FMO DATABASE

FMODB ID: M85JZ

Calculation Name: 6PX3-C-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6PX3

Chain ID: C

ChEMBL ID:

UniProt ID: P06897

Base Structure: ElectronMicroscopy

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	179
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1653513.29641
FMO2-HF: Nuclear repulsion	1585404.439565
FMO2-HF: Total energy	-68108.856845
FMO2-MP2: Total energy	-68312.289457

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:-71:MET)

Summations of interaction energy for fragment #1(A:-71: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.
-63.987	-58.881	26.06	-10.562	-20.601	-0.134

Interaction energy analysis for fragmet #1(A:-71:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.778 / q_NPA : 0.894

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	-69	ILE	0	-0.014	0.001	2.497	0.411	3.561	0.977	-1.346	-2.781	-0.008
4	A	-68	PHE	0	0.004	-0.002	4.682	1.200	1.250	-0.001	-0.015	-0.033	0.000
16	A	-56	GLU	-1	-0.924	-0.953	3.785	-61.714	-61.255	0.000	-0.123	-0.336	0.000
17	A	-55	VAL	0	-0.018	-0.013	2.368	9.024	10.998	1.606	-1.103	-2.476	-0.004
18	A	-54	GLU	-1	-0.871	-0.932	1.785	-101.065	-100.461	12.942	-7.707	-5.839	-0.100
19	A	-53	SER	0	-0.003	-0.016	3.197	3.885	4.748	0.215	-0.140	-0.938	-0.002
20	A	-52	SER	0	0.010	-0.002	3.951	3.950	4.041	0.006	-0.010	-0.087	0.000
56	A	-16	LEU	0	-0.001	-0.010	3.073	0.474	1.044	0.110	-0.120	-0.559	-0.001
57	A	-15	SER	0	0.017	-0.001	5.206	0.074	0.152	-0.001	-0.002	-0.075	0.000
61	A	-11	ILE	0	-0.021	0.003	2.901	0.379	0.822	0.085	-0.099	-0.428	0.000
62	A	-10	GLN	0	0.015	0.005	2.501	-7.835	-7.790	3.498	-0.989	-2.554	-0.013
63	A	-9	LYS	1	0.947	0.948	2.385	39.270	36.878	6.549	-0.016	-4.142	-0.006
64	A	-8	GLU	-1	-0.855	-0.908	3.228	-33.175	-34.004	0.074	1.108	-0.353	0.000
5	A	-67	VAL	0	0.022	0.017	8.503	0.459	0.459	0.000	0.000	0.000	0.000
6	A	-66	LYS	1	0.917	0.967	11.128	17.198	17.198	0.000	0.000	0.000	0.000
7	A	-65	THR	0	0.038	0.032	14.626	0.771	0.771	0.000	0.000	0.000	0.000
8	A	-64	LEU	0	0.023	-0.004	17.615	0.296	0.296	0.000	0.000	0.000	0.000
9	A	-63	THR	0	-0.051	-0.027	20.691	0.512	0.512	0.000	0.000	0.000	0.000
10	A	-62	GLY	0	-0.027	-0.008	19.826	0.400	0.400	0.000	0.000	0.000	0.000
11	A	-61	LYS	1	0.850	0.919	17.641	16.874	16.874	0.000	0.000	0.000	0.000
12	A	-60	THR	0	0.014	-0.008	13.380	0.022	0.022	0.000	0.000	0.000	0.000
13	A	-59	ILE	0	-0.011	0.007	11.879	0.677	0.677	0.000	0.000	0.000	0.000
14	A	-58	THR	0	0.019	0.002	7.988	0.139	0.139	0.000	0.000	0.000	0.000
15	A	-57	LEU	0	-0.022	-0.005	7.148	1.834	1.834	0.000	0.000	0.000	0.000
21	A	-51	ASP	-1	-0.790	-0.878	5.524	-42.174	-42.174	0.000	0.000	0.000	0.000
22	A	-50	THR	0	0.004	-0.026	7.276	0.878	0.878	0.000	0.000	0.000	0.000
