FMO DATABASE

FMODB ID: KK1L3

Calculation Name: 2JZV-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2JZV

Chain ID: A

ChEMBL ID:

UniProt ID: P60747

Base Structure: SolutionNMR

Registration Date: 2025-10-04

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	111
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-836085.686775
FMO2-HF: Nuclear repulsion	793910.097502
FMO2-HF: Total energy	-42175.589273
FMO2-MP2: Total energy	-42300.68751

3D Structure Molmil

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:-5:GLY)

Summations of interaction energy for fragment #1(A:-5:GLY)

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.
9.145	9.785	0.003	-0.341	-0.302	-0.001

Interaction energy analysis for fragmet #1(A:-5:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.848 / q_NPA : 0.914

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	LEU	0	0.015	0.004	3.847	-5.802	-5.162	0.003	-0.341	-0.302	-0.001
4	A	-2	GLY	0	-0.001	0.010	6.730	2.823	2.823	0.000	0.000	0.000	0.000
5	A	-1	SER	0	0.003	-0.005	10.206	-0.265	-0.265	0.000	0.000	0.000	0.000
6	A	140	ASP	-1	-0.890	-0.943	13.517	-18.741	-18.741	0.000	0.000	0.000	0.000
7	A	141	SER	0	-0.038	-0.025	16.078	1.397	1.397	0.000	0.000	0.000	0.000
8	A	142	LYS	1	0.784	0.888	17.822	15.250	15.250	0.000	0.000	0.000	0.000
9	A	143	LYS	1	0.829	0.905	20.258	13.377	13.377	0.000	0.000	0.000	0.000
10	A	144	ALA	0	-0.010	-0.009	23.474	-0.163	-0.163	0.000	0.000	0.000	0.000
11	A	145	SER	0	0.020	0.013	26.298	0.255	0.255	0.000	0.000	0.000	0.000
12	A	146	HIS	0	-0.061	-0.051	29.766	-0.304	-0.304	0.000	0.000	0.000	0.000
13	A	147	ILE	0	0.039	0.027	32.174	0.288	0.288	0.000	0.000	0.000	0.000
14	A	148	LEU	0	-0.025	-0.008	35.209	-0.145	-0.145	0.000	0.000	0.000	0.000
15	A	149	ILE	0	0.004	-0.010	37.637	0.247	0.247	0.000	0.000	0.000	0.000
16	A	150	LYS	1	0.882	0.927	40.586	7.490	7.490	0.000	0.000	0.000	0.000
17	A	151	VAL	0	0.014	0.020	42.135	0.136	0.136	0.000	0.000	0.000	0.000
18	A	152	LYS	1	0.806	0.896	44.273	6.952	6.952	0.000	0.000	0.000	0.000
19	A	153	SER	0	0.024	0.013	47.684	0.030	0.030	0.000	0.000	0.000	0.000
20	A	154	LYS	1	0.851	0.916	49.718	6.191	6.191	0.000	0.000	0.000	0.000
21	A	155	LYS	1	1.000	0.990	52.321	5.616	5.616	0.000	0.000	0.000	0.000
22	A	156	SER	0	-0.022	-0.010	54.390	0.073	0.073	0.000	0.000	0.000	0.000
23	A	157	ASP	-1	-0.854	-0.900	51.248	-6.125	-6.125	0.000	0.000	0.000	0.000
24	A	158	LYS	1	0.975	0.966	51.483	5.634	5.634	0.000	0.000	0.000	0.000
25	A	159	GLU	-1	-0.822	-0.870	45.932	-7.113	-7.113	0.000	0.000	0.000	0.000
26	A	160	GLY	0	-0.011	-0.031	46.398	-0.205	-0.205	0.000	0.000	0.000	0.000
27	A	161	LEU	0	-0.009	0.014	45.540	0.154	0.154	0.000	0.000	0.000	0.000
28	A	162	ASP	-1	-0.828	-0.923	47.041	-6.377	-6.377	0.000	0.000	0.000	0.000
29	A	163	ASP	-1	-0.906	-0.967	44.417	-7.071	-7.071	0.000	0.000	0.000	0.000
30	A	164	LYS	1	0.948	0.974	44.289	6.043	6.043	0.000	0.000	0.000	0.000
31	A	165	GLU	-1	-0.857	-0.932	45.765	-6.533	-6.533	0.000	0.000	0.000	0.000
