FMO DATABASE

FMODB ID: NZLLQ

Calculation Name: 1B7F-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1B7F

Chain ID: A

ChEMBL ID:

UniProt ID: P19339

Base Structure: X-ray

Registration Date: 2025-09-02

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	167
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1604616.912816
FMO2-HF: Nuclear repulsion	1538780.270133
FMO2-HF: Total energy	-65836.642683
FMO2-MP2: Total energy	-66029.856664

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:123:SER)

Summations of interaction energy for fragment #1(A:123:SER)

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.
36.987	42.21	2.71	-3.298	-4.633	-0.024

Interaction energy analysis for fragmet #1(A:123:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.833 / q_NPA : 0.901

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	125	THR	0	0.028	0.007	3.845	1.133	2.570	-0.019	-0.639	-0.779	-0.001
5	A	127	LEU	0	0.000	0.015	4.690	-7.993	-7.867	-0.001	-0.006	-0.118	0.000
78	A	200	TYR	0	0.041	0.013	2.132	-6.769	-4.056	2.721	-2.305	-3.129	-0.021
79	A	201	ALA	0	-0.045	-0.014	4.227	3.455	3.530	-0.001	-0.022	-0.052	0.000
80	A	202	ARG	1	0.881	0.947	3.586	14.790	15.531	0.010	-0.307	-0.443	-0.002
81	A	203	PRO	0	0.008	-0.004	3.854	2.807	2.938	0.000	-0.019	-0.112	0.000
4	A	126	ASN	0	0.015	0.018	5.699	5.469	5.469	0.000	0.000	0.000	0.000
6	A	128	ILE	0	-0.042	-0.020	7.129	2.979	2.979	0.000	0.000	0.000	0.000
7	A	129	VAL	0	0.008	0.005	9.330	-0.215	-0.215	0.000	0.000	0.000	0.000
8	A	130	ASN	0	-0.005	-0.029	12.119	2.195	2.195	0.000	0.000	0.000	0.000
9	A	131	TYR	0	-0.005	-0.005	14.880	0.164	0.164	0.000	0.000	0.000	0.000
10	A	132	LEU	0	0.062	0.029	17.123	0.479	0.479	0.000	0.000	0.000	0.000
11	A	133	PRO	0	-0.048	-0.021	20.019	0.294	0.294	0.000	0.000	0.000	0.000
12	A	134	GLN	0	0.009	-0.016	23.499	-0.091	-0.091	0.000	0.000	0.000	0.000
13	A	135	ASP	-1	-0.833	-0.888	25.588	-11.324	-11.324	0.000	0.000	0.000	0.000
14	A	136	MET	0	-0.019	0.015	20.491	-0.210	-0.210	0.000	0.000	0.000	0.000
15	A	137	THR	0	0.006	0.000	23.761	-0.183	-0.183	0.000	0.000	0.000	0.000
16	A	138	ASP	0	-0.110	-0.179	19.454	-0.115	-0.115	0.000	0.000	0.000	0.000
17	A	139	ARG	1	0.991	0.995	21.459	10.451	10.451	0.000	0.000	0.000	0.000
18	A	140	GLU	-1	-0.792	-0.863	22.915	-12.204	-12.204	0.000	0.000	0.000	0.000
19	A	141	LEU	0	0.016	0.002	15.758	-0.237	-0.237	0.000	0.000	0.000	0.000
20	A	142	TYR	0	0.063	0.011	18.164	-0.451	-0.451	0.000	0.000	0.000	0.000
21	A	143	ALA	0	0.000	-0.007	19.272	-0.383	-0.383	0.000	0.000	0.000	0.000
22	A	144	LEU	0	-0.026	-0.009	18.422	-0.090	-0.090	0.000	0.000	0.000	0.000