23	A	-49	ILE	0	-0.022	-0.008	8.550	-2.012	-2.012	0.000	0.000	0.000	0.000
24	A	-48	ASP	-1	-0.845	-0.922	10.722	-18.368	-18.368	0.000	0.000	0.000	0.000
25	A	-47	ASN	0	-0.006	0.014	9.585	-0.483	-0.483	0.000	0.000	0.000	0.000
26	A	-46	VAL	0	0.009	0.015	6.954	-0.643	-0.643	0.000	0.000	0.000	0.000
27	A	-45	LYS	1	0.835	0.911	9.790	17.925	17.925	0.000	0.000	0.000	0.000
28	A	-44	SER	0	-0.037	-0.020	13.008	0.910	0.910	0.000	0.000	0.000	0.000
29	A	-43	LYS	1	0.842	0.900	6.026	45.019	45.019	0.000	0.000	0.000	0.000
30	A	-42	ILE	0	-0.015	-0.013	11.185	0.442	0.442	0.000	0.000	0.000	0.000
31	A	-41	GLN	0	-0.034	-0.015	13.898	0.729	0.729	0.000	0.000	0.000	0.000
32	A	-40	ASP	-1	-0.892	-0.941	14.105	-20.456	-20.456	0.000	0.000	0.000	0.000
33	A	-39	LYS	1	0.815	0.906	12.070	23.373	23.373	0.000	0.000	0.000	0.000
34	A	-38	GLU	-1	-0.835	-0.911	15.586	-16.638	-16.638	0.000	0.000	0.000	0.000
35	A	-37	GLY	0	0.014	0.021	18.592	0.987	0.987	0.000	0.000	0.000	0.000
36	A	-36	ILE	0	-0.047	-0.026	17.534	0.703	0.703	0.000	0.000	0.000	0.000
37	A	-35	PRO	0	0.030	0.017	18.978	-0.836	-0.836	0.000	0.000	0.000	0.000
38	A	-34	PRO	0	0.050	0.015	17.452	0.136	0.136	0.000	0.000	0.000	0.000
39	A	-33	ASP	-1	-0.865	-0.934	18.745	-13.008	-13.008	0.000	0.000	0.000	0.000
40	A	-32	GLN	0	0.003	0.005	21.617	0.119	0.119	0.000	0.000	0.000	0.000
41	A	-31	GLN	0	-0.014	-0.006	14.800	-0.757	-0.757	0.000	0.000	0.000	0.000
42	A	-30	ARG	1	0.788	0.889	17.223	13.435	13.435	0.000	0.000	0.000	0.000
43	A	-29	LEU	0	0.042	0.025	10.659	0.086	0.086	0.000	0.000	0.000	0.000
44	A	-28	ILE	0	0.001	0.004	13.735	0.468	0.468	0.000	0.000	0.000	0.000
45	A	-27	PHE	0	0.029	-0.003	8.454	-0.998	-0.998	0.000	0.000	0.000	0.000
46	A	-26	ALA	0	-0.009	0.007	11.603	0.797	0.797	0.000	0.000	0.000	0.000
47	A	-25	GLY	0	0.030	0.015	13.329	0.665	0.665	0.000	0.000	0.000	0.000
48	A	-24	LYS	1	0.929	0.975	13.521	16.955	16.955	0.000	0.000	0.000	0.000
49	A	-23	GLN	0	0.022	-0.004	14.642	-0.774	-0.774	0.000	0.000	0.000	0.000
50	A	-22	LEU	0	-0.073	-0.037	9.374	-0.025	-0.025	0.000	0.000	0.000	0.000
51	A	-21	GLU	-1	-0.903	-0.968	13.411	-14.995	-14.995	0.000	0.000	0.000	0.000
52	A	-20	ASP	-1	-0.837	-0.905	13.181	-17.927	-17.927	0.000	0.000	0.000	0.000
53	A	-19	GLY	0	0.062	0.026	13.418	-1.122	-1.122	0.000	0.000	0.000	0.000
54	A	-18	ARG	1	0.816	0.927	11.330	17.617	17.617	0.000	0.000	0.000	0.000
55	A	-17	THR	0	0.008	-0.010	7.805	-1.733	-1.733	0.000	0.000	0.000	0.000
58	A	-14	ASP	-1	-0.866	-0.911	6.362	-19.238	-19.238	0.000	0.000	0.000	0.000
59	A	-13	TYR	0	0.003	0.006	7.869	1.654	1.654	0.000	0.000	0.000	0.000
60	A	-12	ASN	0	-0.063	-0.030	6.540	-0.451	-0.451	0.000	0.000	0.000	0.000
65	A	-7	SER	0	-0.026	-0.012	5.057	4.600	4.600	0.000	0.000	0.000	0.000
66	A	-6	THR	0	-0.032	-0.017	6.923	-1.451	-1.451	0.000	0.000	0.000	0.000
