FMO DATABASE

FMODB ID: G66V1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-568238.513963
FMO2-HF: Nuclear repulsion	534881.070273
FMO2-HF: Total energy	-33357.443691
FMO2-MP2: Total energy	-33456.32295

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.
-3.541	-2.27	-0.007	-0.475	-0.79	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 : -0.032 / 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

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	80	SER	0	0.001	0.011	3.864	-1.417	-0.146	-0.007	-0.475	-0.790	0.001
4	A	81	GLU	-1	-0.958	-0.979	6.047	0.905	0.905	0.000	0.000	0.000	0.000
5	A	82	GLU	-1	-0.853	-0.901	9.292	-0.794	-0.794	0.000	0.000	0.000	0.000
6	A	83	ARG	1	0.946	0.967	10.944	0.380	0.380	0.000	0.000	0.000	0.000
7	A	84	GLU	-1	-0.786	-0.893	14.222	-0.156	-0.156	0.000	0.000	0.000	0.000
8	A	85	PRO	0	-0.071	-0.019	17.818	0.020	0.020	0.000	0.000	0.000	0.000
9	A	86	LEU	0	0.011	0.011	18.830	0.024	0.024	0.000	0.000	0.000	0.000
10	A	87	ALA	0	-0.010	-0.019	21.707	-0.025	-0.025	0.000	0.000	0.000	0.000
11	A	88	ASP	-1	-0.878	-0.928	24.813	-0.062	-0.062	0.000	0.000	0.000	0.000
12	A	89	VAL	0	-0.052	-0.032	28.637	-0.016	-0.016	0.000	0.000	0.000	0.000
13	A	90	ILE	0	0.014	0.021	31.645	0.010	0.010	0.000	0.000	0.000	0.000
14	A	91	GLU	-1	-0.831	-0.907	35.015	-0.077	-0.077	0.000	0.000	0.000	0.000
15	A	92	LYS	1	0.913	0.944	38.047	0.081	0.081	0.000	0.000	0.000	0.000
16	A	93	GLY	0	0.002	0.005	41.273	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	94	ASP	-1	-0.818	-0.906	43.208	-0.087	-0.087	0.000	0.000	0.000	0.000
18	A	95	GLU	-1	-0.779	-0.857	38.354	-0.110	-0.110	0.000	0.000	0.000	0.000
19	A	96	ILE	0	0.031	0.003	34.206	0.007	0.007	0.000	0.000	0.000	0.000
20	A	97	LYS	1	0.749	0.862	32.700	0.114	0.114	0.000	0.000	0.000	0.000
21	A	98	VAL	0	0.026	0.010	27.383	0.008	0.008	0.000	0.000	0.000	0.000
22	A	99	VAL	0	-0.019	-0.014	26.259	-0.013	-0.013	0.000	0.000	0.000	0.000
23	A	100	ALA	0	0.022	0.002	22.045	0.007	0.007	0.000	0.000	0.000	0.000
24	A	101	GLU	-1	-0.930	-0.963	20.022	-0.143	-0.143	0.000	0.000	0.000	0.000
25	A	102	VAL	0	-0.042	-0.025	16.809	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	103	PRO	0	0.030	0.017	15.470	-0.050	-0.050	0.000	0.000	0.000	0.000
27	A	104	GLY	0	0.044	0.019	12.723	-0.018	-0.018	0.000	0.000	0.000	0.000
28	A	105	VAL	0	-0.055	0.001	12.702	-0.145	-0.145	0.000	0.000	0.000	0.000
29	A	106	ASN	0	-0.035	-0.024	15.018	0.146	0.146	0.000	0.000	0.000	0.000
30	A	107	LYS	1	0.942	0.968	17.919	0.322	0.322	0.000	0.000	0.000	0.000
31	A	108	GLU	-1	-0.867	-0.953	19.413	-0.407	-0.407	0.000	0.000	0.000	0.000
32	A	109	ASP	-1	-0.796	-0.885	15.257	-0.767	-0.767	0.000	0.000	0.000	0.000
33	A	110	ILE	0	-0.012	0.007	16.889	-0.024	-0.024	0.000	0.000	0.000	0.000
34	A	111	LYS	1	0.794	0.887	19.422	0.496	0.496	0.000	0.000	0.000	0.000
35	A	112	VAL	0	0.033	0.011	21.594	0.004	0.004	0.000	0.000	0.000	0.000
36	A	113	LYS	1	0.936	0.980	24.125	0.255	0.255	0.000	0.000	0.000	0.000
37	A	114	VAL	0	0.046	0.033	27.045	0.005	0.005	0.000	0.000	0.000	0.000
38	A	115	THR	0	-0.050	-0.023	27.977	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	116	ASN	0	0.026	0.001	30.962	0.005	0.005	0.000	0.000	0.000	0.000
40	A	117	GLY	0	-0.002	0.007	33.635	0.010	0.010	0.000	0.000	0.000	0.000
41	A	118	GLY	0	0.022	-0.004	34.899	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	119	LYS	1	0.854	0.907	34.336	0.086	0.086	0.000	0.000	0.000	0.000
