FMO DATABASE

FMODB ID: 3MLRL

Calculation Name: 3TW8-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3TW8

Chain ID: B

ChEMBL ID:

UniProt ID: Q6P3S1

Base Structure: X-ray

Registration Date: 2025-10-05

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	172
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1848453.377414
FMO2-HF: Nuclear repulsion	1779860.581511
FMO2-HF: Total energy	-68592.795904
FMO2-MP2: Total energy	-68793.470731

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:5:TYR)

Summations of interaction energy for fragment #1(A:5:TYR)

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.
-31.095	-20.133	1.953	-4.593	-8.321	-0.029

Interaction energy analysis for fragmet #1(A:5:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.774 / q_NPA : 0.878

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	7	HIS	0	0.010	-0.001	3.061	6.116	8.968	0.211	-1.123	-1.940	-0.009
4	A	8	LEU	0	-0.073	-0.031	2.883	-8.481	-5.433	1.125	-1.254	-2.919	-0.005
5	A	9	PHE	0	0.013	0.003	4.228	2.415	2.578	0.005	-0.048	-0.119	0.000
52	A	56	LYS	1	0.943	0.970	2.587	48.024	49.286	0.434	-0.538	-1.158	-0.004
53	A	57	VAL	0	0.002	-0.004	3.099	-18.241	-15.813	0.142	-1.390	-1.180	-0.011
54	A	58	LYS	1	0.922	0.966	3.421	36.405	37.564	0.037	-0.233	-0.963	0.000
55	A	59	LEU	0	0.029	0.019	4.731	0.636	0.686	-0.001	-0.007	-0.042	0.000
6	A	10	LYS	1	0.885	0.937	7.943	21.320	21.320	0.000	0.000	0.000	0.000
7	A	11	LEU	0	0.026	0.022	10.816	0.832	0.832	0.000	0.000	0.000	0.000
8	A	12	LEU	0	0.014	0.008	14.308	0.067	0.067	0.000	0.000	0.000	0.000
9	A	13	ILE	0	-0.024	-0.003	17.814	0.106	0.106	0.000	0.000	0.000	0.000
10	A	14	ILE	0	-0.029	-0.012	20.622	0.259	0.259	0.000	0.000	0.000	0.000
11	A	15	GLY	0	0.072	0.020	24.103	0.022	0.022	0.000	0.000	0.000	0.000
12	A	16	ASP	-1	-0.813	-0.906	27.456	-9.315	-9.315	0.000	0.000	0.000	0.000
13	A	17	SER	0	-0.078	-0.076	29.686	-0.366	-0.366	0.000	0.000	0.000	0.000
14	A	18	GLY	0	0.007	0.009	30.150	0.295	0.295	0.000	0.000	0.000	0.000
15	A	19	VAL	0	-0.002	0.004	27.331	0.121	0.121	0.000	0.000	0.000	0.000
16	A	20	GLY	0	0.019	0.017	27.617	-0.118	-0.118	0.000	0.000	0.000	0.000
17	A	21	LYS	1	0.852	0.950	23.317	11.249	11.249	0.000	0.000	0.000	0.000
18	A	22	SER	0	0.053	0.020	22.466	-0.465	-0.465	0.000	0.000	0.000	0.000
19	A	23	SER	0	-0.048	-0.039	22.647	-0.260	-0.260	0.000	0.000	0.000	0.000
20	A	24	LEU	0	0.066	0.024	21.078	-0.262	-0.262	0.000	0.000	0.000	0.000
21	A	25	LEU	0	-0.009	-0.012	17.555	-0.697	-0.697	0.000	0.000	0.000	0.000
22	A	26	LEU	0	-0.036	-0.026	18.070	-0.728	-0.728	0.000	0.000	0.000	0.000
23	A	27	ARG	1	0.841	0.940	19.420	12.145	12.145	0.000	0.000	0.000	0.000