67	A	-5	LEU	0	0.001	0.007	6.470	1.647	1.647	0.000	0.000	0.000	0.000
68	A	-4	HIS	0	-0.019	-0.014	10.136	0.493	0.493	0.000	0.000	0.000	0.000
69	A	-3	LEU	0	-0.005	0.001	13.929	-0.113	-0.113	0.000	0.000	0.000	0.000
70	A	-2	VAL	0	-0.024	-0.017	15.637	0.747	0.747	0.000	0.000	0.000	0.000
71	A	-1	LEU	0	0.025	0.010	18.991	-0.380	-0.380	0.000	0.000	0.000	0.000
72	A	0	ARG	1	0.786	0.883	19.157	14.361	14.361	0.000	0.000	0.000	0.000
73	A	1	LEU	0	0.011	0.006	23.509	-0.068	-0.068	0.000	0.000	0.000	0.000
74	A	2	ARG	1	0.881	0.937	26.173	10.730	10.730	0.000	0.000	0.000	0.000
75	A	3	GLY	-1	-0.866	-0.924	28.986	-9.241	-9.241	0.000	0.000	0.000	0.000
76	A	16	GLY	0	0.095	0.038	43.989	0.051	0.051	0.000	0.000	0.000	0.000
77	A	17	ARG	1	0.912	0.956	42.415	6.557	6.557	0.000	0.000	0.000	0.000
78	A	18	SER	0	-0.004	-0.027	38.523	0.019	0.019	0.000	0.000	0.000	0.000
79	A	19	SER	0	0.017	0.006	37.932	-0.147	-0.147	0.000	0.000	0.000	0.000
80	A	20	ARG	1	0.940	0.964	38.200	7.046	7.046	0.000	0.000	0.000	0.000
81	A	21	ALA	0	-0.038	-0.016	36.024	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	22	GLY	0	0.113	0.073	33.525	-0.202	-0.202	0.000	0.000	0.000	0.000
83	A	23	LEU	0	-0.077	-0.025	32.396	-0.154	-0.154	0.000	0.000	0.000	0.000
84	A	24	GLN	0	0.069	0.021	32.810	0.406	0.406	0.000	0.000	0.000	0.000
85	A	25	PHE	0	0.034	0.026	33.726	0.280	0.280	0.000	0.000	0.000	0.000
86	A	26	PRO	0	0.002	0.018	36.824	0.110	0.110	0.000	0.000	0.000	0.000
87	A	27	VAL	0	0.077	0.025	38.525	0.168	0.168	0.000	0.000	0.000	0.000
88	A	28	GLY	0	-0.018	-0.007	40.927	0.119	0.119	0.000	0.000	0.000	0.000
89	A	29	ARG	1	0.932	0.963	42.784	6.972	6.972	0.000	0.000	0.000	0.000
90	A	30	VAL	0	0.066	0.038	38.970	0.130	0.130	0.000	0.000	0.000	0.000
91	A	31	HIS	0	0.044	0.020	42.379	0.114	0.114	0.000	0.000	0.000	0.000
92	A	32	ARG	1	0.916	0.961	45.040	6.330	6.330	0.000	0.000	0.000	0.000
93	A	33	LEU	0	-0.018	-0.019	43.121	0.129	0.129	0.000	0.000	0.000	0.000
94	A	34	LEU	0	0.036	0.013	41.268	0.074	0.074	0.000	0.000	0.000	0.000
95	A	35	ARG	1	0.922	0.954	45.481	6.116	6.116	0.000	0.000	0.000	0.000
96	A	36	LYS	1	0.922	0.956	49.107	5.657	5.657	0.000	0.000	0.000	0.000
97	A	37	GLY	0	0.012	0.017	47.452	0.075	0.075	0.000	0.000	0.000	0.000
98	A	38	ASN	0	-0.048	-0.016	48.412	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	39	TYR	0	0.020	0.016	44.472	-0.020	-0.020	0.000	0.000	0.000	0.000
100	A	40	ALA	0	0.012	0.004	46.689	-0.043	-0.043	0.000	0.000	0.000	0.000
101	A	41	GLU	-1	-0.898	-0.934	48.591	-5.593	-5.593	0.000	0.000	0.000	0.000
102	A	42	ARG	1	0.921	0.954	49.728	5.956	5.956	0.000	0.000	0.000	0.000
103	A	43	VAL	0	-0.001	0.003	44.507	-0.121	-0.121	0.000	0.000	0.000	0.000
104	A	44	GLY	0	0.030	0.018	44.435	0.072	0.072	0.000	0.000	0.000	0.000
