FMO DATABASE

FMODB ID: YZG92

Calculation Name: 2FCF-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2FCF

Chain ID: A

ChEMBL ID:

UniProt ID: O75970

Base Structure: X-ray

Registration Date: 2023-09-19

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	90
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-596052.84165
FMO2-HF: Nuclear repulsion	561309.109996
FMO2-HF: Total energy	-34743.731654
FMO2-MP2: Total energy	-34844.745305

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:1145:GLN)

Summations of interaction energy for fragment #1(A:1145:GLN)

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.
-1.03	1.821	0.671	-1.268	-2.254	0.002

Interaction energy analysis for fragmet #1(A:1145:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.005 / q_NPA : -0.008

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	1147	MET	0	-0.001	-0.007	3.424	-3.003	-1.129	0.027	-0.908	-0.993	0.002
4	A	1148	GLN	0	0.027	0.027	5.813	0.358	0.358	0.000	0.000	0.000	0.000
5	A	1149	PRO	0	-0.003	0.007	7.143	-0.462	-0.462	0.000	0.000	0.000	0.000
6	A	1150	ARG	1	0.813	0.885	5.908	2.957	2.957	0.000	0.000	0.000	0.000
7	A	1151	ARG	1	0.919	0.925	9.485	0.510	0.510	0.000	0.000	0.000	0.000
8	A	1152	VAL	0	-0.053	-0.030	10.412	-0.155	-0.155	0.000	0.000	0.000	0.000
9	A	1153	GLU	-1	-0.823	-0.889	13.040	-0.346	-0.346	0.000	0.000	0.000	0.000
10	A	1154	LEU	0	-0.057	-0.024	16.017	-0.025	-0.025	0.000	0.000	0.000	0.000
11	A	1155	TRP	0	0.040	0.018	18.845	0.058	0.058	0.000	0.000	0.000	0.000
12	A	1156	ARG	1	0.812	0.884	22.051	0.345	0.345	0.000	0.000	0.000	0.000
13	A	1157	GLU	-1	-0.762	-0.870	24.253	-0.323	-0.323	0.000	0.000	0.000	0.000
14	A	1158	PRO	0	-0.020	-0.021	26.836	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	1159	SER	0	-0.031	-0.022	29.791	0.011	0.011	0.000	0.000	0.000	0.000
16	A	1160	LYS	1	0.988	0.992	27.858	0.230	0.230	0.000	0.000	0.000	0.000
17	A	1161	SER	0	-0.062	-0.014	25.511	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	1162	LEU	0	0.076	0.022	21.132	0.002	0.002	0.000	0.000	0.000	0.000
19	A	1163	GLY	0	0.056	0.021	20.633	-0.040	-0.040	0.000	0.000	0.000	0.000
20	A	1164	ILE	0	-0.005	0.006	17.419	-0.043	-0.043	0.000	0.000	0.000	0.000
21	A	1165	SER	0	-0.044	-0.020	20.369	0.084	0.084	0.000	0.000	0.000	0.000
22	A	1166	ILE	0	0.022	0.013	19.362	-0.069	-0.069	0.000	0.000	0.000	0.000
23	A	1167	VAL	0	-0.006	-0.010	20.888	0.063	0.063	0.000	0.000	0.000	0.000
24	A	1168	GLY	0	0.039	0.028	21.413	-0.048	-0.048	0.000	0.000	0.000	0.000
25	A	1169	GLY	0	0.055	0.035	23.136	0.008	0.008	0.000	0.000	0.000	0.000
26	A	1170	ARG	1	0.772	0.848	24.343	0.385	0.385	0.000	0.000	0.000	0.000
27	A	1184	GLY	0	0.053	0.024	19.323	0.008	0.008	0.000	0.000	0.000	0.000
28	A	1185	ILE	0	-0.073	-0.028	19.236	0.023	0.023	0.000	0.000	0.000	0.000
29	A	1186	PHE	0	0.008	-0.009	15.203	-0.089	-0.089	0.000	0.000	0.000	0.000
30	A	1187	ILE	0	0.022	0.019	13.938	0.123	0.123	0.000	0.000	0.000	0.000
31	A	1188	LYS	1	0.884	0.952	17.146	0.549	0.549	0.000	0.000	0.000	0.000
32	A	1189	HIS	0	0.025	-0.014	19.301	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	1190	VAL	0	0.007	0.000	15.362	-0.013	-0.013	0.000	0.000	0.000	0.000
34	A	1191	LEU	0	-0.032	-0.004	18.764	0.036	0.036	0.000	0.000	0.000	0.000
35	A	1192	GLU	-1	-0.866	-0.916	19.123	-0.561	-0.561	0.000	0.000	0.000	0.000
36	A	1193	ASP	-1	-0.873	-0.936	20.860	-0.331	-0.331	0.000	0.000	0.000	0.000
37	A	1194	SER	0	-0.059	-0.045	20.731	0.005	0.005	0.000	0.000	0.000	0.000
38	A	1195	PRO	0	0.028	0.012	20.461	-0.031	-0.031	0.000	0.000	0.000	0.000
39	A	1196	ALA	0	-0.015	-0.007	16.775	-0.048	-0.048	0.000	0.000	0.000	0.000
40	A	1197	GLY	0	-0.016	0.007	15.814	-0.106	-0.106	0.000	0.000	0.000	0.000
41	A	1198	LYS	1	0.786	0.877	16.720	0.333	0.333	0.000	0.000	0.000	0.000
