FMO DATABASE

FMODB ID: ZV51N

Calculation Name: 2JLJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2JLJ

Chain ID: A

ChEMBL ID:

UniProt ID: P69986

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	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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-979122.097503
FMO2-HF: Nuclear repulsion	933690.656456
FMO2-HF: Total energy	-45431.441047
FMO2-MP2: Total energy	-45567.393902

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:230:GLY)

Summations of interaction energy for fragment #1(A:230:GLY)

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.
0.136	1.683	3.303	-2.655	-2.194	0

Interaction energy analysis for fragmet #1(A:230:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / q_NPA : 0.009

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	232	PRO	0	0.068	0.019	3.779	-1.206	0.672	-0.003	-1.061	-0.813	0.005
4	A	233	GLU	-1	-0.766	-0.854	6.498	-1.163	-1.163	0.000	0.000	0.000	0.000
5	A	234	ILE	0	-0.016	0.002	2.241	1.070	0.352	3.285	-1.464	-1.103	-0.005
6	A	235	LYS	1	0.923	0.966	3.391	3.640	4.027	0.021	-0.130	-0.278	0.000
7	A	236	SER	0	-0.031	-0.014	5.485	0.308	0.308	0.000	0.000	0.000	0.000
8	A	237	LYS	1	0.997	0.996	8.233	-0.215	-0.215	0.000	0.000	0.000	0.000
9	A	238	ARG	1	0.886	0.944	5.197	-1.983	-1.983	0.000	0.000	0.000	0.000
10	A	239	ARG	1	0.822	0.919	8.773	0.390	0.390	0.000	0.000	0.000	0.000
11	A	240	GLN	0	-0.037	-0.013	11.041	-0.012	-0.012	0.000	0.000	0.000	0.000
12	A	241	PHE	0	-0.002	-0.010	11.906	0.016	0.016	0.000	0.000	0.000	0.000
13	A	242	HIS	0	0.012	-0.011	10.581	-0.079	-0.079	0.000	0.000	0.000	0.000
14	A	243	GLN	0	-0.021	-0.013	14.293	-0.042	-0.042	0.000	0.000	0.000	0.000
15	A	244	GLU	-1	-0.892	-0.948	16.622	0.106	0.106	0.000	0.000	0.000	0.000
16	A	245	ILE	0	-0.064	-0.013	16.298	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	246	GLN	0	-0.085	-0.032	18.881	-0.028	-0.028	0.000	0.000	0.000	0.000
18	A	247	SER	0	0.015	0.000	20.504	-0.013	-0.013	0.000	0.000	0.000	0.000
19	A	248	ARG	1	0.854	0.929	22.942	-0.182	-0.182	0.000	0.000	0.000	0.000
20	A	249	ASN	0	0.022	0.017	25.886	-0.015	-0.015	0.000	0.000	0.000	0.000
21	A	250	MET	0	0.017	0.009	27.710	0.001	0.001	0.000	0.000	0.000	0.000
22	A	251	ARG	1	0.824	0.881	28.761	-0.047	-0.047	0.000	0.000	0.000	0.000
23	A	252	GLU	-1	-0.839	-0.907	27.662	0.128	0.128	0.000	0.000	0.000	0.000
24	A	253	ASN	0	-0.002	-0.031	23.266	0.017	0.017	0.000	0.000	0.000	0.000
25	A	254	VAL	0	-0.029	-0.008	26.523	0.000	0.000	0.000	0.000	0.000	0.000
26	A	255	LYS	1	0.905	0.942	28.738	-0.064	-0.064	0.000	0.000	0.000	0.000
27	A	256	ARG	1	0.748	0.869	20.975	-0.167	-0.167	0.000	0.000	0.000	0.000
28	A	257	SER	0	-0.038	-0.011	24.701	0.012	0.012	0.000	0.000	0.000	0.000
29	A	258	SER	0	0.001	-0.007	26.354	0.001	0.001	0.000	0.000	0.000	0.000
30	A	259	VAL	0	-0.002	-0.001	25.963	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	260	VAL	0	-0.005	0.003	26.042	0.006	0.006	0.000	0.000	0.000	0.000
32	A	261	VAL	0	0.022	0.014	23.439	-0.008	-0.008	0.000	0.000	0.000	0.000
