FMO DATABASE

FMODB ID: N9MYQ

Calculation Name: 3OOP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	143
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1193829.991958
FMO2-HF: Nuclear repulsion	1136040.145975
FMO2-HF: Total energy	-57789.845984
FMO2-MP2: Total energy	-57957.714281

3D Structure Molmil

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.
-2.092	0.243	3.868	-2.07	-4.133	-0.002

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 : 0.022 / q_NPA : -0.004

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	0.066	0.038	3.228	-2.347	-0.614	0.043	-0.723	-1.053	0.001
4	A	1	MET	0	0.023	0.004	2.066	-1.390	-0.981	3.823	-1.512	-2.720	-0.003
5	A	2	ARG	1	0.944	0.973	3.276	2.089	2.213	0.003	0.168	-0.295	0.000
6	A	3	GLY	0	0.063	0.040	5.094	0.613	0.682	-0.001	-0.003	-0.065	0.000
7	A	4	TYR	0	0.037	0.005	5.970	0.270	0.270	0.000	0.000	0.000	0.000
8	A	5	TYR	0	-0.029	-0.006	7.005	0.219	0.219	0.000	0.000	0.000	0.000
9	A	6	ASP	-1	-0.900	-0.961	8.733	-1.019	-1.019	0.000	0.000	0.000	0.000
10	A	7	GLU	-1	-0.957	-0.972	10.849	-0.292	-0.292	0.000	0.000	0.000	0.000
11	A	8	ILE	0	0.032	0.025	10.743	0.090	0.090	0.000	0.000	0.000	0.000
12	A	9	SER	0	-0.068	-0.031	12.893	0.090	0.090	0.000	0.000	0.000	0.000
13	A	10	PHE	0	-0.033	-0.020	14.836	0.102	0.102	0.000	0.000	0.000	0.000
14	A	11	ASP	-1	-0.848	-0.935	16.444	-0.309	-0.309	0.000	0.000	0.000	0.000
15	A	12	VAL	0	-0.026	-0.003	16.531	0.053	0.053	0.000	0.000	0.000	0.000
16	A	13	ASN	0	0.003	0.006	19.151	0.054	0.054	0.000	0.000	0.000	0.000
17	A	14	THR	0	-0.079	-0.049	20.825	0.046	0.046	0.000	0.000	0.000	0.000
18	A	15	THR	0	0.015	-0.010	21.354	0.043	0.043	0.000	0.000	0.000	0.000
19	A	16	ALA	0	0.053	0.030	23.273	0.024	0.024	0.000	0.000	0.000	0.000
20	A	17	LYS	1	0.909	0.956	24.600	0.257	0.257	0.000	0.000	0.000	0.000
21	A	18	LYS	1	0.934	0.958	26.746	0.168	0.168	0.000	0.000	0.000	0.000
22	A	19	MET	0	0.027	0.013	26.022	0.010	0.010	0.000	0.000	0.000	0.000
23	A	20	HIS	0	0.060	0.029	29.305	0.009	0.009	0.000	0.000	0.000	0.000
24	A	21	LEU	0	-0.039	-0.032	30.934	0.014	0.014	0.000	0.000	0.000	0.000
25	A	22	PHE	0	-0.096	-0.037	32.211	0.014	0.014	0.000	0.000	0.000	0.000
26	A	23	LEU	0	0.091	0.037	32.827	0.009	0.009	0.000	0.000	0.000	0.000
27	A	24	MET	0	-0.025	0.009	35.560	0.010	0.010	0.000	0.000	0.000	0.000
28	A	25	ARG	1	0.883	0.936	33.194	0.126	0.126	0.000	0.000	0.000	0.000
29	A	26	SER	0	-0.065	-0.027	38.355	0.008	0.008	0.000	0.000	0.000	0.000
30	A	27	ILE	0	0.064	0.027	40.112	0.005	0.005	0.000	0.000	0.000	0.000
31	A	28	ALA	0	-0.023	-0.012	41.684	0.003	0.003	0.000	0.000	0.000	0.000
32	A	29	SER	0	-0.074	-0.039	43.423	0.002	0.002	0.000	0.000	0.000	0.000
33	A	30	TYR	0	-0.007	0.015	45.589	0.004	0.004	0.000	0.000	0.000	0.000