23	A	145	PHE	0	0.034	0.007	12.180	-0.459	-0.459	0.000	0.000	0.000	0.000
24	A	146	ARG	1	0.911	0.965	16.428	14.778	14.778	0.000	0.000	0.000	0.000
25	A	147	ALA	0	0.000	0.009	18.709	0.153	0.153	0.000	0.000	0.000	0.000
26	A	148	ILE	0	-0.102	-0.041	13.689	0.267	0.267	0.000	0.000	0.000	0.000
27	A	149	GLY	0	0.059	0.027	15.681	0.035	0.035	0.000	0.000	0.000	0.000
28	A	150	PRO	0	-0.039	-0.021	16.041	0.441	0.441	0.000	0.000	0.000	0.000
29	A	151	ILE	0	-0.011	0.010	14.488	-1.386	-1.386	0.000	0.000	0.000	0.000
30	A	152	ASN	0	-0.035	-0.011	13.233	2.249	2.249	0.000	0.000	0.000	0.000
31	A	153	THR	0	-0.008	-0.013	13.230	1.224	1.224	0.000	0.000	0.000	0.000
32	A	154	CYS	-1	-0.750	-0.753	13.953	-18.025	-18.025	0.000	0.000	0.000	0.000
33	A	155	ARG	1	0.958	0.972	15.280	18.745	18.745	0.000	0.000	0.000	0.000
34	A	156	ILE	0	0.011	-0.008	15.992	-0.842	-0.842	0.000	0.000	0.000	0.000
35	A	157	MET	0	-0.047	-0.003	15.332	0.419	0.419	0.000	0.000	0.000	0.000
36	A	158	ARG	1	0.901	0.941	18.626	12.833	12.833	0.000	0.000	0.000	0.000
37	A	159	ASP	-1	-0.806	-0.886	22.405	-11.669	-11.669	0.000	0.000	0.000	0.000
38	A	160	TYR	0	0.003	0.005	25.093	0.469	0.469	0.000	0.000	0.000	0.000
39	A	161	LYS	1	0.893	0.953	26.732	10.835	10.835	0.000	0.000	0.000	0.000
40	A	162	THR	0	0.024	-0.014	28.778	0.127	0.127	0.000	0.000	0.000	0.000
41	A	163	GLY	0	0.029	0.030	26.923	0.168	0.168	0.000	0.000	0.000	0.000
42	A	164	TYR	0	0.030	0.024	25.365	-0.345	-0.345	0.000	0.000	0.000	0.000
43	A	165	SER	0	-0.039	-0.020	20.988	-0.484	-0.484	0.000	0.000	0.000	0.000
44	A	166	TYR	0	0.002	-0.011	19.597	0.366	0.366	0.000	0.000	0.000	0.000
45	A	167	GLY	0	0.012	0.010	19.958	-0.301	-0.301	0.000	0.000	0.000	0.000
46	A	168	TYR	0	-0.061	-0.033	13.751	-0.648	-0.648	0.000	0.000	0.000	0.000
47	A	169	ALA	0	0.007	0.002	14.497	0.896	0.896	0.000	0.000	0.000	0.000
48	A	170	PHE	0	-0.011	-0.011	9.473	-1.218	-1.218	0.000	0.000	0.000	0.000
49	A	171	VAL	0	0.002	-0.002	10.421	2.211	2.211	0.000	0.000	0.000	0.000
50	A	172	ASP	-1	-0.840	-0.899	9.138	-34.877	-34.877	0.000	0.000	0.000	0.000
51	A	173	PHE	0	-0.001	-0.006	9.531	2.750	2.750	0.000	0.000	0.000	0.000
52	A	174	THR	0	-0.006	-0.024	11.325	-0.806	-0.806	0.000	0.000	0.000	0.000
53	A	175	SER	0	-0.008	0.005	11.981	-0.884	-0.884	0.000	0.000	0.000	0.000
54	A	176	GLU	-1	-0.900	-0.957	6.544	-38.400	-38.400	0.000	0.000	0.000	0.000
55	A	177	MET	0	0.012	-0.002	8.251	-1.970	-1.970	0.000	0.000	0.000	0.000
56	A	178	ASP	-1	-0.839	-0.929	10.930	-20.515	-20.515	0.000	0.000	0.000	0.000
57	A	179	SER	0	-0.013	-0.012	5.787	1.341	1.341	0.000	0.000	0.000	0.000