32	A	166	ALA	0	-0.036	-0.020	42.823	-0.100	-0.100	0.000	0.000	0.000	0.000
33	A	167	LYS	1	0.831	0.901	39.833	7.605	7.605	0.000	0.000	0.000	0.000
34	A	168	GLN	0	0.018	0.014	41.459	-0.131	-0.131	0.000	0.000	0.000	0.000
35	A	169	LYS	1	0.911	0.962	42.719	7.227	7.227	0.000	0.000	0.000	0.000
36	A	170	ALA	0	0.004	-0.008	38.012	-0.132	-0.132	0.000	0.000	0.000	0.000
37	A	171	GLU	-1	-0.819	-0.912	38.317	-8.072	-8.072	0.000	0.000	0.000	0.000
38	A	172	GLU	-1	-1.008	-1.004	39.364	-7.187	-7.187	0.000	0.000	0.000	0.000
39	A	173	ILE	0	0.015	0.001	37.992	-0.027	-0.027	0.000	0.000	0.000	0.000
40	A	174	GLN	0	0.016	0.007	31.666	-0.164	-0.164	0.000	0.000	0.000	0.000
41	A	175	LYS	1	0.911	0.961	35.267	7.322	7.322	0.000	0.000	0.000	0.000
42	A	176	GLU	-1	-0.842	-0.928	37.021	-7.878	-7.878	0.000	0.000	0.000	0.000
43	A	177	VAL	0	-0.017	-0.008	33.507	-0.047	-0.047	0.000	0.000	0.000	0.000
44	A	178	SER	0	-0.059	-0.018	31.342	-0.217	-0.217	0.000	0.000	0.000	0.000
45	A	179	LYS	1	0.816	0.914	32.202	7.752	7.752	0.000	0.000	0.000	0.000
46	A	180	ASP	-1	-0.834	-0.929	33.886	-9.010	-9.010	0.000	0.000	0.000	0.000
47	A	181	PRO	0	0.049	0.028	29.367	0.169	0.169	0.000	0.000	0.000	0.000
48	A	182	SER	0	-0.031	-0.023	31.885	-0.204	-0.204	0.000	0.000	0.000	0.000
49	A	183	LYS	1	0.867	0.940	33.845	8.203	8.203	0.000	0.000	0.000	0.000
50	A	184	PHE	0	0.004	0.009	32.009	0.185	0.185	0.000	0.000	0.000	0.000
51	A	185	GLY	0	0.035	0.027	34.968	0.117	0.117	0.000	0.000	0.000	0.000
52	A	186	GLU	-1	-0.912	-0.965	36.429	-7.688	-7.688	0.000	0.000	0.000	0.000
53	A	187	ILE	0	-0.015	-0.004	38.240	0.272	0.272	0.000	0.000	0.000	0.000
54	A	188	ALA	0	0.032	0.010	36.170	0.191	0.191	0.000	0.000	0.000	0.000
55	A	189	LYS	1	0.803	0.876	38.323	8.165	8.165	0.000	0.000	0.000	0.000
56	A	190	LYS	1	0.809	0.906	40.874	7.491	7.491	0.000	0.000	0.000	0.000
57	A	191	GLU	-1	-0.841	-0.919	40.884	-7.098	-7.098	0.000	0.000	0.000	0.000
58	A	192	SER	0	0.016	0.024	38.231	0.013	0.013	0.000	0.000	0.000	0.000
59	A	193	MET	0	-0.014	0.003	40.524	0.085	0.085	0.000	0.000	0.000	0.000
60	A	194	ASP	-1	-0.812	-0.870	36.680	-8.683	-8.683	0.000	0.000	0.000	0.000
61	A	195	THR	0	0.006	-0.008	39.500	-0.167	-0.167	0.000	0.000	0.000	0.000
62	A	196	GLY	0	0.014	0.019	38.985	0.033	0.033	0.000	0.000	0.000	0.000
63	A	197	SER	0	-0.046	-0.044	34.964	-0.139	-0.139	0.000	0.000	0.000	0.000
64	A	198	ALA	0	0.046	0.031	36.758	-0.036	-0.036	0.000	0.000	0.000	0.000
65	A	199	LYS	1	0.885	0.927	39.341	7.383	7.383	0.000	0.000	0.000	0.000
66	A	200	LYS	1	0.878	0.947	34.652	9.273	9.273	0.000	0.000	0.000	0.000
67	A	201	ASP	-1	-0.784	-0.866	35.446	-8.736	-8.736	0.000	0.000	0.000	0.000
68	A	202	GLY	0	0.066	0.027	34.764	-0.147	-0.147	0.000	0.000	0.000	0.000
69	A	203	GLU	-1	-1.004	-0.997	30.822	-10.692	-10.692	0.000	0.000	0.000	0.000
70	A	204	LEU	0	-0.063	-0.044	28.711	0.251	0.251	0.000	0.000	0.000	0.000
71	A	205	GLY	0	0.026	0.031	27.869	-0.105	-0.105	0.000	0.000	0.000	0.000
