FMO DATABASE

FMODB ID: 9G322

Calculation Name: 1JHE-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1JHE

Chain ID: A

ChEMBL ID:

UniProt ID: P0A7C2

Base Structure: X-ray

Registration Date: 2023-06-20

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	124
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1008901.630997
FMO2-HF: Nuclear repulsion	961738.222304
FMO2-HF: Total energy	-47163.408693
FMO2-MP2: Total energy	-47302.176003

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:75:GLY)

Summations of interaction energy for fragment #1(A:75: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.
-4.26	0.448	2.886	-3.877	-3.715	-0.016

Interaction energy analysis for fragmet #1(A:75:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.044 / q_NPA : 0.024

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	77	PRO	0	0.020	0.039	3.811	0.003	1.490	-0.007	-0.744	-0.735	0.003
4	A	78	LEU	0	-0.018	0.003	6.329	0.612	0.612	0.000	0.000	0.000	0.000
5	A	79	VAL	0	-0.014	-0.014	9.493	0.068	0.068	0.000	0.000	0.000	0.000
6	A	80	GLY	0	0.114	0.069	12.355	0.149	0.149	0.000	0.000	0.000	0.000
7	A	81	ARG	1	0.878	0.945	15.365	0.359	0.359	0.000	0.000	0.000	0.000
8	A	82	VAL	0	0.039	0.017	18.149	-0.016	-0.016	0.000	0.000	0.000	0.000
9	A	83	ALA	0	0.005	0.015	19.978	0.013	0.013	0.000	0.000	0.000	0.000
10	A	84	ALA	0	-0.022	0.002	23.057	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	85	GLY	0	0.001	-0.044	24.602	0.026	0.026	0.000	0.000	0.000	0.000
12	A	86	GLU	-1	-0.968	-0.967	27.839	-0.196	-0.196	0.000	0.000	0.000	0.000
13	A	87	PRO	0	-0.010	-0.010	26.146	-0.013	-0.013	0.000	0.000	0.000	0.000
14	A	88	LEU	0	0.013	0.026	21.931	0.016	0.016	0.000	0.000	0.000	0.000
15	A	89	PRO	0	0.040	0.012	24.397	-0.028	-0.028	0.000	0.000	0.000	0.000
16	A	90	ALA	0	-0.019	-0.034	19.951	-0.009	-0.009	0.000	0.000	0.000	0.000
17	A	91	GLN	0	0.011	0.019	20.389	-0.019	-0.019	0.000	0.000	0.000	0.000
18	A	92	TRP	0	-0.033	-0.034	15.210	-0.033	-0.033	0.000	0.000	0.000	0.000
19	A	93	HIS	0	0.041	0.014	13.948	0.036	0.036	0.000	0.000	0.000	0.000
20	A	94	ILE	0	-0.031	-0.011	7.816	-0.056	-0.056	0.000	0.000	0.000	0.000
21	A	95	GLU	-1	-0.913	-0.962	10.863	-0.597	-0.597	0.000	0.000	0.000	0.000
22	A	96	GLY	0	-0.028	-0.014	8.404	0.267	0.267	0.000	0.000	0.000	0.000
23	A	97	HIS	0	-0.065	-0.041	2.840	0.897	1.791	0.172	-0.423	-0.643	-0.001
24	A	98	TYR	0	-0.010	-0.002	4.181	1.303	1.496	0.000	-0.033	-0.160	0.000
25	A	99	GLN	0	-0.001	-0.018	2.382	-5.913	-3.827	2.723	-2.640	-2.169	-0.018
26	A	100	VAL	0	-0.001	-0.007	3.788	-0.216	-0.164	0.000	-0.027	-0.025	0.000
27	A	101	ASP	-1	-0.818	-0.906	4.930	-0.128	-0.163	-0.001	-0.003	0.040	0.000
28	A	102	PRO	0	0.013	0.000	4.674	-0.233	-0.202	-0.001	-0.007	-0.023	0.000
29	A	103	SER	0	-0.035	-0.034	7.321	-0.039	-0.039	0.000	0.000	0.000	0.000
30	A	104	LEU	0	-0.050	-0.008	9.581	0.038	0.038	0.000	0.000	0.000	0.000
31	A	105	PHE	0	-0.039	-0.004	8.975	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	106	LYS	1	0.966	0.997	13.258	0.174	0.174	0.000	0.000	0.000	0.000
33	A	107	PRO	0	-0.054	-0.052	15.381	0.029	0.029	0.000	0.000	0.000	0.000
34	A	108	ASN	0	0.039	0.021	9.971	0.020	0.020	0.000	0.000	0.000	0.000
35	A	109	ALA	0	-0.030	0.004	8.852	-0.012	-0.012	0.000	0.000	0.000	0.000
36	A	110	ASP	-1	-0.811	-0.922	8.250	-1.295	-1.295	0.000	0.000	0.000	0.000
