FMO DATABASE

FMODB ID: GNJL1

Calculation Name: 2J49-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2J49

Chain ID: A

ChEMBL ID:

UniProt ID: P38129

Base Structure: X-ray

Registration Date: 2023-06-19

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1304678.287863
FMO2-HF: Nuclear repulsion	1250126.564052
FMO2-HF: Total energy	-54551.723811
FMO2-MP2: Total energy	-54713.402333

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:149:PRO)

Summations of interaction energy for fragment #1(A:149:PRO)

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.
-4.909	-1.449	12.048	-5.665	-9.843	0.002

Interaction energy analysis for fragmet #1(A:149:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.005 / q_NPA : -0.026

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	151	ASN	0	-0.018	-0.016	2.070	4.004	3.777	9.538	-3.946	-5.365	-0.001
4	A	152	TYR	0	0.072	0.036	2.585	-5.548	-2.855	2.466	-1.548	-3.612	0.003
5	A	153	ILE	0	-0.004	-0.009	5.465	-0.751	-0.649	-0.001	-0.007	-0.094	0.000
6	A	154	ARG	1	0.966	0.985	7.317	-0.191	-0.191	0.000	0.000	0.000	0.000
7	A	155	ALA	0	0.054	0.039	7.181	-0.173	-0.173	0.000	0.000	0.000	0.000
8	A	156	TYR	0	0.048	0.021	9.027	-0.192	-0.192	0.000	0.000	0.000	0.000
9	A	157	SER	0	-0.015	-0.006	11.125	-0.200	-0.200	0.000	0.000	0.000	0.000
10	A	158	MET	0	-0.061	-0.010	11.940	-0.119	-0.119	0.000	0.000	0.000	0.000
11	A	159	LEU	0	0.014	0.010	13.431	-0.070	-0.070	0.000	0.000	0.000	0.000
12	A	160	LYS	1	0.857	0.919	15.108	-0.339	-0.339	0.000	0.000	0.000	0.000
13	A	161	ASN	0	-0.009	-0.013	16.763	-0.034	-0.034	0.000	0.000	0.000	0.000
14	A	162	TRP	0	0.031	0.031	18.084	-0.022	-0.022	0.000	0.000	0.000	0.000
15	A	163	VAL	0	0.005	0.010	19.094	-0.028	-0.028	0.000	0.000	0.000	0.000
16	A	164	ASP	-1	-0.843	-0.929	20.964	0.216	0.216	0.000	0.000	0.000	0.000
17	A	165	SER	0	-0.102	-0.045	22.537	-0.027	-0.027	0.000	0.000	0.000	0.000
18	A	166	SER	0	-0.018	-0.015	23.344	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	167	LEU	0	-0.009	-0.014	25.787	-0.012	-0.012	0.000	0.000	0.000	0.000
20	A	168	GLU	-1	-0.780	-0.897	28.925	0.156	0.156	0.000	0.000	0.000	0.000
21	A	169	ILE	0	-0.049	-0.016	31.093	0.003	0.003	0.000	0.000	0.000	0.000
22	A	170	TYR	0	-0.001	-0.017	26.922	0.002	0.002	0.000	0.000	0.000	0.000
23	A	171	LYS	1	0.858	0.927	25.467	-0.145	-0.145	0.000	0.000	0.000	0.000
24	A	172	PRO	0	0.005	0.024	25.891	0.018	0.018	0.000	0.000	0.000	0.000
25	A	173	GLU	-1	-0.780	-0.876	26.321	0.227	0.227	0.000	0.000	0.000	0.000
26	A	174	LEU	0	-0.020	-0.008	21.666	0.027	0.027	0.000	0.000	0.000	0.000
27	A	175	SER	0	0.022	-0.008	21.348	0.041	0.041	0.000	0.000	0.000	0.000