24	A	28	PHE	0	-0.008	0.002	12.004	-0.695	-0.695	0.000	0.000	0.000	0.000
25	A	29	ALA	0	-0.014	-0.009	14.032	-1.271	-1.271	0.000	0.000	0.000	0.000
26	A	30	ASP	-1	-0.760	-0.851	9.328	-25.882	-25.882	0.000	0.000	0.000	0.000
27	A	31	ASN	0	-0.063	-0.043	12.949	0.336	0.336	0.000	0.000	0.000	0.000
28	A	32	THR	0	0.001	0.002	15.259	0.265	0.265	0.000	0.000	0.000	0.000
29	A	33	PHE	0	0.001	0.015	16.478	0.792	0.792	0.000	0.000	0.000	0.000
30	A	34	SER	0	-0.025	-0.023	16.525	-1.409	-1.409	0.000	0.000	0.000	0.000
31	A	35	GLY	0	0.018	0.026	17.937	0.730	0.730	0.000	0.000	0.000	0.000
32	A	36	SER	0	0.030	-0.003	19.930	-0.301	-0.301	0.000	0.000	0.000	0.000
33	A	37	TYR	0	0.019	0.007	17.191	0.358	0.358	0.000	0.000	0.000	0.000
34	A	38	ILE	0	0.023	0.024	22.689	0.395	0.395	0.000	0.000	0.000	0.000
35	A	39	THR	0	-0.017	-0.009	24.954	0.255	0.255	0.000	0.000	0.000	0.000
36	A	40	THR	0	-0.060	-0.025	24.668	0.156	0.156	0.000	0.000	0.000	0.000
37	A	41	ILE	0	-0.008	-0.016	20.511	0.225	0.225	0.000	0.000	0.000	0.000
38	A	42	GLY	0	0.005	0.019	24.563	-0.046	-0.046	0.000	0.000	0.000	0.000
39	A	43	VAL	0	0.000	0.001	19.170	0.004	0.004	0.000	0.000	0.000	0.000
40	A	44	ASP	-1	-0.858	-0.931	19.746	-14.514	-14.514	0.000	0.000	0.000	0.000
41	A	45	PHE	0	0.000	0.007	11.981	-0.333	-0.333	0.000	0.000	0.000	0.000
42	A	46	LYS	1	0.840	0.918	14.590	15.850	15.850	0.000	0.000	0.000	0.000
43	A	47	ILE	0	-0.046	-0.036	8.145	-1.110	-1.110	0.000	0.000	0.000	0.000
44	A	48	ARG	1	0.813	0.870	9.717	20.371	20.371	0.000	0.000	0.000	0.000
45	A	49	THR	0	-0.133	-0.090	5.230	-4.174	-4.174	0.000	0.000	0.000	0.000
46	A	50	VAL	0	0.036	0.018	6.822	2.704	2.704	0.000	0.000	0.000	0.000
47	A	51	GLU	-1	-0.927	-0.969	6.560	-40.904	-40.904	0.000	0.000	0.000	0.000
48	A	52	ILE	0	0.004	0.009	8.641	3.061	3.061	0.000	0.000	0.000	0.000
49	A	53	ASN	0	-0.017	-0.022	10.529	-0.931	-0.931	0.000	0.000	0.000	0.000
50	A	54	GLY	0	0.022	0.015	10.009	0.540	0.540	0.000	0.000	0.000	0.000
51	A	55	GLU	-1	-0.798	-0.845	6.872	-32.845	-32.845	0.000	0.000	0.000	0.000
56	A	60	GLN	0	-0.025	-0.011	8.358	0.986	0.986	0.000	0.000	0.000	0.000
57	A	61	ILE	0	0.015	0.014	10.807	0.468	0.468	0.000	0.000	0.000	0.000
58	A	62	TRP	0	-0.011	-0.020	12.238	0.494	0.494	0.000	0.000	0.000	0.000
59	A	63	ASP	-1	-0.776	-0.874	17.130	-12.100	-12.100	0.000	0.000	0.000	0.000
60	A	64	THR	0	-0.051	-0.038	20.984	-0.078	-0.078	0.000	0.000	0.000	0.000
61	A	65	ALA	0	0.026	0.010	23.845	0.229	0.229	0.000	0.000	0.000	0.000
62	A	66	GLY	0	0.024	0.014	27.471	0.081	0.081	0.000	0.000	0.000	0.000
63	A	67	GLN	0	0.000	0.003	23.448	0.418	0.418	0.000	0.000	0.000	0.000
64	A	68	GLU	-1	-0.700	-0.827	29.043	-9.445	-9.445	0.000	0.000	0.000	0.000
