FMO DATABASE

FMODB ID: V58G1

Calculation Name: 4JU5-A-Xray372

Preferred Name: Protein disulfide-isomerase

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 4JU5

Chain ID: A

ChEMBL ID: CHEMBL5422

UniProt ID: P07237

Base Structure: X-ray

Registration Date: 2023-06-21

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	OptH
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	200
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2067051.349268
FMO2-HF: Nuclear repulsion	1989544.890026
FMO2-HF: Total energy	-77506.459241
FMO2-MP2: Total energy	-77737.177396

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:136:ALA)

Summations of interaction energy for fragment #1(A:136:ALA)

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.
-7.884	-3.162	1.301	-2.59	-3.434	-0.013

Interaction energy analysis for fragmet #1(A:136:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.003 / q_NPA : 0.000

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	138	THR	0	-0.056	-0.012	3.805	1.439	2.841	-0.022	-0.733	-0.648	0.002
4	A	139	THR	0	0.001	-0.001	6.411	-0.728	-0.728	0.000	0.000	0.000	0.000
5	A	140	LEU	0	-0.002	0.000	8.874	-0.120	-0.120	0.000	0.000	0.000	0.000
6	A	141	PRO	0	0.022	0.032	12.325	-0.081	-0.081	0.000	0.000	0.000	0.000
7	A	142	ASP	-1	-0.844	-0.913	15.261	0.268	0.268	0.000	0.000	0.000	0.000
8	A	143	GLY	0	0.027	-0.007	17.092	0.004	0.004	0.000	0.000	0.000	0.000
9	A	144	ALA	0	0.031	0.017	18.961	-0.023	-0.023	0.000	0.000	0.000	0.000
10	A	145	ALA	0	0.019	0.010	13.650	-0.016	-0.016	0.000	0.000	0.000	0.000
11	A	146	ALA	0	-0.002	0.000	14.315	-0.013	-0.013	0.000	0.000	0.000	0.000
12	A	147	GLU	-1	-0.910	-0.966	15.421	0.038	0.038	0.000	0.000	0.000	0.000
13	A	148	SER	0	-0.022	-0.007	15.264	-0.033	-0.033	0.000	0.000	0.000	0.000
14	A	149	LEU	0	-0.014	-0.003	9.389	-0.022	-0.022	0.000	0.000	0.000	0.000
15	A	150	VAL	0	-0.023	-0.024	13.179	-0.077	-0.077	0.000	0.000	0.000	0.000
16	A	151	GLU	-1	-0.921	-0.968	15.740	-0.054	-0.054	0.000	0.000	0.000	0.000
17	A	152	SER	0	-0.083	-0.025	13.165	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	153	SER	0	-0.049	-0.023	13.283	-0.019	-0.019	0.000	0.000	0.000	0.000
19	A	154	GLU	-1	-0.919	-0.948	15.377	-0.119	-0.119	0.000	0.000	0.000	0.000
20	A	155	VAL	0	-0.009	-0.012	14.098	0.016	0.016	0.000	0.000	0.000	0.000
21	A	156	ALA	0	0.019	0.019	12.232	-0.054	-0.054	0.000	0.000	0.000	0.000
22	A	157	VAL	0	0.011	0.019	10.210	0.062	0.062	0.000	0.000	0.000	0.000
23	A	158	ILE	0	-0.029	-0.004	10.254	-0.015	-0.015	0.000	0.000	0.000	0.000
24	A	159	GLY	0	0.024	0.007	9.964	-0.042	-0.042	0.000	0.000	0.000	0.000
