FMO DATABASE

FMODB ID: 4Q48N

Calculation Name: 2FS6-A-Xray547

Preferred Name: Complex of retinoic acid binding (CRABPII) and inhibitor of apoptosis (cIAP1) proteins

Target Type: PROTEIN COMPLEX

Ligand Name: acetate ion | chloride ion

Ligand 3-letter code: ACT | CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FS6

Chain ID: A

ChEMBL ID: CHEMBL2221342

UniProt ID: P29373

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	136
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1255633.542016
FMO2-HF: Nuclear repulsion	1200870.036701
FMO2-HF: Total energy	-54763.505315
FMO2-MP2: Total energy	-54921.38287

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:2:ASN)

Summations of interaction energy for fragment #1(A:2: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.
-133.922	-132.466	19.812	-10.576	-10.691	0.006

Interaction energy analysis for fragmet #1(A:2:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.881 / q_NPA : 0.938

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	4	SER	0	-0.005	0.004	1.861	-5.665	-7.500	13.439	-5.990	-5.615	0.043
4	A	5	GLY	0	0.014	0.008	3.707	-5.262	-5.181	0.017	0.073	-0.171	0.001
44	A	45	GLN	0	0.046	0.023	2.125	-19.325	-17.582	5.926	-4.013	-3.655	-0.032
45	A	46	GLU	-1	-0.869	-0.918	4.786	-25.182	-25.055	-0.001	-0.004	-0.121	0.000
112	A	113	LEU	0	-0.055	-0.018	2.829	-4.612	-3.680	0.431	-0.496	-0.867	-0.006
135	A	136	ARG	1	0.867	0.911	3.804	47.096	47.504	0.000	-0.146	-0.262	0.000
5	A	6	ASN	0	0.018	0.022	7.186	1.234	1.234	0.000	0.000	0.000	0.000
6	A	7	TRP	0	0.002	-0.002	6.331	-0.240	-0.240	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.806	0.885	12.125	18.929	18.929	0.000	0.000	0.000	0.000
8	A	9	ILE	0	-0.037	-0.005	15.865	-0.580	-0.580	0.000	0.000	0.000	0.000
9	A	10	ILE	0	0.018	0.003	15.926	1.114	1.114	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.912	0.961	18.612	15.031	15.031	0.000	0.000	0.000	0.000
11	A	12	SER	0	0.031	0.002	19.239	-0.784	-0.784	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.916	-0.944	21.646	-11.918	-11.918	0.000	0.000	0.000	0.000
13	A	14	ASN	0	0.037	-0.004	23.147	0.065	0.065	0.000	0.000	0.000	0.000
14	A	15	PHE	0	0.029	-0.001	23.162	0.099	0.099	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.770	-0.851	25.172	-9.358	-9.358	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.773	-0.876	28.764	-9.276	-9.276	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.019	0.020	22.778	0.183	0.183	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.005	-0.003	26.155	0.174	0.174	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.764	0.858	28.954	9.415	9.415	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.031	0.019	29.144	0.314	0.314	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.050	-0.013	26.446	0.139	0.139	0.000	0.000	0.000	0.000
22	A	23	GLY	0	0.013	0.020	31.116	0.123	0.123	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.031	-0.004	30.131	0.254	0.254	0.000	0.000	0.000	0.000
24	A	25	ASN	0	0.039	0.014	33.492	0.059	0.059	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.050	0.007	35.100	-0.213	-0.213	0.000	0.000	0.000	0.000
26	A	27	MET	0	0.029	0.022	35.478	-0.125	-0.125	0.000	0.000	0.000	0.000
27	A	28	LEU	0	0.022	0.001	32.626	-0.174	-0.174	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.832	0.916	30.918	8.897	8.897	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.846	0.895	30.686	8.911	8.911	0.000	0.000	0.000	0.000
30	A	31	ILE	0	0.016	0.012	30.492	-0.209	-0.209	0.000	0.000	0.000	0.000
31	A	32	ALA	0	0.017	0.009	27.298	-0.279	-0.279	0.000	0.000	0.000	0.000
32	A	33	VAL	0	-0.007	-0.014	26.512	-0.495	-0.495	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.005	0.009	26.941	-0.314	-0.314	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.001	0.018	26.323	-0.292	-0.292	0.000	0.000	0.000	0.000
