FMO DATABASE

FMODB ID: MN11Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-982161.550446
FMO2-HF: Nuclear repulsion	934796.281343
FMO2-HF: Total energy	-47365.269103
FMO2-MP2: Total energy	-47500.752566

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.
-21.967	-9.479	17.059	-10.211	-19.34	-0.023

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 : -0.011 / q_NPA : -0.019

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	-0.888	-0.928	2.615	-7.481	-2.931	3.634	-2.887	-5.297	0.004
4	A	9	ALA	0	-0.044	-0.007	2.411	-2.223	-0.208	1.439	-1.005	-2.449	0.005
5	A	10	TYR	0	-0.044	-0.050	1.999	-5.262	-6.371	7.408	-2.751	-3.548	-0.012
6	A	11	PRO	0	0.030	0.017	6.356	0.263	0.263	0.000	0.000	0.000	0.000
7	A	12	ASP	-1	-0.764	-0.866	7.582	0.527	0.527	0.000	0.000	0.000	0.000
8	A	13	ASP	-1	-0.904	-0.949	8.992	0.298	0.298	0.000	0.000	0.000	0.000
9	A	14	LEU	0	-0.055	-0.044	12.080	-0.054	-0.054	0.000	0.000	0.000	0.000
10	A	15	SER	0	-0.037	-0.015	10.522	-0.056	-0.056	0.000	0.000	0.000	0.000
11	A	16	HIS	0	-0.024	0.000	11.597	-0.028	-0.028	0.000	0.000	0.000	0.000
12	A	17	CYS	0	-0.017	0.017	10.945	0.008	0.008	0.000	0.000	0.000	0.000
13	A	18	TYR	0	-0.044	-0.024	12.308	-0.085	-0.085	0.000	0.000	0.000	0.000
14	A	19	GLY	0	-0.014	-0.011	7.465	-0.273	-0.273	0.000	0.000	0.000	0.000
15	A	30	LEU	0	-0.031	-0.023	7.681	-0.041	-0.041	0.000	0.000	0.000	0.000
16	A	31	LYS	1	0.820	0.920	3.684	0.923	1.236	0.001	-0.036	-0.279	0.000
17	A	32	SER	0	-0.015	-0.025	3.253	0.007	0.583	0.025	-0.150	-0.451	0.000
18	A	33	TYR	0	-0.019	-0.010	2.492	-7.528	-2.855	4.383	-2.938	-6.119	-0.020
19	A	34	TRP	0	-0.004	-0.006	4.439	-0.308	-0.057	-0.001	-0.010	-0.241	0.000
20	A	35	ARG	1	0.834	0.908	6.513	0.012	0.012	0.000	0.000	0.000	0.000
21	A	36	GLY	0	0.025	0.029	10.183	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	37	GLU	-1	-0.889	-0.962	10.348	0.015	0.015	0.000	0.000	0.000	0.000
23	A	38	GLN	0	-0.056	-0.021	11.095	0.009	0.009	0.000	0.000	0.000	0.000
24	A	39	THR	0	-0.012	-0.030	5.781	-0.094	-0.094	0.000	0.000	0.000	0.000
25	A	40	ILE	0	-0.038	-0.021	7.467	0.027	0.027	0.000	0.000	0.000	0.000
26	A	41	ALA	0	0.036	0.027	7.075	-0.061	-0.061	0.000	0.000	0.000	0.000
27	A	42	HIS	1	0.857	0.922	8.641	0.081	0.081	0.000	0.000	0.000	0.000
28	A	43	PHE	0	0.027	0.008	10.492	-0.049	-0.049	0.000	0.000	0.000	0.000
29	A	44	MET	0	0.040	0.030	13.199	0.020	0.020	0.000	0.000	0.000	0.000
30	A	45	PRO	0	-0.028	-0.007	16.451	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	46	LYS	1	0.985	0.996	17.331	0.029	0.029	0.000	0.000	0.000	0.000
32	A	47	PRO	0	0.044	0.001	20.999	0.010	0.010	0.000	0.000	0.000	0.000
33	A	48	PHE	0	0.036	0.019	21.652	0.002	0.002	0.000	0.000	0.000	0.000
34	A	49	HIS	0	0.001	0.014	18.507	0.000	0.000	0.000	0.000	0.000	0.000
35	A	50	THR	0	0.003	0.002	23.341	0.005	0.005	0.000	0.000	0.000	0.000
36	A	51	ALA	0	-0.049	-0.026	26.174	0.005	0.005	0.000	0.000	0.000	0.000
37	A	52	ILE	0	0.004	0.003	27.506	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	53	PRO	0	0.010	-0.012	29.420	0.000	0.000	0.000	0.000	0.000	0.000
39	A	54	GLY	0	0.040	0.032	29.232	0.000	0.000	0.000	0.000	0.000	0.000
