FMO DATABASE

FMODB ID: LZ439

Calculation Name: 1A68-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1A68

Chain ID: A

ChEMBL ID:

UniProt ID: Q16968

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	OptH
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	87
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-667704.218906
FMO2-HF: Nuclear repulsion	632052.05244
FMO2-HF: Total energy	-35652.166466
FMO2-MP2: Total energy	-35759.618225

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:66:GLU)

Summations of interaction energy for fragment #1(A:66:GLU)

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.
-180.629	-167.978	9.904	-10.446	-12.11	0.12

Interaction energy analysis for fragmet #1(A:66:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.836 / q_NPA : -0.941

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

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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	68	VAL	0	-0.017	0.002	3.825	-4.859	-2.870	-0.029	-0.971	-0.990	0.000
4	A	69	VAL	0	0.073	0.032	6.392	-0.678	-0.678	0.000	0.000	0.000	0.000
5	A	70	ILE	0	-0.031	-0.018	9.798	-0.729	-0.729	0.000	0.000	0.000	0.000
6	A	71	ASN	0	-0.048	-0.036	12.890	-0.852	-0.852	0.000	0.000	0.000	0.000
7	A	72	VAL	0	0.047	0.021	16.069	-0.470	-0.470	0.000	0.000	0.000	0.000
8	A	73	SER	0	0.030	-0.002	19.200	-0.457	-0.457	0.000	0.000	0.000	0.000
9	A	74	GLY	0	-0.018	-0.004	20.275	-0.648	-0.648	0.000	0.000	0.000	0.000
10	A	75	LEU	0	-0.068	-0.027	19.005	-0.077	-0.077	0.000	0.000	0.000	0.000
11	A	76	ARG	1	0.866	0.918	14.404	-16.097	-16.097	0.000	0.000	0.000	0.000
12	A	77	PHE	0	-0.004	0.014	13.281	-0.181	-0.181	0.000	0.000	0.000	0.000
13	A	78	GLU	-1	-0.912	-0.958	8.729	26.455	26.455	0.000	0.000	0.000	0.000
14	A	79	THR	0	-0.003	-0.007	7.534	0.316	0.316	0.000	0.000	0.000	0.000
15	A	80	GLN	0	-0.001	0.002	2.537	-12.906	-9.659	1.268	-1.964	-2.551	0.025
16	A	81	LEU	0	0.029	0.011	3.171	-9.555	-7.397	0.127	-1.089	-1.195	0.007
17	A	82	LYS	1	0.886	0.937	2.213	-126.146	-120.963	8.538	-6.371	-7.350	0.088
18	A	83	THR	0	0.010	0.014	4.452	-6.740	-6.666	0.000	-0.051	-0.024	0.000
19	A	84	LEU	0	0.010	0.005	6.888	-4.941	-4.941	0.000	0.000	0.000	0.000
20	A	85	ASN	0	-0.002	-0.015	6.960	-6.028	-6.028	0.000	0.000	0.000	0.000
21	A	86	GLN	0	-0.052	-0.020	9.014	-1.824	-1.824	0.000	0.000	0.000	0.000
22	A	87	PHE	0	0.016	0.035	10.922	-1.702	-1.702	0.000	0.000	0.000	0.000
23	A	88	PRO	0	0.007	0.017	13.225	-0.232	-0.232	0.000	0.000	0.000	0.000
24	A	89	ASP	-1	-0.932	-0.967	14.436	17.161	17.161	0.000	0.000	0.000	0.000
25	A	90	THR	0	0.009	0.006	15.076	-0.413	-0.413	0.000	0.000	0.000	0.000
26	A	91	LEU	0	0.006	-0.005	16.473	0.798	0.798	0.000	0.000	0.000	0.000
27	A	92	LEU	0	0.004	-0.017	12.527	0.666	0.666	0.000	0.000	0.000	0.000
28	A	93	GLY	0	0.052	0.040	11.484	2.652	2.652	0.000	0.000	0.000	0.000
29	A	94	ASN	0	0.003	0.012	12.568	0.888	0.888	0.000	0.000	0.000	0.000
30	A	95	PRO	0	-0.001	-0.018	11.410	-0.760	-0.760	0.000	0.000	0.000	0.000
31	A	96	GLN	0	0.013	0.007	13.596	-0.571	-0.571	0.000	0.000	0.000	0.000
32	A	97	LYS	1	0.824	0.938	17.075	-16.916	-16.916	0.000	0.000	0.000	0.000
33	A	98	ARG	1	0.890	0.928	9.384	-29.326	-29.326	0.000	0.000	0.000	0.000
34	A	99	ASN	0	0.018	-0.005	12.254	0.807	0.807	0.000	0.000	0.000	0.000
35	A	100	ARG	1	0.906	0.978	14.701	-13.744	-13.744	0.000	0.000	0.000	0.000
36	A	101	TYR	0	-0.014	-0.013	16.103	-0.994	-0.994	0.000	0.000	0.000	0.000
37	A	102	TYR	0	-0.074	-0.046	9.799	-0.211	-0.211	0.000	0.000	0.000	0.000
38	A	103	ASP	-1	-0.804	-0.892	13.896	14.169	14.169	0.000	0.000	0.000	0.000