34	A	31	ASP	-1	-0.870	-0.934	47.956	-0.068	-0.068	0.000	0.000	0.000	0.000
35	A	32	VAL	0	-0.027	-0.007	45.538	0.000	0.000	0.000	0.000	0.000	0.000
36	A	33	THR	0	0.026	0.010	44.781	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	34	PRO	0	0.078	0.016	39.433	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	35	GLU	-1	-0.843	-0.907	41.045	-0.100	-0.100	0.000	0.000	0.000	0.000
39	A	36	GLN	0	0.049	0.019	42.109	0.000	0.000	0.000	0.000	0.000	0.000
40	A	37	TRP	0	0.072	0.036	39.155	0.003	0.003	0.000	0.000	0.000	0.000
41	A	38	SER	0	-0.030	-0.012	38.832	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	39	VAL	0	-0.024	-0.014	40.787	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	40	LEU	0	0.027	0.006	43.792	0.000	0.000	0.000	0.000	0.000	0.000
44	A	41	GLU	-1	-0.936	-0.953	38.237	-0.140	-0.140	0.000	0.000	0.000	0.000
45	A	42	GLY	0	0.005	0.003	41.657	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	43	ILE	0	-0.034	-0.032	42.440	0.001	0.001	0.000	0.000	0.000	0.000
47	A	44	GLU	-1	-0.871	-0.932	44.415	-0.106	-0.106	0.000	0.000	0.000	0.000
48	A	45	ALA	0	-0.001	0.007	41.456	0.001	0.001	0.000	0.000	0.000	0.000
49	A	46	ASN	0	-0.114	-0.075	41.356	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	47	GLU	-1	-0.827	-0.845	45.270	-0.082	-0.082	0.000	0.000	0.000	0.000
51	A	48	PRO	0	0.000	-0.013	48.993	0.000	0.000	0.000	0.000	0.000	0.000
52	A	49	ILE	0	0.025	0.018	44.110	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	50	SER	0	0.045	0.029	47.762	0.003	0.003	0.000	0.000	0.000	0.000
54	A	51	GLN	0	0.063	0.004	47.147	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	52	LYS	1	0.917	0.960	43.676	0.108	0.108	0.000	0.000	0.000	0.000
56	A	53	GLU	-1	-0.873	-0.954	42.507	-0.127	-0.127	0.000	0.000	0.000	0.000
57	A	54	ILE	0	0.049	0.045	42.269	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	55	ALA	0	-0.026	0.005	41.718	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	56	LEU	0	-0.012	-0.015	38.986	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	57	TRP	0	-0.005	0.019	37.577	-0.010	-0.010	0.000	0.000	0.000	0.000
61	A	58	THR	0	-0.068	-0.050	37.215	-0.006	-0.006	0.000	0.000	0.000	0.000
62	A	59	LYS	1	0.901	0.954	31.518	0.195	0.195	0.000	0.000	0.000	0.000
63	A	60	LYS	1	0.908	0.977	37.214	0.125	0.125	0.000	0.000	0.000	0.000
64	A	61	ASP	-1	-0.798	-0.883	40.088	-0.104	-0.104	0.000	0.000	0.000	0.000
65	A	62	THR	0	0.033	-0.009	42.413	0.001	0.001	0.000	0.000	0.000	0.000
66	A	63	PRO	0	-0.003	0.001	45.307	0.003	0.003	0.000	0.000	0.000	0.000
67	A	64	THR	0	-0.031	-0.026	42.441	0.004	0.004	0.000	0.000	0.000	0.000
68	A	65	VAL	0	0.022	0.012	43.625	0.002	0.002	0.000	0.000	0.000	0.000
69	A	66	ASN	0	-0.019	-0.018	46.136	0.001	0.001	0.000	0.000	0.000	0.000
70	A	67	ARG	1	0.863	0.932	44.694	0.091	0.091	0.000	0.000	0.000	0.000