105	A	45	ALA	0	0.005	-0.020	43.796	-0.100	-0.100	0.000	0.000	0.000	0.000
106	A	46	GLY	0	0.062	0.029	40.250	-0.061	-0.061	0.000	0.000	0.000	0.000
107	A	47	ALA	0	0.012	0.019	38.878	-0.187	-0.187	0.000	0.000	0.000	0.000
108	A	48	PRO	0	-0.034	-0.032	38.775	-0.122	-0.122	0.000	0.000	0.000	0.000
109	A	49	VAL	0	-0.008	0.001	36.125	-0.077	-0.077	0.000	0.000	0.000	0.000
110	A	50	TYR	0	0.059	0.033	30.934	-0.147	-0.147	0.000	0.000	0.000	0.000
111	A	51	LEU	0	0.024	0.011	33.841	-0.190	-0.190	0.000	0.000	0.000	0.000
112	A	52	ALA	0	-0.033	-0.025	34.702	-0.104	-0.104	0.000	0.000	0.000	0.000
113	A	53	ALA	0	0.053	0.029	31.116	-0.129	-0.129	0.000	0.000	0.000	0.000
114	A	54	VAL	0	0.019	0.010	29.946	-0.264	-0.264	0.000	0.000	0.000	0.000
115	A	55	LEU	0	-0.021	-0.017	30.134	-0.148	-0.148	0.000	0.000	0.000	0.000
116	A	56	GLU	-1	-0.978	-0.971	29.289	-9.942	-9.942	0.000	0.000	0.000	0.000
117	A	57	TYR	0	0.089	0.049	21.865	-0.302	-0.302	0.000	0.000	0.000	0.000
118	A	58	LEU	0	-0.012	-0.011	26.327	-0.298	-0.298	0.000	0.000	0.000	0.000
119	A	59	THR	0	-0.062	-0.044	27.667	0.009	0.009	0.000	0.000	0.000	0.000
120	A	60	ALA	0	0.005	-0.002	25.773	-0.055	-0.055	0.000	0.000	0.000	0.000
121	A	61	GLU	-1	-0.843	-0.916	20.651	-13.264	-13.264	0.000	0.000	0.000	0.000
122	A	62	ILE	0	-0.020	-0.011	23.609	-0.208	-0.208	0.000	0.000	0.000	0.000
123	A	63	LEU	0	-0.019	-0.023	26.069	0.026	0.026	0.000	0.000	0.000	0.000
124	A	64	GLU	-1	-0.817	-0.889	19.488	-13.692	-13.692	0.000	0.000	0.000	0.000
125	A	65	LEU	0	-0.021	-0.008	19.225	-0.224	-0.224	0.000	0.000	0.000	0.000
126	A	66	ALA	0	-0.002	-0.007	22.444	-0.031	-0.031	0.000	0.000	0.000	0.000
127	A	67	GLY	0	0.011	-0.005	25.547	0.195	0.195	0.000	0.000	0.000	0.000
128	A	68	ASN	0	0.013	0.011	19.656	-0.058	-0.058	0.000	0.000	0.000	0.000
129	A	69	ALA	0	0.038	0.026	22.334	-0.027	-0.027	0.000	0.000	0.000	0.000
130	A	70	ALA	0	-0.023	-0.010	23.828	0.155	0.155	0.000	0.000	0.000	0.000
131	A	71	ARG	1	0.860	0.924	19.532	13.554	13.554	0.000	0.000	0.000	0.000
132	A	72	ASP	-1	-0.834	-0.905	19.862	-13.728	-13.728	0.000	0.000	0.000	0.000
133	A	73	ASN	0	-0.092	-0.051	23.198	0.280	0.280	0.000	0.000	0.000	0.000
134	A	74	LYS	1	0.950	0.974	25.531	11.666	11.666	0.000	0.000	0.000	0.000
135	A	75	LYS	1	0.833	0.910	28.129	9.963	9.963	0.000	0.000	0.000	0.000
136	A	76	THR	0	0.045	0.021	29.169	-0.245	-0.245	0.000	0.000	0.000	0.000
137	A	77	ARG	1	0.913	0.954	31.352	8.454	8.454	0.000	0.000	0.000	0.000
138	A	78	ILE	0	0.055	0.040	28.439	-0.090	-0.090	0.000	0.000	0.000	0.000
139	A	79	ILE	0	0.003	0.005	31.364	0.326	0.326	0.000	0.000	0.000	0.000
140	A	80	PRO	0	0.055	0.010	31.848	-0.283	-0.283	0.000	0.000	0.000	0.000
141	A	81	ARG	1	0.861	0.923	30.171	9.142	9.142	0.000	0.000	0.000	0.000
142	A	82	HIS	0	0.043	0.019	27.616	-0.112	-0.112	0.000	0.000	0.000	0.000
