FMO DATABASE

FMODB ID: N8K1Q

Calculation Name: 5H4U-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5H4U

Chain ID: A

ChEMBL ID:

UniProt ID: D3GDK4

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	201
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2308956.590479
FMO2-HF: Nuclear repulsion	2227374.831108
FMO2-HF: Total energy	-81581.759372
FMO2-MP2: Total energy	-81806.471294

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:1:LEU)

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

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.
42.718	49.823	2.513	-3.695	-5.922	-0.034

Interaction energy analysis for fragmet #1(A:1:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.825 / q_NPA : 0.916

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	SER	0	-0.023	-0.011	3.345	1.188	3.233	0.046	-0.877	-1.214	-0.003
4	A	4	GLY	0	0.061	0.040	5.089	0.889	0.916	-0.001	-0.004	-0.022	0.000
184	A	189	THR	0	-0.024	-0.032	3.135	-3.322	-2.825	0.150	-0.109	-0.538	0.000
185	A	190	GLN	0	0.017	0.027	2.260	-11.237	-8.687	1.382	-1.557	-2.375	-0.014
186	A	191	VAL	0	-0.016	-0.013	2.525	-8.311	-6.368	0.937	-1.146	-1.734	-0.017
187	A	192	ARG	1	0.843	0.899	5.118	29.216	29.259	-0.001	-0.002	-0.039	0.000
5	A	5	SER	0	-0.007	-0.006	8.822	1.237	1.237	0.000	0.000	0.000	0.000
6	A	6	GLY	0	0.025	0.006	12.344	-0.836	-0.836	0.000	0.000	0.000	0.000
7	A	7	VAL	0	0.009	0.020	14.470	0.727	0.727	0.000	0.000	0.000	0.000
8	A	8	THR	0	-0.054	-0.054	16.234	-0.702	-0.702	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.003	-0.020	18.738	0.877	0.877	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.740	0.861	21.167	10.666	10.666	0.000	0.000	0.000	0.000
11	A	11	TYR	0	0.002	0.010	20.726	0.476	0.476	0.000	0.000	0.000	0.000
12	A	12	TRP	0	0.011	-0.021	23.776	-0.367	-0.367	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.772	-0.892	26.135	-11.414	-11.414	0.000	0.000	0.000	0.000
14	A	14	CYS	0	-0.098	-0.035	27.589	0.602	0.602	0.000	0.000	0.000	0.000
15	A	15	CYS	0	-0.087	-0.034	26.243	0.566	0.566	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.826	0.926	24.847	11.427	11.427	0.000	0.000	0.000	0.000
17	A	17	PRO	0	-0.004	0.008	20.424	0.033	0.033	0.000	0.000	0.000	0.000
18	A	18	SER	0	0.002	-0.041	17.987	0.045	0.045	0.000	0.000	0.000	0.000
19	A	19	CYS	0	0.014	0.011	9.933	0.386	0.386	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.041	-0.024	18.266	-0.228	-0.228	0.000	0.000	0.000	0.000
21	A	21	TRP	0	-0.006	-0.003	20.989	0.853	0.853	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.013	0.000	20.679	-0.639	-0.639	0.000	0.000	0.000	0.000