28	A	176	TYR	0	-0.052	-0.024	21.770	0.018	0.018	0.000	0.000	0.000	0.000
29	A	177	ILE	0	-0.002	-0.001	18.856	0.019	0.019	0.000	0.000	0.000	0.000
30	A	178	MET	0	0.010	0.013	15.956	0.068	0.068	0.000	0.000	0.000	0.000
31	A	179	TYR	0	-0.052	-0.046	16.483	0.072	0.072	0.000	0.000	0.000	0.000
32	A	180	PRO	0	0.018	0.009	16.729	0.041	0.041	0.000	0.000	0.000	0.000
33	A	181	ILE	0	0.010	0.011	12.889	0.085	0.085	0.000	0.000	0.000	0.000
34	A	182	PHE	0	-0.016	-0.009	12.405	0.177	0.177	0.000	0.000	0.000	0.000
35	A	183	ILE	0	0.008	0.012	11.978	0.100	0.100	0.000	0.000	0.000	0.000
36	A	184	TYR	0	0.015	-0.012	12.459	0.038	0.038	0.000	0.000	0.000	0.000
37	A	185	LEU	0	-0.033	-0.008	7.575	0.228	0.228	0.000	0.000	0.000	0.000
38	A	186	PHE	0	0.019	-0.002	7.652	0.258	0.258	0.000	0.000	0.000	0.000
39	A	187	LEU	0	0.015	0.012	9.490	-0.049	-0.049	0.000	0.000	0.000	0.000
40	A	188	ASN	0	-0.038	-0.033	6.766	0.005	0.005	0.000	0.000	0.000	0.000
41	A	189	LEU	0	-0.024	-0.012	3.342	-0.373	-0.031	0.043	-0.094	-0.291	0.000
42	A	190	VAL	0	-0.012	0.009	6.208	-0.292	-0.292	0.000	0.000	0.000	0.000
43	A	191	ALA	0	-0.033	-0.013	9.206	-0.134	-0.134	0.000	0.000	0.000	0.000
44	A	192	LYS	1	0.852	0.948	3.801	-2.463	-2.103	0.004	-0.057	-0.306	0.000
45	A	193	ASN	0	0.006	-0.013	4.773	-0.330	-0.245	-0.001	-0.009	-0.075	0.000
46	A	194	PRO	0	0.154	0.072	6.508	-0.006	-0.006	0.000	0.000	0.000	0.000
47	A	195	VAL	0	-0.061	-0.019	9.158	0.040	0.040	0.000	0.000	0.000	0.000
48	A	196	TYR	0	-0.004	-0.017	5.605	-0.154	-0.154	0.000	0.000	0.000	0.000
49	A	197	ALA	0	0.007	0.022	7.618	0.161	0.161	0.000	0.000	0.000	0.000
50	A	198	ARG	1	0.979	0.987	8.612	0.138	0.138	0.000	0.000	0.000	0.000
51	A	199	ARG	1	0.974	0.999	9.825	0.532	0.532	0.000	0.000	0.000	0.000
52	A	200	PHE	0	-0.033	-0.024	8.063	0.070	0.070	0.000	0.000	0.000	0.000
53	A	201	PHE	0	0.006	-0.006	10.261	0.041	0.041	0.000	0.000	0.000	0.000
54	A	202	ASP	-1	-0.874	-0.950	13.061	0.079	0.079	0.000	0.000	0.000	0.000
55	A	203	ARG	1	0.846	0.935	12.629	-0.204	-0.204	0.000	0.000	0.000	0.000
56	A	204	PHE	0	0.003	-0.019	10.625	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	205	SER	0	0.049	0.036	15.540	-0.008	-0.008	0.000	0.000	0.000	0.000
58	A	206	PRO	0	-0.074	-0.074	17.414	-0.011	-0.011	0.000	0.000	0.000	0.000
59	A	207	ASP	-1	-0.837	-0.897	18.910	0.256	0.256	0.000	0.000	0.000	0.000
60	A	208	PHE	0	-0.015	-0.008	16.471	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	209	LYS	1	0.880	0.950	20.242	-0.177	-0.177	0.000	0.000	0.000	0.000
62	A	210	ASP	-1	-0.905	-0.933	24.269	0.136	0.136	0.000	0.000	0.000	0.000
63	A	211	PHE	0	-0.007	-0.014	25.539	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	212	HIS	1	0.835	0.899	22.379	-0.248	-0.248	0.000	0.000	0.000	0.000
