FMO DATABASE

FMODB ID: GRL91

Calculation Name: 2P6C-A-Xray547

Preferred Name:

Target Type:

Ligand Name: phosphate ion

Ligand 3-letter code: PO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2P6C

Chain ID: A

ChEMBL ID:

UniProt ID: O67812

Base Structure: X-ray

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	137
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1274075.83435
FMO2-HF: Nuclear repulsion	1218560.217546
FMO2-HF: Total energy	-55515.616804
FMO2-MP2: Total energy	-55679.588743

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: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.
-222.647	-213.968	15.408	-11.184	-12.903	-0.131

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 : 1 / q_Mulliken : 0.777 / q_NPA : 0.886

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	ALA	0	-0.003	-0.018	2.600	-0.821	1.077	1.939	-1.288	-2.549	-0.011
4	A	4	TYR	0	-0.018	-0.021	4.408	1.557	1.599	-0.001	-0.018	-0.023	0.000
135	A	135	ILE	0	-0.026	-0.021	2.714	-2.827	-1.539	0.928	-0.378	-1.839	0.000
136	A	136	GLY	0	0.056	0.027	2.661	4.982	6.026	0.158	-0.389	-0.813	-0.003
137	A	137	GLU	-2	-1.650	-1.783	1.873	-189.971	-185.564	12.384	-9.111	-7.679	-0.117
5	A	5	THR	0	-0.028	-0.019	8.227	0.576	0.576	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.862	0.931	11.286	16.982	16.982	0.000	0.000	0.000	0.000
7	A	7	TYR	0	-0.015	-0.016	14.910	0.070	0.070	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.024	0.028	18.138	0.175	0.175	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.029	-0.033	21.169	0.087	0.087	0.000	0.000	0.000	0.000
10	A	10	PHE	0	0.042	0.023	23.308	0.170	0.170	0.000	0.000	0.000	0.000
11	A	11	ASN	0	0.013	-0.006	27.770	0.125	0.125	0.000	0.000	0.000	0.000
12	A	12	THR	0	0.021	0.014	30.762	0.061	0.061	0.000	0.000	0.000	0.000
13	A	13	LYS	1	1.003	0.998	33.172	7.693	7.693	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.900	0.967	36.352	8.309	8.309	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.973	1.002	35.553	7.099	7.099	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.857	0.917	34.370	7.514	7.514	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.899	-0.979	32.584	-8.425	-8.425	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.026	0.019	28.864	-0.196	-0.196	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.040	-0.008	27.303	0.153	0.153	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.859	0.920	26.373	9.600	9.600	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.009	-0.011	20.607	-0.019	-0.019	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.013	-0.036	20.949	-0.874	-0.874	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.812	-0.905	20.243	-13.303	-13.303	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.923	-0.968	20.195	-13.088	-13.088	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.018	-0.014	15.556	-1.012	-1.012	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.875	0.940	15.780	12.239	12.239	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.957	0.991	16.457	13.409	13.409	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.035	-0.020	13.903	-0.718	-0.718	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.014	-0.008	11.901	-1.691	-1.691	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.948	-0.949	12.297	-18.300	-18.300	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.813	-0.888	14.082	-18.045	-18.045	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.083	-0.051	8.687	-1.919	-1.919	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.942	-0.974	8.784	-32.010	-32.010	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.098	-0.034	5.753	-3.262	-3.262	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.844	0.900	7.351	41.296	41.296	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.773	-0.890	8.215	-21.889	-21.889	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.001	-0.018	6.011	-6.605	-6.605	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.045	-0.005	6.281	3.604	3.604	0.000	0.000	0.000	0.000