65	A	69	ARG	1	0.818	0.917	28.887	9.891	9.891	0.000	0.000	0.000	0.000
66	A	70	PHE	0	-0.046	-0.021	27.434	0.185	0.185	0.000	0.000	0.000	0.000
67	A	71	ARG	1	0.994	0.997	31.859	7.691	7.691	0.000	0.000	0.000	0.000
68	A	72	THR	0	0.005	-0.013	30.343	0.105	0.105	0.000	0.000	0.000	0.000
69	A	73	ILE	0	-0.027	0.015	24.964	0.081	0.081	0.000	0.000	0.000	0.000
70	A	74	THR	0	0.049	0.019	27.585	-0.222	-0.222	0.000	0.000	0.000	0.000
71	A	75	SER	0	0.078	0.020	24.703	-0.361	-0.361	0.000	0.000	0.000	0.000
72	A	76	THR	0	-0.088	-0.046	22.978	-0.486	-0.486	0.000	0.000	0.000	0.000
73	A	77	TYR	0	-0.011	-0.004	21.638	-0.435	-0.435	0.000	0.000	0.000	0.000
74	A	78	TYR	0	0.068	0.022	19.216	-0.383	-0.383	0.000	0.000	0.000	0.000
75	A	79	ARG	1	0.968	0.987	17.820	11.261	11.261	0.000	0.000	0.000	0.000
76	A	80	GLY	0	-0.006	0.001	14.228	-0.312	-0.312	0.000	0.000	0.000	0.000
77	A	81	THR	0	-0.036	-0.015	12.457	-1.633	-1.633	0.000	0.000	0.000	0.000
78	A	82	HIS	0	0.038	0.023	8.378	-0.163	-0.163	0.000	0.000	0.000	0.000
79	A	83	GLY	0	0.064	0.022	13.571	0.453	0.453	0.000	0.000	0.000	0.000
80	A	84	VAL	0	-0.051	-0.032	16.110	-0.210	-0.210	0.000	0.000	0.000	0.000
81	A	85	ILE	0	0.014	0.010	16.787	0.213	0.213	0.000	0.000	0.000	0.000
82	A	86	VAL	0	-0.004	-0.011	20.628	0.227	0.227	0.000	0.000	0.000	0.000
83	A	87	VAL	0	-0.019	-0.013	23.500	0.242	0.242	0.000	0.000	0.000	0.000
84	A	88	TYR	0	0.012	0.006	26.177	0.292	0.292	0.000	0.000	0.000	0.000
85	A	89	ASP	-1	-0.779	-0.865	29.640	-9.219	-9.219	0.000	0.000	0.000	0.000
86	A	90	VAL	0	0.017	0.011	31.915	0.248	0.248	0.000	0.000	0.000	0.000
87	A	91	THR	0	-0.030	-0.027	34.293	0.307	0.307	0.000	0.000	0.000	0.000
88	A	92	SER	0	-0.004	0.002	35.265	0.250	0.250	0.000	0.000	0.000	0.000
89	A	93	ALA	0	0.069	0.028	35.846	-0.212	-0.212	0.000	0.000	0.000	0.000
90	A	94	GLU	-1	-0.957	-0.980	37.421	-7.695	-7.695	0.000	0.000	0.000	0.000
91	A	95	SER	0	0.027	0.005	32.160	-0.233	-0.233	0.000	0.000	0.000	0.000
92	A	96	PHE	0	0.029	0.011	32.430	-0.242	-0.242	0.000	0.000	0.000	0.000
93	A	97	VAL	0	-0.050	-0.032	33.670	-0.085	-0.085	0.000	0.000	0.000	0.000
94	A	98	ASN	0	-0.033	-0.017	32.215	0.194	0.194	0.000	0.000	0.000	0.000
95	A	99	VAL	0	0.046	0.027	28.359	-0.127	-0.127	0.000	0.000	0.000	0.000
96	A	100	LYS	1	0.896	0.961	29.904	8.054	8.054	0.000	0.000	0.000	0.000
97	A	101	ARG	1	0.849	0.925	32.152	8.369	8.369	0.000	0.000	0.000	0.000
98	A	102	TRP	0	0.001	0.000	27.226	-0.181	-0.181	0.000	0.000	0.000	0.000
99	A	103	LEU	0	0.038	0.018	25.560	-0.243	-0.243	0.000	0.000	0.000	0.000
100	A	104	HIS	0	0.003	0.001	28.315	-0.163	-0.163	0.000	0.000	0.000	0.000
101	A	105	GLU	-1	-0.907	-0.956	28.345	-9.356	-9.356	0.000	0.000	0.000	0.000