33	A	262	ALA	0	-0.007	-0.016	24.890	0.000	0.000	0.000	0.000	0.000	0.000
34	A	263	ALA	0	-0.005	-0.003	25.897	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	264	ALA	0	-0.022	-0.043	27.639	0.003	0.003	0.000	0.000	0.000	0.000
36	A	265	THR	0	-0.048	-0.035	30.877	-0.007	-0.007	0.000	0.000	0.000	0.000
37	A	266	HIS	0	0.044	0.053	26.249	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	267	ILE	0	0.018	0.008	21.647	0.001	0.001	0.000	0.000	0.000	0.000
39	A	268	ALA	0	-0.021	-0.006	24.481	0.000	0.000	0.000	0.000	0.000	0.000
40	A	269	ILE	0	-0.014	-0.001	19.290	0.005	0.005	0.000	0.000	0.000	0.000
41	A	270	GLY	0	0.018	0.022	22.283	-0.007	-0.007	0.000	0.000	0.000	0.000
42	A	271	ILE	0	0.010	-0.005	19.881	0.009	0.009	0.000	0.000	0.000	0.000
43	A	272	LEU	0	0.006	0.006	22.070	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	273	TYR	0	-0.001	-0.009	22.580	0.013	0.013	0.000	0.000	0.000	0.000
45	A	274	LYS	1	0.995	1.019	24.836	-0.110	-0.110	0.000	0.000	0.000	0.000
46	A	275	ARG	1	0.973	0.966	24.317	-0.082	-0.082	0.000	0.000	0.000	0.000
47	A	276	GLY	0	-0.014	-0.008	26.767	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	277	GLU	-1	-0.897	-0.935	26.310	0.129	0.129	0.000	0.000	0.000	0.000
49	A	278	THR	0	-0.027	-0.017	21.757	0.019	0.019	0.000	0.000	0.000	0.000
50	A	279	PRO	0	-0.019	-0.005	19.002	-0.023	-0.023	0.000	0.000	0.000	0.000
51	A	280	LEU	0	-0.027	-0.019	16.039	-0.024	-0.024	0.000	0.000	0.000	0.000
52	A	281	PRO	0	0.012	0.002	19.562	0.017	0.017	0.000	0.000	0.000	0.000
53	A	282	LEU	0	0.006	0.019	17.827	0.012	0.012	0.000	0.000	0.000	0.000
54	A	283	VAL	0	0.023	0.015	16.392	-0.034	-0.034	0.000	0.000	0.000	0.000
55	A	284	THR	0	-0.020	-0.014	18.233	0.033	0.033	0.000	0.000	0.000	0.000
56	A	285	PHE	0	0.038	0.015	20.610	0.011	0.011	0.000	0.000	0.000	0.000
57	A	286	LYS	1	0.795	0.876	14.167	0.006	0.006	0.000	0.000	0.000	0.000
58	A	287	TYR	0	0.024	0.025	20.993	0.011	0.011	0.000	0.000	0.000	0.000
59	A	288	THR	0	0.007	-0.034	22.671	-0.009	-0.009	0.000	0.000	0.000	0.000
60	A	289	ASP	-1	-0.832	-0.896	25.555	-0.039	-0.039	0.000	0.000	0.000	0.000
61	A	290	ALA	0	0.014	0.004	28.860	0.004	0.004	0.000	0.000	0.000	0.000
62	A	291	GLN	0	0.027	0.017	25.931	0.003	0.003	0.000	0.000	0.000	0.000
63	A	292	VAL	0	-0.012	-0.006	27.347	0.007	0.007	0.000	0.000	0.000	0.000
64	A	293	GLN	0	-0.006	-0.010	29.799	0.000	0.000	0.000	0.000	0.000	0.000
65	A	294	THR	0	0.012	0.012	31.996	0.003	0.003	0.000	0.000	0.000	0.000
66	A	295	VAL	0	0.016	-0.001	27.617	0.004	0.004	0.000	0.000	0.000	0.000
67	A	296	ARG	1	0.900	0.956	30.658	0.022	0.022	0.000	0.000	0.000	0.000
68	A	297	LYS	1	0.892	0.946	33.537	-0.022	-0.022	0.000	0.000	0.000	0.000
69	A	298	ILE	0	-0.009	-0.014	32.192	0.002	0.002	0.000	0.000	0.000	0.000
70	A	299	ALA	0	-0.014	-0.018	31.785	0.004	0.004	0.000	0.000	0.000	0.000
71	A	300	GLU	-1	-0.935	-0.960	33.645	0.009	0.009	0.000	0.000	0.000	0.000
72	A	301	GLU	-1	-0.818	-0.886	37.290	0.032	0.032	0.000	0.000	0.000	0.000
73	A	302	GLU	-1	-0.835	-0.903	33.841	0.057	0.057	0.000	0.000	0.000	0.000
74	A	303	GLY	0	-0.002	0.024	35.788	0.004	0.004	0.000	0.000	0.000	0.000
