FMO DATABASE

FMODB ID: 2NRRR

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1004362.152969
FMO2-HF: Nuclear repulsion	952556.884567
FMO2-HF: Total energy	-51805.268402
FMO2-MP2: Total energy	-51960.512954

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.
-44.904	-35.99	12.956	-10.631	-11.239	-0.023

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 : 0.078 / q_NPA : 0.036

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	-0.032	-0.024	2.911	-5.333	-1.145	0.433	-2.215	-2.407	0.016
4	A	20	GLU	-1	-0.772	-0.868	1.891	-36.008	-32.108	12.487	-8.200	-8.188	-0.040
5	A	21	ASP	-1	-0.810	-0.874	3.545	-2.189	-1.415	0.037	-0.215	-0.595	0.001
6	A	22	LYS	1	0.933	0.963	5.542	0.109	0.109	0.000	0.000	0.000	0.000
7	A	23	VAL	0	-0.007	0.002	6.882	0.026	0.026	0.000	0.000	0.000	0.000
8	A	24	SER	0	0.017	0.002	7.045	0.079	0.079	0.000	0.000	0.000	0.000
9	A	25	LYS	1	0.875	0.919	8.061	1.510	1.510	0.000	0.000	0.000	0.000
10	A	26	GLN	0	-0.047	-0.011	11.428	0.136	0.136	0.000	0.000	0.000	0.000
11	A	27	LEU	0	0.025	0.007	11.402	0.101	0.101	0.000	0.000	0.000	0.000
12	A	28	GLU	-1	-0.876	-0.936	11.550	-1.005	-1.005	0.000	0.000	0.000	0.000
13	A	29	SER	0	-0.094	-0.041	15.313	0.103	0.103	0.000	0.000	0.000	0.000
14	A	30	LYS	1	0.888	0.946	17.212	0.206	0.206	0.000	0.000	0.000	0.000
15	A	31	GLY	0	-0.002	0.001	18.598	0.026	0.026	0.000	0.000	0.000	0.000
16	A	32	ILE	0	-0.075	-0.045	16.499	0.025	0.025	0.000	0.000	0.000	0.000
17	A	33	LYS	1	0.913	0.958	16.612	0.329	0.329	0.000	0.000	0.000	0.000
18	A	34	PHE	0	-0.006	-0.013	10.627	0.053	0.053	0.000	0.000	0.000	0.000
19	A	35	GLU	-1	-0.856	-0.906	14.643	-0.557	-0.557	0.000	0.000	0.000	0.000
20	A	36	TYR	0	-0.084	-0.079	4.644	0.316	0.368	-0.001	-0.001	-0.049	0.000
21	A	37	GLU	-1	-0.954	-0.976	7.219	-2.470	-2.470	0.000	0.000	0.000	0.000
22	A	38	GLU	-1	-0.936	-0.952	10.576	-0.567	-0.567	0.000	0.000	0.000	0.000
23	A	39	TRP	0	-0.081	-0.046	14.252	0.157	0.157	0.000	0.000	0.000	0.000
24	A	40	LYS	1	0.930	0.959	14.714	0.404	0.404	0.000	0.000	0.000	0.000
25	A	41	VAL	0	0.036	0.014	16.618	0.044	0.044	0.000	0.000	0.000	0.000
26	A	42	PRO	0	-0.032	-0.015	18.436	0.013	0.013	0.000	0.000	0.000	0.000
27	A	43	TYR	0	-0.010	-0.006	16.854	0.031	0.031	0.000	0.000	0.000	0.000
28	A	44	VAL	0	0.015	0.001	22.266	0.000	0.000	0.000	0.000	0.000	0.000
29	A	45	ILE	0	-0.016	0.002	20.129	0.008	0.008	0.000	0.000	0.000	0.000
30	A	46	PRO	0	-0.005	0.000	24.456	0.001	0.001	0.000	0.000	0.000	0.000
31	A	47	ALA	0	0.037	0.024	27.811	0.007	0.007	0.000	0.000	0.000	0.000
32	A	48	SER	0	0.019	-0.001	28.531	0.005	0.005	0.000	0.000	0.000	0.000
33	A	49	ASN	0	-0.020	-0.003	31.070	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	50	HIS	0	-0.010	-0.009	29.180	0.010	0.010	0.000	0.000	0.000	0.000
35	A	51	THR	0	-0.027	-0.015	34.562	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	52	TYR	0	0.066	0.031	35.865	0.006	0.006	0.000	0.000	0.000	0.000
37	A	53	THR	0	-0.021	-0.014	37.892	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	54	PRO	0	0.009	0.008	40.640	0.004	0.004	0.000	0.000	0.000	0.000
39	A	55	ASP	-1	-0.754	-0.851	41.666	0.056	0.056	0.000	0.000	0.000	0.000
40	A	56	PHE	0	-0.004	0.002	44.071	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	57	LEU	0	0.003	0.011	47.297	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	58	LEU	0	-0.006	-0.005	49.746	0.000	0.000	0.000	0.000	0.000	0.000
