FMO DATABASE

FMODB ID: 14L8Z

Calculation Name: 4S03-A-Xray372

Preferred Name:

Target Type:

Ligand Name: (r)-2-amino-3-(4-phenylcyclohexyl)propanoic acid

ligand 3-letter code: BIF

PDB ID: 4S03

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UZ14

Base Structure: X-ray

Registration Date: 2023-06-19

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1341664.353929
FMO2-HF: Nuclear repulsion	1285756.388916
FMO2-HF: Total energy	-55907.965013
FMO2-MP2: Total energy	-56071.450855

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: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.
-34.878	-29.419	45.814	-18.951	-32.325	-0.125

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 : 0 / q_Mulliken : -0.042 / q_NPA : -0.030

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	VAL	0	0.016	-0.009	2.269	-1.097	0.469	3.101	-1.365	-3.301	-0.002
4	A	4	LEU	0	-0.008	0.002	4.509	-0.250	-0.174	-0.001	-0.024	-0.051	0.000
5	A	5	LEU	0	-0.023	-0.006	7.710	0.167	0.167	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.030	0.003	10.599	-0.125	-0.125	0.000	0.000	0.000	0.000
7	A	7	HIS	0	0.015	0.022	14.137	0.020	0.020	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.022	0.000	17.099	-0.050	-0.050	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.800	-0.871	19.488	0.196	0.196	0.000	0.000	0.000	0.000
10	A	10	TYR	0	-0.019	-0.013	21.710	-0.008	-0.008	0.000	0.000	0.000	0.000
11	A	11	BIF	0	0.047	0.003	14.893	-0.016	-0.016	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.829	-0.900	19.490	0.072	0.072	0.000	0.000	0.000	0.000
13	A	13	TYR	0	-0.069	-0.038	17.037	-0.010	-0.010	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.811	-0.889	19.788	-0.013	-0.013	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.009	-0.009	18.509	-0.016	-0.016	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.805	0.895	20.893	0.068	0.068	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.860	-0.926	22.158	-0.142	-0.142	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.853	0.919	20.012	0.181	0.181	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.037	0.019	16.818	0.002	0.002	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.015	0.002	14.116	-0.033	-0.033	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.944	0.959	18.695	0.261	0.261	0.000	0.000	0.000	0.000
22	A	22	ASN	0	-0.027	-0.027	20.064	0.034	0.034	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.014	0.039	16.798	-0.037	-0.037	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.757	-0.853	13.416	-0.122	-0.122	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.021	0.003	16.641	0.014	0.014	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.007	-0.011	18.295	0.011	0.011	0.000	0.000	0.000	0.000
27	A	27	SER	0	0.006	-0.026	20.851	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.833	-0.924	23.670	-0.044	-0.044	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.849	-0.898	23.135	0.025	0.025	0.000	0.000	0.000	0.000
30	A	30	MET	0	0.032	0.022	17.158	0.003	0.003	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.814	0.916	19.580	0.043	0.043	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.862	0.915	21.278	-0.028	-0.028	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.040	0.034	19.736	0.006	0.006	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.737	0.839	20.713	-0.124	-0.124	0.000	0.000	0.000	0.000
35	A	35	MET	0	-0.050	-0.001	17.122	0.017	0.017	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.792	-0.897	20.608	0.131	0.131	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.795	-0.885	21.710	0.266	0.266	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.047	-0.011	16.068	0.033	0.033	0.000	0.000	0.000	0.000
39	A	39	LEU	0	0.021	0.014	11.903	-0.020	-0.020	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.010	-0.009	12.526	0.073	0.073	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.020	0.004	7.802	0.077	0.077	0.000	0.000	0.000	0.000