25	A	160	PHE	0	-0.055	-0.044	10.893	0.148	0.148	0.000	0.000	0.000	0.000
26	A	161	PHE	0	0.050	0.015	10.313	-0.054	-0.054	0.000	0.000	0.000	0.000
27	A	162	LYS	1	0.902	0.956	13.372	-0.051	-0.051	0.000	0.000	0.000	0.000
28	A	163	ASP	-1	-0.900	-0.943	14.094	0.291	0.291	0.000	0.000	0.000	0.000
29	A	164	VAL	0	0.020	0.003	8.006	-0.046	-0.046	0.000	0.000	0.000	0.000
30	A	165	GLU	-1	-0.972	-0.991	9.252	0.508	0.508	0.000	0.000	0.000	0.000
31	A	166	SER	0	0.019	0.016	11.290	-0.079	-0.079	0.000	0.000	0.000	0.000
32	A	167	ASP	-1	-0.880	-0.952	11.940	-0.061	-0.061	0.000	0.000	0.000	0.000
33	A	168	SER	0	0.004	-0.003	12.067	-0.050	-0.050	0.000	0.000	0.000	0.000
34	A	169	ALA	0	0.021	0.023	9.504	-0.093	-0.093	0.000	0.000	0.000	0.000
35	A	170	LYS	1	0.904	0.943	7.737	-0.223	-0.223	0.000	0.000	0.000	0.000
36	A	171	GLN	0	-0.026	-0.011	7.504	-0.236	-0.236	0.000	0.000	0.000	0.000
37	A	172	PHE	0	0.024	0.001	6.632	-0.217	-0.217	0.000	0.000	0.000	0.000
38	A	173	LEU	0	-0.020	-0.013	2.950	-0.750	-0.248	0.148	-0.134	-0.515	0.000
39	A	174	GLN	0	0.029	0.023	3.343	-2.094	-1.214	0.034	-0.448	-0.466	-0.004
40	A	175	ALA	0	-0.056	-0.032	5.977	-0.027	-0.027	0.000	0.000	0.000	0.000
41	A	176	ALA	0	-0.044	-0.023	3.183	-0.142	0.108	0.022	-0.077	-0.196	0.000
42	A	177	GLU	-1	-0.954	-0.984	2.428	-4.558	-3.027	1.121	-1.171	-1.481	-0.011
43	A	178	ALA	0	-0.073	-0.022	4.533	0.461	0.492	-0.001	-0.014	-0.016	0.000
44	A	179	ILE	0	-0.047	-0.025	7.145	0.335	0.335	0.000	0.000	0.000	0.000
45	A	180	ASP	-1	-0.881	-0.937	7.291	-1.279	-1.279	0.000	0.000	0.000	0.000
46	A	181	ASP	-1	-1.004	-1.009	8.946	-0.481	-0.481	0.000	0.000	0.000	0.000
47	A	182	ILE	0	-0.066	-0.035	9.733	0.148	0.148	0.000	0.000	0.000	0.000
48	A	183	PRO	0	-0.002	0.019	7.620	-0.287	-0.287	0.000	0.000	0.000	0.000
49	A	184	PHE	0	0.050	0.019	5.288	0.043	0.169	-0.001	-0.013	-0.112	0.000
50	A	185	GLY	0	-0.013	-0.007	6.643	0.355	0.355	0.000	0.000	0.000	0.000
51	A	186	ILE	0	0.011	0.009	6.225	-0.234	-0.234	0.000	0.000	0.000	0.000
52	A	187	THR	0	-0.020	-0.035	8.872	0.163	0.163	0.000	0.000	0.000	0.000
53	A	188	SER	0	0.050	0.017	12.209	-0.025	-0.025	0.000	0.000	0.000	0.000
54	A	189	ASN	0	-0.065	-0.046	14.468	-0.067	-0.067	0.000	0.000	0.000	0.000
55	A	190	SER	0	0.007	-0.016	17.418	-0.021	-0.021	0.000	0.000	0.000	0.000
56	A	191	ASP	-1	-0.894	-0.938	20.350	0.130	0.130	0.000	0.000	0.000	0.000
57	A	192	VAL	0	-0.028	-0.021	15.783	-0.026	-0.026	0.000	0.000	0.000	0.000
58	A	193	PHE	0	-0.020	-0.017	15.762	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	194	SER	0	0.019	0.015	19.570	-0.027	-0.027	0.000	0.000	0.000	0.000
60	A	195	LYS	1	0.819	0.951	20.257	-0.094	-0.094	0.000	0.000	0.000	0.000