39	A	39	CYS	0	0.003	0.000	7.775	-1.606	-1.606	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.031	0.009	10.519	1.357	1.357	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.016	-0.003	12.218	-0.301	-0.301	0.000	0.000	0.000	0.000
42	A	42	SER	0	0.029	-0.005	15.777	0.847	0.847	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.031	0.023	18.031	-0.138	-0.138	0.000	0.000	0.000	0.000
44	A	44	MET	0	-0.095	-0.045	18.140	-0.202	-0.202	0.000	0.000	0.000	0.000
45	A	45	HIS	0	0.002	0.003	21.729	0.152	0.152	0.000	0.000	0.000	0.000
46	A	46	LEU	0	0.035	0.025	24.869	-0.068	-0.068	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.011	0.006	26.973	0.268	0.268	0.000	0.000	0.000	0.000
48	A	48	SER	0	0.011	-0.011	26.700	0.227	0.227	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.026	0.012	23.946	-0.247	-0.247	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.061	-0.021	19.362	0.132	0.132	0.000	0.000	0.000	0.000
51	A	51	ILE	0	0.016	0.013	21.600	-0.104	-0.104	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.015	-0.008	18.860	-0.250	-0.250	0.000	0.000	0.000	0.000
53	A	53	GLN	0	-0.058	-0.027	23.308	0.643	0.643	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.761	-0.870	26.151	-9.705	-9.705	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.808	-0.912	28.831	-10.099	-10.099	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.873	-0.919	31.181	-7.787	-7.787	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-1.009	-1.000	34.484	-7.504	-7.504	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.057	0.018	37.265	0.019	0.019	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.022	0.012	32.806	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	60	HIS	1	0.769	0.869	30.791	8.941	8.941	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.958	-0.958	34.738	-7.171	-7.171	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.824	-0.916	36.448	-7.619	-7.619	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.060	-0.035	30.898	0.008	0.008	0.000	0.000	0.000	0.000
64	A	64	TRP	0	-0.060	-0.033	32.406	-0.069	-0.069	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.921	-0.954	36.508	-6.928	-6.928	0.000	0.000	0.000	0.000
66	A	66	TRP	0	-0.022	-0.022	31.276	0.058	0.058	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.015	-0.021	31.260	0.001	0.001	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.772	-0.858	35.411	-7.451	-7.451	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.901	0.953	38.889	6.937	6.937	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.057	-0.028	34.893	0.151	0.151	0.000	0.000	0.000	0.000
71	A	71	ALA	0	-0.018	0.002	34.923	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	72	PRO	0	0.020	0.033	36.961	-0.080	-0.080	0.000	0.000	0.000	0.000
73	A	73	TYR	0	-0.042	-0.046	39.774	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.800	0.854	41.091	6.697	6.697	0.000	0.000	0.000	0.000
75	A	75	PRO	0	0.024	0.026	42.610	-0.109	-0.109	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.810	-0.867	44.854	-6.414	-6.414	0.000	0.000	0.000	0.000
77	A	77	TYR	0	-0.033	-0.042	39.392	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.917	0.943	40.024	6.669	6.669	0.000	0.000	0.000	0.000
79	A	79	HIS	0	-0.005	0.004	35.405	0.097	0.097	0.000	0.000	0.000	0.000
80	A	80	HIS	0	0.096	0.060	38.823	-0.114	-0.114	0.000	0.000	0.000	0.000
81	A	81	ARG	1	0.879	0.947	40.112	7.117	7.117	0.000	0.000	0.000	0.000
82	A	82	THR	0	-0.053	-0.045	37.922	0.074	0.074	0.000	0.000	0.000	0.000
83	A	83	GLY	0	-0.024	0.000	41.318	0.011	0.011	0.000	0.000	0.000	0.000
84	A	84	GLU	-1	-0.906	-0.946	36.012	-8.107	-8.107	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.861	-0.912	39.923	-7.054	-7.054	0.000	0.000	0.000	0.000
