FMO DATABASE

FMODB ID: N3RRQ

Calculation Name: 2Z5E-A-Xray317

Preferred Name: Proteasome assembly chaperone 3

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2Z5E

Chain ID: A

ChEMBL ID: CHEMBL1075137

UniProt ID: Q9BT73

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	122
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-941736.172577
FMO2-HF: Nuclear repulsion	895421.127927
FMO2-HF: Total energy	-46315.04465
FMO2-MP2: Total energy	-46448.256003

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:1:MET )

Summations of interaction energy for fragment #1(A:1: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.
-7.098	-4.455	3.596	-2.297	-3.942	-0.021

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.055 / q_NPA : -0.047

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	3	ASP	-1	-0.946	-0.953	2.308	-7.606	-6.139	3.315	-2.066	-2.716	-0.021
4	A	4	THR	0	-0.034	-0.027	3.664	1.211	1.510	0.001	-0.042	-0.259	0.000
5	A	5	PRO	0	-0.001	-0.010	4.815	0.390	0.522	0.000	-0.005	-0.127	0.000
6	A	6	LEU	0	0.032	0.019	2.852	-1.086	-0.341	0.280	-0.184	-0.840	0.000
7	A	7	VAL	0	-0.053	-0.017	6.607	-0.017	-0.017	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.011	0.007	10.349	-0.106	-0.106	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.012	-0.016	13.006	0.047	0.047	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.914	0.973	15.711	0.103	0.103	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.016	0.002	18.737	0.016	0.016	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.950	0.977	21.468	0.110	0.110	0.000	0.000	0.000	0.000
13	A	13	THR	0	0.004	-0.002	24.985	0.009	0.009	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.929	-0.969	27.924	-0.099	-0.099	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.007	0.005	31.333	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.018	0.007	33.279	0.003	0.003	0.000	0.000	0.000	0.000
17	A	17	CYS	0	-0.043	-0.015	36.170	0.002	0.002	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.047	0.025	39.335	0.002	0.002	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.014	0.001	35.546	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.017	-0.004	33.342	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.025	-0.006	30.189	0.005	0.005	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.025	-0.004	26.001	0.003	0.003	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.010	-0.004	24.827	0.012	0.012	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.030	0.009	19.276	-0.018	-0.018	0.000	0.000	0.000	0.000
25	A	25	CYS	0	-0.053	-0.003	20.597	0.025	0.025	0.000	0.000	0.000	0.000
26	A	26	THR	0	0.049	0.021	14.689	-0.038	-0.038	0.000	0.000	0.000	0.000
27	A	27	ALA	0	-0.018	0.009	15.288	0.023	0.023	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.013	-0.010	13.557	0.028	0.028	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.007	0.000	14.423	-0.039	-0.039	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.033	-0.004	15.882	-0.016	-0.016	0.000	0.000	0.000	0.000
31	A	31	HIS	0	0.013	0.016	18.569	-0.027	-0.027	0.000	0.000	0.000	0.000
32	A	32	ILE	0	0.010	0.022	18.584	0.008	0.008	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.024	-0.001	18.815	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.027	0.002	20.904	-0.017	-0.017	0.000	0.000	0.000	0.000
35	A	35	VAL	0	0.003	0.001	22.464	0.007	0.007	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.005	-0.007	25.039	-0.011	-0.011	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.020	-0.009	26.813	0.004	0.004	0.000	0.000	0.000	0.000
38	A	38	GLN	0	0.112	0.033	29.618	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	39	PHE	0	-0.041	-0.048	32.872	0.004	0.004	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.062	0.037	29.914	0.002	0.002	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.899	0.962	29.676	0.053	0.053	0.000	0.000	0.000	0.000
42	A	42	MET	0	0.058	0.032	26.198	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.021	-0.015	28.836	0.003	0.003	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.043	-0.017	31.216	0.004	0.004	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.007	0.013	25.329	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.011	-0.013	29.068	0.004	0.004	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.043	0.033	27.795	0.000	0.000	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.078	-0.051	27.975	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.885	-0.947	27.858	0.072	0.072	0.000	0.000	0.000	0.000
50	A	50	PRO	0	0.024	0.013	28.494	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.035	-0.024	31.623	0.005	0.005	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.062	0.018	33.950	0.000	0.000	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.021	0.003	35.399	0.000	0.000	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.086	-0.040	35.969	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.078	0.038	36.335	0.003	0.003	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.961	-0.972	37.567	0.028	0.028	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.053	-0.001	38.595	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	58	SER	0	0.010	-0.019	35.978	0.001	0.001	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.872	0.958	33.972	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.109	0.054	32.123	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.025	-0.011	35.011	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.005	-0.005	30.901	0.003	0.003	0.000	0.000	0.000	0.000