58	A	180	GLN	0	0.042	0.013	7.379	2.663	2.663	0.000	0.000	0.000	0.000
59	A	181	ARG	1	0.919	0.959	8.181	19.026	19.026	0.000	0.000	0.000	0.000
60	A	182	ALA	0	0.039	0.019	10.804	1.476	1.476	0.000	0.000	0.000	0.000
61	A	183	ILE	0	-0.036	-0.017	5.851	1.349	1.349	0.000	0.000	0.000	0.000
62	A	184	LYS	1	0.871	0.927	10.247	23.430	23.430	0.000	0.000	0.000	0.000
63	A	185	VAL	0	-0.026	0.004	12.752	1.333	1.333	0.000	0.000	0.000	0.000
64	A	186	LEU	0	0.019	-0.003	14.329	0.985	0.985	0.000	0.000	0.000	0.000
65	A	187	ASN	0	-0.002	0.003	12.409	0.639	0.639	0.000	0.000	0.000	0.000
66	A	188	GLY	0	-0.004	0.004	14.503	0.697	0.697	0.000	0.000	0.000	0.000
67	A	189	ILE	0	-0.015	0.012	17.834	1.035	1.035	0.000	0.000	0.000	0.000
68	A	190	THR	0	-0.018	-0.019	20.059	-0.093	-0.093	0.000	0.000	0.000	0.000
69	A	191	VAL	0	0.010	0.004	21.056	0.207	0.207	0.000	0.000	0.000	0.000
70	A	192	ARG	1	0.747	0.811	23.861	11.563	11.563	0.000	0.000	0.000	0.000
71	A	193	ASN	0	0.030	0.017	26.712	-0.134	-0.134	0.000	0.000	0.000	0.000
72	A	194	LYS	1	0.874	0.953	21.686	12.914	12.914	0.000	0.000	0.000	0.000
73	A	195	ARG	1	0.981	0.988	20.697	13.401	13.401	0.000	0.000	0.000	0.000
74	A	196	LEU	0	0.011	0.015	16.204	-0.279	-0.279	0.000	0.000	0.000	0.000
75	A	197	LYS	1	0.934	0.975	11.527	22.904	22.904	0.000	0.000	0.000	0.000
76	A	198	VAL	0	-0.006	0.008	9.923	-0.611	-0.611	0.000	0.000	0.000	0.000
77	A	199	SER	0	-0.014	-0.009	7.622	0.652	0.652	0.000	0.000	0.000	0.000
82	A	204	GLY	0	0.027	0.021	6.585	2.326	2.326	0.000	0.000	0.000	0.000
83	A	205	GLY	0	0.038	0.012	10.166	0.001	0.001	0.000	0.000	0.000	0.000
84	A	206	GLU	-1	-0.866	-0.946	13.605	-15.163	-15.163	0.000	0.000	0.000	0.000
85	A	207	SER	0	0.049	0.033	11.806	0.925	0.925	0.000	0.000	0.000	0.000
86	A	208	ILE	0	-0.003	0.010	9.412	-0.070	-0.070	0.000	0.000	0.000	0.000
87	A	209	LYS	1	0.851	0.927	13.246	15.521	15.521	0.000	0.000	0.000	0.000
88	A	210	ASP	-1	-0.831	-0.918	16.976	-14.573	-14.573	0.000	0.000	0.000	0.000
89	A	211	THR	0	0.024	0.010	14.044	0.526	0.526	0.000	0.000	0.000	0.000
90	A	212	ASN	0	-0.118	-0.052	17.275	-0.809	-0.809	0.000	0.000	0.000	0.000
91	A	213	LEU	0	0.066	0.036	19.459	0.620	0.620	0.000	0.000	0.000	0.000
92	A	214	TYR	0	-0.027	-0.020	22.417	0.031	0.031	0.000	0.000	0.000	0.000
93	A	215	VAL	0	0.010	0.006	24.165	0.241	0.241	0.000	0.000	0.000	0.000
94	A	216	THR	0	-0.043	-0.038	26.921	0.061	0.061	0.000	0.000	0.000	0.000
95	A	217	ASN	0	-0.007	-0.001	30.464	-0.083	-0.083	0.000	0.000	0.000	0.000
96	A	218	LEU	0	0.027	0.035	26.408	0.097	0.097	0.000	0.000	0.000	0.000
97	A	219	PRO	0	0.068	0.030	30.146	0.283	0.283	0.000	0.000	0.000	0.000
98	A	220	ARG	1	0.903	0.942	31.564	8.555	8.555	0.000	0.000	0.000	0.000