23	A	23	GLY	0	0.002	-0.009	19.921	0.061	0.061	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.807	0.899	16.816	14.788	14.788	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.011	-0.001	12.622	-1.132	-1.132	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.006	0.012	13.122	1.331	1.331	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.010	-0.017	13.313	-1.663	-1.663	0.000	0.000	0.000	0.000
28	A	28	THR	0	0.010	0.005	15.627	0.655	0.655	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.893	0.941	18.473	13.869	13.869	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.032	0.012	18.610	-0.789	-0.789	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.030	-0.013	17.496	0.188	0.188	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.830	0.901	19.986	11.997	11.997	0.000	0.000	0.000	0.000
33	A	33	THR	0	0.039	0.025	23.426	-0.060	-0.060	0.000	0.000	0.000	0.000
34	A	34	CYS	0	-0.122	-0.043	25.375	0.622	0.622	0.000	0.000	0.000	0.000
35	A	35	LYS	1	1.028	1.015	29.604	8.414	8.414	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.067	0.035	32.527	-0.144	-0.144	0.000	0.000	0.000	0.000
37	A	37	ASN	0	0.044	0.018	34.033	-0.324	-0.324	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.061	0.041	30.424	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	39	ASN	0	0.017	0.011	29.683	-0.572	-0.572	0.000	0.000	0.000	0.000
40	A	40	THR	0	0.003	-0.002	30.986	-0.064	-0.064	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.042	0.011	27.710	-0.088	-0.088	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.054	-0.004	28.909	0.385	0.385	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.766	-0.876	28.602	-10.788	-10.788	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.002	0.002	24.458	-0.075	-0.075	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.021	-0.019	26.010	-0.588	-0.588	0.000	0.000	0.000	0.000
46	A	46	THR	0	-0.058	-0.029	28.418	0.304	0.304	0.000	0.000	0.000	0.000
47	A	47	GLN	0	0.090	0.048	29.305	-0.622	-0.622	0.000	0.000	0.000	0.000
48	A	48	SER	0	0.063	0.014	28.221	0.192	0.192	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.030	0.022	30.004	0.255	0.255	0.000	0.000	0.000	0.000
50	A	51	ASN	0	-0.049	-0.021	28.607	0.094	0.094	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.022	0.016	32.902	0.118	0.118	0.000	0.000	0.000	0.000
52	A	53	GLY	0	-0.030	-0.007	33.635	0.182	0.182	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.026	-0.025	33.454	0.138	0.138	0.000	0.000	0.000	0.000
54	A	55	SER	0	-0.039	-0.012	28.369	-0.119	-0.119	0.000	0.000	0.000	0.000
55	A	56	TYR	0	0.025	-0.008	28.884	0.072	0.072	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.032	0.033	23.795	-0.220	-0.220	0.000	0.000	0.000	0.000
