FMO DATABASE

FMODB ID: V55Y1

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	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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-566948.932812
FMO2-HF: Nuclear repulsion	533593.323198
FMO2-HF: Total energy	-33355.609613
FMO2-MP2: Total energy	-33454.293895

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.
-3.895	-2.061	-0.038	-0.773	-1.022	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 : -0.038 / q_NPA : -0.029

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	-0.015	0.001	3.764	-1.325	0.509	-0.038	-0.773	-1.022	0.001
4	A	81	GLU	-1	-0.941	-0.970	6.643	-0.091	-0.091	0.000	0.000	0.000	0.000
5	A	82	GLU	-1	-0.996	-0.987	9.685	-0.299	-0.299	0.000	0.000	0.000	0.000
6	A	83	ARG	1	0.957	0.971	11.442	0.563	0.563	0.000	0.000	0.000	0.000
7	A	84	GLU	-1	-0.863	-0.946	14.718	-0.146	-0.146	0.000	0.000	0.000	0.000
8	A	85	PRO	0	-0.055	-0.023	18.211	-0.007	-0.007	0.000	0.000	0.000	0.000
9	A	86	LEU	0	0.000	0.008	19.569	0.025	0.025	0.000	0.000	0.000	0.000
10	A	87	ALA	0	-0.014	-0.030	22.409	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	88	ASP	-1	-0.901	-0.940	25.444	-0.111	-0.111	0.000	0.000	0.000	0.000
12	A	89	VAL	0	-0.034	-0.013	29.113	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	90	ILE	0	0.043	0.027	31.818	0.006	0.006	0.000	0.000	0.000	0.000
14	A	91	GLU	-1	-0.949	-0.977	35.201	-0.068	-0.068	0.000	0.000	0.000	0.000
15	A	92	LYS	1	0.935	0.964	38.232	0.084	0.084	0.000	0.000	0.000	0.000
16	A	93	GLY	0	-0.017	-0.004	41.256	0.000	0.000	0.000	0.000	0.000	0.000
17	A	94	ASP	-1	-0.807	-0.900	43.091	-0.057	-0.057	0.000	0.000	0.000	0.000
18	A	95	GLU	-1	-0.938	-0.975	38.332	-0.080	-0.080	0.000	0.000	0.000	0.000
19	A	96	ILE	0	0.060	0.026	34.268	0.001	0.001	0.000	0.000	0.000	0.000
20	A	97	LYS	1	0.872	0.939	33.599	0.093	0.093	0.000	0.000	0.000	0.000
21	A	98	VAL	0	0.031	0.013	27.884	0.001	0.001	0.000	0.000	0.000	0.000
22	A	99	VAL	0	0.015	0.008	26.798	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	100	ALA	0	0.003	-0.008	22.770	0.001	0.001	0.000	0.000	0.000	0.000
24	A	101	GLU	-1	-0.928	-0.946	20.848	-0.245	-0.245	0.000	0.000	0.000	0.000
25	A	102	VAL	0	-0.015	-0.023	16.711	-0.011	-0.011	0.000	0.000	0.000	0.000
26	A	103	PRO	0	0.063	0.045	16.217	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	104	GLY	0	-0.019	0.023	13.587	-0.054	-0.054	0.000	0.000	0.000	0.000
28	A	105	VAL	0	-0.005	0.007	13.863	-0.037	-0.037	0.000	0.000	0.000	0.000
29	A	106	ASN	0	0.021	0.019	15.013	0.069	0.069	0.000	0.000	0.000	0.000
30	A	107	LYS	1	1.015	0.988	17.625	0.188	0.188	0.000	0.000	0.000	0.000
31	A	108	GLU	-1	-0.910	-0.968	18.560	-0.233	-0.233	0.000	0.000	0.000	0.000
32	A	109	ASP	-1	-0.943	-0.952	14.294	-0.417	-0.417	0.000	0.000	0.000	0.000
33	A	110	ILE	0	-0.051	-0.026	16.787	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	111	LYS	1	0.846	0.921	19.286	0.219	0.219	0.000	0.000	0.000	0.000
35	A	112	VAL	0	0.046	0.027	21.618	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	113	LYS	1	0.937	0.967	23.845	0.098	0.098	0.000	0.000	0.000	0.000
37	A	114	VAL	0	0.034	0.073	27.160	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	115	THR	0	-0.027	-0.016	28.134	0.006	0.006	0.000	0.000	0.000	0.000
39	A	116	ASN	0	-0.008	-0.018	31.113	0.000	0.000	0.000	0.000	0.000	0.000
40	A	117	GLY	0	0.013	0.007	34.016	0.001	0.001	0.000	0.000	0.000	0.000
41	A	118	GLY	0	-0.028	-0.036	35.096	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	119	LYS	1	1.017	0.996	35.271	0.038	0.038	0.000	0.000	0.000	0.000