42	A	1199	ASN	0	-0.031	0.000	12.791	-0.158	-0.158	0.000	0.000	0.000	0.000
43	A	1200	GLY	0	0.047	0.038	13.226	-0.072	-0.072	0.000	0.000	0.000	0.000
44	A	1201	THR	0	-0.070	-0.034	8.445	-0.278	-0.278	0.000	0.000	0.000	0.000
45	A	1202	LEU	0	-0.008	0.015	9.480	-0.369	-0.369	0.000	0.000	0.000	0.000
46	A	1203	LYS	1	0.892	0.929	8.060	2.741	2.741	0.000	0.000	0.000	0.000
47	A	1204	PRO	0	0.000	-0.019	12.900	-0.016	-0.016	0.000	0.000	0.000	0.000
48	A	1205	GLY	0	-0.024	-0.008	13.330	-0.135	-0.135	0.000	0.000	0.000	0.000
49	A	1206	ASP	-1	-0.756	-0.839	10.238	-2.459	-2.459	0.000	0.000	0.000	0.000
50	A	1207	ARG	1	0.857	0.929	12.286	0.990	0.990	0.000	0.000	0.000	0.000
51	A	1208	ILE	0	-0.009	-0.001	13.323	-0.118	-0.118	0.000	0.000	0.000	0.000
52	A	1209	VAL	0	-0.025	-0.023	13.550	0.070	0.070	0.000	0.000	0.000	0.000
53	A	1210	GLU	-1	-0.806	-0.889	16.320	-0.469	-0.469	0.000	0.000	0.000	0.000
54	A	1211	VAL	0	-0.018	-0.015	17.772	-0.081	-0.081	0.000	0.000	0.000	0.000
55	A	1212	ASP	-1	-0.791	-0.898	20.196	-0.366	-0.366	0.000	0.000	0.000	0.000
56	A	1213	GLY	0	0.001	0.012	20.594	0.044	0.044	0.000	0.000	0.000	0.000
57	A	1214	MET	0	-0.049	-0.014	21.695	0.032	0.032	0.000	0.000	0.000	0.000
58	A	1215	ASP	-1	-0.802	-0.899	20.612	-0.542	-0.542	0.000	0.000	0.000	0.000
59	A	1216	LEU	0	-0.026	-0.030	19.751	0.030	0.030	0.000	0.000	0.000	0.000
60	A	1217	ARG	1	0.763	0.862	15.285	0.560	0.560	0.000	0.000	0.000	0.000
61	A	1218	ASP	-1	-0.866	-0.937	19.363	-0.543	-0.543	0.000	0.000	0.000	0.000
62	A	1219	ALA	0	-0.017	0.012	22.588	0.044	0.044	0.000	0.000	0.000	0.000
63	A	1220	SER	0	-0.008	-0.034	24.690	-0.020	-0.020	0.000	0.000	0.000	0.000
64	A	1221	HIS	0	-0.028	-0.025	24.705	0.001	0.001	0.000	0.000	0.000	0.000
65	A	1222	GLU	-1	-0.768	-0.854	26.520	-0.337	-0.337	0.000	0.000	0.000	0.000
66	A	1223	GLN	0	0.070	0.058	27.147	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	1224	ALA	0	0.050	0.034	22.939	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	1225	VAL	0	-0.021	-0.012	24.796	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	1226	GLU	-1	-0.896	-0.934	26.693	-0.249	-0.249	0.000	0.000	0.000	0.000
70	A	1227	ALA	0	0.032	0.013	24.913	0.010	0.010	0.000	0.000	0.000	0.000
71	A	1228	ILE	0	0.016	0.001	21.022	0.000	0.000	0.000	0.000	0.000	0.000
72	A	1229	ARG	1	0.869	0.933	24.361	0.335	0.335	0.000	0.000	0.000	0.000
73	A	1230	LYS	1	0.824	0.894	27.828	0.262	0.262	0.000	0.000	0.000	0.000
74	A	1231	ALA	0	0.005	0.034	23.743	0.017	0.017	0.000	0.000	0.000	0.000
75	A	1232	GLY	0	0.040	0.030	25.292	0.015	0.015	0.000	0.000	0.000	0.000
76	A	1233	ASN	0	-0.016	-0.003	24.496	-0.046	-0.046	0.000	0.000	0.000	0.000
77	A	1234	PRO	0	0.014	0.003	20.192	0.031	0.031	0.000	0.000	0.000	0.000
78	A	1235	VAL	0	-0.028	0.005	20.010	0.015	0.015	0.000	0.000	0.000	0.000
79	A	1236	VAL	0	-0.008	-0.017	17.260	-0.063	-0.063	0.000	0.000	0.000	0.000
80	A	1237	PHE	0	0.019	-0.001	15.023	0.031	0.031	0.000	0.000	0.000	0.000
81	A	1238	MET	0	-0.014	0.023	12.455	-0.052	-0.052	0.000	0.000	0.000	0.000
82	A	1239	VAL	0	-0.002	-0.014	10.665	0.081	0.081	0.000	0.000	0.000	0.000
83	A	1240	GLN	0	-0.040	-0.031	7.918	-0.099	-0.099	0.000	0.000	0.000	0.000
84	A	1241	SER	0	-0.027	-0.046	6.327	0.086	0.086	0.000	0.000	0.000	0.000
85	A	1242	ILE	0	-0.025	0.001	2.529	-1.337	-0.360	0.644	-0.360	-1.261	0.000
86	A	1243	ILE	0	0.021	0.014	5.961	0.578	0.578	0.000	0.000	0.000	0.000
87	A	1244	SER	0	0.017	0.008	7.636	-0.098	-0.098	0.000	0.000	0.000	0.000
88	A	1245	THR	0	-0.015	-0.025	9.499	0.116	0.116	0.000	0.000	0.000	0.000
89	A	1246	ARG	1	0.951	0.991	13.188	0.391	0.391	0.000	0.000	0.000	0.000
90	A	1247	LEU	0	0.051	0.031	15.773	0.028	0.028	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1145:GLN)