FMO DATABASE

FMODB ID: LZNZ9

Calculation Name: 1A3A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1A3A

Chain ID: A

ChEMBL ID:

UniProt ID: P00550

Base Structure: X-ray

Registration Date: 2023-06-22

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	145
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1361192.028354
FMO2-HF: Nuclear repulsion	1305699.427618
FMO2-HF: Total energy	-55492.600737
FMO2-MP2: Total energy	-55657.160196

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:4:LEU)

Summations of interaction energy for fragment #1(A:4:LEU)

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.
-2.998	0.723	0.81	-1.455	-3.075	0

Interaction energy analysis for fragmet #1(A:4:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.010 / q_NPA : -0.011

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	6	LYS	1	0.985	0.988	3.795	0.070	2.098	-0.034	-1.002	-0.992	-0.001
4	A	7	LEU	0	-0.006	0.002	6.918	-0.218	-0.218	0.000	0.000	0.000	0.000
5	A	8	GLY	0	0.040	0.018	10.067	0.083	0.083	0.000	0.000	0.000	0.000
6	A	9	ALA	0	0.054	0.016	13.605	-0.041	-0.041	0.000	0.000	0.000	0.000
7	A	10	GLU	-1	-0.976	-0.981	14.973	-0.067	-0.067	0.000	0.000	0.000	0.000
8	A	11	ASN	0	-0.066	-0.046	9.702	0.045	0.045	0.000	0.000	0.000	0.000
9	A	12	ILE	0	0.021	0.023	13.709	0.000	0.000	0.000	0.000	0.000	0.000
10	A	13	PHE	0	-0.024	-0.029	15.798	-0.018	-0.018	0.000	0.000	0.000	0.000
11	A	14	LEU	0	0.015	0.006	18.528	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	15	GLY	0	0.002	0.007	21.229	-0.012	-0.012	0.000	0.000	0.000	0.000
13	A	16	ARG	1	0.834	0.938	21.178	0.010	0.010	0.000	0.000	0.000	0.000
14	A	17	LYS	1	0.847	0.885	24.197	-0.009	-0.009	0.000	0.000	0.000	0.000
15	A	18	ALA	0	-0.028	-0.021	25.229	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	19	ALA	0	0.001	0.011	27.156	0.004	0.004	0.000	0.000	0.000	0.000
17	A	20	THR	0	-0.020	-0.008	27.875	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	21	LYS	1	0.937	0.960	22.922	0.099	0.099	0.000	0.000	0.000	0.000
19	A	22	GLU	-1	-0.897	-0.960	22.909	-0.102	-0.102	0.000	0.000	0.000	0.000
20	A	23	GLU	-1	-0.873	-0.930	23.727	-0.058	-0.058	0.000	0.000	0.000	0.000
21	A	24	ALA	0	0.017	0.010	21.276	-0.004	-0.004	0.000	0.000	0.000	0.000
22	A	25	ILE	0	-0.024	-0.016	18.405	-0.015	-0.015	0.000	0.000	0.000	0.000
23	A	26	ARG	1	0.892	0.952	19.171	0.101	0.101	0.000	0.000	0.000	0.000
24	A	27	PHE	0	0.020	0.012	19.841	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	28	ALA	0	0.018	-0.002	15.789	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	29	GLY	0	0.058	0.003	16.073	-0.032	-0.032	0.000	0.000	0.000	0.000
27	A	30	GLU	-1	-0.909	-0.964	16.802	-0.133	-0.133	0.000	0.000	0.000	0.000
28	A	31	GLN	0	-0.029	-0.009	16.742	0.000	0.000	0.000	0.000	0.000	0.000
29	A	32	LEU	0	-0.027	-0.002	10.599	-0.019	-0.019	0.000	0.000	0.000	0.000