86	A	86	ASN	0	0.010	-0.006	34.915	0.060	0.060	0.000	0.000	0.000	0.000
87	A	87	GLY	0	-0.004	-0.014	35.479	-0.211	-0.211	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.804	-0.888	35.259	-8.012	-8.012	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.013	0.013	32.444	-0.177	-0.177	0.000	0.000	0.000	0.000
90	A	90	HIS	0	-0.001	-0.002	30.445	-0.487	-0.487	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.035	-0.007	30.236	-0.216	-0.216	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.819	0.889	31.147	7.926	7.926	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.078	-0.021	24.506	-0.192	-0.192	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.011	-0.015	26.288	-0.282	-0.282	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.058	-0.022	27.112	-0.164	-0.164	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.040	-0.038	26.582	-0.173	-0.173	0.000	0.000	0.000	0.000
97	A	97	HIS	0	0.020	0.028	18.678	-0.061	-0.061	0.000	0.000	0.000	0.000
98	A	98	LEU	0	0.028	0.011	19.521	-0.033	-0.033	0.000	0.000	0.000	0.000
99	A	99	GLN	0	-0.027	-0.007	15.529	-0.358	-0.358	0.000	0.000	0.000	0.000
100	A	100	VAL	0	0.034	0.028	16.900	0.305	0.305	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.030	-0.032	11.212	-0.733	-0.733	0.000	0.000	0.000	0.000
102	A	102	LEU	0	0.005	0.013	12.810	0.835	0.835	0.000	0.000	0.000	0.000
103	A	103	PRO	0	0.019	0.008	11.002	-1.611	-1.611	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.062	-0.023	8.577	1.018	1.018	0.000	0.000	0.000	0.000
105	A	105	THR	0	0.023	-0.014	10.662	-2.140	-2.140	0.000	0.000	0.000	0.000
106	A	106	ASN	0	-0.075	-0.052	13.347	1.379	1.379	0.000	0.000	0.000	0.000
107	A	107	GLY	0	-0.030	-0.016	12.531	1.143	1.143	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.893	0.962	13.514	17.716	17.716	0.000	0.000	0.000	0.000
109	A	109	LEU	0	0.003	-0.003	14.028	-0.893	-0.893	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.900	-0.920	14.980	-16.044	-16.044	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.009	-0.015	16.694	0.031	0.031	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.021	0.009	19.888	0.254	0.254	0.000	0.000	0.000	0.000
113	A	113	PRO	0	-0.039	-0.037	23.109	-0.017	-0.017	0.000	0.000	0.000	0.000
114	A	114	TRP	0	-0.004	0.001	26.205	0.268	0.268	0.000	0.000	0.000	0.000
115	A	115	GLN	0	-0.006	0.009	21.053	-0.197	-0.197	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.760	-0.845	23.627	-12.102	-12.102	0.000	0.000	0.000	0.000
117	A	117	ILE	0	-0.025	-0.028	18.197	0.024	0.024	0.000	0.000	0.000	0.000
118	A	118	PHE	0	0.026	-0.003	22.470	0.201	0.201	0.000	0.000	0.000	0.000
119	A	119	TYR	0	-0.035	-0.028	23.827	-0.382	-0.382	0.000	0.000	0.000	0.000
120	A	120	ALA	0	0.008	0.007	25.136	0.402	0.402	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.759	-0.852	27.856	-9.909	-9.909	0.000	0.000	0.000	0.000
122	A	122	PHE	0	0.025	-0.008	28.251	0.319	0.319	0.000	0.000	0.000	0.000
123	A	123	ASP	-1	-0.841	-0.907	32.222	-8.137	-8.137	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.007	0.012	32.406	-0.194	-0.194	0.000	0.000	0.000	0.000
125	A	125	GLN	0	-0.111	-0.062	33.361	0.257	0.257	0.000	0.000	0.000	0.000
126	A	126	ARG	1	0.871	0.928	30.478	9.204	9.204	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.039	-0.028	29.173	-0.191	-0.191	0.000	0.000	0.000	0.000
128	A	128	LYS	1	0.758	0.882	26.984	9.657	9.657	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.941	0.956	19.780	13.000	13.000	0.000	0.000	0.000	0.000
130	A	130	VAL	0	0.028	0.030	18.910	0.136	0.136	0.000	0.000	0.000	0.000
131	A	131	VAL	0	-0.057	-0.036	14.307	-0.211	-0.211	0.000	0.000	0.000	0.000
132	A	132	ILE	0	0.047	0.035	12.649	0.119	0.119	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.854	0.907	7.923	23.856	23.856	0.000	0.000	0.000	0.000
134	A	134	ILE	0	0.046	0.030	7.021	0.393	0.393	0.000	0.000	0.000	0.000

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