42	A	42	PHE	0	0.003	0.010	8.272	0.027	0.027	0.000	0.000	0.000	0.000
43	A	43	ILE	0	0.004	-0.012	2.378	-0.990	-0.535	2.333	-0.473	-2.315	-0.002
44	A	44	SER	0	-0.031	-0.021	4.205	-0.662	-0.320	-0.001	-0.058	-0.284	0.000
45	A	45	VAL	0	-0.001	0.002	2.344	-4.618	-2.164	3.829	-2.450	-3.834	-0.020
46	A	46	GLU	-1	-0.738	-0.814	1.956	-11.149	-12.409	10.771	-4.678	-4.832	-0.030
47	A	47	LYS	1	0.839	0.926	3.930	0.977	1.107	0.002	-0.009	-0.123	0.000
48	A	48	VAL	0	-0.017	-0.026	3.145	0.287	0.600	0.032	-0.077	-0.268	0.000
49	A	49	ASP	-1	-0.703	-0.869	1.859	-16.609	-17.891	12.967	-5.949	-5.736	-0.069
50	A	50	GLU	-1	-0.814	-0.901	4.646	-0.327	-0.271	-0.001	-0.027	-0.028	0.000
51	A	51	LYS	1	0.902	0.968	7.367	0.900	0.900	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.010	-0.007	7.940	0.262	0.262	0.000	0.000	0.000	0.000
53	A	53	PRO	0	0.091	0.045	5.891	0.115	0.115	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.852	-0.891	5.933	0.201	0.201	0.000	0.000	0.000	0.000
55	A	55	GLH	0	0.052	0.040	7.635	0.117	0.117	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.002	0.002	2.294	0.125	-0.427	3.607	-0.611	-2.443	0.001
57	A	57	SER	0	0.028	-0.016	3.441	0.946	1.517	0.018	-0.143	-0.446	-0.001
58	A	58	LEU	0	0.013	0.007	4.364	0.523	0.597	-0.001	-0.002	-0.072	0.000
59	A	59	LYS	1	0.844	0.915	6.397	-1.812	-1.812	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.032	0.004	2.874	-0.507	-0.496	2.263	-0.725	-1.549	0.000
61	A	61	ILE	0	-0.005	0.010	4.832	-0.780	-0.652	0.002	-0.059	-0.070	0.000
62	A	62	GLU	-1	-0.814	-0.852	7.613	0.855	0.855	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.831	-0.911	7.307	1.212	1.212	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.025	-0.007	5.606	-0.316	-0.255	-0.001	-0.004	-0.056	0.000
65	A	65	SER	0	-0.017	-0.024	9.340	-0.345	-0.345	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.853	0.907	12.232	-1.282	-1.282	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.005	0.002	12.172	-0.139	-0.139	0.000	0.000	0.000	0.000
68	A	68	ALA	0	0.022	0.020	13.656	-0.125	-0.125	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.899	-0.960	15.487	0.627	0.627	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.081	-0.041	17.254	-0.038	-0.038	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.048	-0.035	17.093	-0.066	-0.066	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.837	0.921	19.313	-0.425	-0.425	0.000	0.000	0.000	0.000
73	A	73	ALA	0	-0.017	0.017	16.864	-0.038	-0.038	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.882	-0.949	17.882	0.342	0.342	0.000	0.000	0.000	0.000
75	A	75	ASN	0	-0.050	-0.010	17.917	-0.009	-0.009	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.028	0.010	11.388	0.051	0.051	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.021	-0.005	13.032	-0.086	-0.086	0.000	0.000	0.000	0.000
78	A	78	VAL	0	0.011	0.011	6.882	0.086	0.086	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.008	-0.005	8.824	-0.244	-0.244	0.000	0.000	0.000	0.000
80	A	80	PRO	0	0.003	-0.007	7.310	0.021	0.021	0.000	0.000	0.000	0.000
81	A	81	TRP	0	0.019	0.002	7.442	0.026	0.026	0.000	0.000	0.000	0.000
82	A	82	ALA	0	-0.007	0.018	7.675	-0.235	-0.235	0.000	0.000	0.000	0.000
83	A	83	HIS	0	-0.015	-0.014	9.337	-0.056	-0.056	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.000	0.006	6.019	0.152	0.152	0.000	0.000	0.000	0.000
85	A	85	SER	0	-0.048	-0.064	5.361	-0.026	-0.026	0.000	0.000	0.000	0.000
86	A	86	SER	0	0.006	0.009	7.486	0.218	0.218	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.893	-0.950	7.312	-1.161	-1.161	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.010	0.013	5.831	-0.681	-0.681	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.044	-0.012	6.548	0.297	0.297	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.881	0.928	8.175	1.076	1.076	0.000	0.000	0.000	0.000
91	A	91	PRO	0	0.040	-0.001	10.551	-0.067	-0.067	0.000	0.000	0.000	0.000