35	A	36	ALA	0	0.007	0.001	22.441	-0.465	-0.465	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.022	-0.014	22.603	-0.682	-0.682	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.855	0.916	20.743	13.907	13.907	0.000	0.000	0.000	0.000
38	A	39	PRO	0	0.002	0.012	18.126	0.234	0.234	0.000	0.000	0.000	0.000
39	A	40	ALA	0	-0.006	0.000	16.583	-0.459	-0.459	0.000	0.000	0.000	0.000
40	A	41	VAL	0	-0.033	-0.019	11.360	0.486	0.486	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.829	-0.906	10.930	-19.170	-19.170	0.000	0.000	0.000	0.000
42	A	43	ILE	0	-0.022	-0.013	5.694	0.274	0.274	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.849	0.900	5.688	25.046	25.046	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.009	0.009	6.313	2.807	2.807	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.806	-0.895	6.214	-33.413	-33.413	0.000	0.000	0.000	0.000
48	A	49	THR	0	-0.013	-0.009	8.889	2.353	2.353	0.000	0.000	0.000	0.000
49	A	50	PHE	0	-0.024	-0.023	5.138	-3.618	-3.618	0.000	0.000	0.000	0.000
50	A	51	TYR	0	-0.041	-0.026	8.852	1.812	1.812	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.018	-0.021	9.263	-1.832	-1.832	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.915	0.970	11.531	17.583	17.583	0.000	0.000	0.000	0.000
53	A	54	THR	0	-0.023	-0.008	13.984	-0.919	-0.919	0.000	0.000	0.000	0.000
54	A	55	SER	0	-0.010	-0.001	16.484	0.991	0.991	0.000	0.000	0.000	0.000
55	A	56	THR	0	-0.034	-0.022	19.471	-0.031	-0.031	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.012	-0.010	22.555	0.082	0.082	0.000	0.000	0.000	0.000
57	A	58	VAL	0	-0.007	0.002	25.700	0.331	0.331	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.943	0.977	23.215	11.618	11.618	0.000	0.000	0.000	0.000
59	A	60	THR	0	0.050	0.030	18.850	-0.191	-0.191	0.000	0.000	0.000	0.000
60	A	61	THR	0	-0.048	-0.028	18.124	0.557	0.557	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.862	-0.916	16.326	-15.766	-15.766	0.000	0.000	0.000	0.000
62	A	63	ILE	0	-0.028	-0.003	13.844	0.617	0.617	0.000	0.000	0.000	0.000
63	A	64	ASN	0	0.002	-0.009	13.743	-1.611	-1.611	0.000	0.000	0.000	0.000
64	A	65	PHE	0	0.005	0.003	10.243	0.772	0.772	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.904	0.937	11.843	17.910	17.910	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.034	-0.005	9.495	1.364	1.364	0.000	0.000	0.000	0.000
67	A	68	GLY	0	-0.025	-0.009	12.543	0.376	0.376	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.881	-0.926	15.793	-16.221	-16.221	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.854	-0.918	17.223	-13.138	-13.138	0.000	0.000	0.000	0.000
70	A	71	PHE	0	-0.027	-0.010	16.286	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.929	-0.969	19.770	-11.261	-11.261	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.758	-0.846	17.777	-17.105	-17.105	0.000	0.000	0.000	0.000
73	A	74	GLN	0	-0.097	-0.060	21.191	0.530	0.530	0.000	0.000	0.000	0.000
74	A	75	THR	0	0.013	-0.014	21.872	-0.533	-0.533	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.011	0.001	22.271	0.131	0.131	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.797	-0.869	23.688	-10.951	-10.951	0.000	0.000	0.000	0.000
77	A	78	GLY	0	-0.026	-0.008	26.087	0.413	0.413	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.860	0.926	27.144	10.799	10.799	0.000	0.000	0.000	0.000
79	A	80	PRO	0	0.005	0.003	26.008	-0.365	-0.365	0.000	0.000	0.000	0.000
80	A	81	CYS	0	-0.018	-0.004	22.395	0.398	0.398	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.867	0.933	22.998	11.822	11.822	0.000	0.000	0.000	0.000
82	A	83	SER	0	-0.047	-0.058	18.670	0.479	0.479	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.028	0.018	17.575	-0.030	-0.030	0.000	0.000	0.000	0.000
84	A	85	VAL	0	0.035	0.015	11.474	0.099	0.099	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.851	0.906	13.741	17.189	17.189	0.000	0.000	0.000	0.000