61	A	196	TYR	0	-0.022	-0.015	17.981	-0.022	-0.022	0.000	0.000	0.000	0.000
62	A	197	GLN	0	-0.026	-0.004	21.459	-0.029	-0.029	0.000	0.000	0.000	0.000
63	A	198	LEU	0	0.008	0.024	18.087	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	199	ASP	-1	-0.906	-0.956	21.563	0.020	0.020	0.000	0.000	0.000	0.000
65	A	200	LYS	1	0.883	0.939	20.794	0.041	0.041	0.000	0.000	0.000	0.000
66	A	201	ASP	-1	-0.821	-0.936	15.935	0.075	0.075	0.000	0.000	0.000	0.000
67	A	202	GLY	0	-0.004	-0.008	15.432	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	203	VAL	0	-0.012	0.007	11.787	0.010	0.010	0.000	0.000	0.000	0.000
69	A	204	VAL	0	-0.013	0.008	14.190	0.010	0.010	0.000	0.000	0.000	0.000
70	A	205	LEU	0	-0.008	0.012	14.394	-0.034	-0.034	0.000	0.000	0.000	0.000
71	A	206	PHE	0	-0.010	-0.037	15.098	0.058	0.058	0.000	0.000	0.000	0.000
72	A	207	LYS	1	0.888	0.947	16.703	0.140	0.140	0.000	0.000	0.000	0.000
73	A	208	LYS	1	0.866	0.942	18.887	0.103	0.103	0.000	0.000	0.000	0.000
74	A	209	PHE	0	-0.005	-0.003	19.956	0.012	0.012	0.000	0.000	0.000	0.000
75	A	210	ASP	-1	-0.844	-0.924	23.991	-0.135	-0.135	0.000	0.000	0.000	0.000
76	A	211	GLU	-1	-0.855	-0.940	24.005	-0.126	-0.126	0.000	0.000	0.000	0.000
77	A	212	GLY	0	-0.016	0.018	22.950	0.010	0.010	0.000	0.000	0.000	0.000
78	A	213	ARG	1	0.792	0.846	20.106	0.051	0.051	0.000	0.000	0.000	0.000
79	A	214	ASN	0	-0.012	-0.004	19.317	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	215	ASN	0	0.056	0.038	18.458	-0.017	-0.017	0.000	0.000	0.000	0.000
81	A	216	PHE	0	-0.022	-0.007	15.844	-0.008	-0.008	0.000	0.000	0.000	0.000
82	A	217	GLU	-1	-0.943	-0.972	17.930	-0.073	-0.073	0.000	0.000	0.000	0.000
83	A	218	GLY	0	-0.016	-0.012	20.092	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	219	GLU	-1	-0.913	-0.939	17.829	-0.123	-0.123	0.000	0.000	0.000	0.000
85	A	220	VAL	0	0.000	-0.014	12.347	-0.034	-0.034	0.000	0.000	0.000	0.000
86	A	221	THR	0	-0.043	-0.015	14.084	0.013	0.013	0.000	0.000	0.000	0.000
87	A	222	LYS	1	1.007	0.999	9.349	0.640	0.640	0.000	0.000	0.000	0.000
88	A	223	GLU	-1	-0.891	-0.973	11.748	-0.467	-0.467	0.000	0.000	0.000	0.000
89	A	224	ASN	0	-0.015	-0.002	14.945	0.000	0.000	0.000	0.000	0.000	0.000
90	A	225	LEU	0	-0.032	-0.004	10.036	0.009	0.009	0.000	0.000	0.000	0.000
91	A	226	LEU	0	-0.027	-0.018	10.091	-0.014	-0.014	0.000	0.000	0.000	0.000
92	A	227	ASP	-1	-0.885	-0.935	13.508	-0.261	-0.261	0.000	0.000	0.000	0.000
93	A	228	PHE	0	-0.072	-0.030	14.468	0.026	0.026	0.000	0.000	0.000	0.000
94	A	229	ILE	0	-0.002	-0.012	10.858	0.024	0.024	0.000	0.000	0.000	0.000
95	A	230	LYS	1	0.858	0.939	14.809	0.490	0.490	0.000	0.000	0.000	0.000