63	A	63	THR	0	0.002	0.000	33.364	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.023	0.000	32.634	0.000	0.000	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.962	0.987	31.553	-0.043	-0.043	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.012	0.011	32.090	0.000	0.000	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.055	-0.031	27.508	0.003	0.003	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.040	0.013	27.837	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.020	0.010	31.878	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.021	-0.017	34.767	0.005	0.005	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.843	-0.910	37.756	0.006	0.006	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.768	-0.888	38.867	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.038	0.007	40.194	0.000	0.000	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.003	-0.007	40.861	0.001	0.001	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.016	-0.005	35.234	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	76	HIS	1	0.806	0.882	36.166	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.008	0.006	36.617	0.001	0.001	0.000	0.000	0.000	0.000
78	A	78	PHE	0	-0.009	-0.015	34.245	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	79	ALA	0	0.032	0.023	32.231	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	80	LYS	1	1.006	0.983	32.692	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	81	ASN	0	-0.062	-0.024	34.013	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.029	-0.014	30.761	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.030	0.003	27.769	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.027	0.016	29.210	0.005	0.005	0.000	0.000	0.000	0.000
85	A	85	PHE	0	-0.076	-0.046	28.160	0.005	0.005	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.054	0.043	24.247	0.001	0.001	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.001	0.004	25.634	0.004	0.004	0.000	0.000	0.000	0.000
88	A	88	GLN	0	-0.028	-0.030	26.781	0.006	0.006	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.746	-0.812	26.264	-0.021	-0.021	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.024	0.008	22.099	0.001	0.001	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.007	-0.001	22.203	0.012	0.012	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.060	-0.044	24.332	0.006	0.006	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.890	0.964	16.378	-0.060	-0.060	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.048	0.037	23.429	-0.013	-0.013	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.010	-0.020	23.387	0.000	0.000	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.008	0.007	22.291	0.002	0.002	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.011	-0.013	24.328	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	98	ALA	0	0.024	0.026	25.800	0.004	0.004	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.010	0.005	27.456	-0.010	-0.010	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.011	-0.008	30.600	0.004	0.004	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.009	0.006	32.833	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.870	0.948	35.545	0.056	0.056	0.000	0.000	0.000	0.000
103	A	103	ASP	-1	-0.861	-0.928	38.822	-0.038	-0.038	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.857	0.933	37.225	0.029	0.029	0.000	0.000	0.000	0.000
105	A	105	SER	0	0.093	0.042	40.089	0.001	0.001	0.000	0.000	0.000	0.000
106	A	106	MET	0	0.028	0.020	40.243	0.000	0.000	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.886	-0.959	40.424	-0.033	-0.033	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.035	-0.004	38.271	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.047	-0.018	35.134	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.929	0.951	35.188	0.027	0.027	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.075	0.038	35.244	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.025	-0.012	31.945	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.856	0.930	30.750	0.023	0.023	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.893	-0.939	30.293	-0.050	-0.050	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.006	-0.002	27.491	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.006	-0.014	25.700	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.774	0.846	25.345	0.037	0.037	0.000	0.000	0.000	0.000
118	A	118	VAL	0	-0.014	-0.006	25.151	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	119	CYS	0	-0.110	-0.046	22.110	-0.021	-0.021	0.000	0.000	0.000	0.000
120	A	120	GLN	0	0.009	0.015	21.458	0.000	0.000	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.068	-0.049	17.161	-0.019	-0.019	0.000	0.000	0.000	0.000
122	A	122	TRP	-1	-0.882	-0.956	18.026	-0.013	-0.013	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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