FMO DATABASE

FMODB ID: N1Q5Q

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

Total energy (hartree)

FMO2-HF: Electronic energy	-942462.273913
FMO2-HF: Nuclear repulsion	896145.643991
FMO2-HF: Total energy	-46316.629922
FMO2-MP2: Total energy	-46449.742823

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.
-5.77	-2.843	2.838	-1.93	-3.835	-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 : -0.018 / q_NPA : -0.012

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	-0.943	-0.958	2.688	-7.120	-4.296	0.620	-1.511	-1.933	-0.007
4	A	4	THR	0	-0.044	-0.031	3.679	0.938	1.391	0.006	-0.110	-0.350	0.000
5	A	5	PRO	0	-0.042	-0.028	4.127	-0.207	-0.043	0.000	-0.033	-0.130	0.000
6	A	6	LEU	0	0.041	0.028	2.359	-0.158	-0.672	2.212	-0.276	-1.422	0.000
7	A	7	VAL	0	-0.049	-0.015	5.604	0.355	0.355	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.005	0.013	9.373	-0.163	-0.163	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.018	-0.009	12.071	0.138	0.138	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.865	0.945	14.437	0.287	0.287	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.003	-0.001	17.655	0.044	0.044	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.828	0.900	20.520	0.238	0.238	0.000	0.000	0.000	0.000
13	A	13	THR	0	0.005	0.002	24.090	0.013	0.013	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.794	-0.878	27.049	-0.229	-0.229	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.003	0.000	30.398	0.005	0.005	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.011	0.011	32.534	0.006	0.006	0.000	0.000	0.000	0.000
17	A	17	CYS	0	-0.042	-0.024	35.396	0.004	0.004	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.050	0.035	38.380	0.005	0.005	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.011	-0.004	34.655	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.012	-0.004	32.550	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.032	-0.014	29.369	0.012	0.012	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.035	-0.010	24.585	0.002	0.002	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.001	-0.005	23.641	0.022	0.022	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.042	0.018	18.422	-0.033	-0.033	0.000	0.000	0.000	0.000
25	A	25	CYS	0	-0.066	-0.018	19.205	0.057	0.057	0.000	0.000	0.000	0.000
26	A	26	THR	0	0.006	-0.007	13.506	-0.054	-0.054	0.000	0.000	0.000	0.000
27	A	27	ALA	0	-0.012	0.009	14.660	0.062	0.062	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.046	0.010	12.407	-0.011	-0.011	0.000	0.000	0.000	0.000
29	A	29	SER	0	0.025	0.006	13.748	0.001	0.001	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.028	-0.020	15.323	0.014	0.014	0.000	0.000	0.000	0.000
31	A	31	HIS	0	0.017	0.008	17.984	-0.023	-0.023	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.029	0.000	17.919	-0.012	-0.012	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.009	0.019	17.460	0.017	0.017	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.023	-0.009	19.880	-0.035	-0.035	0.000	0.000	0.000	0.000
35	A	35	VAL	0	-0.011	0.001	21.322	0.020	0.020	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.024	0.002	23.951	-0.016	-0.016	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.006	-0.023	25.894	0.015	0.015	0.000	0.000	0.000	0.000
38	A	38	GLN	0	0.099	0.025	28.566	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	39	PHE	0	-0.036	-0.036	31.694	0.006	0.006	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.059	0.038	29.391	0.006	0.006	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.924	0.979	29.568	0.112	0.112	0.000	0.000	0.000	0.000
42	A	42	MET	0	0.058	0.040	25.561	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.006	-0.014	27.871	0.000	0.000	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.031	-0.009	30.424	0.004	0.004	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.003	0.015	24.589	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.003	-0.019	28.011	0.012	0.012	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.030	-0.022	26.725	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.009	-0.021	27.045	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.808	-0.888	26.813	0.044	0.044	0.000	0.000	0.000	0.000
50	A	50	PRO	0	0.016	-0.002	27.812	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.015	0.009	30.839	0.010	0.010	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.023	-0.002	32.642	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.004	0.009	34.584	0.003	0.003	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.104	-0.039	34.968	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.049	0.006	35.463	0.004	0.004	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.889	-0.917	37.393	0.033	0.033	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.040	-0.012	37.906	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.023	-0.027	35.847	0.000	0.000	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.835	0.914	33.178	0.020	0.020	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.101	0.050	31.159	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.015	-0.011	33.734	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.017	-0.004	29.934	0.005	0.005	0.000	0.000	0.000	0.000