96	A	231	HIS	0	0.017	0.019	17.477	0.027	0.027	0.000	0.000	0.000	0.000
97	A	232	ASN	0	-0.077	-0.049	18.482	0.052	0.052	0.000	0.000	0.000	0.000
98	A	233	GLN	0	0.014	0.025	14.052	0.043	0.043	0.000	0.000	0.000	0.000
99	A	234	LEU	0	-0.009	-0.005	17.819	0.004	0.004	0.000	0.000	0.000	0.000
100	A	235	PRO	0	-0.014	-0.010	20.908	0.011	0.011	0.000	0.000	0.000	0.000
101	A	236	LEU	0	-0.044	-0.024	24.165	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	237	VAL	0	-0.066	-0.031	27.321	0.003	0.003	0.000	0.000	0.000	0.000
103	A	238	ILE	0	0.005	0.013	22.526	0.003	0.003	0.000	0.000	0.000	0.000
104	A	239	GLU	-1	-0.847	-0.929	26.425	-0.099	-0.099	0.000	0.000	0.000	0.000
105	A	240	PHE	0	-0.019	-0.035	26.007	-0.015	-0.015	0.000	0.000	0.000	0.000
106	A	241	THR	0	0.049	0.024	24.183	0.002	0.002	0.000	0.000	0.000	0.000
107	A	242	GLU	-1	-0.853	-0.947	23.510	-0.145	-0.145	0.000	0.000	0.000	0.000
108	A	243	GLN	0	-0.032	-0.016	16.478	-0.040	-0.040	0.000	0.000	0.000	0.000
109	A	244	THR	0	-0.007	-0.003	19.554	-0.038	-0.038	0.000	0.000	0.000	0.000
110	A	245	ALA	0	0.008	0.011	21.842	-0.012	-0.012	0.000	0.000	0.000	0.000
111	A	246	PRO	0	-0.006	-0.009	18.578	0.004	0.004	0.000	0.000	0.000	0.000
112	A	247	LYS	1	0.916	0.962	15.668	0.362	0.362	0.000	0.000	0.000	0.000
113	A	248	ILE	0	0.002	0.014	19.694	0.004	0.004	0.000	0.000	0.000	0.000
114	A	249	PHE	0	-0.040	-0.025	23.368	0.009	0.009	0.000	0.000	0.000	0.000
115	A	250	GLY	0	-0.012	-0.001	20.036	0.006	0.006	0.000	0.000	0.000	0.000
116	A	251	GLY	0	0.022	0.033	20.956	-0.012	-0.012	0.000	0.000	0.000	0.000
117	A	252	GLU	-1	-0.837	-0.936	20.474	-0.261	-0.261	0.000	0.000	0.000	0.000
118	A	253	ILE	0	-0.026	-0.011	23.698	0.017	0.017	0.000	0.000	0.000	0.000
119	A	254	LYS	1	0.870	0.933	24.458	0.222	0.222	0.000	0.000	0.000	0.000
120	A	255	THR	0	0.002	0.023	28.493	0.010	0.010	0.000	0.000	0.000	0.000
121	A	256	HIS	0	0.017	0.002	26.335	0.006	0.006	0.000	0.000	0.000	0.000
122	A	257	ILE	0	-0.016	-0.007	31.443	0.009	0.009	0.000	0.000	0.000	0.000
123	A	258	LEU	0	0.015	-0.001	31.950	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	259	LEU	0	-0.035	-0.021	34.064	0.008	0.008	0.000	0.000	0.000	0.000
125	A	260	PHE	0	0.010	-0.003	34.965	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	261	LEU	0	-0.013	-0.026	35.885	0.006	0.006	0.000	0.000	0.000	0.000
127	A	262	PRO	0	0.013	0.016	36.805	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	263	LYS	1	0.911	0.942	31.123	0.086	0.086	0.000	0.000	0.000	0.000
129	A	264	SER	0	-0.047	-0.011	38.031	0.004	0.004	0.000	0.000	0.000	0.000
130	A	265	VAL	0	-0.084	-0.015	40.792	0.004	0.004	0.000	0.000	0.000	0.000