102	A	106	ILE	0	-0.039	-0.030	23.195	-0.161	-0.161	0.000	0.000	0.000	0.000
103	A	107	ASN	0	0.007	0.002	25.659	-0.314	-0.314	0.000	0.000	0.000	0.000
104	A	108	GLN	0	-0.039	-0.002	27.788	0.169	0.169	0.000	0.000	0.000	0.000
105	A	109	ASN	0	-0.088	-0.062	26.919	0.090	0.090	0.000	0.000	0.000	0.000
106	A	110	CYS	0	-0.096	-0.035	21.743	-0.084	-0.084	0.000	0.000	0.000	0.000
107	A	111	ASP	-1	-0.801	-0.879	22.267	-11.748	-11.748	0.000	0.000	0.000	0.000
108	A	112	ASP	-1	-0.891	-0.941	19.143	-13.791	-13.791	0.000	0.000	0.000	0.000
109	A	113	VAL	0	-0.070	-0.020	17.301	-0.885	-0.885	0.000	0.000	0.000	0.000
110	A	114	CYS	0	0.005	0.016	16.560	0.499	0.499	0.000	0.000	0.000	0.000
111	A	115	ARG	1	0.830	0.892	18.654	11.648	11.648	0.000	0.000	0.000	0.000
112	A	116	ILE	0	0.003	0.009	19.840	0.260	0.260	0.000	0.000	0.000	0.000
113	A	117	LEU	0	-0.012	0.007	22.841	0.011	0.011	0.000	0.000	0.000	0.000
114	A	118	VAL	0	0.021	-0.014	22.703	-0.068	-0.068	0.000	0.000	0.000	0.000
115	A	119	GLY	0	0.043	0.017	26.088	0.183	0.183	0.000	0.000	0.000	0.000
116	A	120	ASN	0	-0.010	-0.016	26.749	-0.137	-0.137	0.000	0.000	0.000	0.000
117	A	121	LYS	1	0.831	0.910	28.618	9.634	9.634	0.000	0.000	0.000	0.000
118	A	122	ASN	0	0.002	0.005	30.790	0.382	0.382	0.000	0.000	0.000	0.000
119	A	123	ASP	-1	-0.813	-0.876	31.594	-9.693	-9.693	0.000	0.000	0.000	0.000
120	A	124	ASP	-1	-0.842	-0.913	34.457	-7.944	-7.944	0.000	0.000	0.000	0.000
121	A	125	PRO	0	-0.013	-0.024	38.046	0.064	0.064	0.000	0.000	0.000	0.000
122	A	126	GLU	-1	-0.966	-0.979	39.950	-6.861	-6.861	0.000	0.000	0.000	0.000
123	A	127	ARG	1	0.847	0.915	39.370	7.678	7.678	0.000	0.000	0.000	0.000
124	A	128	LYS	1	0.799	0.904	34.653	8.539	8.539	0.000	0.000	0.000	0.000
125	A	129	VAL	0	-0.024	-0.013	38.472	0.183	0.183	0.000	0.000	0.000	0.000
126	A	130	VAL	0	-0.055	-0.022	34.894	0.100	0.100	0.000	0.000	0.000	0.000
127	A	131	GLU	-1	-0.890	-0.943	37.048	-7.398	-7.398	0.000	0.000	0.000	0.000
128	A	132	THR	0	-0.033	-0.063	33.774	-0.034	-0.034	0.000	0.000	0.000	0.000
129	A	133	GLU	-1	-0.875	-0.942	34.968	-7.668	-7.668	0.000	0.000	0.000	0.000
130	A	134	ASP	-1	-0.868	-0.934	37.025	-7.717	-7.717	0.000	0.000	0.000	0.000
131	A	135	ALA	0	-0.020	-0.011	31.998	-0.129	-0.129	0.000	0.000	0.000	0.000
132	A	136	TYR	0	0.009	0.007	31.427	-0.185	-0.185	0.000	0.000	0.000	0.000
133	A	137	LYS	1	0.840	0.915	33.501	7.471	7.471	0.000	0.000	0.000	0.000
134	A	138	PHE	0	-0.037	-0.022	30.674	0.026	0.026	0.000	0.000	0.000	0.000
135	A	139	ALA	0	0.005	-0.008	29.133	-0.126	-0.126	0.000	0.000	0.000	0.000
136	A	140	GLY	0	0.026	0.014	30.006	-0.208	-0.208	0.000	0.000	0.000	0.000
137	A	141	GLN	0	-0.087	-0.047	32.149	-0.004	-0.004	0.000	0.000	0.000	0.000