43	A	120	LYS	1	0.819	0.920	27.748	0.117	0.117	0.000	0.000	0.000	0.000
44	A	121	LEU	0	0.017	0.019	27.450	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	122	VAL	0	-0.010	-0.015	22.870	0.004	0.004	0.000	0.000	0.000	0.000
46	A	123	ILE	0	0.005	0.000	20.896	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	124	THR	0	-0.030	-0.022	16.835	0.001	0.001	0.000	0.000	0.000	0.000
48	A	125	ALA	0	-0.023	-0.005	16.470	0.020	0.020	0.000	0.000	0.000	0.000
49	A	126	LYS	1	0.805	0.880	11.650	0.803	0.803	0.000	0.000	0.000	0.000
50	A	127	SER	0	0.037	0.022	10.639	-0.030	-0.030	0.000	0.000	0.000	0.000
51	A	128	GLU	-1	-0.937	-0.978	5.756	-2.640	-2.640	0.000	0.000	0.000	0.000
52	A	129	ASP	-1	-0.837	-0.881	5.857	-1.628	-1.628	0.000	0.000	0.000	0.000
53	A	130	ARG	1	0.811	0.870	6.964	0.958	0.958	0.000	0.000	0.000	0.000
54	A	131	GLN	0	-0.055	-0.026	7.157	0.073	0.073	0.000	0.000	0.000	0.000
55	A	132	TYR	0	0.004	-0.007	11.707	0.158	0.158	0.000	0.000	0.000	0.000
56	A	133	TYR	0	-0.048	-0.049	15.125	-0.046	-0.046	0.000	0.000	0.000	0.000
57	A	134	LYS	1	0.840	0.908	18.193	0.156	0.156	0.000	0.000	0.000	0.000
58	A	135	GLU	-1	-0.833	-0.877	21.755	-0.170	-0.170	0.000	0.000	0.000	0.000
59	A	136	ILE	0	-0.004	-0.015	25.182	0.015	0.015	0.000	0.000	0.000	0.000
60	A	137	ASP	-1	-0.845	-0.916	28.364	-0.099	-0.099	0.000	0.000	0.000	0.000
61	A	138	LEU	0	-0.020	-0.012	31.373	0.004	0.004	0.000	0.000	0.000	0.000
62	A	139	PRO	0	-0.013	0.006	34.120	0.004	0.004	0.000	0.000	0.000	0.000
63	A	140	ALA	0	-0.023	-0.023	37.479	0.006	0.006	0.000	0.000	0.000	0.000
64	A	141	GLU	-1	-0.812	-0.879	37.542	-0.099	-0.099	0.000	0.000	0.000	0.000
65	A	142	VAL	0	0.037	0.032	34.417	0.002	0.002	0.000	0.000	0.000	0.000
66	A	143	ASP	-1	-0.852	-0.948	37.416	-0.100	-0.100	0.000	0.000	0.000	0.000
67	A	144	GLU	-1	-0.835	-0.917	33.315	-0.157	-0.157	0.000	0.000	0.000	0.000
68	A	145	LYS	1	0.802	0.884	33.443	0.144	0.144	0.000	0.000	0.000	0.000
69	A	146	ALA	0	-0.032	0.000	35.583	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	147	ALA	0	0.024	0.004	32.070	0.001	0.001	0.000	0.000	0.000	0.000
71	A	148	LYS	1	0.789	0.878	33.597	0.118	0.118	0.000	0.000	0.000	0.000
72	A	149	ALA	0	0.020	0.013	28.222	0.002	0.002	0.000	0.000	0.000	0.000
73	A	150	ASN	0	-0.069	-0.036	28.448	0.001	0.001	0.000	0.000	0.000	0.000
74	A	151	PHE	0	0.049	0.025	19.118	0.003	0.003	0.000	0.000	0.000	0.000
75	A	152	LYS	1	0.969	0.983	24.759	0.154	0.154	0.000	0.000	0.000	0.000
76	A	153	ASN	0	-0.028	-0.023	22.638	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	154	GLY	0	0.054	0.041	19.584	0.008	0.008	0.000	0.000	0.000	0.000
78	A	155	VAL	0	0.001	0.009	20.165	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	156	LEU	0	-0.024	-0.005	22.373	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	157	GLU	-1	-0.787	-0.884	24.472	-0.117	-0.117	0.000	0.000	0.000	0.000
81	A	158	ILE	0	-0.005	-0.004	27.454	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	159	THR	0	-0.028	-0.013	29.879	0.015	0.015	0.000	0.000	0.000	0.000
83	A	160	LEU	0	0.015	0.008	31.529	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	161	LYS	1	0.829	0.888	35.368	0.105	0.105	0.000	0.000	0.000	0.000
85	A	162	LYS	1	0.862	0.917	38.461	0.071	0.071	0.000	0.000	0.000	0.000
86	A	163	LYS	1	0.805	0.912	38.668	0.097	0.097	0.000	0.000	0.000	0.000
87	A	164	ALA	0	-0.012	0.009	41.940	0.007	0.007	0.000	0.000	0.000	0.000

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