43	A	59	PRO	0	0.042	0.006	52.759	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	60	ASN	0	-0.047	-0.033	54.154	0.000	0.000	0.000	0.000	0.000	0.000
45	A	61	GLY	0	0.047	0.007	52.661	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	62	ILE	0	-0.073	-0.007	48.742	0.000	0.000	0.000	0.000	0.000	0.000
47	A	63	PHE	0	0.034	0.000	45.258	0.002	0.002	0.000	0.000	0.000	0.000
48	A	64	VAL	0	-0.002	-0.009	45.018	0.000	0.000	0.000	0.000	0.000	0.000
49	A	65	LYS	1	0.767	0.877	37.892	-0.056	-0.056	0.000	0.000	0.000	0.000
50	A	66	THR	0	-0.044	-0.023	41.567	0.000	0.000	0.000	0.000	0.000	0.000
51	A	67	LYS	1	0.817	0.876	32.743	-0.077	-0.077	0.000	0.000	0.000	0.000
52	A	68	GLY	0	0.079	0.051	36.659	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	69	LEU	0	-0.018	-0.011	28.595	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	70	TRP	0	0.015	-0.002	32.363	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	71	GLU	-1	-0.858	-0.922	26.063	0.130	0.130	0.000	0.000	0.000	0.000
56	A	72	SER	0	0.000	-0.009	25.158	-0.013	-0.013	0.000	0.000	0.000	0.000
57	A	73	ASP	-1	-0.749	-0.867	25.029	0.064	0.064	0.000	0.000	0.000	0.000
58	A	74	ASP	-1	-0.788	-0.882	27.502	0.073	0.073	0.000	0.000	0.000	0.000
59	A	75	ARG	1	0.787	0.878	28.127	-0.085	-0.085	0.000	0.000	0.000	0.000
60	A	76	LYS	1	0.905	0.947	23.597	-0.065	-0.065	0.000	0.000	0.000	0.000
61	A	77	LYS	1	0.874	0.930	27.724	-0.069	-0.069	0.000	0.000	0.000	0.000
62	A	78	HIS	0	-0.013	-0.010	32.665	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	79	LEU	0	-0.002	0.006	32.548	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	80	LEU	0	0.063	0.037	30.774	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	81	ILE	0	-0.015	-0.011	35.254	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	82	ARG	1	0.890	0.948	38.195	-0.022	-0.022	0.000	0.000	0.000	0.000
67	A	83	GLU	-1	-0.958	-0.986	35.730	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	84	GLN	0	-0.049	-0.020	35.914	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	85	HIS	0	-0.101	-0.046	40.383	0.000	0.000	0.000	0.000	0.000	0.000
70	A	86	PRO	0	0.017	0.010	43.365	0.002	0.002	0.000	0.000	0.000	0.000
71	A	87	GLU	-1	-0.817	-0.908	45.238	0.012	0.012	0.000	0.000	0.000	0.000
72	A	88	LEU	0	-0.038	-0.003	43.591	0.002	0.002	0.000	0.000	0.000	0.000
73	A	89	ASP	-1	-0.750	-0.833	46.028	0.022	0.022	0.000	0.000	0.000	0.000
74	A	90	ILE	0	-0.028	-0.019	41.322	0.002	0.002	0.000	0.000	0.000	0.000
75	A	91	ARG	1	0.668	0.773	43.380	-0.025	-0.025	0.000	0.000	0.000	0.000
76	A	92	ILE	0	-0.022	-0.010	37.940	0.002	0.002	0.000	0.000	0.000	0.000
77	A	93	VAL	0	0.024	0.024	42.216	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	94	PHE	0	0.021	-0.001	36.517	0.004	0.004	0.000	0.000	0.000	0.000
79	A	95	SER	0	-0.006	-0.009	39.236	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	96	SER	0	0.001	-0.015	38.840	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	97	SER	0	-0.041	-0.047	38.368	0.004	0.004	0.000	0.000	0.000	0.000
82	A	98	ARG	1	1.007	0.987	38.790	-0.047	-0.047	0.000	0.000	0.000	0.000
83	A	99	THR	0	-0.036	-0.003	32.983	0.003	0.003	0.000	0.000	0.000	0.000
84	A	100	LYS	1	0.877	0.936	31.519	-0.069	-0.069	0.000	0.000	0.000	0.000
85	A	101	LEU	0	-0.031	-0.009	29.174	0.007	0.007	0.000	0.000	0.000	0.000
86	A	102	TYR	0	0.042	0.000	25.346	0.009	0.009	0.000	0.000	0.000	0.000