72	A	206	TYR	0	-0.004	-0.019	20.116	-0.045	-0.045	0.000	0.000	0.000	0.000
73	A	207	VAL	0	0.007	0.011	23.854	0.302	0.302	0.000	0.000	0.000	0.000
74	A	208	LEU	0	0.041	0.007	20.742	-0.784	-0.784	0.000	0.000	0.000	0.000
75	A	209	LYS	1	0.935	0.963	16.865	18.486	18.486	0.000	0.000	0.000	0.000
76	A	210	GLY	0	-0.031	-0.014	21.725	0.092	0.092	0.000	0.000	0.000	0.000
77	A	211	GLN	0	-0.043	-0.010	24.721	0.446	0.446	0.000	0.000	0.000	0.000
78	A	212	THR	0	-0.009	0.005	27.096	0.343	0.343	0.000	0.000	0.000	0.000
79	A	213	ASP	-1	-0.840	-0.932	28.247	-9.998	-9.998	0.000	0.000	0.000	0.000
80	A	214	LYS	1	0.968	0.974	26.821	10.577	10.577	0.000	0.000	0.000	0.000
81	A	215	ASP	-1	-0.925	-0.970	26.374	-11.023	-11.023	0.000	0.000	0.000	0.000
82	A	216	PHE	0	0.047	0.024	27.281	-0.180	-0.180	0.000	0.000	0.000	0.000
83	A	217	GLU	-1	-0.847	-0.924	21.770	-14.857	-14.857	0.000	0.000	0.000	0.000
84	A	218	LYS	1	0.916	0.953	22.964	11.331	11.331	0.000	0.000	0.000	0.000
85	A	219	ALA	0	-0.014	-0.009	23.440	-0.346	-0.346	0.000	0.000	0.000	0.000
86	A	220	LEU	0	0.079	0.045	22.805	-0.094	-0.094	0.000	0.000	0.000	0.000
87	A	221	PHE	0	0.006	-0.025	17.709	-0.512	-0.512	0.000	0.000	0.000	0.000
88	A	222	LYS	1	0.814	0.908	18.484	11.374	11.374	0.000	0.000	0.000	0.000
89	A	223	LEU	0	-0.056	0.001	19.934	-0.216	-0.216	0.000	0.000	0.000	0.000
90	A	224	LYS	1	0.980	0.989	17.959	15.459	15.459	0.000	0.000	0.000	0.000
91	A	225	ASP	-1	-0.803	-0.887	19.588	-15.055	-15.055	0.000	0.000	0.000	0.000
92	A	226	GLY	0	-0.024	-0.018	21.385	0.318	0.318	0.000	0.000	0.000	0.000
93	A	227	GLU	-1	-0.928	-0.937	23.574	-11.648	-11.648	0.000	0.000	0.000	0.000
94	A	228	VAL	0	-0.024	-0.027	25.423	-0.023	-0.023	0.000	0.000	0.000	0.000
95	A	229	SER	0	-0.038	-0.035	26.936	-0.102	-0.102	0.000	0.000	0.000	0.000
96	A	230	GLU	-1	-0.873	-0.930	28.275	-10.758	-10.758	0.000	0.000	0.000	0.000
97	A	231	VAL	0	-0.005	0.001	31.539	0.022	0.022	0.000	0.000	0.000	0.000
98	A	232	VAL	0	0.010	0.018	29.811	0.004	0.004	0.000	0.000	0.000	0.000
99	A	233	LYS	1	0.915	0.959	32.803	8.330	8.330	0.000	0.000	0.000	0.000
100	A	234	SER	0	-0.018	-0.020	32.989	-0.392	-0.392	0.000	0.000	0.000	0.000
101	A	235	SER	0	0.017	0.009	35.226	0.290	0.290	0.000	0.000	0.000	0.000
102	A	236	PHE	0	-0.028	0.001	35.129	0.334	0.334	0.000	0.000	0.000	0.000
103	A	237	GLY	0	0.000	-0.020	38.820	0.251	0.251	0.000	0.000	0.000	0.000
104	A	238	TYR	0	-0.020	-0.009	36.816	-0.158	-0.158	0.000	0.000	0.000	0.000
105	A	239	HIS	0	0.017	-0.002	33.016	0.233	0.233	0.000	0.000	0.000	0.000
106	A	240	ILE	0	0.000	0.017	32.394	0.013	0.013	0.000	0.000	0.000	0.000
107	A	241	ILE	0	-0.018	-0.005	27.338	0.055	0.055	0.000	0.000	0.000	0.000
108	A	242	LYS	1	0.901	0.971	27.674	11.174	11.174	0.000	0.000	0.000	0.000
109	A	243	ALA	0	0.013	0.011	22.470	-0.097	-0.097	0.000	0.000	0.000	0.000
110	A	244	ASP	-1	-0.869	-0.932	23.880	-11.421	-11.421	0.000	0.000	0.000	0.000
111	A	245	LYS	0	0.013	0.021	22.509	-0.769	-0.769	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-5:GLY)