86	A	87	TRP	0	0.005	-0.009	5.341	-2.030	-2.030	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.889	-0.922	11.417	-17.999	-17.999	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.014	-0.023	10.917	0.582	0.582	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.909	-0.948	5.478	-47.238	-47.238	0.000	0.000	0.000	0.000
90	A	91	ASN	0	-0.025	-0.004	5.112	-12.158	-12.158	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.866	0.922	6.197	20.610	20.610	0.000	0.000	0.000	0.000
92	A	93	MET	0	-0.023	0.012	7.287	3.090	3.090	0.000	0.000	0.000	0.000
93	A	94	VAL	0	0.012	-0.010	10.152	1.014	1.014	0.000	0.000	0.000	0.000
94	A	95	CYS	0	-0.052	-0.013	13.938	0.265	0.265	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.804	-0.896	16.266	-14.536	-14.536	0.000	0.000	0.000	0.000
96	A	97	GLN	0	0.016	-0.002	19.889	0.319	0.319	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.920	0.947	22.278	10.981	10.981	0.000	0.000	0.000	0.000
98	A	99	LEU	0	0.014	0.021	25.968	-0.135	-0.135	0.000	0.000	0.000	0.000
99	A	100	LEU	0	-0.026	-0.004	26.312	0.242	0.242	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.918	0.955	29.512	9.438	9.438	0.000	0.000	0.000	0.000
101	A	102	GLY	0	-0.002	-0.001	32.604	-0.106	-0.106	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.931	-0.964	32.837	-8.869	-8.869	0.000	0.000	0.000	0.000
103	A	104	GLY	0	-0.033	-0.033	31.967	0.129	0.129	0.000	0.000	0.000	0.000
104	A	105	PRO	0	-0.010	0.007	29.158	-0.075	-0.075	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.860	0.940	22.123	13.045	13.045	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.021	-0.030	23.005	0.050	0.050	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.013	-0.011	19.047	0.191	0.191	0.000	0.000	0.000	0.000
108	A	109	TRP	0	-0.040	-0.024	11.739	-0.441	-0.441	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.039	-0.022	13.377	-0.647	-0.647	0.000	0.000	0.000	0.000
110	A	111	ARG	1	0.917	0.953	9.143	23.358	23.358	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.898	-0.953	8.090	-27.599	-27.599	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.018	-0.052	6.577	-1.079	-1.079	0.000	0.000	0.000	0.000
114	A	115	ASN	0	-0.007	-0.013	7.523	-4.875	-4.875	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.929	-0.955	9.266	-23.889	-23.889	0.000	0.000	0.000	0.000
116	A	117	GLY	0	-0.043	-0.014	7.256	0.685	0.685	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.898	-0.921	8.331	-22.911	-22.911	0.000	0.000	0.000	0.000
118	A	119	LEU	0	-0.026	-0.005	8.028	-3.055	-3.055	0.000	0.000	0.000	0.000
119	A	120	ILE	0	0.007	-0.004	9.806	3.443	3.443	0.000	0.000	0.000	0.000
120	A	121	LEU	0	-0.018	-0.004	11.432	-1.346	-1.346	0.000	0.000	0.000	0.000
121	A	122	THR	0	0.010	0.007	13.861	0.988	0.988	0.000	0.000	0.000	0.000
122	A	123	MET	0	-0.022	-0.016	16.668	-0.415	-0.415	0.000	0.000	0.000	0.000
123	A	124	THR	0	0.013	0.009	19.488	0.392	0.392	0.000	0.000	0.000	0.000
124	A	125	ALA	0	-0.011	-0.021	22.490	-0.039	-0.039	0.000	0.000	0.000	0.000
125	A	126	ASP	-1	-0.833	-0.917	26.089	-10.100	-10.100	0.000	0.000	0.000	0.000
126	A	127	ASP	-1	-0.916	-0.953	26.473	-10.562	-10.562	0.000	0.000	0.000	0.000
127	A	128	VAL	0	-0.034	-0.004	26.594	-0.181	-0.181	0.000	0.000	0.000	0.000
128	A	129	VAL	0	0.026	0.009	20.904	-0.395	-0.395	0.000	0.000	0.000	0.000
129	A	130	CYS	0	-0.114	-0.032	21.782	0.286	0.286	0.000	0.000	0.000	0.000
130	A	131	THR	0	0.043	0.012	17.003	-0.879	-0.879	0.000	0.000	0.000	0.000
131	A	132	ARG	1	0.793	0.885	17.071	16.025	16.025	0.000	0.000	0.000	0.000
132	A	133	VAL	0	0.045	0.027	13.753	-1.033	-1.033	0.000	0.000	0.000	0.000
133	A	134	TYR	0	-0.008	-0.008	12.666	2.352	2.352	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.051	0.033	12.033	-1.729	-1.729	0.000	0.000	0.000	0.000
136	A	137	GLU	-2	-1.766	-1.855	11.352	-38.031	-38.031	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:2:ASN)