FMO DATABASE

FMODB ID: 2NJZR

Calculation Name: 3LOF-A-Xray372

Preferred Name: Heat shock 70 kDa protein 1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3LOF

Chain ID: A

ChEMBL ID: CHEMBL5460

UniProt ID: P0DMV8

Base Structure: X-ray

Registration Date: 2023-09-21

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	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	84
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-537331.933711
FMO2-HF: Nuclear repulsion	504175.95802
FMO2-HF: Total energy	-33155.975691
FMO2-MP2: Total energy	-33251.918177

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:530:ASN)

Summations of interaction energy for fragment #1(A:530:ASN)

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.
-26.666	-21.09	6.636	-4.716	-7.495	0.036

Interaction energy analysis for fragmet #1(A:530:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.045 / q_NPA : 0.027

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	532	ALA	0	0.008	0.014	2.231	-7.245	-5.357	4.096	-2.400	-3.584	0.025
4	A	533	ALA	0	0.014	-0.006	2.285	-10.010	-8.417	2.400	-1.273	-2.720	0.017
5	A	534	GLU	-1	-0.914	-0.962	3.078	-9.665	-7.570	0.140	-1.043	-1.191	-0.006
6	A	535	ARG	1	0.830	0.910	5.651	-1.623	-1.623	0.000	0.000	0.000	0.000
7	A	536	VAL	0	-0.020	-0.007	6.966	-0.473	-0.473	0.000	0.000	0.000	0.000
8	A	537	SER	0	-0.027	-0.008	7.850	-0.209	-0.209	0.000	0.000	0.000	0.000
9	A	538	ALA	0	0.007	0.002	9.616	-0.051	-0.051	0.000	0.000	0.000	0.000
10	A	539	LYS	1	0.874	0.956	11.619	-0.343	-0.343	0.000	0.000	0.000	0.000
11	A	540	ASN	0	0.039	-0.002	12.428	0.043	0.043	0.000	0.000	0.000	0.000
12	A	541	ALA	0	-0.002	0.034	13.919	-0.033	-0.033	0.000	0.000	0.000	0.000
13	A	542	LEU	0	-0.011	-0.005	15.659	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	543	GLU	-1	-0.881	-0.942	17.356	0.127	0.127	0.000	0.000	0.000	0.000
15	A	544	SER	0	-0.022	-0.030	17.257	-0.022	-0.022	0.000	0.000	0.000	0.000
16	A	545	TYR	0	0.014	0.007	19.767	0.003	0.003	0.000	0.000	0.000	0.000
17	A	546	ALA	0	0.016	0.005	21.704	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	547	PHE	0	0.044	0.010	22.204	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	548	ASN	0	-0.066	-0.041	22.154	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	549	MET	0	0.001	0.006	25.413	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	550	LYS	1	0.827	0.903	27.458	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	551	SER	0	0.018	0.012	28.634	0.001	0.001	0.000	0.000	0.000	0.000
23	A	552	ALA	0	-0.037	-0.014	29.315	0.000	0.000	0.000	0.000	0.000	0.000
24	A	553	VAL	0	0.021	-0.004	31.127	0.001	0.001	0.000	0.000	0.000	0.000
25	A	554	GLU	-1	-0.915	-0.949	32.707	0.000	0.000	0.000	0.000	0.000	0.000
26	A	555	ASP	-1	-0.835	-0.896	34.345	-0.049	-0.049	0.000	0.000	0.000	0.000
27	A	556	GLU	-1	-0.873	-0.932	36.180	-0.028	-0.028	0.000	0.000	0.000	0.000
28	A	557	GLY	0	-0.018	-0.011	38.741	0.002	0.002	0.000	0.000	0.000	0.000
29	A	558	LEU	0	-0.034	-0.031	34.094	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	559	LYS	1	0.876	0.923	38.817	0.028	0.028	0.000	0.000	0.000	0.000
31	A	560	GLY	0	-0.027	-0.005	42.126	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	561	LYS	1	0.900	0.958	38.960	0.047	0.047	0.000	0.000	0.000	0.000
33	A	562	ILE	0	0.001	0.015	34.802	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	563	SER	0	-0.033	-0.032	38.814	0.004	0.004	0.000	0.000	0.000	0.000
35	A	564	GLU	-1	-0.827	-0.944	39.362	-0.008	-0.008	0.000	0.000	0.000	0.000
36	A	565	ALA	0	-0.004	0.009	39.739	0.003	0.003	0.000	0.000	0.000	0.000
