FMO DATABASE

FMODB ID: 6Y77Z

Calculation Name: 1FZR-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1FZR

Chain ID: A

ChEMBL ID:

UniProt ID: P00641

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	OptAll
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	129
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1004621.592183
FMO2-HF: Nuclear repulsion	952815.832715
FMO2-HF: Total energy	-51805.759468
FMO2-MP2: Total energy	-51960.936796

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:17:SER)

Summations of interaction energy for fragment #1(A:17:SER)

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.
-54.84	-54.821	27.185	-15.596	-11.605	-0.087

Interaction energy analysis for fragmet #1(A:17:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.050 / q_NPA : -0.005

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	19	LEU	0	0.020	0.012	3.278	-5.093	-1.384	0.027	-2.032	-1.703	0.010
4	A	20	GLU	-1	-0.717	-0.816	1.708	-48.274	-53.005	27.153	-13.283	-9.138	-0.097
5	A	21	ASP	-1	-0.806	-0.884	3.552	-1.760	-0.949	0.007	-0.264	-0.554	0.000
6	A	22	LYS	1	0.861	0.921	4.955	0.567	0.696	-0.001	-0.010	-0.117	0.000
7	A	23	VAL	0	-0.010	-0.002	7.168	0.184	0.184	0.000	0.000	0.000	0.000
8	A	24	SER	0	0.002	0.003	6.614	0.210	0.210	0.000	0.000	0.000	0.000
9	A	25	LYS	1	0.901	0.940	7.798	1.444	1.444	0.000	0.000	0.000	0.000
10	A	26	GLN	0	-0.028	-0.003	11.058	0.191	0.191	0.000	0.000	0.000	0.000
11	A	27	LEU	0	0.026	0.017	11.839	0.130	0.130	0.000	0.000	0.000	0.000
12	A	28	GLU	-1	-0.854	-0.936	10.569	-1.077	-1.077	0.000	0.000	0.000	0.000
13	A	29	SER	0	-0.097	-0.050	14.820	0.120	0.120	0.000	0.000	0.000	0.000
14	A	30	LYS	1	0.836	0.910	16.929	0.348	0.348	0.000	0.000	0.000	0.000
15	A	31	GLY	0	0.015	0.020	18.393	0.026	0.026	0.000	0.000	0.000	0.000
16	A	32	ILE	0	-0.017	-0.004	16.453	0.020	0.020	0.000	0.000	0.000	0.000
17	A	33	LYS	1	0.860	0.923	16.646	0.374	0.374	0.000	0.000	0.000	0.000
18	A	34	PHE	0	-0.025	-0.016	10.278	0.060	0.060	0.000	0.000	0.000	0.000
19	A	35	GLU	-1	-0.846	-0.901	14.027	-0.609	-0.609	0.000	0.000	0.000	0.000
20	A	36	TYR	0	-0.059	-0.066	4.047	0.756	0.857	-0.001	-0.007	-0.093	0.000
21	A	37	GLU	-1	-0.960	-0.985	7.341	-2.221	-2.221	0.000	0.000	0.000	0.000
22	A	38	GLU	-1	-0.971	-0.971	10.425	-0.546	-0.546	0.000	0.000	0.000	0.000
23	A	39	TRP	0	-0.069	-0.034	14.108	0.169	0.169	0.000	0.000	0.000	0.000
24	A	40	LYS	1	0.947	0.959	14.093	0.501	0.501	0.000	0.000	0.000	0.000
25	A	41	VAL	0	0.022	0.007	16.284	0.051	0.051	0.000	0.000	0.000	0.000
26	A	42	PRO	0	-0.020	-0.013	18.375	0.016	0.016	0.000	0.000	0.000	0.000
27	A	43	TYR	0	-0.017	-0.003	16.850	0.032	0.032	0.000	0.000	0.000	0.000
28	A	44	VAL	0	0.007	-0.002	22.127	0.002	0.002	0.000	0.000	0.000	0.000
29	A	45	ILE	0	0.002	0.008	19.987	0.006	0.006	0.000	0.000	0.000	0.000
30	A	46	PRO	0	-0.007	0.006	24.143	0.003	0.003	0.000	0.000	0.000	0.000
31	A	47	ALA	0	0.027	0.010	27.790	0.009	0.009	0.000	0.000	0.000	0.000
32	A	48	SER	0	0.020	0.004	28.637	0.004	0.004	0.000	0.000	0.000	0.000
33	A	49	ASN	0	-0.013	0.001	31.210	0.000	0.000	0.000	0.000	0.000	0.000
34	A	50	HIS	0	0.000	-0.002	29.126	0.010	0.010	0.000	0.000	0.000	0.000
35	A	51	THR	0	-0.041	-0.024	34.431	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	52	TYR	0	0.085	0.037	35.868	0.005	0.005	0.000	0.000	0.000	0.000
37	A	53	THR	0	-0.036	-0.026	38.074	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	54	PRO	0	0.008	0.015	40.607	0.004	0.004	0.000	0.000	0.000	0.000