75	A	304	VAL	0	-0.063	-0.022	29.682	0.001	0.001	0.000	0.000	0.000	0.000
76	A	305	PRO	0	0.026	0.023	31.453	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	306	ILE	0	0.005	-0.019	29.621	0.001	0.001	0.000	0.000	0.000	0.000
78	A	307	LEU	0	-0.026	0.005	27.345	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	308	GLN	0	0.045	0.026	28.865	0.003	0.003	0.000	0.000	0.000	0.000
80	A	309	ARG	1	0.872	0.911	25.673	0.051	0.051	0.000	0.000	0.000	0.000
81	A	310	ILE	0	0.017	0.009	25.135	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	311	PRO	0	0.022	0.007	23.271	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	312	LEU	0	0.051	0.035	19.763	-0.018	-0.018	0.000	0.000	0.000	0.000
84	A	313	ALA	0	0.020	0.014	20.181	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	314	ARG	1	0.969	0.963	20.295	0.140	0.140	0.000	0.000	0.000	0.000
86	A	315	ALA	0	0.039	0.038	16.965	-0.017	-0.017	0.000	0.000	0.000	0.000
87	A	316	LEU	0	0.007	-0.008	15.569	-0.022	-0.022	0.000	0.000	0.000	0.000
88	A	317	TYR	0	0.017	0.010	15.754	0.015	0.015	0.000	0.000	0.000	0.000
89	A	318	TRP	0	0.009	0.012	14.659	0.018	0.018	0.000	0.000	0.000	0.000
90	A	319	ASP	-1	-0.818	-0.910	10.523	-0.684	-0.684	0.000	0.000	0.000	0.000
91	A	320	ALA	0	-0.064	-0.020	10.733	0.029	0.029	0.000	0.000	0.000	0.000
92	A	321	LEU	0	-0.016	-0.007	7.944	0.001	0.001	0.000	0.000	0.000	0.000
93	A	322	VAL	0	0.029	0.020	12.212	0.000	0.000	0.000	0.000	0.000	0.000
94	A	323	ASP	-1	-0.787	-0.877	14.652	0.299	0.299	0.000	0.000	0.000	0.000
95	A	324	HIS	0	-0.035	-0.016	10.684	0.266	0.266	0.000	0.000	0.000	0.000
96	A	325	TYR	0	0.008	-0.008	14.221	-0.079	-0.079	0.000	0.000	0.000	0.000
97	A	326	ILE	0	-0.009	-0.001	13.410	0.006	0.006	0.000	0.000	0.000	0.000
98	A	327	PRO	0	0.008	-0.001	11.474	0.023	0.023	0.000	0.000	0.000	0.000
99	A	328	ALA	0	0.045	0.010	11.924	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	329	GLU	-1	-0.932	-0.960	13.274	-0.452	-0.452	0.000	0.000	0.000	0.000
101	A	330	GLN	0	0.006	-0.010	15.184	0.050	0.050	0.000	0.000	0.000	0.000
102	A	331	ILE	0	0.005	0.021	15.850	0.036	0.036	0.000	0.000	0.000	0.000
103	A	332	GLU	-1	-0.911	-0.946	19.027	-0.102	-0.102	0.000	0.000	0.000	0.000
104	A	333	ALA	0	0.026	0.006	21.468	0.015	0.015	0.000	0.000	0.000	0.000
105	A	334	THR	0	-0.002	-0.025	19.932	0.017	0.017	0.000	0.000	0.000	0.000
106	A	335	ALA	0	0.002	-0.004	22.585	0.015	0.015	0.000	0.000	0.000	0.000
107	A	336	GLU	-1	-0.896	-0.936	24.678	-0.052	-0.052	0.000	0.000	0.000	0.000
108	A	337	VAL	0	0.005	-0.005	25.493	0.006	0.006	0.000	0.000	0.000	0.000
109	A	338	LEU	0	-0.002	-0.005	23.825	0.007	0.007	0.000	0.000	0.000	0.000
110	A	339	ARG	1	0.980	1.003	26.772	0.038	0.038	0.000	0.000	0.000	0.000
111	A	340	TRP	0	-0.062	-0.035	30.503	0.001	0.001	0.000	0.000	0.000	0.000
112	A	341	LEU	0	0.017	0.005	28.886	0.002	0.002	0.000	0.000	0.000	0.000
113	A	342	GLU	-1	-0.941	-0.972	31.769	0.038	0.038	0.000	0.000	0.000	0.000
114	A	343	ARG	1	0.857	0.940	33.035	0.014	0.014	0.000	0.000	0.000	0.000
115	A	344	GLN	0	-0.057	-0.006	34.593	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:230:GLY)