57	A	59	ASN	0	0.003	-0.041	25.947	-0.342	-0.342	0.000	0.000	0.000	0.000
58	A	60	ASP	-1	-0.862	-0.932	24.928	-12.190	-12.190	0.000	0.000	0.000	0.000
59	A	61	GLN	0	-0.094	-0.049	20.931	-0.414	-0.414	0.000	0.000	0.000	0.000
60	A	62	GLN	0	0.013	-0.003	22.307	-0.063	-0.063	0.000	0.000	0.000	0.000
61	A	63	PRO	0	-0.018	0.002	20.916	-0.399	-0.399	0.000	0.000	0.000	0.000
62	A	64	PHE	0	-0.020	-0.025	18.866	0.619	0.619	0.000	0.000	0.000	0.000
63	A	65	THR	0	0.010	0.007	20.523	-0.373	-0.373	0.000	0.000	0.000	0.000
64	A	66	GLN	0	-0.008	-0.007	18.113	0.766	0.766	0.000	0.000	0.000	0.000
65	A	67	GLY	0	0.028	0.020	19.700	-0.483	-0.483	0.000	0.000	0.000	0.000
66	A	68	ASN	0	0.014	-0.006	20.550	0.477	0.477	0.000	0.000	0.000	0.000
67	A	69	VAL	0	-0.019	0.013	14.765	-0.156	-0.156	0.000	0.000	0.000	0.000
68	A	70	GLY	0	0.056	0.032	17.542	0.543	0.543	0.000	0.000	0.000	0.000
69	A	71	TYR	0	-0.026	-0.026	14.373	-1.030	-1.030	0.000	0.000	0.000	0.000
70	A	72	GLY	0	0.059	0.021	16.436	0.970	0.970	0.000	0.000	0.000	0.000
71	A	73	PHE	0	-0.027	-0.001	16.241	-1.017	-1.017	0.000	0.000	0.000	0.000
72	A	74	ALA	0	0.019	0.010	14.895	0.580	0.580	0.000	0.000	0.000	0.000
73	A	75	ALA	0	0.005	0.014	16.474	-0.373	-0.373	0.000	0.000	0.000	0.000
74	A	76	ALA	0	-0.007	-0.012	13.036	-0.407	-0.407	0.000	0.000	0.000	0.000
75	A	77	SER	0	0.035	0.031	14.756	0.132	0.132	0.000	0.000	0.000	0.000
76	A	78	ILE	0	-0.007	-0.005	8.632	-0.290	-0.290	0.000	0.000	0.000	0.000
77	A	79	SER	0	-0.013	-0.043	11.300	-0.950	-0.950	0.000	0.000	0.000	0.000
78	A	80	GLY	0	0.042	0.035	12.524	-0.702	-0.702	0.000	0.000	0.000	0.000
79	A	81	GLN	0	-0.036	-0.023	5.830	-0.120	-0.120	0.000	0.000	0.000	0.000
80	A	82	PRO	0	0.027	0.023	10.619	1.637	1.637	0.000	0.000	0.000	0.000
81	A	83	GLU	-1	-0.674	-0.790	11.580	-18.345	-18.345	0.000	0.000	0.000	0.000
82	A	84	SER	0	0.034	0.020	12.342	-1.123	-1.123	0.000	0.000	0.000	0.000
83	A	85	GLN	0	-0.048	-0.022	5.986	1.010	1.010	0.000	0.000	0.000	0.000
84	A	86	THR	0	0.036	0.022	7.763	-2.275	-2.275	0.000	0.000	0.000	0.000
85	A	88	CYS	0	-0.055	0.008	11.498	-0.944	-0.944	0.000	0.000	0.000	0.000
86	A	89	ALA	0	0.027	0.031	7.191	-0.822	-0.822	0.000	0.000	0.000	0.000
87	A	90	CYS	0	-0.064	-0.023	7.787	4.596	4.596	0.000	0.000	0.000	0.000
88	A	91	TYR	0	0.065	0.018	6.229	-4.425	-4.425	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.867	-0.892	7.260	-20.189	-20.189	0.000	0.000	0.000	0.000
90	A	93	MET	0	0.019	0.000	8.643	-2.221	-2.221	0.000	0.000	0.000	0.000
91	A	94	THR	0	-0.042	-0.010	11.384	1.154	1.154	0.000	0.000	0.000	0.000