37	A	111	PHE	0	-0.054	-0.039	7.858	-0.548	-0.548	0.000	0.000	0.000	0.000
38	A	112	LEU	0	-0.012	-0.005	7.488	0.376	0.376	0.000	0.000	0.000	0.000
39	A	113	LEU	0	0.012	0.009	10.644	0.009	0.009	0.000	0.000	0.000	0.000
40	A	114	ARG	1	0.887	0.935	14.118	0.527	0.527	0.000	0.000	0.000	0.000
41	A	115	VAL	0	-0.005	-0.008	16.135	0.024	0.024	0.000	0.000	0.000	0.000
42	A	116	SER	0	-0.036	-0.001	19.338	0.026	0.026	0.000	0.000	0.000	0.000
43	A	117	GLY	0	0.034	0.018	22.570	0.004	0.004	0.000	0.000	0.000	0.000
44	A	118	MET	0	0.008	-0.004	24.905	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	119	SER	0	0.014	0.021	27.164	0.009	0.009	0.000	0.000	0.000	0.000
46	A	120	MET	0	0.008	0.019	24.076	0.015	0.015	0.000	0.000	0.000	0.000
47	A	121	LYS	1	0.904	0.920	25.378	0.130	0.130	0.000	0.000	0.000	0.000
48	A	122	ASP	-1	-0.870	-0.912	27.305	-0.128	-0.128	0.000	0.000	0.000	0.000
49	A	123	ILE	0	-0.055	-0.030	23.776	0.008	0.008	0.000	0.000	0.000	0.000
50	A	124	GLY	0	-0.027	-0.011	23.768	-0.008	-0.008	0.000	0.000	0.000	0.000
51	A	125	ILE	0	-0.043	-0.013	20.257	-0.015	-0.015	0.000	0.000	0.000	0.000
52	A	126	MET	0	-0.022	-0.028	21.630	0.019	0.019	0.000	0.000	0.000	0.000
53	A	127	ASP	-1	-0.813	-0.916	21.194	-0.292	-0.292	0.000	0.000	0.000	0.000
54	A	128	GLY	0	0.016	0.003	19.406	0.018	0.018	0.000	0.000	0.000	0.000
55	A	129	ASP	-1	-0.778	-0.831	17.379	-0.310	-0.310	0.000	0.000	0.000	0.000
56	A	130	LEU	0	-0.035	-0.014	10.733	-0.043	-0.043	0.000	0.000	0.000	0.000
57	A	131	LEU	0	-0.001	-0.006	14.219	0.056	0.056	0.000	0.000	0.000	0.000
58	A	132	ALA	0	0.010	0.000	11.342	-0.140	-0.140	0.000	0.000	0.000	0.000
59	A	133	VAL	0	0.002	-0.009	11.750	0.180	0.180	0.000	0.000	0.000	0.000
60	A	134	HIS	0	-0.011	0.019	12.041	-0.087	-0.087	0.000	0.000	0.000	0.000
61	A	135	LYS	1	0.802	0.873	13.238	0.787	0.787	0.000	0.000	0.000	0.000
62	A	136	THR	0	-0.008	-0.012	14.942	0.053	0.053	0.000	0.000	0.000	0.000
63	A	137	GLN	0	-0.010	0.002	18.424	-0.014	-0.014	0.000	0.000	0.000	0.000
64	A	138	ASP	-1	-0.908	-0.956	21.865	-0.237	-0.237	0.000	0.000	0.000	0.000
65	A	139	VAL	0	-0.002	0.013	21.335	0.002	0.002	0.000	0.000	0.000	0.000
66	A	140	ARG	1	0.927	0.960	24.065	0.187	0.187	0.000	0.000	0.000	0.000
67	A	141	ASN	0	-0.001	-0.018	27.008	-0.017	-0.017	0.000	0.000	0.000	0.000
68	A	142	GLY	0	0.014	0.009	28.968	0.008	0.008	0.000	0.000	0.000	0.000
69	A	143	GLN	0	0.000	0.011	22.516	0.003	0.003	0.000	0.000	0.000	0.000
70	A	144	VAL	0	0.031	0.022	21.603	0.009	0.009	0.000	0.000	0.000	0.000
71	A	145	VAL	0	0.005	-0.005	21.273	-0.026	-0.026	0.000	0.000	0.000	0.000
72	A	146	VAL	0	0.044	0.028	17.553	0.010	0.010	0.000	0.000	0.000	0.000
73	A	147	ALA	0	-0.041	-0.028	20.808	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	148	ARG	1	0.826	0.904	19.314	0.464	0.464	0.000	0.000	0.000	0.000
75	A	149	ILE	0	-0.004	-0.015	24.781	0.018	0.018	0.000	0.000	0.000	0.000
76	A	150	ASP	-1	-0.876	-0.933	28.313	-0.223	-0.223	0.000	0.000	0.000	0.000
77	A	151	ASP	-1	-0.928	-0.964	25.808	-0.284	-0.284	0.000	0.000	0.000	0.000
78	A	152	ALA	0	-0.032	-0.010	24.864	-0.030	-0.030	0.000	0.000	0.000	0.000
79	A	153	VAL	0	-0.020	-0.012	20.192	0.001	0.001	0.000	0.000	0.000	0.000
80	A	154	THR	0	-0.002	-0.013	23.268	0.017	0.017	0.000	0.000	0.000	0.000
81	A	155	VAL	0	-0.007	0.000	20.723	-0.029	-0.029	0.000	0.000	0.000	0.000