39	A	55	ASP	-1	-0.765	-0.840	42.097	0.053	0.053	0.000	0.000	0.000	0.000
40	A	56	PHE	0	0.000	-0.005	44.484	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	57	LEU	0	0.005	0.000	47.304	0.000	0.000	0.000	0.000	0.000	0.000
42	A	58	LEU	0	-0.006	0.006	50.031	0.000	0.000	0.000	0.000	0.000	0.000
43	A	59	PRO	0	0.031	0.001	53.100	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	60	ASN	0	-0.028	-0.027	54.232	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	61	GLY	0	0.046	0.017	52.991	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	62	ILE	0	-0.067	-0.012	48.821	0.000	0.000	0.000	0.000	0.000	0.000
47	A	63	PHE	0	0.046	0.016	45.315	0.002	0.002	0.000	0.000	0.000	0.000
48	A	64	VAL	0	-0.007	-0.014	44.970	0.000	0.000	0.000	0.000	0.000	0.000
49	A	65	LYS	1	0.766	0.877	38.117	-0.054	-0.054	0.000	0.000	0.000	0.000
50	A	66	THR	0	-0.018	-0.014	41.559	0.001	0.001	0.000	0.000	0.000	0.000
51	A	67	LYS	1	0.807	0.870	32.622	-0.078	-0.078	0.000	0.000	0.000	0.000
52	A	68	GLY	0	0.065	0.039	36.632	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	69	LEU	0	-0.004	0.005	28.476	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	70	TRP	0	0.035	0.013	32.466	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	71	GLU	-1	-0.859	-0.927	26.065	0.132	0.132	0.000	0.000	0.000	0.000
56	A	72	SER	0	-0.012	-0.021	24.679	-0.014	-0.014	0.000	0.000	0.000	0.000
57	A	73	ASP	-1	-0.752	-0.869	24.895	0.054	0.054	0.000	0.000	0.000	0.000
58	A	74	ASP	-1	-0.805	-0.880	27.330	0.072	0.072	0.000	0.000	0.000	0.000
59	A	75	ARG	1	0.780	0.874	28.363	-0.088	-0.088	0.000	0.000	0.000	0.000
60	A	76	LYS	1	0.900	0.945	23.428	-0.059	-0.059	0.000	0.000	0.000	0.000
61	A	77	LYS	1	0.884	0.931	27.976	-0.059	-0.059	0.000	0.000	0.000	0.000
62	A	78	HIS	0	0.002	-0.001	32.944	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	79	LEU	0	0.009	0.009	32.362	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	80	LEU	0	0.075	0.040	30.665	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	81	ILE	0	-0.027	-0.015	35.160	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	82	ARG	1	0.855	0.928	38.218	-0.020	-0.020	0.000	0.000	0.000	0.000
67	A	83	GLU	-1	-0.933	-0.966	35.470	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	84	GLN	0	-0.038	-0.024	35.726	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	85	HIS	0	-0.086	-0.054	40.143	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	86	PRO	0	0.019	0.020	43.146	0.003	0.003	0.000	0.000	0.000	0.000
71	A	87	GLU	-1	-0.802	-0.895	44.866	0.008	0.008	0.000	0.000	0.000	0.000
72	A	88	LEU	0	-0.029	-0.007	43.294	0.002	0.002	0.000	0.000	0.000	0.000
73	A	89	ASP	-1	-0.760	-0.841	44.985	0.022	0.022	0.000	0.000	0.000	0.000
74	A	90	ILE	0	-0.040	-0.024	41.035	0.002	0.002	0.000	0.000	0.000	0.000
75	A	91	ARG	1	0.695	0.801	43.525	-0.025	-0.025	0.000	0.000	0.000	0.000
76	A	92	ILE	0	-0.023	-0.011	37.790	0.002	0.002	0.000	0.000	0.000	0.000
77	A	93	VAL	0	-0.002	0.002	42.006	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	94	PHE	0	0.029	0.005	36.528	0.004	0.004	0.000	0.000	0.000	0.000
79	A	95	SER	0	0.005	-0.009	39.188	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	96	SER	0	-0.003	-0.010	38.732	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	97	SER	0	-0.030	-0.040	38.297	0.005	0.005	0.000	0.000	0.000	0.000
82	A	98	ARG	1	0.978	0.986	38.267	-0.053	-0.053	0.000	0.000	0.000	0.000
83	A	99	THR	0	-0.043	-0.023	33.038	0.005	0.005	0.000	0.000	0.000	0.000
84	A	100	LYS	1	0.854	0.915	31.325	-0.086	-0.086	0.000	0.000	0.000	0.000
