FMO DATABASE

FMODB ID: JLZ59

Calculation Name: 3OOP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3OOP

Chain ID: A

ChEMBL ID:

UniProt ID: Q926T1

Base Structure: X-ray

Registration Date: 2023-09-20

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	143
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1195290.640669
FMO2-HF: Nuclear repulsion	1137500.011171
FMO2-HF: Total energy	-57790.629498
FMO2-MP2: Total energy	-57958.5024

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:-2:SER)

Summations of interaction energy for fragment #1(A:-2:SER)

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.
-0.716	1.064	4.109	-1.935	-3.953	-0.004

Interaction energy analysis for fragmet #1(A:-2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.019 / q_NPA : -0.005

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	0	ALA	0	0.062	0.037	3.235	-2.286	-0.439	0.043	-0.782	-1.107	0.001
4	A	1	MET	0	0.036	0.013	2.110	-0.543	-0.862	4.066	-1.235	-2.512	-0.005
5	A	2	ARG	1	0.918	0.965	3.426	2.350	2.537	0.001	0.084	-0.272	0.000
6	A	3	GLY	0	0.046	0.028	5.357	0.672	0.737	-0.001	-0.002	-0.062	0.000
7	A	4	TYR	0	0.012	-0.002	6.159	0.284	0.284	0.000	0.000	0.000	0.000
8	A	5	TYR	0	-0.025	-0.004	7.166	0.213	0.213	0.000	0.000	0.000	0.000
9	A	6	ASP	-1	-0.878	-0.956	8.926	-1.023	-1.023	0.000	0.000	0.000	0.000
10	A	7	GLU	-1	-0.909	-0.950	11.010	-0.204	-0.204	0.000	0.000	0.000	0.000
11	A	8	ILE	0	0.024	0.016	10.717	0.081	0.081	0.000	0.000	0.000	0.000
12	A	9	SER	0	-0.074	-0.032	13.107	0.070	0.070	0.000	0.000	0.000	0.000
13	A	10	PHE	0	-0.040	-0.024	15.063	0.073	0.073	0.000	0.000	0.000	0.000
14	A	11	ASP	-1	-0.832	-0.927	16.603	-0.186	-0.186	0.000	0.000	0.000	0.000
15	A	12	VAL	0	-0.032	-0.003	17.100	0.041	0.041	0.000	0.000	0.000	0.000
16	A	13	ASN	0	0.010	0.012	19.335	0.056	0.056	0.000	0.000	0.000	0.000
17	A	14	THR	0	-0.021	-0.024	21.074	0.031	0.031	0.000	0.000	0.000	0.000
18	A	15	THR	0	0.011	-0.010	21.474	0.031	0.031	0.000	0.000	0.000	0.000
19	A	16	ALA	0	0.045	0.023	23.461	0.018	0.018	0.000	0.000	0.000	0.000
20	A	17	LYS	1	0.857	0.930	24.219	0.215	0.215	0.000	0.000	0.000	0.000
21	A	18	LYS	1	0.932	0.962	26.842	0.115	0.115	0.000	0.000	0.000	0.000
22	A	19	MET	0	0.026	0.011	26.198	0.007	0.007	0.000	0.000	0.000	0.000
23	A	20	HIS	0	0.052	0.028	29.464	0.007	0.007	0.000	0.000	0.000	0.000
24	A	21	LEU	0	-0.024	-0.024	31.005	0.009	0.009	0.000	0.000	0.000	0.000
25	A	22	PHE	0	-0.101	-0.049	32.423	0.009	0.009	0.000	0.000	0.000	0.000
26	A	23	LEU	0	0.095	0.046	33.008	0.006	0.006	0.000	0.000	0.000	0.000
27	A	24	MET	0	-0.022	0.010	35.721	0.006	0.006	0.000	0.000	0.000	0.000
28	A	25	ARG	1	0.875	0.935	33.640	0.078	0.078	0.000	0.000	0.000	0.000
29	A	26	SER	0	-0.061	-0.025	38.515	0.005	0.005	0.000	0.000	0.000	0.000
30	A	27	ILE	0	0.059	0.028	40.257	0.003	0.003	0.000	0.000	0.000	0.000