30	A	33	VAL	0	-0.040	-0.011	13.742	-0.034	-0.034	0.000	0.000	0.000	0.000
31	A	34	LYS	1	0.927	0.961	16.359	0.084	0.084	0.000	0.000	0.000	0.000
32	A	35	GLY	0	0.044	0.038	14.050	0.016	0.016	0.000	0.000	0.000	0.000
33	A	36	GLY	0	0.003	-0.003	13.200	-0.022	-0.022	0.000	0.000	0.000	0.000
34	A	37	TYR	0	-0.050	-0.036	7.796	-0.061	-0.061	0.000	0.000	0.000	0.000
35	A	38	VAL	0	-0.016	-0.007	10.673	-0.105	-0.105	0.000	0.000	0.000	0.000
36	A	39	GLU	-1	-0.829	-0.894	13.261	-0.203	-0.203	0.000	0.000	0.000	0.000
37	A	40	PRO	0	0.043	-0.003	16.837	-0.015	-0.015	0.000	0.000	0.000	0.000
38	A	41	GLU	-1	-0.843	-0.915	19.437	-0.205	-0.205	0.000	0.000	0.000	0.000
39	A	42	TYR	0	-0.028	-0.049	10.803	-0.018	-0.018	0.000	0.000	0.000	0.000
40	A	43	VAL	0	0.003	0.005	16.654	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	44	GLN	0	-0.056	-0.035	18.799	0.015	0.015	0.000	0.000	0.000	0.000
42	A	45	ALA	0	0.040	0.023	16.351	0.005	0.005	0.000	0.000	0.000	0.000
43	A	46	MET	0	-0.064	-0.019	14.670	-0.013	-0.013	0.000	0.000	0.000	0.000
44	A	47	LEU	0	-0.030	-0.006	17.253	0.016	0.016	0.000	0.000	0.000	0.000
45	A	48	ASP	-1	-0.857	-0.921	20.140	-0.168	-0.168	0.000	0.000	0.000	0.000
46	A	49	ARG	1	0.858	0.914	13.599	0.336	0.336	0.000	0.000	0.000	0.000
47	A	50	GLU	-1	-0.763	-0.843	18.558	-0.142	-0.142	0.000	0.000	0.000	0.000
48	A	51	LYS	1	0.906	0.957	20.554	0.125	0.125	0.000	0.000	0.000	0.000
49	A	52	LEU	0	-0.069	-0.024	19.899	0.008	0.008	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.085	-0.057	18.522	0.002	0.002	0.000	0.000	0.000	0.000
51	A	54	PRO	0	0.037	0.029	19.099	-0.020	-0.020	0.000	0.000	0.000	0.000
52	A	55	THR	0	-0.101	-0.076	15.953	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	56	TYR	0	0.002	0.000	17.524	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	57	LEU	0	-0.050	-0.044	13.620	-0.013	-0.013	0.000	0.000	0.000	0.000
55	A	58	GLY	0	0.058	0.045	18.358	0.008	0.008	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.876	-0.944	19.371	0.035	0.035	0.000	0.000	0.000	0.000
57	A	60	SER	0	-0.025	-0.005	19.862	0.016	0.016	0.000	0.000	0.000	0.000
58	A	61	ILE	0	0.011	0.013	14.356	0.003	0.003	0.000	0.000	0.000	0.000
59	A	62	ALA	0	0.036	0.023	16.823	-0.018	-0.018	0.000	0.000	0.000	0.000
60	A	63	VAL	0	-0.026	-0.008	11.959	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	64	PRO	0	0.074	0.054	13.742	-0.060	-0.060	0.000	0.000	0.000	0.000
62	A	65	HIS	1	0.868	0.914	11.069	0.330	0.330	0.000	0.000	0.000	0.000
63	A	66	GLY	0	0.074	0.045	12.016	0.054	0.054	0.000	0.000	0.000	0.000
64	A	67	THR	0	-0.050	-0.035	13.724	-0.010	-0.010	0.000	0.000	0.000	0.000
65	A	68	VAL	0	0.026	0.015	13.199	-0.043	-0.043	0.000	0.000	0.000	0.000
66	A	69	GLU	-1	-0.849	-0.929	14.261	-0.289	-0.289	0.000	0.000	0.000	0.000
67	A	70	ALA	0	-0.010	0.003	15.164	0.010	0.010	0.000	0.000	0.000	0.000
68	A	71	LYS	1	0.942	0.972	11.150	0.345	0.345	0.000	0.000	0.000	0.000