87	A	103	LYS	1	0.980	0.970	23.424	-0.206	-0.206	0.000	0.000	0.000	0.000
88	A	104	GLY	0	0.057	0.053	26.535	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	105	SER	0	-0.048	-0.005	27.515	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	106	PRO	0	0.028	0.011	29.287	0.002	0.002	0.000	0.000	0.000	0.000
91	A	107	THR	0	0.006	0.014	31.739	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	108	SER	0	-0.027	-0.052	32.952	0.007	0.007	0.000	0.000	0.000	0.000
93	A	109	TYR	0	-0.013	-0.006	31.560	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	110	GLY	0	0.097	0.036	35.937	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	111	GLU	-1	-0.757	-0.828	36.778	0.044	0.044	0.000	0.000	0.000	0.000
96	A	112	PHE	0	-0.005	-0.007	31.616	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	113	CYS	0	-0.081	-0.048	36.107	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	114	GLU	-1	-0.911	-0.941	39.059	0.026	0.026	0.000	0.000	0.000	0.000
99	A	115	LYS	1	0.905	0.965	33.339	-0.021	-0.021	0.000	0.000	0.000	0.000
100	A	116	HIS	0	-0.063	-0.052	34.141	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	117	GLY	0	0.039	0.039	39.217	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	118	ILE	0	-0.072	-0.036	37.494	0.000	0.000	0.000	0.000	0.000	0.000
103	A	119	LYS	1	0.935	0.972	41.958	-0.020	-0.020	0.000	0.000	0.000	0.000
104	A	120	PHE	0	0.005	-0.020	42.076	0.003	0.003	0.000	0.000	0.000	0.000
105	A	121	ALA	0	0.033	0.025	44.144	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	122	ASP	-1	-0.764	-0.850	43.052	0.053	0.053	0.000	0.000	0.000	0.000
107	A	123	LYS	1	0.943	0.962	44.392	-0.054	-0.054	0.000	0.000	0.000	0.000
108	A	124	LEU	0	-0.005	-0.006	46.191	0.001	0.001	0.000	0.000	0.000	0.000
109	A	125	ILE	0	-0.007	0.006	48.421	0.000	0.000	0.000	0.000	0.000	0.000
110	A	126	PRO	0	0.021	0.015	49.085	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	127	ALA	0	0.064	0.021	52.298	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	128	GLU	-1	-0.836	-0.929	54.505	0.024	0.024	0.000	0.000	0.000	0.000
113	A	129	TRP	0	-0.026	-0.009	45.752	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	130	ILE	0	0.010	-0.004	53.424	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	131	LYS	1	0.842	0.929	55.697	-0.024	-0.024	0.000	0.000	0.000	0.000
116	A	132	GLU	-1	-0.817	-0.858	52.862	0.019	0.019	0.000	0.000	0.000	0.000
117	A	133	PRO	0	0.026	0.014	57.247	0.001	0.001	0.000	0.000	0.000	0.000
118	A	134	LYS	1	0.821	0.913	57.235	-0.016	-0.016	0.000	0.000	0.000	0.000
119	A	135	LYS	1	0.881	0.953	51.714	-0.020	-0.020	0.000	0.000	0.000	0.000
120	A	136	GLU	-1	-0.859	-0.934	55.287	0.017	0.017	0.000	0.000	0.000	0.000
121	A	137	VAL	0	0.005	0.014	49.868	0.000	0.000	0.000	0.000	0.000	0.000
122	A	138	PRO	0	0.023	0.029	48.898	0.000	0.000	0.000	0.000	0.000	0.000
123	A	139	PHE	0	0.004	-0.038	49.676	0.001	0.001	0.000	0.000	0.000	0.000
124	A	140	ASP	-1	-0.896	-0.931	49.770	0.013	0.013	0.000	0.000	0.000	0.000
125	A	141	ARG	1	0.851	0.930	44.095	-0.010	-0.010	0.000	0.000	0.000	0.000
126	A	142	LEU	0	-0.056	-0.019	45.239	0.002	0.002	0.000	0.000	0.000	0.000
127	A	143	LYS	1	0.950	0.975	43.443	-0.034	-0.034	0.000	0.000	0.000	0.000
128	A	144	ARG	1	0.975	0.988	45.452	-0.024	-0.024	0.000	0.000	0.000	0.000
129	A	145	LYS	1	0.957	0.970	39.949	-0.049	-0.049	0.000	0.000	0.000	0.000

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