92	A	95	PHE	0	0.052	0.018	14.043	-0.415	-0.415	0.000	0.000	0.000	0.000
93	A	96	THR	0	-0.025	-0.025	16.458	-0.095	-0.095	0.000	0.000	0.000	0.000
94	A	97	ASN	0	0.061	0.032	18.847	0.032	0.032	0.000	0.000	0.000	0.000
95	A	98	THR	0	0.050	0.039	22.378	0.437	0.437	0.000	0.000	0.000	0.000
96	A	99	ALA	0	0.061	0.022	24.280	-0.128	-0.128	0.000	0.000	0.000	0.000
97	A	100	ILE	0	-0.039	-0.005	20.704	0.176	0.176	0.000	0.000	0.000	0.000
98	A	101	SER	0	-0.039	-0.011	20.212	-0.937	-0.937	0.000	0.000	0.000	0.000
99	A	102	GLY	0	0.012	0.006	18.109	0.439	0.439	0.000	0.000	0.000	0.000
100	A	103	GLN	0	-0.026	-0.014	17.783	0.080	0.080	0.000	0.000	0.000	0.000
101	A	104	LYS	1	0.857	0.907	10.978	19.992	19.992	0.000	0.000	0.000	0.000
102	A	105	MET	0	-0.017	-0.002	14.147	1.077	1.077	0.000	0.000	0.000	0.000
103	A	106	ILE	0	-0.015	-0.011	10.340	-1.527	-1.527	0.000	0.000	0.000	0.000
104	A	107	VAL	0	0.022	0.008	11.813	1.364	1.364	0.000	0.000	0.000	0.000
105	A	108	GLN	0	-0.002	-0.003	11.364	-0.849	-0.849	0.000	0.000	0.000	0.000
106	A	109	VAL	0	-0.006	0.002	11.473	1.328	1.328	0.000	0.000	0.000	0.000
107	A	110	THR	0	-0.009	-0.019	13.560	-0.397	-0.397	0.000	0.000	0.000	0.000
108	A	111	ASN	0	0.045	0.016	16.659	0.793	0.793	0.000	0.000	0.000	0.000
109	A	112	THR	0	-0.003	-0.018	16.242	-1.548	-1.548	0.000	0.000	0.000	0.000
110	A	113	GLY	0	0.010	0.006	17.343	0.899	0.899	0.000	0.000	0.000	0.000
111	A	114	SER	0	-0.031	-0.024	19.357	0.459	0.459	0.000	0.000	0.000	0.000
112	A	115	ASP	-1	-0.958	-0.976	18.704	-16.906	-16.906	0.000	0.000	0.000	0.000
113	A	116	LEU	0	0.004	0.008	19.340	0.835	0.835	0.000	0.000	0.000	0.000
114	A	117	ASN	0	0.031	0.011	18.361	-1.704	-1.704	0.000	0.000	0.000	0.000
115	A	118	GLY	0	0.036	0.041	15.639	0.571	0.571	0.000	0.000	0.000	0.000
116	A	119	ASN	0	-0.059	-0.024	11.209	-1.816	-1.816	0.000	0.000	0.000	0.000
117	A	120	HIS	0	0.029	0.006	14.084	1.135	1.135	0.000	0.000	0.000	0.000
118	A	121	PHE	0	-0.013	-0.017	9.831	-1.069	-1.069	0.000	0.000	0.000	0.000
119	A	122	ASP	-1	-0.816	-0.877	16.125	-14.509	-14.509	0.000	0.000	0.000	0.000
120	A	123	LEU	0	-0.001	-0.018	17.281	-0.292	-0.292	0.000	0.000	0.000	0.000
121	A	124	MET	0	-0.034	-0.012	19.585	0.523	0.523	0.000	0.000	0.000	0.000
122	A	125	ILE	0	-0.007	-0.013	21.795	0.038	0.038	0.000	0.000	0.000	0.000
123	A	126	PRO	0	-0.029	-0.002	24.646	0.257	0.257	0.000	0.000	0.000	0.000
124	A	127	GLY	0	0.053	0.020	28.207	0.120	0.120	0.000	0.000	0.000	0.000
125	A	128	GLY	0	-0.023	-0.013	27.163	0.209	0.209	0.000	0.000	0.000	0.000
126	A	129	GLY	0	0.056	0.042	28.250	-0.068	-0.068	0.000	0.000	0.000	0.000
127	A	130	VAL	0	-0.075	-0.032	28.374	-0.316	-0.316	0.000	0.000	0.000	0.000