37	A	566	ASP	-1	-0.827	-0.899	35.894	-0.016	-0.016	0.000	0.000	0.000	0.000
38	A	567	LYS	1	0.935	0.978	35.042	0.016	0.016	0.000	0.000	0.000	0.000
39	A	568	LYS	1	0.831	0.897	35.077	-0.020	-0.020	0.000	0.000	0.000	0.000
40	A	569	LYS	1	0.886	0.934	33.114	0.013	0.013	0.000	0.000	0.000	0.000
41	A	570	VAL	0	0.000	0.004	29.678	0.004	0.004	0.000	0.000	0.000	0.000
42	A	571	LEU	0	0.027	0.012	30.610	0.005	0.005	0.000	0.000	0.000	0.000
43	A	572	ASP	-1	-0.828	-0.882	31.345	0.033	0.033	0.000	0.000	0.000	0.000
44	A	573	LYS	1	0.799	0.882	26.710	-0.041	-0.041	0.000	0.000	0.000	0.000
45	A	574	CYS	0	-0.060	-0.031	26.802	0.006	0.006	0.000	0.000	0.000	0.000
46	A	575	GLN	0	0.023	-0.008	26.696	0.005	0.005	0.000	0.000	0.000	0.000
47	A	576	GLU	-1	-0.817	-0.882	26.820	0.094	0.094	0.000	0.000	0.000	0.000
48	A	577	VAL	0	0.027	0.004	22.055	0.018	0.018	0.000	0.000	0.000	0.000
49	A	578	ILE	0	-0.029	-0.009	22.959	0.025	0.025	0.000	0.000	0.000	0.000
50	A	579	SER	0	0.004	0.001	23.681	0.016	0.016	0.000	0.000	0.000	0.000
51	A	580	TRP	0	-0.010	-0.007	17.396	0.009	0.009	0.000	0.000	0.000	0.000
52	A	581	LEU	0	-0.020	-0.015	16.875	0.036	0.036	0.000	0.000	0.000	0.000
53	A	582	ASP	-1	-0.945	-0.972	19.650	0.225	0.225	0.000	0.000	0.000	0.000
54	A	583	ALA	0	-0.037	-0.002	21.843	0.021	0.021	0.000	0.000	0.000	0.000
55	A	584	ASN	0	-0.077	-0.043	18.487	0.050	0.050	0.000	0.000	0.000	0.000
56	A	585	THR	0	0.045	0.018	15.332	0.050	0.050	0.000	0.000	0.000	0.000
57	A	586	LEU	0	-0.085	-0.064	12.438	0.109	0.109	0.000	0.000	0.000	0.000
58	A	587	ALA	0	0.037	0.049	13.962	0.089	0.089	0.000	0.000	0.000	0.000
59	A	588	GLU	-1	-0.819	-0.927	10.839	1.570	1.570	0.000	0.000	0.000	0.000
60	A	589	LYS	1	0.858	0.924	7.442	0.455	0.455	0.000	0.000	0.000	0.000
61	A	590	ASP	-1	-0.943	-0.977	11.498	0.167	0.167	0.000	0.000	0.000	0.000
62	A	591	GLU	-1	-0.790	-0.891	13.868	0.394	0.394	0.000	0.000	0.000	0.000
63	A	592	PHE	0	-0.027	-0.020	12.060	-0.076	-0.076	0.000	0.000	0.000	0.000
64	A	593	GLU	-1	-0.892	-0.936	11.692	-0.366	-0.366	0.000	0.000	0.000	0.000
65	A	594	HIS	0	-0.028	-0.016	15.714	-0.048	-0.048	0.000	0.000	0.000	0.000
66	A	595	LYS	1	0.866	0.927	19.078	-0.128	-0.128	0.000	0.000	0.000	0.000
67	A	596	ARG	1	0.881	0.915	14.566	0.149	0.149	0.000	0.000	0.000	0.000
68	A	597	LYS	1	0.875	0.930	15.467	0.101	0.101	0.000	0.000	0.000	0.000
69	A	598	GLU	-1	-0.812	-0.873	21.068	0.071	0.071	0.000	0.000	0.000	0.000
70	A	599	LEU	0	-0.023	-0.010	22.560	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	600	GLU	-1	-0.807	-0.890	19.628	-0.141	-0.141	0.000	0.000	0.000	0.000
72	A	601	GLN	0	-0.083	-0.031	24.090	0.001	0.001	0.000	0.000	0.000	0.000
73	A	602	VAL	0	-0.018	-0.002	26.921	0.001	0.001	0.000	0.000	0.000	0.000
74	A	603	CYS	0	-0.022	-0.005	26.287	0.001	0.001	0.000	0.000	0.000	0.000
75	A	604	ASN	0	0.030	0.005	23.985	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	605	PRO	0	0.003	0.015	28.118	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	606	ILE	0	0.010	0.013	31.467	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	607	ILE	0	0.007	0.001	26.158	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	608	SER	0	-0.014	-0.024	30.024	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	609	GLY	0	-0.026	-0.013	31.788	0.000	0.000	0.000	0.000	0.000	0.000
81	A	610	LEU	0	-0.037	-0.028	32.734	0.002	0.002	0.000	0.000	0.000	0.000
82	A	611	TYR	0	-0.030	-0.017	28.155	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	612	GLN	0	-0.060	-0.011	33.686	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	613	GLY	0	-0.061	-0.016	36.560	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:530:ASN)