69	A	72	ASP	-1	-0.897	-0.956	11.509	-0.460	-0.460	0.000	0.000	0.000	0.000
70	A	73	ARG	1	0.786	0.879	13.853	0.271	0.271	0.000	0.000	0.000	0.000
71	A	74	VAL	0	-0.024	0.001	8.051	0.000	0.000	0.000	0.000	0.000	0.000
72	A	75	LEU	0	-0.002	0.003	10.774	-0.020	-0.020	0.000	0.000	0.000	0.000
73	A	76	LYS	1	0.769	0.885	7.165	0.444	0.444	0.000	0.000	0.000	0.000
74	A	77	THR	0	0.024	0.012	2.496	-0.944	0.123	0.837	-0.346	-1.558	0.001
75	A	78	GLY	0	-0.027	-0.019	4.803	-0.219	-0.181	-0.001	-0.013	-0.024	0.000
76	A	79	VAL	0	0.002	0.012	6.272	0.008	0.008	0.000	0.000	0.000	0.000
77	A	80	VAL	0	-0.016	0.011	9.148	0.095	0.095	0.000	0.000	0.000	0.000
78	A	81	PHE	0	0.035	0.010	12.140	-0.018	-0.018	0.000	0.000	0.000	0.000
79	A	82	CYS	0	-0.058	-0.026	13.654	0.008	0.008	0.000	0.000	0.000	0.000
80	A	83	GLN	0	0.024	0.010	17.330	-0.018	-0.018	0.000	0.000	0.000	0.000
81	A	84	TYR	0	-0.014	-0.016	19.689	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	85	PRO	0	0.027	0.017	22.936	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.858	-0.921	25.029	0.018	0.018	0.000	0.000	0.000	0.000
84	A	87	GLY	0	-0.009	0.004	24.672	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	88	VAL	0	-0.031	-0.013	23.505	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	89	ARG	1	0.936	0.977	24.514	0.044	0.044	0.000	0.000	0.000	0.000
87	A	90	PHE	0	-0.039	-0.052	19.615	-0.012	-0.012	0.000	0.000	0.000	0.000
88	A	91	GLY	0	0.006	0.008	23.970	-0.014	-0.014	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.963	-0.991	25.660	-0.072	-0.072	0.000	0.000	0.000	0.000
90	A	93	GLU	-1	-0.988	-0.985	29.110	-0.025	-0.025	0.000	0.000	0.000	0.000
91	A	94	GLU	-1	-0.961	-0.990	29.725	-0.017	-0.017	0.000	0.000	0.000	0.000
92	A	95	ASP	-1	-0.903	-0.955	29.434	0.001	0.001	0.000	0.000	0.000	0.000
93	A	96	ASP	-1	-0.868	-0.886	25.574	-0.032	-0.032	0.000	0.000	0.000	0.000
94	A	97	ILE	0	-0.022	-0.026	24.977	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	98	ALA	0	-0.027	-0.017	19.934	0.006	0.006	0.000	0.000	0.000	0.000
96	A	99	ARG	1	0.789	0.832	20.988	-0.062	-0.062	0.000	0.000	0.000	0.000
97	A	100	LEU	0	-0.023	0.007	15.783	0.014	0.014	0.000	0.000	0.000	0.000
98	A	101	VAL	0	-0.003	-0.002	16.732	-0.023	-0.023	0.000	0.000	0.000	0.000
99	A	102	ILE	0	-0.007	-0.013	10.024	0.010	0.010	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.024	0.021	12.757	-0.047	-0.047	0.000	0.000	0.000	0.000
101	A	104	ILE	0	-0.034	-0.028	7.187	-0.070	-0.070	0.000	0.000	0.000	0.000
102	A	105	ALA	0	0.020	0.040	8.408	0.095	0.095	0.000	0.000	0.000	0.000
103	A	106	ALA	0	0.017	-0.020	5.694	-0.385	-0.385	0.000	0.000	0.000	0.000
104	A	107	ARG	1	0.889	0.970	6.062	1.193	1.193	0.000	0.000	0.000	0.000
105	A	108	ASN	0	-0.036	-0.027	7.623	0.053	0.053	0.000	0.000	0.000	0.000
106	A	109	ASN	0	0.018	-0.001	9.511	0.023	0.023	0.000	0.000	0.000	0.000
107	A	110	GLU	-1	-0.845	-0.931	3.887	-1.453	-1.256	0.000	-0.023	-0.175	0.000