92	A	92	SER	0	0.010	0.010	10.696	-0.037	-0.037	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.037	0.015	6.804	0.085	0.085	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.007	0.009	6.059	-0.132	-0.132	0.000	0.000	0.000	0.000
95	A	95	MET	0	0.006	-0.005	6.333	0.085	0.085	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.836	-0.893	8.868	-0.255	-0.255	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.005	0.001	2.402	0.180	-0.621	2.896	-0.420	-1.676	-0.002
98	A	98	LEU	0	0.000	-0.002	4.488	0.167	0.344	-0.001	-0.009	-0.167	0.000
99	A	99	ASN	0	0.006	0.012	5.933	0.339	0.339	0.000	0.000	0.000	0.000
100	A	100	ARG	1	0.791	0.865	6.480	0.315	0.315	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.007	-0.006	3.134	-0.202	0.132	0.034	-0.074	-0.294	0.000
102	A	102	TYR	0	0.010	0.006	6.439	0.083	0.083	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.001	-0.017	9.709	0.030	0.030	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.043	0.015	9.975	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.009	-0.013	8.526	0.044	0.044	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.867	0.937	11.657	-0.316	-0.316	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-1.002	-0.986	13.901	0.430	0.430	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.850	0.903	12.144	-0.897	-0.897	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.012	0.023	15.424	-0.015	-0.015	0.000	0.000	0.000	0.000
110	A	110	PHE	0	-0.052	-0.011	13.933	-0.014	-0.014	0.000	0.000	0.000	0.000
111	A	111	ASN	0	0.008	0.001	17.084	-0.038	-0.038	0.000	0.000	0.000	0.000
112	A	112	VAL	0	-0.020	-0.022	11.963	0.053	0.053	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.022	0.022	14.817	-0.071	-0.071	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.796	0.868	11.013	0.117	0.117	0.000	0.000	0.000	0.000
115	A	115	ALA	0	0.041	0.037	12.001	-0.043	-0.043	0.000	0.000	0.000	0.000
116	A	116	PRO	0	-0.044	-0.011	12.407	-0.015	-0.015	0.000	0.000	0.000	0.000
117	A	117	PHE	0	0.036	-0.006	8.406	-0.028	-0.028	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.024	-0.008	12.615	0.017	0.017	0.000	0.000	0.000	0.000
119	A	119	TYR	0	-0.059	-0.045	14.956	0.016	0.016	0.000	0.000	0.000	0.000
120	A	120	TYR	0	0.032	0.023	16.220	-0.035	-0.035	0.000	0.000	0.000	0.000
121	A	121	ILE	0	-0.034	-0.027	15.033	0.024	0.024	0.000	0.000	0.000	0.000
122	A	122	ALA	0	-0.005	0.019	18.840	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	123	ALA	0	0.008	-0.009	18.348	0.013	0.013	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.825	0.911	20.425	-0.057	-0.057	0.000	0.000	0.000	0.000
125	A	125	ILE	0	0.004	-0.002	16.478	0.020	0.020	0.000	0.000	0.000	0.000
126	A	126	SER	0	-0.043	-0.029	20.656	-0.030	-0.030	0.000	0.000	0.000	0.000
127	A	127	CYS	0	-0.025	-0.007	17.931	0.028	0.028	0.000	0.000	0.000	0.000
128	A	128	LYS	1	0.782	0.870	20.154	-0.263	-0.263	0.000	0.000	0.000	0.000
129	A	129	GLY	0	0.026	0.010	21.104	0.007	0.007	0.000	0.000	0.000	0.000
130	A	130	HIS	0	-0.047	-0.031	19.527	-0.027	-0.027	0.000	0.000	0.000	0.000
131	A	131	PRO	0	0.012	-0.019	20.739	0.014	0.014	0.000	0.000	0.000	0.000
132	A	132	LEU	0	-0.029	-0.008	17.692	0.012	0.012	0.000	0.000	0.000	0.000
133	A	133	ALA	0	-0.022	0.012	16.768	0.068	0.068	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.835	-0.920	14.606	0.198	0.198	0.000	0.000	0.000	0.000
135	A	135	LEU	0	-0.037	-0.013	12.331	-0.018	-0.018	0.000	0.000	0.000	0.000
136	A	136	SER	0	0.026	0.016	9.023	0.035	0.035	0.000	0.000	0.000	0.000
137	A	137	ARG	1	0.885	0.936	6.348	-0.963	-0.963	0.000	0.000	0.000	0.000
138	A	138	THR	0	-0.024	-0.020	4.269	-1.271	-1.039	-0.001	-0.075	-0.157	0.000
139	A	139	ILE	0	-0.057	-0.012	2.116	-2.719	-0.961	2.174	-0.982	-2.951	0.004
140	A	140	VAL	0	0.038	0.018	2.999	4.792	5.253	1.792	-0.716	-1.537	-0.004
141	A	141	PRO	0	-0.097	-0.052	3.924	-0.798	-0.643	0.000	-0.021	-0.135	0.000

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