31	A	28	ALA	0	-0.030	-0.015	41.826	0.001	0.001	0.000	0.000	0.000	0.000
32	A	29	SER	0	-0.063	-0.032	43.592	0.001	0.001	0.000	0.000	0.000	0.000
33	A	30	TYR	0	-0.008	0.009	45.925	0.002	0.002	0.000	0.000	0.000	0.000
34	A	31	ASP	-1	-0.822	-0.901	48.141	-0.047	-0.047	0.000	0.000	0.000	0.000
35	A	32	VAL	0	-0.018	-0.005	45.634	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	33	THR	0	0.025	0.015	45.002	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	34	PRO	0	0.087	0.024	39.609	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	35	GLU	-1	-0.826	-0.875	41.269	-0.074	-0.074	0.000	0.000	0.000	0.000
39	A	36	GLN	0	0.047	0.008	42.317	0.000	0.000	0.000	0.000	0.000	0.000
40	A	37	TRP	0	0.045	0.027	39.449	0.003	0.003	0.000	0.000	0.000	0.000
41	A	38	SER	0	-0.037	-0.025	39.537	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	39	VAL	0	-0.028	-0.018	40.941	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	40	LEU	0	0.032	0.015	43.859	0.000	0.000	0.000	0.000	0.000	0.000
44	A	41	GLU	-1	-0.911	-0.944	38.532	-0.090	-0.090	0.000	0.000	0.000	0.000
45	A	42	GLY	0	0.012	0.003	41.666	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	43	ILE	0	-0.023	-0.028	42.453	0.000	0.000	0.000	0.000	0.000	0.000
47	A	44	GLU	-1	-0.854	-0.910	44.644	-0.065	-0.065	0.000	0.000	0.000	0.000
48	A	45	ALA	0	-0.021	-0.005	41.434	0.001	0.001	0.000	0.000	0.000	0.000
49	A	46	ASN	0	-0.108	-0.081	41.168	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	47	GLU	-1	-0.806	-0.819	45.167	-0.054	-0.054	0.000	0.000	0.000	0.000
51	A	48	PRO	0	0.003	-0.009	48.909	0.001	0.001	0.000	0.000	0.000	0.000
52	A	49	ILE	0	0.014	0.009	43.896	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	50	SER	0	0.046	0.028	47.696	0.001	0.001	0.000	0.000	0.000	0.000
54	A	51	GLN	0	0.054	-0.001	47.004	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	52	LYS	1	0.844	0.908	43.495	0.085	0.085	0.000	0.000	0.000	0.000
56	A	53	GLU	-1	-0.771	-0.891	42.499	-0.094	-0.094	0.000	0.000	0.000	0.000
57	A	54	ILE	0	0.046	0.042	42.128	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	55	ALA	0	-0.015	0.016	41.564	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	56	LEU	0	0.000	-0.004	38.852	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	57	TRP	0	0.032	0.036	37.434	-0.009	-0.009	0.000	0.000	0.000	0.000
61	A	58	THR	0	-0.081	-0.069	37.094	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	59	LYS	1	0.830	0.928	33.158	0.125	0.125	0.000	0.000	0.000	0.000
63	A	60	LYS	1	0.899	0.973	37.057	0.093	0.093	0.000	0.000	0.000	0.000
64	A	61	ASP	-1	-0.789	-0.872	39.946	-0.084	-0.084	0.000	0.000	0.000	0.000
65	A	62	THR	0	0.048	-0.007	42.263	0.002	0.002	0.000	0.000	0.000	0.000
66	A	63	PRO	0	0.001	0.003	45.369	0.003	0.003	0.000	0.000	0.000	0.000
67	A	64	THR	0	-0.038	-0.032	42.344	0.005	0.005	0.000	0.000	0.000	0.000
68	A	65	VAL	0	0.016	0.011	43.577	0.002	0.002	0.000	0.000	0.000	0.000