40	A	55	PHE	0	0.003	-0.001	26.362	0.000	0.000	0.000	0.000	0.000	0.000
41	A	56	VAL	0	0.014	0.008	20.105	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	57	TYR	0	-0.003	-0.003	21.648	0.011	0.011	0.000	0.000	0.000	0.000
43	A	58	GLY	0	0.073	0.022	21.466	0.011	0.011	0.000	0.000	0.000	0.000
44	A	59	GLY	0	0.053	0.034	21.095	0.018	0.018	0.000	0.000	0.000	0.000
45	A	60	LEU	0	-0.019	0.006	16.125	0.024	0.024	0.000	0.000	0.000	0.000
46	A	61	ILE	0	0.024	0.007	16.572	0.030	0.030	0.000	0.000	0.000	0.000
47	A	62	ALA	0	0.029	0.015	16.408	0.034	0.034	0.000	0.000	0.000	0.000
48	A	63	SER	0	-0.009	-0.019	15.266	0.051	0.051	0.000	0.000	0.000	0.000
49	A	64	LEU	0	-0.046	-0.024	12.109	0.082	0.082	0.000	0.000	0.000	0.000
50	A	65	ILE	0	0.038	0.005	11.256	0.123	0.123	0.000	0.000	0.000	0.000
51	A	66	ASP	-1	-0.839	-0.892	11.861	0.700	0.700	0.000	0.000	0.000	0.000
52	A	67	CYS	0	0.019	-0.001	8.857	0.136	0.136	0.000	0.000	0.000	0.000
53	A	68	HIS	0	0.034	0.042	6.985	0.841	0.841	0.000	0.000	0.000	0.000
54	A	69	GLY	0	0.022	0.016	7.017	0.396	0.396	0.000	0.000	0.000	0.000
55	A	70	THR	0	0.010	-0.015	8.283	0.018	0.018	0.000	0.000	0.000	0.000
56	A	71	GLY	0	-0.015	0.000	4.585	-0.193	-0.097	0.000	-0.038	-0.059	0.000
57	A	72	SER	0	0.011	-0.013	3.760	0.236	0.769	0.031	-0.194	-0.371	0.000
58	A	73	ALA	0	-0.013	0.000	5.477	-0.575	-0.575	0.000	0.000	0.000	0.000
59	A	74	SER	0	-0.051	-0.034	4.341	-0.308	-0.251	-0.001	-0.014	-0.041	0.000
60	A	75	ALA	0	0.002	0.007	2.692	-1.225	-0.714	0.141	-0.178	-0.474	0.000
61	A	76	ALA	0	0.022	0.000	4.725	-0.104	-0.082	-0.001	-0.010	-0.011	0.000
62	A	77	ALA	0	-0.063	-0.030	8.237	-0.070	-0.070	0.000	0.000	0.000	0.000
63	A	78	GLN	0	-0.088	-0.030	5.995	-0.309	-0.309	0.000	0.000	0.000	0.000
64	A	92	PRO	0	-0.027	-0.008	6.381	0.019	0.019	0.000	0.000	0.000	0.000
65	A	93	ARG	1	0.956	0.972	7.690	-0.048	-0.048	0.000	0.000	0.000	0.000
66	A	94	PHE	0	-0.015	-0.012	8.390	-0.161	-0.161	0.000	0.000	0.000	0.000
67	A	95	VAL	0	0.018	0.011	10.223	0.059	0.059	0.000	0.000	0.000	0.000
68	A	96	THR	0	0.039	-0.005	12.723	-0.030	-0.030	0.000	0.000	0.000	0.000
69	A	97	ALA	0	-0.087	-0.040	14.600	-0.046	-0.046	0.000	0.000	0.000	0.000
70	A	98	ALA	0	-0.004	-0.008	17.594	-0.037	-0.037	0.000	0.000	0.000	0.000
71	A	99	LEU	0	-0.008	-0.006	15.332	0.037	0.037	0.000	0.000	0.000	0.000
72	A	100	ASN	0	-0.040	-0.005	18.300	-0.032	-0.032	0.000	0.000	0.000	0.000
73	A	101	ILE	0	0.004	-0.016	17.698	0.022	0.022	0.000	0.000	0.000	0.000
74	A	102	ASP	-1	-0.894	-0.921	20.936	0.119	0.119	0.000	0.000	0.000	0.000
75	A	103	TYR	0	-0.045	-0.060	21.404	0.006	0.006	0.000	0.000	0.000	0.000
76	A	104	LEU	0	-0.014	-0.009	23.196	-0.011	-0.011	0.000	0.000	0.000	0.000
77	A	105	ALA	0	0.029	0.017	25.065	-0.009	-0.009	0.000	0.000	0.000	0.000
78	A	106	PRO	0	-0.024	-0.012	25.004	0.007	0.007	0.000	0.000	0.000	0.000
79	A	107	THR	0	0.030	0.016	20.483	0.001	0.001	0.000	0.000	0.000	0.000
80	A	108	PRO	0	0.015	0.007	23.755	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	109	MET	0	-0.032	-0.008	23.103	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	110	GLY	0	-0.016	-0.011	22.742	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	111	VAL	0	-0.027	-0.008	20.649	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	112	GLU	-1	-0.938	-0.975	13.901	-0.067	-0.067	0.000	0.000	0.000	0.000