99	A	221	THR	0	0.024	0.004	32.545	0.016	0.016	0.000	0.000	0.000	0.000
100	A	222	ILE	0	-0.045	0.007	26.215	-0.145	-0.145	0.000	0.000	0.000	0.000
101	A	223	THR	0	0.034	-0.001	25.783	-0.102	-0.102	0.000	0.000	0.000	0.000
102	A	224	ASP	-1	-0.825	-0.935	20.314	-13.946	-13.946	0.000	0.000	0.000	0.000
103	A	225	ASP	-1	-0.843	-0.913	21.188	-13.500	-13.500	0.000	0.000	0.000	0.000
104	A	226	GLN	0	-0.037	-0.008	22.388	0.086	0.086	0.000	0.000	0.000	0.000
105	A	227	LEU	0	-0.029	-0.012	21.124	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	228	ASP	-1	-0.837	-0.917	17.084	-16.413	-16.413	0.000	0.000	0.000	0.000
107	A	229	THR	0	-0.035	-0.028	19.452	-0.228	-0.228	0.000	0.000	0.000	0.000
108	A	230	ILE	0	-0.051	-0.022	22.211	0.078	0.078	0.000	0.000	0.000	0.000
109	A	231	PHE	0	0.024	-0.007	19.792	0.124	0.124	0.000	0.000	0.000	0.000
110	A	232	GLY	0	0.049	0.030	16.992	-0.484	-0.484	0.000	0.000	0.000	0.000
111	A	233	LYS	1	0.894	0.960	17.212	12.062	12.062	0.000	0.000	0.000	0.000
112	A	234	TYR	0	-0.012	-0.009	19.381	0.306	0.306	0.000	0.000	0.000	0.000
113	A	235	GLY	0	0.036	0.008	15.422	-0.178	-0.178	0.000	0.000	0.000	0.000
114	A	236	SER	0	-0.024	-0.015	10.153	-0.153	-0.153	0.000	0.000	0.000	0.000
115	A	237	ILE	0	-0.017	-0.003	12.536	-0.427	-0.427	0.000	0.000	0.000	0.000
116	A	238	VAL	0	-0.041	-0.007	9.529	-1.499	-1.499	0.000	0.000	0.000	0.000
117	A	239	GLN	0	-0.112	-0.082	11.600	-0.399	-0.399	0.000	0.000	0.000	0.000
118	A	240	LYS	1	0.878	0.942	14.827	16.189	16.189	0.000	0.000	0.000	0.000
119	A	241	ASN	0	-0.046	-0.028	18.379	0.041	0.041	0.000	0.000	0.000	0.000
120	A	242	ILE	0	0.051	0.044	21.656	0.368	0.368	0.000	0.000	0.000	0.000
121	A	243	LEU	0	-0.037	-0.016	24.934	0.159	0.159	0.000	0.000	0.000	0.000
122	A	244	ARG	1	0.949	0.978	24.742	11.596	11.596	0.000	0.000	0.000	0.000
123	A	245	ASP	-1	-0.846	-0.915	30.181	-8.489	-8.489	0.000	0.000	0.000	0.000
124	A	246	LYS	1	0.926	0.955	32.933	9.048	9.048	0.000	0.000	0.000	0.000
125	A	247	LEU	0	0.023	0.027	34.453	-0.016	-0.016	0.000	0.000	0.000	0.000
126	A	248	THR	0	-0.047	-0.044	36.389	0.086	0.086	0.000	0.000	0.000	0.000
127	A	249	GLY	0	0.023	0.020	32.183	-0.023	-0.023	0.000	0.000	0.000	0.000
128	A	250	ARG	1	0.948	0.962	31.306	8.071	8.071	0.000	0.000	0.000	0.000
129	A	251	PRO	0	0.021	0.020	29.272	-0.034	-0.034	0.000	0.000	0.000	0.000
130	A	252	ARG	1	0.934	0.951	30.903	9.721	9.721	0.000	0.000	0.000	0.000
131	A	253	GLY	0	0.005	0.006	31.364	0.219	0.219	0.000	0.000	0.000	0.000
132	A	254	VAL	0	-0.048	-0.017	27.930	0.001	0.001	0.000	0.000	0.000	0.000