69	A	66	ASN	0	-0.015	-0.004	46.042	0.002	0.002	0.000	0.000	0.000	0.000
70	A	67	ARG	1	0.831	0.889	44.818	0.071	0.071	0.000	0.000	0.000	0.000
71	A	68	ILE	0	-0.036	-0.019	44.118	0.003	0.003	0.000	0.000	0.000	0.000
72	A	69	VAL	0	0.029	0.007	48.238	0.002	0.002	0.000	0.000	0.000	0.000
73	A	70	ASP	-1	-0.813	-0.900	50.441	-0.050	-0.050	0.000	0.000	0.000	0.000
74	A	71	VAL	0	-0.116	-0.059	50.755	0.003	0.003	0.000	0.000	0.000	0.000
75	A	72	LEU	0	0.028	0.009	47.596	0.002	0.002	0.000	0.000	0.000	0.000
76	A	73	LEU	0	-0.020	-0.001	52.222	0.002	0.002	0.000	0.000	0.000	0.000
77	A	74	ARG	1	0.907	0.960	54.742	0.047	0.047	0.000	0.000	0.000	0.000
78	A	75	LYS	1	0.792	0.899	50.415	0.051	0.051	0.000	0.000	0.000	0.000
79	A	76	GLU	-1	-0.874	-0.918	55.914	-0.037	-0.037	0.000	0.000	0.000	0.000
80	A	77	LEU	0	-0.006	0.016	50.993	0.000	0.000	0.000	0.000	0.000	0.000
81	A	78	ILE	0	-0.008	-0.011	50.314	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	79	VAL	0	0.014	0.015	53.730	0.002	0.002	0.000	0.000	0.000	0.000
83	A	80	ARG	1	0.797	0.884	53.138	0.051	0.051	0.000	0.000	0.000	0.000
84	A	81	GLU	-1	-0.906	-0.947	56.102	-0.042	-0.042	0.000	0.000	0.000	0.000
85	A	82	ILE	0	-0.042	-0.020	56.695	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	83	SER	0	-0.046	-0.055	57.639	0.000	0.000	0.000	0.000	0.000	0.000
87	A	84	THR	0	0.041	0.023	54.509	0.000	0.000	0.000	0.000	0.000	0.000
88	A	85	GLU	-1	-0.918	-0.960	50.525	-0.066	-0.066	0.000	0.000	0.000	0.000
89	A	86	ASP	-1	-0.885	-0.932	54.589	-0.050	-0.050	0.000	0.000	0.000	0.000
90	A	87	ARG	1	0.885	0.944	53.314	0.058	0.058	0.000	0.000	0.000	0.000
91	A	88	ARG	1	0.936	0.963	58.194	0.042	0.042	0.000	0.000	0.000	0.000
92	A	89	ILE	0	0.003	0.014	51.629	0.000	0.000	0.000	0.000	0.000	0.000
93	A	90	SER	0	-0.049	-0.036	53.047	0.002	0.002	0.000	0.000	0.000	0.000
94	A	91	LEU	0	-0.012	0.001	50.916	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	92	LEU	0	-0.020	-0.016	48.691	0.003	0.003	0.000	0.000	0.000	0.000
96	A	93	SER	0	0.055	0.018	50.827	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	94	LEU	0	-0.025	-0.009	48.740	0.001	0.001	0.000	0.000	0.000	0.000
98	A	95	THR	0	-0.025	-0.018	52.698	0.001	0.001	0.000	0.000	0.000	0.000
99	A	96	ASP	-1	-0.864	-0.944	54.694	-0.041	-0.041	0.000	0.000	0.000	0.000
100	A	97	LYS	1	0.792	0.897	55.384	0.040	0.040	0.000	0.000	0.000	0.000
101	A	98	GLY	0	0.062	0.021	52.179	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	99	ARG	1	0.856	0.911	50.746	0.049	0.049	0.000	0.000	0.000	0.000
103	A	100	LYS	1	0.892	0.969	50.700	0.040	0.040	0.000	0.000	0.000	0.000
104	A	101	GLU	-1	-0.909	-0.975	50.329	-0.045	-0.045	0.000	0.000	0.000	0.000
105	A	102	THR	0	-0.017	-0.029	45.470	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	103	THR	0	-0.021	-0.021	45.977	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	104	GLU	-1	-0.874	-0.932	46.492	-0.043	-0.043	0.000	0.000	0.000	0.000