43	A	120	LYS	1	0.983	1.031	28.512	0.058	0.058	0.000	0.000	0.000	0.000
44	A	121	LEU	0	-0.014	-0.017	27.437	0.002	0.002	0.000	0.000	0.000	0.000
45	A	122	VAL	0	-0.006	-0.004	23.346	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	123	ILE	0	-0.014	-0.008	20.901	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	124	THR	0	-0.006	-0.008	16.868	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	125	ALA	0	-0.039	-0.007	16.560	0.010	0.010	0.000	0.000	0.000	0.000
49	A	126	LYS	1	0.960	0.972	11.360	0.297	0.297	0.000	0.000	0.000	0.000
50	A	127	SER	0	0.023	0.019	10.857	0.008	0.008	0.000	0.000	0.000	0.000
51	A	128	GLU	-1	-0.918	-0.962	5.430	-1.704	-1.704	0.000	0.000	0.000	0.000
52	A	129	ASP	-1	-0.947	-0.968	6.199	-1.780	-1.780	0.000	0.000	0.000	0.000
53	A	130	ARG	1	0.898	0.949	7.420	0.800	0.800	0.000	0.000	0.000	0.000
54	A	131	GLN	0	-0.025	-0.012	7.674	0.026	0.026	0.000	0.000	0.000	0.000
55	A	132	TYR	0	-0.049	-0.086	12.020	0.020	0.020	0.000	0.000	0.000	0.000
56	A	133	TYR	0	0.011	0.013	15.654	0.021	0.021	0.000	0.000	0.000	0.000
57	A	134	LYS	1	0.928	0.969	18.551	0.152	0.152	0.000	0.000	0.000	0.000
58	A	135	GLU	-1	-0.958	-0.973	22.032	-0.073	-0.073	0.000	0.000	0.000	0.000
59	A	136	ILE	0	0.009	-0.001	25.447	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	137	ASP	-1	-0.919	-0.949	28.610	-0.067	-0.067	0.000	0.000	0.000	0.000
61	A	138	LEU	0	-0.059	-0.055	31.952	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	139	PRO	0	0.009	0.017	34.457	0.005	0.005	0.000	0.000	0.000	0.000
63	A	140	ALA	0	-0.025	-0.015	37.740	0.005	0.005	0.000	0.000	0.000	0.000
64	A	141	GLU	-1	-0.937	-0.965	37.787	-0.045	-0.045	0.000	0.000	0.000	0.000
65	A	142	VAL	0	0.065	0.043	34.781	0.000	0.000	0.000	0.000	0.000	0.000
66	A	143	ASP	-1	-0.920	-0.963	36.954	-0.054	-0.054	0.000	0.000	0.000	0.000
67	A	144	GLU	-1	-0.845	-0.957	33.270	-0.061	-0.061	0.000	0.000	0.000	0.000
68	A	145	LYS	1	0.800	0.884	33.609	0.052	0.052	0.000	0.000	0.000	0.000
69	A	146	ALA	0	-0.006	0.006	34.811	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	147	ALA	0	0.051	0.011	31.944	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	148	LYS	1	0.852	0.953	33.598	0.088	0.088	0.000	0.000	0.000	0.000
72	A	149	ALA	0	0.011	0.004	28.100	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	150	ASN	0	-0.072	-0.038	28.649	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	151	PHE	0	0.051	0.031	19.767	0.001	0.001	0.000	0.000	0.000	0.000
75	A	152	LYS	1	0.976	0.982	25.502	0.161	0.161	0.000	0.000	0.000	0.000
76	A	153	ASN	0	-0.032	-0.017	23.099	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	154	GLY	0	0.045	0.024	20.355	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	155	VAL	0	0.026	0.019	20.990	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	156	LEU	0	-0.055	-0.033	23.189	0.010	0.010	0.000	0.000	0.000	0.000
80	A	157	GLU	-1	-0.907	-0.938	25.044	-0.126	-0.126	0.000	0.000	0.000	0.000
81	A	158	ILE	0	0.001	-0.004	27.593	0.002	0.002	0.000	0.000	0.000	0.000
82	A	159	THR	0	-0.078	-0.054	30.300	0.006	0.006	0.000	0.000	0.000	0.000
83	A	160	LEU	0	-0.001	-0.003	31.560	0.001	0.001	0.000	0.000	0.000	0.000
84	A	161	LYS	1	0.885	0.923	35.361	0.065	0.065	0.000	0.000	0.000	0.000
85	A	162	LYS	1	0.978	0.994	38.740	0.058	0.058	0.000	0.000	0.000	0.000
86	A	163	LYS	1	0.869	0.953	40.294	0.045	0.045	0.000	0.000	0.000	0.000
87	A	164	ALA	0	-0.018	-0.003	42.498	0.002	0.002	0.000	0.000	0.000	0.000

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