39	A	104	PRO	0	0.009	-0.016	13.214	0.842	0.842	0.000	0.000	0.000	0.000
40	A	105	LEU	0	-0.046	-0.008	14.085	0.154	0.154	0.000	0.000	0.000	0.000
41	A	106	ARG	1	0.878	0.920	14.752	-13.995	-13.995	0.000	0.000	0.000	0.000
42	A	107	ASN	0	-0.016	0.033	7.203	0.993	0.993	0.000	0.000	0.000	0.000
43	A	108	GLU	-1	-0.780	-0.870	9.959	19.051	19.051	0.000	0.000	0.000	0.000
44	A	109	TYR	0	-0.028	-0.016	8.559	0.176	0.176	0.000	0.000	0.000	0.000
45	A	110	PHE	0	-0.006	0.001	13.474	0.013	0.013	0.000	0.000	0.000	0.000
46	A	111	PHE	0	-0.011	-0.019	15.189	-0.259	-0.259	0.000	0.000	0.000	0.000
47	A	112	ASP	-1	-0.912	-0.940	19.743	11.726	11.726	0.000	0.000	0.000	0.000
48	A	113	ARG	1	0.863	0.912	22.019	-13.189	-13.189	0.000	0.000	0.000	0.000
49	A	114	ASN	0	0.051	0.052	23.891	0.378	0.378	0.000	0.000	0.000	0.000
50	A	115	ARG	1	0.944	0.968	22.428	-12.418	-12.418	0.000	0.000	0.000	0.000
51	A	116	PRO	0	-0.025	-0.016	22.076	0.503	0.503	0.000	0.000	0.000	0.000
52	A	117	SER	0	0.029	-0.029	23.321	0.080	0.080	0.000	0.000	0.000	0.000
53	A	118	PHE	0	0.023	0.009	14.603	0.407	0.407	0.000	0.000	0.000	0.000
54	A	119	ASP	-1	-0.848	-0.911	17.842	16.670	16.670	0.000	0.000	0.000	0.000
55	A	120	ALA	0	-0.058	-0.035	18.014	0.677	0.677	0.000	0.000	0.000	0.000
56	A	121	ILE	0	-0.038	-0.004	16.506	0.287	0.287	0.000	0.000	0.000	0.000
57	A	122	LEU	0	0.022	0.007	11.036	1.131	1.131	0.000	0.000	0.000	0.000
58	A	123	TYR	0	0.036	0.015	13.596	1.331	1.331	0.000	0.000	0.000	0.000
59	A	124	PHE	0	0.027	0.037	15.745	0.099	0.099	0.000	0.000	0.000	0.000
60	A	125	TYR	0	-0.028	-0.034	10.991	-0.024	-0.024	0.000	0.000	0.000	0.000
61	A	126	GLN	0	0.001	-0.011	10.769	-0.408	-0.408	0.000	0.000	0.000	0.000
62	A	127	SER	0	-0.102	-0.054	12.253	-0.267	-0.267	0.000	0.000	0.000	0.000
63	A	128	GLY	0	0.038	0.022	14.033	-0.792	-0.792	0.000	0.000	0.000	0.000
64	A	129	GLY	0	0.028	0.014	14.974	-0.810	-0.810	0.000	0.000	0.000	0.000
65	A	130	ARG	1	0.847	0.935	17.811	-16.386	-16.386	0.000	0.000	0.000	0.000
66	A	131	LEU	0	0.049	0.022	19.419	0.431	0.431	0.000	0.000	0.000	0.000
67	A	132	ARG	1	0.899	0.936	21.816	-13.290	-13.290	0.000	0.000	0.000	0.000
68	A	133	ARG	1	0.909	0.950	23.742	-10.023	-10.023	0.000	0.000	0.000	0.000
69	A	134	PRO	0	0.014	0.020	23.904	-0.332	-0.332	0.000	0.000	0.000	0.000
70	A	135	VAL	0	0.039	0.014	26.577	-0.259	-0.259	0.000	0.000	0.000	0.000
71	A	136	ASN	0	-0.006	-0.004	26.693	-0.186	-0.186	0.000	0.000	0.000	0.000
72	A	137	VAL	0	-0.010	0.005	26.075	-0.118	-0.118	0.000	0.000	0.000	0.000
73	A	138	PRO	0	0.048	0.031	29.483	-0.027	-0.027	0.000	0.000	0.000	0.000
74	A	139	LEU	0	-0.005	-0.021	30.654	0.328	0.328	0.000	0.000	0.000	0.000
75	A	140	ASP	-1	-0.849	-0.931	30.946	9.554	9.554	0.000	0.000	0.000	0.000
76	A	141	VAL	0	0.053	0.038	28.318	0.198	0.198	0.000	0.000	0.000	0.000
77	A	142	PHE	0	0.005	-0.020	22.821	0.345	0.345	0.000	0.000	0.000	0.000
78	A	143	SER	0	-0.043	-0.018	26.197	0.360	0.360	0.000	0.000	0.000	0.000
79	A	144	GLU	-1	-0.849	-0.939	27.466	10.349	10.349	0.000	0.000	0.000	0.000
80	A	145	GLU	-1	-0.860	-0.917	23.133	13.212	13.212	0.000	0.000	0.000	0.000
81	A	146	ILE	0	-0.037	-0.015	22.634	0.583	0.583	0.000	0.000	0.000	0.000
82	A	147	LYS	1	0.892	0.948	23.096	-9.963	-9.963	0.000	0.000	0.000	0.000
83	A	148	PHE	0	-0.024	0.004	20.476	0.168	0.168	0.000	0.000	0.000	0.000
84	A	149	TYR	0	-0.007	-0.024	18.155	0.298	0.298	0.000	0.000	0.000	0.000
85	A	150	GLU	-1	-0.900	-0.946	19.053	15.862	15.862	0.000	0.000	0.000	0.000
86	A	151	LEU	0	0.000	-0.001	17.336	0.346	0.346	0.000	0.000	0.000	0.000
87	A	152	GLY	0	-0.028	0.006	20.634	-0.290	-0.290	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:66:GLU)