85	A	101	LEU	0	-0.034	-0.009	29.241	0.006	0.006	0.000	0.000	0.000	0.000
86	A	102	TYR	0	0.043	0.012	25.122	0.002	0.002	0.000	0.000	0.000	0.000
87	A	103	LYS	1	0.978	0.968	23.636	-0.222	-0.222	0.000	0.000	0.000	0.000
88	A	104	GLY	0	0.055	0.049	26.732	0.001	0.001	0.000	0.000	0.000	0.000
89	A	105	SER	0	-0.033	0.006	27.710	-0.009	-0.009	0.000	0.000	0.000	0.000
90	A	106	PRO	0	0.046	0.016	29.298	0.000	0.000	0.000	0.000	0.000	0.000
91	A	107	THR	0	-0.008	-0.009	31.765	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	108	SER	0	-0.029	-0.063	32.765	0.008	0.008	0.000	0.000	0.000	0.000
93	A	109	TYR	0	0.002	-0.002	31.285	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	110	GLY	0	0.082	0.038	35.911	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	111	GLU	-1	-0.753	-0.806	36.850	0.054	0.054	0.000	0.000	0.000	0.000
96	A	112	PHE	0	-0.006	-0.013	31.288	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	113	CYS	0	-0.071	-0.029	36.146	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	114	GLU	-1	-0.916	-0.958	39.137	0.032	0.032	0.000	0.000	0.000	0.000
99	A	115	LYS	1	0.876	0.939	33.535	-0.026	-0.026	0.000	0.000	0.000	0.000
100	A	116	HIS	0	-0.030	-0.022	34.060	-0.007	-0.007	0.000	0.000	0.000	0.000
101	A	117	GLY	0	0.036	0.040	39.190	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	118	ILE	0	-0.052	-0.016	37.529	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	119	LYS	1	0.892	0.943	41.991	-0.020	-0.020	0.000	0.000	0.000	0.000
104	A	120	PHE	0	0.015	-0.006	41.906	0.002	0.002	0.000	0.000	0.000	0.000
105	A	121	ALA	0	0.032	0.018	43.893	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	122	ASP	-1	-0.774	-0.853	42.957	0.058	0.058	0.000	0.000	0.000	0.000
107	A	123	LYS	1	0.943	0.961	44.316	-0.060	-0.060	0.000	0.000	0.000	0.000
108	A	124	LEU	0	-0.010	-0.005	45.996	0.000	0.000	0.000	0.000	0.000	0.000
109	A	125	ILE	0	0.008	0.011	48.333	0.000	0.000	0.000	0.000	0.000	0.000
110	A	126	PRO	0	0.015	0.011	48.911	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	127	ALA	0	0.066	0.025	52.107	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	128	GLU	-1	-0.828	-0.917	54.114	0.026	0.026	0.000	0.000	0.000	0.000
113	A	129	TRP	0	-0.025	-0.014	45.635	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	130	ILE	0	0.003	-0.001	53.304	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	131	LYS	1	0.858	0.921	55.840	-0.025	-0.025	0.000	0.000	0.000	0.000
116	A	132	GLU	-1	-0.782	-0.838	52.454	0.020	0.020	0.000	0.000	0.000	0.000
117	A	133	PRO	0	0.030	0.020	56.956	0.000	0.000	0.000	0.000	0.000	0.000
118	A	134	LYS	1	0.751	0.870	56.911	-0.014	-0.014	0.000	0.000	0.000	0.000
119	A	135	LYS	1	0.865	0.945	51.700	-0.019	-0.019	0.000	0.000	0.000	0.000
120	A	136	GLU	-1	-0.825	-0.917	55.057	0.014	0.014	0.000	0.000	0.000	0.000
121	A	137	VAL	0	-0.007	0.001	49.620	0.000	0.000	0.000	0.000	0.000	0.000
122	A	138	PRO	0	0.031	0.034	48.472	0.000	0.000	0.000	0.000	0.000	0.000
123	A	139	PHE	0	-0.018	-0.041	49.397	0.001	0.001	0.000	0.000	0.000	0.000
124	A	140	ASP	-1	-0.883	-0.933	50.006	0.007	0.007	0.000	0.000	0.000	0.000
125	A	141	ARG	1	0.833	0.920	43.727	-0.005	-0.005	0.000	0.000	0.000	0.000
126	A	142	LEU	0	-0.031	-0.008	45.138	0.001	0.001	0.000	0.000	0.000	0.000
127	A	143	LYS	1	0.914	0.959	43.261	-0.025	-0.025	0.000	0.000	0.000	0.000
128	A	144	ARG	1	1.006	1.003	45.110	-0.018	-0.018	0.000	0.000	0.000	0.000
129	A	145	LYS	1	0.931	0.961	39.817	-0.043	-0.043	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:17:SER)