FMO DATABASE

FMODB ID: 1779Z

Calculation Name: 4RZK-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4RZK

Chain ID: A

ChEMBL ID:

UniProt ID: Q97W19

Base Structure: X-ray

Registration Date: 2023-06-21

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	87
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-567919.392991
FMO2-HF: Nuclear repulsion	534562.513147
FMO2-HF: Total energy	-33356.879844
FMO2-MP2: Total energy	-33455.596929

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:78:MET)

Summations of interaction energy for fragment #1(A:78:MET)

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.
-4.499	-2.659	-0.042	-0.774	-1.024	0.001

Interaction energy analysis for fragmet #1(A:78:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.046 / q_NPA : -0.032

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	80	SER	0	-0.009	0.007	3.764	-1.974	-0.134	-0.042	-0.774	-1.024	0.001
4	A	81	GLU	-1	-0.954	-0.975	6.502	0.653	0.653	0.000	0.000	0.000	0.000
5	A	82	GLU	-1	-0.913	-0.949	9.654	-0.639	-0.639	0.000	0.000	0.000	0.000
6	A	83	ARG	1	0.929	0.955	11.451	0.400	0.400	0.000	0.000	0.000	0.000
7	A	84	GLU	-1	-0.794	-0.905	14.705	-0.148	-0.148	0.000	0.000	0.000	0.000
8	A	85	PRO	0	-0.064	-0.018	18.408	0.019	0.019	0.000	0.000	0.000	0.000
9	A	86	LEU	0	0.018	0.017	19.574	0.023	0.023	0.000	0.000	0.000	0.000
10	A	87	ALA	0	-0.014	-0.030	22.408	-0.020	-0.020	0.000	0.000	0.000	0.000
11	A	88	ASP	-1	-0.905	-0.942	25.451	-0.067	-0.067	0.000	0.000	0.000	0.000
12	A	89	VAL	0	-0.036	-0.013	29.120	-0.011	-0.011	0.000	0.000	0.000	0.000
13	A	90	ILE	0	0.038	0.022	31.830	0.010	0.010	0.000	0.000	0.000	0.000
14	A	91	GLU	-1	-0.840	-0.915	35.216	-0.074	-0.074	0.000	0.000	0.000	0.000
15	A	92	LYS	1	0.924	0.959	38.251	0.082	0.082	0.000	0.000	0.000	0.000
16	A	93	GLY	0	-0.009	-0.002	41.280	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	94	ASP	-1	-0.804	-0.904	43.034	-0.081	-0.081	0.000	0.000	0.000	0.000
18	A	95	GLU	-1	-0.830	-0.900	38.327	-0.103	-0.103	0.000	0.000	0.000	0.000
19	A	96	ILE	0	0.030	0.012	34.465	0.006	0.006	0.000	0.000	0.000	0.000
20	A	97	LYS	1	0.809	0.894	33.547	0.106	0.106	0.000	0.000	0.000	0.000
21	A	98	VAL	0	0.015	0.001	27.920	0.006	0.006	0.000	0.000	0.000	0.000
22	A	99	VAL	0	0.003	0.000	26.836	-0.013	-0.013	0.000	0.000	0.000	0.000
23	A	100	ALA	0	0.018	-0.002	22.840	0.006	0.006	0.000	0.000	0.000	0.000
24	A	101	GLU	-1	-0.937	-0.945	20.785	-0.159	-0.159	0.000	0.000	0.000	0.000
25	A	102	VAL	0	-0.031	-0.025	17.067	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	103	PRO	0	0.051	0.028	16.260	-0.047	-0.047	0.000	0.000	0.000	0.000
27	A	104	GLY	0	0.008	0.006	13.516	-0.030	-0.030	0.000	0.000	0.000	0.000
28	A	105	VAL	0	-0.052	-0.014	13.581	-0.078	-0.078	0.000	0.000	0.000	0.000
29	A	106	ASN	0	0.002	0.005	15.067	0.128	0.128	0.000	0.000	0.000	0.000
30	A	107	LYS	1	0.968	0.980	17.883	0.292	0.292	0.000	0.000	0.000	0.000
31	A	108	GLU	-1	-0.873	-0.956	19.415	-0.375	-0.375	0.000	0.000	0.000	0.000
32	A	109	ASP	-1	-0.879	-0.919	15.244	-0.706	-0.706	0.000	0.000	0.000	0.000
33	A	110	ILE	0	-0.015	-0.008	16.911	-0.019	-0.019	0.000	0.000	0.000	0.000
34	A	111	LYS	1	0.786	0.882	19.453	0.442	0.442	0.000	0.000	0.000	0.000
35	A	112	VAL	0	0.042	0.024	21.592	0.004	0.004	0.000	0.000	0.000	0.000
36	A	113	LYS	1	0.943	0.977	23.970	0.237	0.237	0.000	0.000	0.000	0.000
37	A	114	VAL	0	0.055	0.042	26.949	0.002	0.002	0.000	0.000	0.000	0.000
38	A	115	THR	0	-0.039	-0.015	27.670	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	116	ASN	0	0.014	-0.001	30.856	0.005	0.005	0.000	0.000	0.000	0.000
40	A	117	GLY	0	-0.008	-0.001	33.522	0.008	0.008	0.000	0.000	0.000	0.000
