FMO DATABASE

FMODB ID: 82M3Y

Calculation Name: 2Z5E-A-Xray372

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: 2023-06-20

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	122
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-942640.367275
FMO2-HF: Nuclear repulsion	896324.113128
FMO2-HF: Total energy	-46316.254146
FMO2-MP2: Total energy	-46449.430699

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.
-7.029	-3.837	2.799	-2.152	-3.84	-0.007

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 : -0.030 / q_NPA : -0.017

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	3	ASP	-1	-0.949	-0.956	2.574	-8.055	-5.129	1.086	-1.826	-2.187	-0.006
4	A	4	THR	0	-0.026	-0.027	4.286	1.386	1.626	-0.001	-0.025	-0.214	0.000
5	A	5	PRO	0	-0.023	-0.018	4.152	-0.404	-0.248	-0.001	-0.028	-0.127	0.000
6	A	6	LEU	0	0.035	0.023	2.418	-0.468	-0.598	1.715	-0.273	-1.312	-0.001
7	A	7	VAL	0	-0.049	-0.014	6.009	0.255	0.255	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.007	0.007	9.774	-0.145	-0.145	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.038	-0.002	12.284	0.118	0.118	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.882	0.955	14.819	0.224	0.224	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.001	-0.002	17.970	0.034	0.034	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.851	0.913	20.690	0.201	0.201	0.000	0.000	0.000	0.000
13	A	13	THR	0	-0.002	-0.005	24.269	0.014	0.014	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.812	-0.890	27.196	-0.193	-0.193	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.004	0.003	30.606	0.006	0.006	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.007	0.002	32.440	0.004	0.004	0.000	0.000	0.000	0.000
17	A	17	CYS	0	-0.039	-0.018	35.342	0.004	0.004	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.045	0.023	38.528	0.004	0.004	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.010	0.004	34.666	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.015	-0.006	32.492	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.018	-0.007	29.241	0.010	0.010	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.023	-0.001	24.973	0.001	0.001	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.001	-0.009	23.934	0.020	0.020	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.027	0.007	18.477	-0.032	-0.032	0.000	0.000	0.000	0.000
25	A	25	CYS	0	-0.053	0.005	19.632	0.047	0.047	0.000	0.000	0.000	0.000
26	A	26	THR	0	0.020	-0.007	13.862	-0.048	-0.048	0.000	0.000	0.000	0.000
27	A	27	ALA	0	-0.023	0.001	14.695	0.051	0.051	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.029	-0.001	12.737	0.000	0.000	0.000	0.000	0.000	0.000
29	A	29	SER	0	0.033	0.013	13.587	-0.008	-0.008	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.005	-0.016	15.138	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	31	HIS	0	0.017	0.014	17.806	-0.028	-0.028	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.016	0.007	17.861	-0.007	-0.007	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.008	0.011	17.946	0.012	0.012	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.024	-0.003	20.141	-0.032	-0.032	0.000	0.000	0.000	0.000
35	A	35	VAL	0	0.004	0.005	21.489	0.019	0.019	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.008	-0.009	24.058	-0.019	-0.019	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.013	-0.025	26.091	0.011	0.011	0.000	0.000	0.000	0.000
38	A	38	GLN	0	0.102	0.046	28.694	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	39	PHE	0	-0.037	-0.045	31.954	0.007	0.007	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.055	0.033	29.513	0.005	0.005	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.913	0.972	29.423	0.087	0.087	0.000	0.000	0.000	0.000
42	A	42	MET	0	0.049	0.039	25.810	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.015	-0.012	28.316	0.002	0.002	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.029	-0.012	30.755	0.004	0.004	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.004	0.014	24.826	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.000	-0.022	28.361	0.010	0.010	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.024	0.001	26.767	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.038	-0.037	27.213	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.839	-0.917	26.899	0.084	0.084	0.000	0.000	0.000	0.000
