0.000
63	A	78	GLN	0	-0.053	-0.011	6.179	-0.215	-0.215	0.000	0.000	0.000	0.000
64	A	92	PRO	0	-0.015	0.002	6.118	0.017	0.017	0.000	0.000	0.000	0.000
65	A	93	ARG	1	1.036	1.058	6.781	0.009	0.009	0.000	0.000	0.000	0.000
66	A	94	PHE	0	-0.038	-0.009	8.088	-0.055	-0.055	0.000	0.000	0.000	0.000
67	A	95	VAL	0	0.042	0.019	9.812	0.083	0.083	0.000	0.000	0.000	0.000
68	A	96	THR	0	0.042	0.008	12.476	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	97	ALA	0	-0.084	-0.038	14.412	-0.043	-0.043	0.000	0.000	0.000	0.000
70	A	98	ALA	0	-0.011	-0.015	17.437	-0.024	-0.024	0.000	0.000	0.000	0.000
71	A	99	LEU	0	0.016	-0.001	15.199	0.035	0.035	0.000	0.000	0.000	0.000
72	A	100	ASN	0	-0.046	-0.003	18.263	-0.022	-0.022	0.000	0.000	0.000	0.000
73	A	101	ILE	0	0.023	0.001	18.026	0.024	0.024	0.000	0.000	0.000	0.000
74	A	102	ASP	-1	-0.904	-0.923	21.273	0.131	0.131	0.000	0.000	0.000	0.000
75	A	103	TYR	0	-0.030	-0.039	21.446	0.013	0.013	0.000	0.000	0.000	0.000
76	A	104	LEU	0	-0.024	-0.016	23.105	-0.012	-0.012	0.000	0.000	0.000	0.000
77	A	105	ALA	0	0.025	0.010	25.624	-0.012	-0.012	0.000	0.000	0.000	0.000
78	A	106	PRO	0	-0.028	-0.004	25.659	0.009	0.009	0.000	0.000	0.000	0.000
79	A	107	THR	0	0.052	0.008	20.908	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	108	PRO	0	0.010	0.007	24.313	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	109	MET	0	-0.048	-0.017	23.487	0.007	0.007	0.000	0.000	0.000	0.000
82	A	110	GLY	0	-0.025	-0.010	23.327	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	111	VAL	0	-0.004	-0.005	21.004	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	112	GLU	-1	-0.972	-0.982	15.512	0.074	0.074	0.000	0.000	0.000	0.000
85	A	113	LEU	0	-0.012	-0.025	15.918	0.009	0.009	0.000	0.000	0.000	0.000
86	A	114	GLU	-1	-0.869	-0.915	13.823	0.199	0.199	0.000	0.000	0.000	0.000
87	A	115	LEU	0	-0.038	-0.024	11.179	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	116	VAL	0	0.036	0.023	11.210	0.064	0.064	0.000	0.000	0.000	0.000
89	A	117	GLY	0	-0.019	-0.002	10.390	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	118	GLU	-1	-0.862	-0.956	11.384	0.156	0.156	0.000	0.000	0.000	0.000
91	A	119	ILE	0	0.012	0.005	8.744	0.028	0.028	0.000	0.000	0.000	0.000
92	A	120	LYS	1	0.909	0.957	12.790	-0.209	-0.209	0.000	0.000	0.000	0.000
93	A	121	GLU	-1	-0.771	-0.905	14.832	0.070	0.070	0.000	0.000	0.000	0.000
94	A	122	VAL	0	0.010	0.025	11.915	0.026	0.026	0.000	0.000	0.000	0.000
95	A	123	LYS	1	0.825	0.901	14.427	-0.074	-0.074	0.000	0.000	0.000	0.000
96	A	124	PRO	0	0.043	0.026	13.264	0.015	0.015	0.000	0.000	0.000	0.000
97	A	125	ARG	1	0.854	0.922	13.103	-0.024	-0.024	0.000	0.000	0.000	0.000
98	A	126	LYS	1	0.916	0.951	14.289	-0.097	-0.097	0.000	0.000	0.000	0.000
99	A	127	VAL	0	0.020	0.034	9.898	-0.034	-0.034	0.000	0.000	0.000	0.000
100	A	128	VAL	0	-0.050	-0.012	13.012	0.035	0.035	0.000	0.000	0.000	0.000
101	A	129	VAL	0	-0.008	-0.009	10.123	-0.010	-0.010	0.000	0.000	0.000	0.000
102	A	130	GLU	-1	-0.961	-0.972	13.288	0.181	0.181	0.000	0.000	0.000	0.000
103	A	131	ILE	0	-0.005	0.005	11.686	0.037	0.037	0.000	0.000	0.000	0.000
104	A	132	ALA	0	-0.007	-0.002	14.272	-0.054	-0.054	0.000	0.000	0.000	0.000
105	A	133	LEU	0	0.021	0.020	15.346	0.026	0.026	0.000	0.000	0.000	0.000
106	A	134	SER	0	-0.018	-0.017	17.086	-0.038	-0.038	0.000	0.000	0.000	0.000
107	A	135	ALA	0	0.065	0.012	18.534	0.010	0.010	0.000	0.000	0.000	0.000
108	A	136	ASP	-1	-0.815	-0.902	21.486	0.085	0.085	0.000	0.000	0.000	0.000
109	A	137	GLY	0	-0.002	0.010	24.146	0.003	0.003	0.000	0.000	0.000	0.000
110	A	138	LYS	1	0.746	0.854	20.946	-0.117	-0.117	0.000	0.000	0.000	0.000
111	A	139	LEU	0	0.015	0.034	20.198	0.001	0.001	0.000	0.000	0.000	0.000
112	A	140	CYS	0	-0.016	-0.001	21.202	-0.013	-0.013	0.000	0.000	0.000	0.000
113	A	141	ALA	0	0.005	-0.004	20.000	-0.008	-0.008	0.000	0.000	0.000	0.000
114	A	142	ARG	1	0.952	0.990	18.908	-0.161	-0.161	0.000	0.000	0.000	0.000
115	A	143	GLY	0	0.045	0.025	17.112	-0.014	-0.014	0.000	0.000	0.000	0.000
116	A	144	HIS	0	-0.023	-0.020	16.904	0.018	0.018	0.000	0.000	0.000	0.000
117	A	145	MET	0	0.016	0.036	11.860	0.016	0.016	0.000	0.000	0.000	0.000
118	A	146	VAL	0	-0.028	-0.009	15.476	-0.032	-0.032	0.000	0.000	0.000	0.000
119	A	147	ALA	0	0.049	0.032	11.401	0.001	0.001	0.000	0.000	0.000	0.000
120	A	148	VAL	0	0.024	-0.003	13.400	-0.059	-0.059	0.000	0.000	0.000	0.000
121	A	149	LYS	1	0.927	0.981	11.939	0.184	0.184	0.000	0.000	0.000	0.000
122	A	150	MET	0	0.019	-0.006	11.357	-0.020	-0.020	0.000	0.000	0.000	0.000
123	A	151	PRO	0	-0.040	-0.011	13.710	-0.041	-0.041	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:PHE)