143	A	83	LEU	0	0.032	0.022	27.152	-0.321	-0.321	0.000	0.000	0.000	0.000
144	A	84	GLN	0	-0.021	-0.008	28.197	-0.171	-0.171	0.000	0.000	0.000	0.000
145	A	85	LEU	0	-0.018	-0.016	24.900	-0.167	-0.167	0.000	0.000	0.000	0.000
146	A	86	ALA	0	-0.014	0.006	23.545	-0.410	-0.410	0.000	0.000	0.000	0.000
147	A	87	VAL	0	0.000	-0.006	23.625	-0.267	-0.267	0.000	0.000	0.000	0.000
148	A	88	ARG	1	0.857	0.918	24.805	9.118	9.118	0.000	0.000	0.000	0.000
149	A	89	ASN	0	-0.031	-0.013	20.437	-0.090	-0.090	0.000	0.000	0.000	0.000
150	A	90	ASP	0	0.017	0.026	19.364	-0.508	-0.508	0.000	0.000	0.000	0.000
151	A	91	GLU	-1	-0.868	-0.941	17.660	-12.794	-12.794	0.000	0.000	0.000	0.000
152	A	92	GLU	-1	-0.917	-0.952	18.612	-13.153	-13.153	0.000	0.000	0.000	0.000
153	A	93	LEU	0	0.003	-0.011	22.158	0.617	0.617	0.000	0.000	0.000	0.000
154	A	94	ASN	0	-0.006	-0.010	23.996	0.837	0.837	0.000	0.000	0.000	0.000
155	A	95	LYS	1	0.927	0.966	24.381	10.291	10.291	0.000	0.000	0.000	0.000
156	A	96	LEU	0	-0.040	-0.013	26.180	0.372	0.372	0.000	0.000	0.000	0.000
157	A	97	LEU	0	-0.021	-0.018	28.279	0.405	0.405	0.000	0.000	0.000	0.000
158	A	98	GLY	0	0.046	0.036	29.563	0.168	0.168	0.000	0.000	0.000	0.000
159	A	99	ARG	1	0.893	0.936	30.418	7.987	7.987	0.000	0.000	0.000	0.000
160	A	100	VAL	0	0.010	0.024	32.315	0.275	0.275	0.000	0.000	0.000	0.000
161	A	101	THR	0	0.009	0.003	33.708	-0.218	-0.218	0.000	0.000	0.000	0.000
162	A	102	ILE	0	0.003	0.011	31.128	0.151	0.151	0.000	0.000	0.000	0.000
163	A	103	ALA	0	0.031	0.008	35.300	0.014	0.014	0.000	0.000	0.000	0.000
164	A	104	GLN	0	0.021	-0.005	37.202	-0.169	-0.169	0.000	0.000	0.000	0.000
165	A	105	GLY	0	0.020	0.028	33.531	-0.144	-0.144	0.000	0.000	0.000	0.000
166	A	106	GLY	0	0.019	0.008	32.640	-0.228	-0.228	0.000	0.000	0.000	0.000
167	A	107	VAL	0	0.042	0.013	31.311	-0.095	-0.095	0.000	0.000	0.000	0.000
168	A	108	LEU	0	0.035	0.020	24.360	0.066	0.066	0.000	0.000	0.000	0.000
169	A	109	PRO	0	-0.031	-0.020	26.287	0.255	0.255	0.000	0.000	0.000	0.000
170	A	110	ASN	0	-0.001	0.005	26.252	-0.451	-0.451	0.000	0.000	0.000	0.000
171	A	111	ILE	0	0.021	0.015	27.467	0.367	0.367	0.000	0.000	0.000	0.000
172	A	112	GLN	0	0.026	0.015	27.785	-0.278	-0.278	0.000	0.000	0.000	0.000
173	A	113	SER	0	0.057	0.017	26.392	0.291	0.291	0.000	0.000	0.000	0.000
174	A	114	VAL	0	0.017	0.002	28.493	0.087	0.087	0.000	0.000	0.000	0.000
175	A	115	LEU	0	-0.040	-0.017	31.947	0.238	0.238	0.000	0.000	0.000	0.000
176	A	116	LEU	0	-0.018	0.012	27.729	0.130	0.130	0.000	0.000	0.000	0.000
177	A	117	PRO	0	-0.007	-0.020	32.170	0.184	0.184	0.000	0.000	0.000	0.000
178	A	118	LYS	1	0.905	0.958	32.390	7.932	7.932	0.000	0.000	0.000	0.000
179	A	119	LYS	0	0.065	0.047	30.447	0.275	0.275	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-71:MET)