128	A	131	GLY	0	0.040	0.018	27.868	-0.338	-0.338	0.000	0.000	0.000	0.000
129	A	132	ILE	0	0.023	0.015	26.159	0.408	0.408	0.000	0.000	0.000	0.000
130	A	133	PHE	0	0.032	0.024	25.417	0.471	0.471	0.000	0.000	0.000	0.000
131	A	134	ASN	0	-0.026	-0.046	30.130	-0.089	-0.089	0.000	0.000	0.000	0.000
132	A	135	GLY	0	0.086	0.040	31.116	0.248	0.248	0.000	0.000	0.000	0.000
133	A	137	GLN	0	-0.042	-0.013	33.714	0.223	0.223	0.000	0.000	0.000	0.000
134	A	138	SER	0	-0.024	-0.012	35.023	0.131	0.131	0.000	0.000	0.000	0.000
135	A	139	GLN	0	-0.054	-0.020	30.540	-0.057	-0.057	0.000	0.000	0.000	0.000
136	A	140	TRP	0	-0.052	-0.049	31.820	0.187	0.187	0.000	0.000	0.000	0.000
137	A	141	GLY	0	0.032	0.033	37.317	0.154	0.154	0.000	0.000	0.000	0.000
138	A	142	ALA	0	-0.039	-0.006	36.238	0.123	0.123	0.000	0.000	0.000	0.000
139	A	143	PRO	0	0.068	0.028	37.805	0.083	0.083	0.000	0.000	0.000	0.000
140	A	144	SER	0	0.078	0.040	37.574	-0.240	-0.240	0.000	0.000	0.000	0.000
141	A	145	ASN	0	-0.047	-0.028	36.531	-0.059	-0.059	0.000	0.000	0.000	0.000
142	A	146	GLY	0	0.044	0.021	33.980	-0.280	-0.280	0.000	0.000	0.000	0.000
143	A	147	TRP	0	-0.019	-0.032	31.140	0.151	0.151	0.000	0.000	0.000	0.000
144	A	148	GLY	0	0.026	0.012	34.108	-0.235	-0.235	0.000	0.000	0.000	0.000
145	A	149	GLN	0	0.013	0.007	33.869	0.114	0.114	0.000	0.000	0.000	0.000
146	A	150	ARG	1	0.867	0.929	32.454	9.156	9.156	0.000	0.000	0.000	0.000
147	A	151	TYR	0	0.021	0.007	28.180	-0.242	-0.242	0.000	0.000	0.000	0.000
148	A	152	GLY	0	0.046	0.026	28.835	0.255	0.255	0.000	0.000	0.000	0.000
149	A	153	GLY	0	0.034	0.018	29.840	-0.081	-0.081	0.000	0.000	0.000	0.000
150	A	154	ILE	0	-0.041	-0.013	32.043	0.248	0.248	0.000	0.000	0.000	0.000
151	A	155	SER	0	0.012	0.010	33.225	-0.311	-0.311	0.000	0.000	0.000	0.000
152	A	156	SER	0	-0.045	-0.035	34.568	-0.110	-0.110	0.000	0.000	0.000	0.000
153	A	157	GLN	0	-0.008	-0.012	34.050	0.127	0.127	0.000	0.000	0.000	0.000
154	A	158	SER	0	0.035	0.016	35.145	-0.061	-0.061	0.000	0.000	0.000	0.000
155	A	159	GLU	-1	-0.734	-0.871	36.753	-8.171	-8.171	0.000	0.000	0.000	0.000
156	A	160	CYS	0	-0.069	-0.012	27.027	-0.235	-0.235	0.000	0.000	0.000	0.000
157	A	161	ASN	0	-0.082	-0.049	35.548	-0.039	-0.039	0.000	0.000	0.000	0.000
158	A	162	GLN	0	0.007	0.000	38.210	0.211	0.211	0.000	0.000	0.000	0.000
159	A	163	LEU	0	-0.005	0.010	31.847	-0.074	-0.074	0.000	0.000	0.000	0.000
160	A	164	PRO	0	0.041	0.025	34.226	0.220	0.220	0.000	0.000	0.000	0.000
161	A	165	THR	0	0.035	0.010	34.715	-0.260	-0.260	0.000	0.000	0.000	0.000
162	A	166	SER	0	-0.011	-0.004	32.314	-0.069	-0.069	0.000	0.000	0.000	0.000