138	A	142	MET	0	-0.031	-0.004	29.098	0.141	0.141	0.000	0.000	0.000	0.000
139	A	143	GLY	0	0.002	0.022	28.293	-0.291	-0.291	0.000	0.000	0.000	0.000
140	A	144	ILE	0	-0.054	-0.016	24.802	-0.478	-0.478	0.000	0.000	0.000	0.000
141	A	145	GLN	0	0.031	0.004	23.174	0.006	0.006	0.000	0.000	0.000	0.000
142	A	146	LEU	0	-0.018	-0.012	25.458	-0.120	-0.120	0.000	0.000	0.000	0.000
143	A	147	PHE	0	-0.002	-0.002	22.271	-0.100	-0.100	0.000	0.000	0.000	0.000
144	A	148	GLU	-1	-0.777	-0.840	26.344	-8.973	-8.973	0.000	0.000	0.000	0.000
145	A	149	THR	0	0.008	-0.008	24.062	-0.137	-0.137	0.000	0.000	0.000	0.000
146	A	150	SER	0	-0.043	-0.055	27.036	0.224	0.224	0.000	0.000	0.000	0.000
147	A	151	ALA	0	0.020	0.007	24.872	-0.290	-0.290	0.000	0.000	0.000	0.000
148	A	152	LYS	1	0.902	0.970	25.799	8.663	8.663	0.000	0.000	0.000	0.000
149	A	153	GLU	-1	-0.882	-0.967	28.510	-9.436	-9.436	0.000	0.000	0.000	0.000
150	A	154	ASN	0	-0.082	-0.035	22.433	-0.339	-0.339	0.000	0.000	0.000	0.000
151	A	155	VAL	0	0.043	0.022	25.612	-0.161	-0.161	0.000	0.000	0.000	0.000
152	A	156	ASN	0	0.021	-0.014	24.831	-0.254	-0.254	0.000	0.000	0.000	0.000
153	A	157	VAL	0	0.017	0.012	20.148	-0.185	-0.185	0.000	0.000	0.000	0.000
154	A	158	GLU	-1	-0.767	-0.850	16.955	-17.421	-17.421	0.000	0.000	0.000	0.000
155	A	159	GLU	-1	-0.894	-0.948	18.241	-13.560	-13.560	0.000	0.000	0.000	0.000
156	A	160	MET	0	-0.024	0.018	19.839	-0.517	-0.517	0.000	0.000	0.000	0.000
157	A	161	PHE	0	0.018	-0.021	15.244	-0.431	-0.431	0.000	0.000	0.000	0.000
158	A	162	ASN	0	-0.030	-0.013	14.518	-2.185	-2.185	0.000	0.000	0.000	0.000
159	A	163	CYS	0	-0.008	0.021	15.640	-0.628	-0.628	0.000	0.000	0.000	0.000
160	A	164	ILE	0	-0.016	-0.007	15.117	-0.365	-0.365	0.000	0.000	0.000	0.000
161	A	165	THR	0	-0.038	-0.034	10.396	-1.249	-1.249	0.000	0.000	0.000	0.000
162	A	166	GLU	-1	-0.864	-0.923	12.590	-17.561	-17.561	0.000	0.000	0.000	0.000
163	A	167	LEU	0	0.011	0.004	14.854	-0.195	-0.195	0.000	0.000	0.000	0.000
164	A	168	VAL	0	0.018	0.005	10.666	0.052	0.052	0.000	0.000	0.000	0.000
165	A	169	LEU	0	-0.045	-0.023	8.993	-1.010	-1.010	0.000	0.000	0.000	0.000
166	A	170	ARG	1	0.846	0.923	11.613	14.949	14.949	0.000	0.000	0.000	0.000
167	A	171	ALA	0	0.044	0.028	14.895	0.228	0.228	0.000	0.000	0.000	0.000
168	A	172	LYS	1	0.808	0.891	6.485	33.146	33.146	0.000	0.000	0.000	0.000
169	A	173	LYS	1	0.811	0.872	10.722	25.685	25.685	0.000	0.000	0.000	0.000
170	A	174	ASP	-1	-0.883	-0.949	14.315	-14.926	-14.926	0.000	0.000	0.000	0.000
171	A	175	ASN	0	-0.112	-0.055	15.362	1.475	1.475	0.000	0.000	0.000	0.000
172	A	176	LEU	-1	-1.012	-0.978	12.213	-16.495	-16.495	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:TYR)