71	A	68	ILE	0	-0.038	-0.022	44.060	0.003	0.003	0.000	0.000	0.000	0.000
72	A	69	VAL	0	0.028	0.007	48.334	0.002	0.002	0.000	0.000	0.000	0.000
73	A	70	ASP	-1	-0.879	-0.942	50.437	-0.067	-0.067	0.000	0.000	0.000	0.000
74	A	71	VAL	0	-0.122	-0.060	50.614	0.003	0.003	0.000	0.000	0.000	0.000
75	A	72	LEU	0	0.027	0.005	47.468	0.002	0.002	0.000	0.000	0.000	0.000
76	A	73	LEU	0	-0.020	-0.001	52.082	0.002	0.002	0.000	0.000	0.000	0.000
77	A	74	ARG	1	0.924	0.967	54.576	0.064	0.064	0.000	0.000	0.000	0.000
78	A	75	LYS	1	0.803	0.910	50.239	0.075	0.075	0.000	0.000	0.000	0.000
79	A	76	GLU	-1	-0.940	-0.964	55.690	-0.055	-0.055	0.000	0.000	0.000	0.000
80	A	77	LEU	0	-0.023	0.006	50.733	0.000	0.000	0.000	0.000	0.000	0.000
81	A	78	ILE	0	-0.002	-0.007	50.251	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	79	VAL	0	0.015	0.016	53.647	0.003	0.003	0.000	0.000	0.000	0.000
83	A	80	ARG	1	0.864	0.931	53.562	0.068	0.068	0.000	0.000	0.000	0.000
84	A	81	GLU	-1	-0.910	-0.953	56.197	-0.060	-0.060	0.000	0.000	0.000	0.000
85	A	82	ILE	0	-0.037	-0.008	56.839	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	83	SER	0	-0.044	-0.058	57.810	0.000	0.000	0.000	0.000	0.000	0.000
87	A	84	THR	0	0.026	0.016	54.864	0.000	0.000	0.000	0.000	0.000	0.000
88	A	85	GLU	-1	-0.915	-0.958	50.631	-0.090	-0.090	0.000	0.000	0.000	0.000
89	A	86	ASP	-1	-0.871	-0.929	54.802	-0.067	-0.067	0.000	0.000	0.000	0.000
90	A	87	ARG	1	0.880	0.943	53.618	0.078	0.078	0.000	0.000	0.000	0.000
91	A	88	ARG	1	0.936	0.957	58.300	0.056	0.056	0.000	0.000	0.000	0.000
92	A	89	ILE	0	0.004	0.019	51.951	0.001	0.001	0.000	0.000	0.000	0.000
93	A	90	SER	0	-0.050	-0.041	53.295	0.002	0.002	0.000	0.000	0.000	0.000
94	A	91	LEU	0	-0.010	0.005	51.252	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	92	LEU	0	-0.021	-0.019	48.866	0.004	0.004	0.000	0.000	0.000	0.000
96	A	93	SER	0	0.051	0.019	50.922	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	94	LEU	0	-0.026	-0.008	48.527	0.002	0.002	0.000	0.000	0.000	0.000
98	A	95	THR	0	-0.018	-0.015	52.609	0.001	0.001	0.000	0.000	0.000	0.000
99	A	96	ASP	-1	-0.857	-0.938	54.509	-0.065	-0.065	0.000	0.000	0.000	0.000
100	A	97	LYS	1	0.871	0.945	55.015	0.060	0.060	0.000	0.000	0.000	0.000
101	A	98	GLY	0	0.068	0.024	51.974	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	99	ARG	1	0.874	0.933	50.551	0.076	0.076	0.000	0.000	0.000	0.000
103	A	100	LYS	1	0.947	0.975	50.521	0.061	0.061	0.000	0.000	0.000	0.000
104	A	101	GLU	-1	-0.903	-0.964	50.060	-0.072	-0.072	0.000	0.000	0.000	0.000
105	A	102	THR	0	-0.024	-0.030	45.293	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	103	THR	0	-0.019	-0.005	45.802	-0.005	-0.005	0.000	0.000	0.000	0.000
107	A	104	GLU	-1	-0.900	-0.945	46.338	-0.074	-0.074	0.000	0.000	0.000	0.000