85	A	113	LEU	0	-0.010	-0.010	15.642	0.015	0.015	0.000	0.000	0.000	0.000
86	A	114	GLU	-1	-0.809	-0.905	13.319	0.049	0.049	0.000	0.000	0.000	0.000
87	A	115	LEU	0	-0.023	-0.014	10.944	0.020	0.020	0.000	0.000	0.000	0.000
88	A	116	VAL	0	0.006	0.016	10.897	0.023	0.023	0.000	0.000	0.000	0.000
89	A	117	GLY	0	-0.017	-0.010	9.888	0.043	0.043	0.000	0.000	0.000	0.000
90	A	118	GLU	-1	-0.806	-0.881	10.877	0.083	0.083	0.000	0.000	0.000	0.000
91	A	119	ILE	0	0.026	0.005	8.351	0.037	0.037	0.000	0.000	0.000	0.000
92	A	120	LYS	1	0.803	0.882	12.480	-0.197	-0.197	0.000	0.000	0.000	0.000
93	A	121	GLU	-1	-0.780	-0.870	14.897	0.123	0.123	0.000	0.000	0.000	0.000
94	A	122	VAL	0	0.052	0.028	12.131	0.046	0.046	0.000	0.000	0.000	0.000
95	A	123	LYS	1	0.871	0.919	14.583	-0.134	-0.134	0.000	0.000	0.000	0.000
96	A	124	PRO	0	0.078	0.042	13.102	0.019	0.019	0.000	0.000	0.000	0.000
97	A	125	ARG	1	0.875	0.928	13.253	-0.135	-0.135	0.000	0.000	0.000	0.000
98	A	126	LYS	1	0.798	0.891	14.765	-0.147	-0.147	0.000	0.000	0.000	0.000
99	A	127	VAL	0	0.011	0.016	10.345	-0.036	-0.036	0.000	0.000	0.000	0.000
100	A	128	VAL	0	-0.074	-0.023	13.443	0.020	0.020	0.000	0.000	0.000	0.000
101	A	129	VAL	0	0.010	0.004	10.020	-0.020	-0.020	0.000	0.000	0.000	0.000
102	A	130	GLU	-1	-0.780	-0.862	13.169	0.140	0.140	0.000	0.000	0.000	0.000
103	A	131	ILE	0	-0.029	-0.022	11.869	0.036	0.036	0.000	0.000	0.000	0.000
104	A	132	ALA	0	0.016	0.001	14.165	-0.040	-0.040	0.000	0.000	0.000	0.000
105	A	133	LEU	0	0.023	0.028	15.232	-0.007	-0.007	0.000	0.000	0.000	0.000
106	A	134	SER	0	-0.016	-0.028	16.656	-0.019	-0.019	0.000	0.000	0.000	0.000
107	A	135	ALA	0	0.001	-0.010	18.290	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	136	ASP	-1	-0.826	-0.921	21.127	0.046	0.046	0.000	0.000	0.000	0.000
109	A	137	GLY	0	-0.008	0.010	23.642	0.000	0.000	0.000	0.000	0.000	0.000
110	A	138	LYS	1	0.751	0.863	20.202	-0.057	-0.057	0.000	0.000	0.000	0.000
111	A	139	LEU	0	0.045	0.039	19.643	0.005	0.005	0.000	0.000	0.000	0.000
112	A	140	CYS	0	-0.043	-0.004	20.938	-0.012	-0.012	0.000	0.000	0.000	0.000
113	A	141	ALA	0	0.012	0.007	19.362	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	142	ARG	1	0.844	0.920	18.687	-0.132	-0.132	0.000	0.000	0.000	0.000
115	A	143	GLY	0	0.039	0.016	16.990	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	144	HIS	0	-0.001	0.005	16.853	0.005	0.005	0.000	0.000	0.000	0.000
117	A	145	MET	0	-0.001	0.027	11.786	0.029	0.029	0.000	0.000	0.000	0.000
118	A	146	VAL	0	-0.031	-0.011	15.608	-0.019	-0.019	0.000	0.000	0.000	0.000
119	A	147	ALA	0	0.065	0.036	11.909	0.005	0.005	0.000	0.000	0.000	0.000
120	A	148	VAL	0	-0.004	-0.023	13.819	-0.058	-0.058	0.000	0.000	0.000	0.000
121	A	149	LYS	1	0.960	0.989	12.111	-0.009	-0.009	0.000	0.000	0.000	0.000
122	A	150	MET	0	-0.019	-0.004	12.147	-0.065	-0.065	0.000	0.000	0.000	0.000
123	A	151	PRO	0	-0.035	-0.005	14.318	-0.043	-0.043	0.000	0.000	0.000	0.000

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