133	A	255	ALA	0	-0.002	-0.007	23.704	-0.082	-0.082	0.000	0.000	0.000	0.000
134	A	256	PHE	0	-0.024	0.006	21.292	0.236	0.236	0.000	0.000	0.000	0.000
135	A	257	VAL	0	0.016	0.006	18.548	-0.290	-0.290	0.000	0.000	0.000	0.000
136	A	258	ARG	1	0.901	0.968	14.582	18.523	18.523	0.000	0.000	0.000	0.000
137	A	259	TYR	0	0.034	0.007	14.604	-0.566	-0.566	0.000	0.000	0.000	0.000
138	A	260	ASN	0	-0.051	-0.052	8.264	-2.031	-2.031	0.000	0.000	0.000	0.000
139	A	261	LYS	0	0.007	0.017	10.918	-2.177	-2.177	0.000	0.000	0.000	0.000
140	A	262	ARG	1	0.824	0.900	13.769	16.300	16.300	0.000	0.000	0.000	0.000
141	A	263	GLU	-1	-0.887	-0.953	15.837	-18.421	-18.421	0.000	0.000	0.000	0.000
142	A	264	GLU	-1	-0.726	-0.856	13.682	-20.976	-20.976	0.000	0.000	0.000	0.000
143	A	265	ALA	0	-0.013	-0.005	17.968	0.718	0.718	0.000	0.000	0.000	0.000
144	A	266	GLN	0	-0.014	-0.009	19.732	1.186	1.186	0.000	0.000	0.000	0.000
145	A	267	GLU	-1	-0.896	-0.937	21.359	-12.237	-12.237	0.000	0.000	0.000	0.000
146	A	268	ALA	0	0.022	0.009	20.928	0.607	0.607	0.000	0.000	0.000	0.000
147	A	269	ILE	0	-0.065	-0.038	22.972	0.569	0.569	0.000	0.000	0.000	0.000
148	A	270	SER	0	-0.075	-0.049	25.720	0.555	0.555	0.000	0.000	0.000	0.000
149	A	271	ALA	0	0.025	0.021	25.465	0.411	0.411	0.000	0.000	0.000	0.000
150	A	272	LEU	0	-0.036	-0.019	23.852	0.225	0.225	0.000	0.000	0.000	0.000
151	A	273	ASN	0	-0.005	-0.005	27.839	0.371	0.371	0.000	0.000	0.000	0.000
152	A	274	ASN	0	-0.045	-0.020	30.007	0.225	0.225	0.000	0.000	0.000	0.000
153	A	275	VAL	0	0.026	0.030	30.468	0.336	0.336	0.000	0.000	0.000	0.000
154	A	276	ILE	0	-0.027	-0.015	32.599	-0.102	-0.102	0.000	0.000	0.000	0.000
155	A	277	PRO	0	-0.017	0.011	29.700	-0.128	-0.128	0.000	0.000	0.000	0.000
156	A	278	GLU	-1	-0.820	-0.925	30.270	-9.160	-9.160	0.000	0.000	0.000	0.000
157	A	279	GLY	0	-0.026	-0.013	31.054	-0.252	-0.252	0.000	0.000	0.000	0.000
158	A	280	GLY	0	-0.084	-0.046	33.566	0.092	0.092	0.000	0.000	0.000	0.000
159	A	281	SER	0	-0.006	-0.002	34.728	0.036	0.036	0.000	0.000	0.000	0.000
160	A	282	GLN	0	-0.021	-0.014	35.880	0.136	0.136	0.000	0.000	0.000	0.000
161	A	283	PRO	0	0.027	0.011	34.662	-0.228	-0.228	0.000	0.000	0.000	0.000
162	A	284	LEU	0	0.021	0.010	27.803	0.004	0.004	0.000	0.000	0.000	0.000
163	A	285	SER	0	-0.035	-0.007	30.953	0.114	0.114	0.000	0.000	0.000	0.000
164	A	286	VAL	0	0.002	-0.011	24.958	-0.296	-0.296	0.000	0.000	0.000	0.000
165	A	287	ARG	1	0.972	0.991	26.750	10.391	10.391	0.000	0.000	0.000	0.000
166	A	288	LEU	0	0.018	0.005	22.102	-0.352	-0.352	0.000	0.000	0.000	0.000
167	A	289	ALA	-1	-0.961	-0.971	23.152	-11.947	-11.947	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:123:SER)