108	A	105	LEU	0	-0.022	-0.024	43.907	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	106	ARG	1	0.839	0.896	40.162	0.113	0.113	0.000	0.000	0.000	0.000
110	A	107	ASP	-1	-0.851	-0.905	41.350	-0.098	-0.098	0.000	0.000	0.000	0.000
111	A	108	ILE	0	-0.076	-0.028	41.537	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	109	VAL	0	-0.041	-0.035	37.052	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	110	GLU	-1	-0.926	-0.958	37.319	-0.130	-0.130	0.000	0.000	0.000	0.000
114	A	111	ALA	0	0.069	0.039	37.345	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	112	SER	0	-0.075	-0.049	36.325	0.000	0.000	0.000	0.000	0.000	0.000
116	A	113	CYS	0	-0.048	-0.036	33.041	-0.011	-0.011	0.000	0.000	0.000	0.000
117	A	114	GLU	-1	-0.887	-0.941	32.656	-0.126	-0.126	0.000	0.000	0.000	0.000
118	A	115	LYS	1	0.864	0.928	33.395	0.098	0.098	0.000	0.000	0.000	0.000
119	A	116	MET	0	-0.104	-0.024	29.259	0.000	0.000	0.000	0.000	0.000	0.000
120	A	117	PHE	0	0.003	0.002	25.865	-0.018	-0.018	0.000	0.000	0.000	0.000
121	A	118	ALA	0	0.038	0.029	29.485	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	119	GLY	0	-0.054	-0.029	28.980	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	120	VAL	0	-0.021	0.010	24.223	-0.010	-0.010	0.000	0.000	0.000	0.000
124	A	121	THR	0	-0.034	-0.029	25.714	0.007	0.007	0.000	0.000	0.000	0.000
125	A	122	ARG	1	0.932	0.947	25.310	0.201	0.201	0.000	0.000	0.000	0.000
126	A	123	THR	0	0.005	-0.009	23.359	-0.021	-0.021	0.000	0.000	0.000	0.000
127	A	124	ASP	-1	-0.787	-0.875	21.662	-0.268	-0.268	0.000	0.000	0.000	0.000
128	A	125	LEU	0	-0.022	-0.009	20.208	-0.045	-0.045	0.000	0.000	0.000	0.000
129	A	126	GLU	-1	-0.899	-0.961	20.178	-0.326	-0.326	0.000	0.000	0.000	0.000
130	A	127	GLN	0	-0.006	-0.006	17.862	-0.007	-0.007	0.000	0.000	0.000	0.000
131	A	128	PHE	0	0.030	0.014	12.259	-0.071	-0.071	0.000	0.000	0.000	0.000
132	A	129	THR	0	0.007	-0.001	15.676	-0.088	-0.088	0.000	0.000	0.000	0.000
133	A	130	ALA	0	-0.010	-0.002	16.720	-0.045	-0.045	0.000	0.000	0.000	0.000
134	A	131	ILE	0	-0.012	0.005	10.563	-0.073	-0.073	0.000	0.000	0.000	0.000
135	A	132	LEU	0	0.017	0.006	12.046	-0.193	-0.193	0.000	0.000	0.000	0.000
136	A	133	LYS	1	0.965	0.988	13.904	0.444	0.444	0.000	0.000	0.000	0.000
137	A	134	ASN	0	-0.006	0.002	11.255	0.084	0.084	0.000	0.000	0.000	0.000
138	A	135	ILE	0	-0.028	-0.011	8.319	-0.082	-0.082	0.000	0.000	0.000	0.000
139	A	136	SER	0	-0.036	-0.043	10.627	0.008	0.008	0.000	0.000	0.000	0.000
140	A	137	THR	0	-0.037	-0.012	13.725	0.096	0.096	0.000	0.000	0.000	0.000
141	A	138	ASN	0	-0.051	-0.025	8.211	0.310	0.310	0.000	0.000	0.000	0.000
142	A	139	ILE	0	-0.100	-0.033	9.117	-0.033	-0.033	0.000	0.000	0.000	0.000
143	A	140	GLU	-1	-0.940	-0.959	12.234	-0.514	-0.514	0.000	0.000	0.000	0.000

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