65	A	213	GLY	0	0.058	0.041	23.238	0.009	0.009	0.000	0.000	0.000	0.000
66	A	214	SER	0	-0.029	-0.018	24.269	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	215	GLU	-1	-0.771	-0.851	21.569	0.241	0.241	0.000	0.000	0.000	0.000
68	A	216	ILE	0	-0.002	-0.002	18.176	0.013	0.013	0.000	0.000	0.000	0.000
69	A	217	ASN	0	0.034	-0.004	20.085	0.003	0.003	0.000	0.000	0.000	0.000
70	A	218	ARG	1	0.812	0.897	22.572	-0.162	-0.162	0.000	0.000	0.000	0.000
71	A	219	LEU	0	-0.003	0.007	16.858	0.006	0.006	0.000	0.000	0.000	0.000
72	A	220	PHE	0	0.003	0.018	17.063	0.014	0.014	0.000	0.000	0.000	0.000
73	A	221	SER	0	-0.038	-0.010	17.927	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	222	VAL	0	-0.022	0.004	14.629	-0.014	-0.014	0.000	0.000	0.000	0.000
75	A	223	ASN	0	0.005	0.005	14.241	0.038	0.038	0.000	0.000	0.000	0.000
76	A	224	SER	0	0.024	-0.007	13.391	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	225	ILE	0	0.030	-0.002	11.403	0.037	0.037	0.000	0.000	0.000	0.000
78	A	226	ASP	-1	-0.910	-0.944	14.658	0.111	0.111	0.000	0.000	0.000	0.000
79	A	227	HIS	0	-0.003	-0.021	17.214	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	228	ILE	0	-0.041	-0.013	13.241	0.012	0.012	0.000	0.000	0.000	0.000
81	A	229	LYS	1	0.941	0.956	17.270	-0.190	-0.190	0.000	0.000	0.000	0.000
82	A	230	GLU	-1	-0.956	-0.949	20.524	0.096	0.096	0.000	0.000	0.000	0.000
83	A	231	ASN	0	-0.015	-0.013	19.627	0.007	0.007	0.000	0.000	0.000	0.000
84	A	232	GLU	-1	-0.773	-0.875	21.691	0.156	0.156	0.000	0.000	0.000	0.000
85	A	233	VAL	0	-0.025	-0.013	20.268	0.007	0.007	0.000	0.000	0.000	0.000
86	A	234	ALA	0	0.016	-0.004	17.041	0.027	0.027	0.000	0.000	0.000	0.000
87	A	235	SER	0	-0.002	-0.010	18.575	0.035	0.035	0.000	0.000	0.000	0.000
88	A	236	ALA	0	-0.043	-0.008	21.052	0.003	0.003	0.000	0.000	0.000	0.000
89	A	237	PHE	0	-0.020	-0.014	17.342	0.014	0.014	0.000	0.000	0.000	0.000
90	A	238	GLN	0	-0.025	-0.012	14.571	0.079	0.079	0.000	0.000	0.000	0.000
91	A	239	SER	0	-0.027	0.001	18.415	0.003	0.003	0.000	0.000	0.000	0.000
92	A	240	HIS	0	-0.041	-0.011	21.580	-0.030	-0.030	0.000	0.000	0.000	0.000
93	A	241	LYS	1	0.863	0.932	20.214	-0.339	-0.339	0.000	0.000	0.000	0.000
94	A	242	TYR	0	0.021	0.009	20.024	-0.037	-0.037	0.000	0.000	0.000	0.000
95	A	243	ARG	1	0.956	0.979	21.823	-0.198	-0.198	0.000	0.000	0.000	0.000
96	A	244	ILE	0	-0.003	0.007	22.002	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	245	THR	0	0.003	0.010	25.158	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	246	MET	0	-0.059	-0.008	22.657	0.015	0.015	0.000	0.000	0.000	0.000
99	A	247	SER	0	0.072	0.019	27.870	-0.008	-0.008	0.000	0.000	0.000	0.000