163	A	167	LEU	0	0.004	0.011	28.949	-0.328	-0.328	0.000	0.000	0.000	0.000
164	A	168	ARG	1	0.895	0.946	30.637	7.939	7.939	0.000	0.000	0.000	0.000
165	A	169	ALA	0	0.015	0.030	28.472	0.018	0.018	0.000	0.000	0.000	0.000
166	A	170	GLY	0	0.061	0.009	26.187	-0.144	-0.144	0.000	0.000	0.000	0.000
167	A	172	ASN	0	0.021	-0.013	29.817	0.163	0.163	0.000	0.000	0.000	0.000
168	A	173	TRP	0	-0.027	-0.010	20.054	0.057	0.057	0.000	0.000	0.000	0.000
169	A	174	ARG	1	0.816	0.900	25.853	9.902	9.902	0.000	0.000	0.000	0.000
170	A	175	PHE	0	0.021	-0.003	26.867	-0.072	-0.072	0.000	0.000	0.000	0.000
171	A	176	GLY	0	0.023	0.022	28.702	0.149	0.149	0.000	0.000	0.000	0.000
172	A	177	TRP	0	-0.032	-0.023	18.182	-0.125	-0.125	0.000	0.000	0.000	0.000
173	A	178	PHE	0	-0.002	-0.008	20.538	-0.320	-0.320	0.000	0.000	0.000	0.000
174	A	179	LYS	1	0.878	0.941	24.208	11.202	11.202	0.000	0.000	0.000	0.000
175	A	180	ASN	0	0.006	0.012	27.568	-0.004	-0.004	0.000	0.000	0.000	0.000
176	A	181	ALA	0	-0.024	0.006	23.769	0.127	0.127	0.000	0.000	0.000	0.000
177	A	182	ASP	-1	-0.830	-0.914	25.487	-11.073	-11.073	0.000	0.000	0.000	0.000
178	A	183	ASN	0	-0.005	-0.005	22.784	-0.285	-0.285	0.000	0.000	0.000	0.000
179	A	184	PRO	0	-0.027	0.014	20.164	-0.149	-0.149	0.000	0.000	0.000	0.000
180	A	185	SER	0	0.030	0.018	18.154	-0.702	-0.702	0.000	0.000	0.000	0.000
181	A	186	MET	0	-0.069	-0.028	12.342	-0.100	-0.100	0.000	0.000	0.000	0.000
182	A	187	LYS	1	0.975	1.000	11.272	19.712	19.712	0.000	0.000	0.000	0.000
183	A	188	PHE	0	0.009	-0.012	7.427	0.192	0.192	0.000	0.000	0.000	0.000
188	A	194	PRO	0	0.044	0.032	10.691	0.975	0.975	0.000	0.000	0.000	0.000
189	A	195	THR	0	0.072	0.013	13.268	0.377	0.377	0.000	0.000	0.000	0.000
190	A	196	ILE	0	-0.021	0.005	16.447	0.469	0.469	0.000	0.000	0.000	0.000
191	A	197	LEU	0	0.013	0.016	13.372	0.628	0.628	0.000	0.000	0.000	0.000
192	A	198	THR	0	0.047	0.015	14.024	0.822	0.822	0.000	0.000	0.000	0.000
193	A	199	GLN	0	-0.004	0.011	16.963	0.637	0.637	0.000	0.000	0.000	0.000
194	A	200	LYS	1	0.870	0.954	19.950	13.804	13.804	0.000	0.000	0.000	0.000
195	A	201	SER	0	-0.002	-0.035	16.462	0.621	0.621	0.000	0.000	0.000	0.000
196	A	202	GLN	0	-0.046	-0.020	19.647	0.438	0.438	0.000	0.000	0.000	0.000
197	A	204	VAL	0	0.018	-0.003	13.555	-0.948	-0.948	0.000	0.000	0.000	0.000
198	A	205	ARG	1	0.847	0.909	7.959	30.440	30.440	0.000	0.000	0.000	0.000
199	A	206	THR	0	0.003	-0.012	12.062	-0.124	-0.124	0.000	0.000	0.000	0.000
200	A	207	PRO	0	-0.056	-0.021	10.937	0.740	0.740	0.000	0.000	0.000	0.000
201	A	208	GLY	-1	-0.817	-0.862	8.032	-33.443	-33.443	0.000	0.000	0.000	0.000

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