41	A	118	GLY	0	-0.034	-0.032	34.708	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	119	LYS	1	0.949	0.944	34.586	0.075	0.075	0.000	0.000	0.000	0.000
43	A	120	LYS	1	0.851	0.944	27.811	0.107	0.107	0.000	0.000	0.000	0.000
44	A	121	LEU	0	-0.031	-0.014	27.353	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	122	VAL	0	0.003	-0.006	22.874	0.000	0.000	0.000	0.000	0.000	0.000
46	A	123	ILE	0	-0.013	-0.005	20.893	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	124	THR	0	-0.021	-0.019	16.687	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	125	ALA	0	-0.019	0.002	16.549	0.010	0.010	0.000	0.000	0.000	0.000
49	A	126	LYS	1	0.867	0.929	11.984	0.736	0.736	0.000	0.000	0.000	0.000
50	A	127	SER	0	0.047	0.022	11.084	0.037	0.037	0.000	0.000	0.000	0.000
51	A	128	GLU	-1	-0.913	-0.958	6.188	-2.506	-2.506	0.000	0.000	0.000	0.000
52	A	129	ASP	-1	-0.840	-0.897	6.130	-1.882	-1.882	0.000	0.000	0.000	0.000
53	A	130	ARG	1	0.783	0.876	7.295	0.831	0.831	0.000	0.000	0.000	0.000
54	A	131	GLN	0	-0.025	-0.015	7.480	0.019	0.019	0.000	0.000	0.000	0.000
55	A	132	TYR	0	-0.005	-0.025	11.901	0.126	0.126	0.000	0.000	0.000	0.000
56	A	133	TYR	0	-0.013	-0.018	15.550	-0.035	-0.035	0.000	0.000	0.000	0.000
57	A	134	LYS	1	0.850	0.923	18.166	0.153	0.153	0.000	0.000	0.000	0.000
58	A	135	GLU	-1	-0.856	-0.902	21.774	-0.151	-0.151	0.000	0.000	0.000	0.000
59	A	136	ILE	0	-0.012	-0.012	25.041	0.014	0.014	0.000	0.000	0.000	0.000
60	A	137	ASP	-1	-0.843	-0.910	28.376	-0.094	-0.094	0.000	0.000	0.000	0.000
61	A	138	LEU	0	-0.031	-0.037	31.555	0.004	0.004	0.000	0.000	0.000	0.000
62	A	139	PRO	0	-0.006	0.018	34.186	0.004	0.004	0.000	0.000	0.000	0.000
63	A	140	ALA	0	-0.017	-0.018	37.503	0.005	0.005	0.000	0.000	0.000	0.000
64	A	141	GLU	-1	-0.889	-0.936	37.411	-0.088	-0.088	0.000	0.000	0.000	0.000
65	A	142	VAL	0	0.026	0.025	34.445	0.002	0.002	0.000	0.000	0.000	0.000
66	A	143	ASP	-1	-0.908	-0.957	36.678	-0.095	-0.095	0.000	0.000	0.000	0.000
67	A	144	GLU	-1	-0.844	-0.939	33.116	-0.139	-0.139	0.000	0.000	0.000	0.000
68	A	145	LYS	1	0.792	0.885	33.508	0.127	0.127	0.000	0.000	0.000	0.000
69	A	146	ALA	0	-0.015	0.008	34.818	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	147	ALA	0	0.057	0.019	31.951	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	148	LYS	1	0.813	0.905	33.771	0.112	0.112	0.000	0.000	0.000	0.000
72	A	149	ALA	0	0.027	0.008	28.230	0.001	0.001	0.000	0.000	0.000	0.000
73	A	150	ASN	0	-0.062	-0.032	28.762	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	151	PHE	0	0.062	0.032	19.508	0.003	0.003	0.000	0.000	0.000	0.000
75	A	152	LYS	1	0.975	0.982	25.384	0.153	0.153	0.000	0.000	0.000	0.000
76	A	153	ASN	0	-0.025	-0.016	23.025	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	154	GLY	0	0.040	0.023	20.238	0.006	0.006	0.000	0.000	0.000	0.000
78	A	155	VAL	0	0.006	0.013	20.974	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	156	LEU	0	-0.036	-0.025	22.740	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	157	GLU	-1	-0.824	-0.878	24.954	-0.115	-0.115	0.000	0.000	0.000	0.000
81	A	158	ILE	0	-0.024	-0.018	27.605	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	159	THR	0	-0.077	-0.043	30.263	0.014	0.014	0.000	0.000	0.000	0.000
83	A	160	LEU	0	0.020	0.005	31.391	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	161	LYS	1	0.837	0.894	35.243	0.097	0.097	0.000	0.000	0.000	0.000
85	A	162	LYS	1	0.876	0.939	38.548	0.069	0.069	0.000	0.000	0.000	0.000
86	A	163	LYS	1	0.883	0.965	39.814	0.084	0.084	0.000	0.000	0.000	0.000
87	A	164	ALA	0	0.003	0.007	42.242	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:78:MET)