63	A	63	THR	0	0.048	0.029	32.093	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.003	-0.010	31.806	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.940	0.982	30.362	-0.047	-0.047	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.016	0.023	30.935	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.058	-0.034	26.669	0.011	0.011	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.032	0.011	27.520	0.003	0.003	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.033	0.018	31.321	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.010	-0.004	34.151	0.011	0.011	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.832	-0.903	36.643	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.786	-0.879	38.084	-0.034	-0.034	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.038	-0.001	39.227	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.004	-0.005	39.816	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.017	-0.015	33.897	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	76	HIS	1	0.807	0.887	35.094	0.007	0.007	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.010	0.010	35.567	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	78	PHE	0	0.010	0.003	33.331	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	79	ALA	0	0.043	0.020	31.365	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.897	0.938	31.775	0.006	0.006	0.000	0.000	0.000	0.000
81	A	81	ASN	0	-0.068	-0.044	33.176	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.021	0.006	30.025	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.034	-0.001	27.045	-0.010	-0.010	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.027	0.012	28.097	0.004	0.004	0.000	0.000	0.000	0.000
85	A	85	PHE	0	-0.057	-0.037	27.218	0.010	0.010	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.045	0.033	23.277	0.003	0.003	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.010	-0.009	24.593	0.006	0.006	0.000	0.000	0.000	0.000
88	A	88	GLN	0	0.016	0.011	25.758	0.013	0.013	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.761	-0.848	25.330	-0.096	-0.096	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.032	-0.002	21.135	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.002	0.013	21.487	0.014	0.014	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.047	-0.032	24.000	0.011	0.011	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.861	0.937	16.512	0.025	0.025	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.048	0.042	23.014	-0.015	-0.015	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.027	-0.021	22.551	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.006	0.007	20.996	0.011	0.011	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.011	-0.006	23.189	-0.022	-0.022	0.000	0.000	0.000	0.000
98	A	98	ALA	0	0.007	0.015	24.751	0.013	0.013	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.005	-0.008	26.470	-0.018	-0.018	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.016	-0.010	29.639	0.011	0.011	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.022	0.001	31.739	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.829	0.908	34.011	0.102	0.102	0.000	0.000	0.000	0.000
103	A	103	ASP	-1	-0.826	-0.895	37.328	-0.083	-0.083	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.862	0.932	36.303	0.071	0.071	0.000	0.000	0.000	0.000
105	A	105	SER	0	0.023	-0.014	39.363	0.003	0.003	0.000	0.000	0.000	0.000
106	A	106	MET	0	0.038	0.019	39.420	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.834	-0.909	39.305	-0.081	-0.081	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.058	0.015	36.942	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.049	-0.019	34.522	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.925	0.954	34.345	0.076	0.076	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.041	0.024	34.095	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.008	-0.005	30.787	-0.012	-0.012	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.875	0.943	29.457	0.075	0.075	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.879	-0.939	29.014	-0.136	-0.136	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.017	-0.005	26.417	-0.015	-0.015	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.002	-0.008	24.639	-0.021	-0.021	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.780	0.862	24.408	0.121	0.121	0.000	0.000	0.000	0.000
118	A	118	VAL	0	-0.010	-0.002	23.883	-0.013	-0.013	0.000	0.000	0.000	0.000
119	A	119	CYS	0	-0.091	-0.047	21.270	-0.038	-0.038	0.000	0.000	0.000	0.000
120	A	120	GLN	0	0.052	0.033	20.425	-0.008	-0.008	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.029	-0.012	16.331	-0.033	-0.033	0.000	0.000	0.000	0.000
122	A	122	TRP	0	0.033	0.012	17.466	0.008	0.008	0.000	0.000	0.000	0.000

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