108	A	111	HIS	0	0.039	0.009	5.178	-0.309	-0.263	-0.001	0.000	-0.043	0.000
109	A	112	ILE	0	-0.004	0.014	7.545	0.041	0.041	0.000	0.000	0.000	0.000
110	A	113	GLN	0	0.036	0.013	4.933	0.031	0.031	0.000	0.000	0.000	0.000
111	A	114	VAL	0	-0.021	-0.001	3.465	-0.389	-0.044	0.009	-0.071	-0.283	0.000
112	A	115	ILE	0	0.075	0.028	5.654	0.300	0.300	0.000	0.000	0.000	0.000
113	A	116	THR	0	-0.030	0.000	8.386	0.162	0.162	0.000	0.000	0.000	0.000
114	A	117	SER	0	-0.086	-0.057	4.808	0.352	0.352	0.000	0.000	0.000	0.000
115	A	118	LEU	0	-0.021	-0.023	6.719	0.251	0.251	0.000	0.000	0.000	0.000
116	A	119	THR	0	0.005	-0.019	8.788	0.055	0.055	0.000	0.000	0.000	0.000
117	A	120	ASN	0	-0.044	-0.024	10.023	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	121	ALA	0	-0.072	-0.029	9.235	0.056	0.056	0.000	0.000	0.000	0.000
119	A	122	LEU	0	-0.054	-0.027	11.285	0.014	0.014	0.000	0.000	0.000	0.000
120	A	123	ASP	-1	-0.876	-0.924	14.112	0.185	0.185	0.000	0.000	0.000	0.000
121	A	124	ASP	-1	-0.831	-0.927	16.538	0.167	0.167	0.000	0.000	0.000	0.000
122	A	125	GLU	-1	-0.869	-0.939	18.800	0.091	0.091	0.000	0.000	0.000	0.000
123	A	126	SER	0	-0.013	-0.015	21.286	0.001	0.001	0.000	0.000	0.000	0.000
124	A	127	VAL	0	-0.040	-0.006	15.260	0.002	0.002	0.000	0.000	0.000	0.000
125	A	128	ILE	0	-0.006	0.003	17.102	0.010	0.010	0.000	0.000	0.000	0.000
126	A	129	GLU	-1	-0.786	-0.847	18.772	0.072	0.072	0.000	0.000	0.000	0.000
127	A	130	ARG	1	0.855	0.920	20.354	-0.225	-0.225	0.000	0.000	0.000	0.000
128	A	131	LEU	0	-0.010	-0.001	14.599	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	132	ALA	0	-0.015	-0.001	18.768	-0.014	-0.014	0.000	0.000	0.000	0.000
130	A	133	HIS	0	-0.007	-0.008	21.093	-0.018	-0.018	0.000	0.000	0.000	0.000
131	A	134	THR	0	-0.028	-0.022	19.683	-0.010	-0.010	0.000	0.000	0.000	0.000
132	A	135	THR	0	-0.017	-0.007	22.723	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	136	SER	0	-0.001	-0.002	22.202	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	137	VAL	0	0.043	0.009	17.166	0.017	0.017	0.000	0.000	0.000	0.000
135	A	138	ASP	-1	-0.917	-0.960	17.464	0.295	0.295	0.000	0.000	0.000	0.000
136	A	139	GLU	-1	-0.817	-0.885	18.046	0.248	0.248	0.000	0.000	0.000	0.000
137	A	140	VAL	0	0.009	0.004	14.034	0.039	0.039	0.000	0.000	0.000	0.000
138	A	141	LEU	0	-0.073	-0.042	12.811	0.086	0.086	0.000	0.000	0.000	0.000
139	A	142	GLU	-1	-0.970	-0.978	13.359	0.473	0.473	0.000	0.000	0.000	0.000
140	A	143	LEU	0	-0.031	-0.017	15.116	0.046	0.046	0.000	0.000	0.000	0.000
141	A	144	LEU	0	0.005	0.013	10.085	0.046	0.046	0.000	0.000	0.000	0.000
142	A	145	ALA	0	-0.016	0.004	9.765	0.367	0.367	0.000	0.000	0.000	0.000
143	A	146	GLY	0	-0.005	-0.003	10.488	0.171	0.171	0.000	0.000	0.000	0.000
144	A	147	ARG	1	0.892	0.966	5.399	-2.628	-2.628	0.000	0.000	0.000	0.000
145	A	148	LYS	1	0.855	0.934	4.828	-0.940	-0.940	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:LEU)