50	A	50	PRO	0	0.015	0.006	27.931	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.034	-0.023	30.881	0.009	0.009	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.041	0.010	32.633	0.001	0.001	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.005	0.005	34.631	0.002	0.002	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.088	-0.041	35.250	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.042	0.016	35.617	0.005	0.005	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.901	-0.934	36.889	0.046	0.046	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.059	-0.005	37.988	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	58	SER	0	0.011	-0.018	35.483	0.001	0.001	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.828	0.923	33.341	0.007	0.007	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.102	0.048	31.632	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.017	-0.006	34.321	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.014	-0.007	30.518	0.005	0.005	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.008	-0.010	32.519	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.010	0.000	31.861	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.958	0.990	30.596	-0.070	-0.070	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.012	0.015	31.316	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.054	-0.031	27.003	0.007	0.007	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.039	0.013	27.758	0.002	0.002	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.024	0.010	31.635	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.015	-0.013	34.451	0.009	0.009	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.822	-0.893	37.249	0.010	0.010	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.789	-0.887	38.339	-0.020	-0.020	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.049	0.007	39.465	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.004	-0.010	40.142	0.000	0.000	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.023	-0.012	34.396	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	76	HIS	1	0.798	0.882	35.469	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.012	0.007	35.909	0.000	0.000	0.000	0.000	0.000	0.000
78	A	78	PHE	0	0.004	-0.001	33.484	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	79	ALA	0	0.041	0.023	31.573	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.984	0.983	32.028	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	81	ASN	0	-0.085	-0.042	33.363	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.011	0.002	30.017	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.037	0.002	27.139	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.033	0.022	28.570	0.006	0.006	0.000	0.000	0.000	0.000
85	A	85	PHE	0	-0.069	-0.048	27.583	0.009	0.009	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.050	0.040	23.674	0.001	0.001	0.000	0.000	0.000	0.000
87	A	87	SER	0	0.007	-0.001	25.031	0.005	0.005	0.000	0.000	0.000	0.000
88	A	88	GLN	0	-0.002	0.007	26.142	0.011	0.011	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.751	-0.835	25.666	-0.065	-0.065	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.049	-0.009	21.437	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	91	GLY	0	-0.008	-0.002	21.590	0.014	0.014	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.037	-0.031	23.729	0.011	0.011	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.880	0.953	16.181	-0.022	-0.022	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.041	0.039	22.687	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.010	-0.021	22.654	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.003	0.011	21.535	0.010	0.010	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.013	-0.016	23.628	-0.017	-0.017	0.000	0.000	0.000	0.000
98	A	98	ALA	0	0.028	0.031	24.970	0.010	0.010	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.005	-0.003	26.715	-0.017	-0.017	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.002	0.001	29.740	0.010	0.010	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.001	0.000	32.028	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.792	0.891	34.585	0.084	0.084	0.000	0.000	0.000	0.000
103	A	103	ASP	-1	-0.805	-0.893	37.928	-0.066	-0.066	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.878	0.950	36.432	0.051	0.051	0.000	0.000	0.000	0.000
105	A	105	SER	0	0.044	-0.007	39.161	0.001	0.001	0.000	0.000	0.000	0.000
106	A	106	MET	0	0.033	0.024	39.365	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.840	-0.913	39.594	-0.063	-0.063	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.037	0.003	37.365	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.039	-0.018	34.464	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.934	0.955	34.367	0.057	0.057	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.062	0.034	34.428	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.018	-0.011	30.915	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.858	0.927	29.862	0.051	0.051	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.900	-0.944	29.537	-0.106	-0.106	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.005	0.001	26.561	-0.012	-0.012	0.000	0.000	0.000	0.000
116	A	116	ILE	0	0.009	-0.003	24.976	-0.016	-0.016	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.780	0.864	24.575	0.088	0.088	0.000	0.000	0.000	0.000
118	A	118	VAL	0	-0.010	-0.007	24.612	-0.010	-0.010	0.000	0.000	0.000	0.000
119	A	119	CYS	0	-0.106	-0.045	21.302	-0.035	-0.035	0.000	0.000	0.000	0.000
120	A	120	GLN	0	0.033	0.024	20.683	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.036	-0.020	16.556	-0.032	-0.032	0.000	0.000	0.000	0.000
122	A	122	TRP	0	0.031	0.008	17.529	0.003	0.003	0.000	0.000	0.000	0.000

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