82	A	156	ALA	0	0.006	-0.005	22.962	0.027	0.027	0.000	0.000	0.000	0.000
83	A	157	ARG	1	0.782	0.873	25.008	0.175	0.175	0.000	0.000	0.000	0.000
84	A	158	LEU	0	0.035	0.031	26.250	0.011	0.011	0.000	0.000	0.000	0.000
85	A	159	LYS	1	0.905	0.959	28.430	0.145	0.145	0.000	0.000	0.000	0.000
86	A	160	LYS	1	0.958	0.989	30.770	0.176	0.176	0.000	0.000	0.000	0.000
87	A	161	GLN	0	-0.003	-0.007	33.230	0.005	0.005	0.000	0.000	0.000	0.000
88	A	162	GLY	0	0.036	0.020	36.818	0.003	0.003	0.000	0.000	0.000	0.000
89	A	163	ASN	0	-0.017	-0.024	35.868	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	164	LYS	1	0.937	0.975	36.887	0.126	0.126	0.000	0.000	0.000	0.000
91	A	165	VAL	0	-0.021	-0.023	30.153	0.002	0.002	0.000	0.000	0.000	0.000
92	A	166	GLU	-1	-0.856	-0.920	33.268	-0.135	-0.135	0.000	0.000	0.000	0.000
93	A	167	LEU	0	0.002	0.005	27.170	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	168	LEU	0	-0.032	-0.030	30.045	0.011	0.011	0.000	0.000	0.000	0.000
95	A	169	PRO	0	0.044	0.024	28.918	-0.017	-0.017	0.000	0.000	0.000	0.000
96	A	170	GLU	-1	-0.867	-0.929	27.309	-0.164	-0.164	0.000	0.000	0.000	0.000
97	A	171	ASN	0	0.038	0.003	29.814	0.013	0.013	0.000	0.000	0.000	0.000
98	A	172	SER	0	-0.025	-0.008	32.205	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	173	GLU	-1	-0.933	-0.943	34.386	-0.111	-0.111	0.000	0.000	0.000	0.000
100	A	174	PHE	0	-0.030	-0.015	30.306	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	175	LYS	1	0.960	0.977	34.375	0.125	0.125	0.000	0.000	0.000	0.000
102	A	176	PRO	0	-0.007	-0.004	33.372	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	177	ILE	0	0.022	0.018	30.055	0.007	0.007	0.000	0.000	0.000	0.000
104	A	178	VAL	0	-0.045	-0.033	33.407	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	179	VAL	0	0.050	0.031	31.386	0.000	0.000	0.000	0.000	0.000	0.000
106	A	180	ASP	-1	-0.779	-0.857	34.750	-0.127	-0.127	0.000	0.000	0.000	0.000
107	A	181	LEU	0	-0.006	-0.032	31.881	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	182	ARG	1	0.787	0.873	35.387	0.117	0.117	0.000	0.000	0.000	0.000
109	A	183	GLN	0	-0.046	-0.022	37.876	0.006	0.006	0.000	0.000	0.000	0.000
110	A	184	GLN	0	-0.034	-0.003	32.547	0.007	0.007	0.000	0.000	0.000	0.000
111	A	185	SER	0	0.006	0.007	29.672	0.006	0.006	0.000	0.000	0.000	0.000
112	A	186	PHE	0	0.005	-0.008	27.735	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	187	THR	0	0.007	0.007	22.485	0.014	0.014	0.000	0.000	0.000	0.000
114	A	188	ILE	0	-0.009	0.014	21.842	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	189	GLU	-1	-0.819	-0.904	18.094	-0.575	-0.575	0.000	0.000	0.000	0.000
116	A	190	GLY	0	0.049	0.015	17.241	-0.057	-0.057	0.000	0.000	0.000	0.000
117	A	191	LEU	0	-0.070	-0.015	17.686	0.058	0.058	0.000	0.000	0.000	0.000
118	A	192	ALA	0	0.020	0.010	16.569	-0.073	-0.073	0.000	0.000	0.000	0.000
119	A	193	VAL	0	-0.041	-0.028	13.496	0.061	0.061	0.000	0.000	0.000	0.000
120	A	194	GLY	0	0.020	-0.005	14.400	0.039	0.039	0.000	0.000	0.000	0.000
121	A	195	VAL	0	-0.017	0.005	15.132	-0.061	-0.061	0.000	0.000	0.000	0.000
122	A	196	ILE	0	-0.010	0.008	9.697	0.056	0.056	0.000	0.000	0.000	0.000
123	A	197	ARG	1	0.822	0.874	13.980	0.178	0.178	0.000	0.000	0.000	0.000
124	A	198	ASN	0	-0.001	0.003	12.272	0.014	0.014	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:75:GLY)