108	A	105	LEU	0	-0.018	-0.023	44.180	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	106	ARG	1	0.842	0.896	40.334	0.071	0.071	0.000	0.000	0.000	0.000
110	A	107	ASP	-1	-0.872	-0.918	41.499	-0.053	-0.053	0.000	0.000	0.000	0.000
111	A	108	ILE	0	-0.064	-0.024	41.793	0.000	0.000	0.000	0.000	0.000	0.000
112	A	109	VAL	0	-0.020	-0.021	37.227	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	110	GLU	-1	-0.923	-0.960	37.457	-0.071	-0.071	0.000	0.000	0.000	0.000
114	A	111	ALA	0	0.057	0.037	37.460	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	112	SER	0	-0.090	-0.062	36.619	0.002	0.002	0.000	0.000	0.000	0.000
116	A	113	CYS	0	-0.033	-0.025	32.775	-0.006	-0.006	0.000	0.000	0.000	0.000
117	A	114	GLU	-1	-0.906	-0.945	32.761	-0.058	-0.058	0.000	0.000	0.000	0.000
118	A	115	LYS	1	0.872	0.929	33.467	0.050	0.050	0.000	0.000	0.000	0.000
119	A	116	MET	0	-0.097	-0.027	29.360	0.001	0.001	0.000	0.000	0.000	0.000
120	A	117	PHE	0	0.001	-0.002	26.143	-0.011	-0.011	0.000	0.000	0.000	0.000
121	A	118	ALA	0	0.041	0.031	29.539	0.003	0.003	0.000	0.000	0.000	0.000
122	A	119	GLY	0	-0.049	-0.025	28.983	0.000	0.000	0.000	0.000	0.000	0.000
123	A	120	VAL	0	-0.038	-0.003	24.225	0.000	0.000	0.000	0.000	0.000	0.000
124	A	121	THR	0	-0.027	-0.044	25.676	0.000	0.000	0.000	0.000	0.000	0.000
125	A	122	ARG	1	0.853	0.870	25.360	0.085	0.085	0.000	0.000	0.000	0.000
126	A	123	THR	0	0.026	0.005	23.728	-0.015	-0.015	0.000	0.000	0.000	0.000
127	A	124	ASP	-1	-0.815	-0.875	21.677	-0.074	-0.074	0.000	0.000	0.000	0.000
128	A	125	LEU	0	-0.005	0.004	20.255	-0.019	-0.019	0.000	0.000	0.000	0.000
129	A	126	GLU	-1	-0.814	-0.881	20.276	-0.143	-0.143	0.000	0.000	0.000	0.000
130	A	127	GLN	0	-0.013	-0.004	18.161	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	128	PHE	0	0.029	0.013	12.443	-0.018	-0.018	0.000	0.000	0.000	0.000
132	A	129	THR	0	-0.007	-0.012	15.797	-0.057	-0.057	0.000	0.000	0.000	0.000
133	A	130	ALA	0	-0.010	-0.001	17.196	-0.039	-0.039	0.000	0.000	0.000	0.000
134	A	131	ILE	0	-0.007	0.006	10.939	-0.029	-0.029	0.000	0.000	0.000	0.000
135	A	132	LEU	0	0.025	0.015	12.268	-0.111	-0.111	0.000	0.000	0.000	0.000
136	A	133	LYS	1	0.967	0.997	13.830	0.220	0.220	0.000	0.000	0.000	0.000
137	A	134	ASN	0	-0.006	0.004	12.044	-0.015	-0.015	0.000	0.000	0.000	0.000
138	A	135	ILE	0	-0.018	-0.005	8.208	-0.072	-0.072	0.000	0.000	0.000	0.000
139	A	136	SER	0	-0.040	-0.052	10.597	-0.074	-0.074	0.000	0.000	0.000	0.000
140	A	137	THR	0	-0.047	-0.026	13.712	0.037	0.037	0.000	0.000	0.000	0.000
141	A	138	ASN	0	-0.069	-0.035	8.844	0.111	0.111	0.000	0.000	0.000	0.000
142	A	139	ILE	0	-0.083	-0.024	8.996	-0.104	-0.104	0.000	0.000	0.000	0.000
143	A	140	GLU	-1	-0.950	-0.961	12.319	-0.311	-0.311	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:-2:SER)