100	A	248	LYS	1	0.930	0.951	27.748	-0.168	-0.168	0.000	0.000	0.000	0.000
101	A	249	THR	0	-0.004	-0.011	27.585	0.014	0.014	0.000	0.000	0.000	0.000
102	A	250	THR	0	0.037	0.001	24.468	0.002	0.002	0.000	0.000	0.000	0.000
103	A	251	LEU	0	0.018	0.010	21.597	0.024	0.024	0.000	0.000	0.000	0.000
104	A	252	ASN	0	-0.021	-0.018	22.652	0.006	0.006	0.000	0.000	0.000	0.000
105	A	253	LEU	0	0.039	0.030	23.638	0.006	0.006	0.000	0.000	0.000	0.000
106	A	254	LEU	0	0.014	0.004	17.651	0.010	0.010	0.000	0.000	0.000	0.000
107	A	255	LEU	0	-0.025	-0.026	18.230	0.041	0.041	0.000	0.000	0.000	0.000
108	A	256	TYR	0	-0.057	-0.029	18.992	0.019	0.019	0.000	0.000	0.000	0.000
109	A	257	PHE	0	0.041	0.026	16.022	0.002	0.002	0.000	0.000	0.000	0.000
110	A	258	LEU	0	-0.029	-0.015	13.550	0.027	0.027	0.000	0.000	0.000	0.000
111	A	259	ASN	0	-0.043	-0.034	14.668	0.041	0.041	0.000	0.000	0.000	0.000
112	A	260	GLU	-1	-0.841	-0.889	16.362	0.208	0.208	0.000	0.000	0.000	0.000
113	A	261	ASN	0	-0.064	-0.048	13.815	-0.069	-0.069	0.000	0.000	0.000	0.000
114	A	262	GLU	-1	-0.902	-0.943	12.113	0.441	0.441	0.000	0.000	0.000	0.000
115	A	263	SER	0	-0.013	-0.010	10.005	0.190	0.190	0.000	0.000	0.000	0.000
116	A	264	ILE	0	-0.079	-0.040	9.355	-0.110	-0.110	0.000	0.000	0.000	0.000
117	A	265	GLY	0	-0.001	-0.020	7.736	0.217	0.217	0.000	0.000	0.000	0.000
118	A	266	GLY	0	0.018	0.010	8.610	0.217	0.217	0.000	0.000	0.000	0.000
119	A	267	SER	0	0.063	0.013	9.209	0.015	0.015	0.000	0.000	0.000	0.000
120	A	268	LEU	0	-0.047	-0.009	4.972	-0.166	-0.061	-0.001	-0.004	-0.100	0.000
121	A	269	ILE	0	-0.001	-0.002	8.562	-0.087	-0.087	0.000	0.000	0.000	0.000
122	A	270	ILE	0	0.048	0.021	11.654	-0.126	-0.126	0.000	0.000	0.000	0.000
123	A	271	SER	0	-0.015	-0.004	10.241	-0.155	-0.155	0.000	0.000	0.000	0.000
124	A	272	VAL	0	-0.010	-0.006	10.131	-0.094	-0.094	0.000	0.000	0.000	0.000
125	A	273	ILE	0	0.009	-0.004	12.792	-0.121	-0.121	0.000	0.000	0.000	0.000
126	A	274	ASN	0	-0.043	-0.021	15.657	-0.113	-0.113	0.000	0.000	0.000	0.000
127	A	275	GLN	0	-0.081	-0.039	11.960	-0.103	-0.103	0.000	0.000	0.000	0.000
128	A	276	HIS	0	0.022	0.013	12.533	-0.092	-0.092	0.000	0.000	0.000	0.000
129	A	277	LEU	0	-0.023	0.006	16.794	-0.040	-0.040	0.000	0.000	0.000	0.000
130	A	278	ASP	-1	-0.892	-0.936	19.786	0.271	0.271	0.000	0.000	0.000	0.000
131	A	279	PRO	0	-0.001	-0.013	22.087	-0.019	-0.019	0.000	0.000	0.000	0.000
132	A	280	ASN	0	-0.026	-0.015	24.817	-0.021	-0.021	0.000	0.000	0.000	0.000
133	A	281	ILE	0	0.003	-0.012	25.914	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	282	VAL	0	-0.015	0.018	29.361	-0.016	-0.016	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:149:PRO)