131	A	266	SER	0	0.009	-0.001	42.515	0.000	0.000	0.000	0.000	0.000	0.000
132	A	267	ASP	-1	-0.879	-0.952	43.457	-0.047	-0.047	0.000	0.000	0.000	0.000
133	A	268	TYR	0	0.049	0.032	33.504	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	269	ASP	-1	-0.842	-0.946	35.696	-0.062	-0.062	0.000	0.000	0.000	0.000
135	A	270	GLY	0	0.006	0.016	38.237	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	271	LYS	1	0.833	0.899	40.483	0.048	0.048	0.000	0.000	0.000	0.000
137	A	272	LEU	0	0.007	0.010	32.719	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	273	SER	0	-0.036	-0.018	35.771	-0.006	-0.006	0.000	0.000	0.000	0.000
139	A	274	ASN	0	0.013	0.001	37.447	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	275	PHE	0	-0.011	0.000	32.242	0.000	0.000	0.000	0.000	0.000	0.000
141	A	276	LYS	1	0.992	0.996	32.043	0.072	0.072	0.000	0.000	0.000	0.000
142	A	277	THR	0	0.004	0.004	34.371	-0.001	-0.001	0.000	0.000	0.000	0.000
143	A	278	ALA	0	-0.035	-0.025	37.212	0.000	0.000	0.000	0.000	0.000	0.000
144	A	279	ALA	0	0.019	0.010	31.606	-0.002	-0.002	0.000	0.000	0.000	0.000
145	A	280	GLU	-1	-0.935	-0.966	32.400	-0.092	-0.092	0.000	0.000	0.000	0.000
146	A	281	SER	0	-0.053	-0.024	33.916	0.000	0.000	0.000	0.000	0.000	0.000
147	A	282	PHE	0	-0.038	-0.019	33.885	0.002	0.002	0.000	0.000	0.000	0.000
148	A	283	LYS	1	1.056	1.050	26.542	0.121	0.121	0.000	0.000	0.000	0.000
149	A	284	GLY	0	0.002	-0.003	27.488	0.004	0.004	0.000	0.000	0.000	0.000
150	A	285	LYS	1	0.778	0.894	28.497	0.099	0.099	0.000	0.000	0.000	0.000
151	A	286	ILE	0	-0.013	-0.020	31.334	0.000	0.000	0.000	0.000	0.000	0.000
152	A	287	LEU	0	0.024	0.028	24.982	0.002	0.002	0.000	0.000	0.000	0.000
153	A	288	PHE	0	-0.015	-0.015	28.881	0.007	0.007	0.000	0.000	0.000	0.000
154	A	289	ILE	0	0.014	0.015	27.579	-0.007	-0.007	0.000	0.000	0.000	0.000
155	A	290	PHE	0	-0.037	-0.009	29.278	0.010	0.010	0.000	0.000	0.000	0.000
156	A	291	ILE	0	0.029	0.011	30.638	-0.008	-0.008	0.000	0.000	0.000	0.000
157	A	292	ASP	-1	-0.794	-0.903	32.803	-0.065	-0.065	0.000	0.000	0.000	0.000
158	A	293	SER	0	-0.001	-0.062	34.871	-0.002	-0.002	0.000	0.000	0.000	0.000
159	A	294	ASP	-1	-0.895	-0.947	38.064	-0.054	-0.054	0.000	0.000	0.000	0.000
160	A	295	HIS	0	-0.026	0.008	33.298	0.003	0.003	0.000	0.000	0.000	0.000
161	A	296	THR	0	-0.012	-0.027	36.058	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	297	ASP	-1	-0.967	-0.977	31.637	-0.094	-0.094	0.000	0.000	0.000	0.000
163	A	298	ASN	0	0.066	0.026	32.139	-0.012	-0.012	0.000	0.000	0.000	0.000
164	A	299	GLN	0	-0.015	-0.016	34.590	0.000	0.000	0.000	0.000	0.000	0.000
165	A	300	ARG	1	0.924	0.967	34.995	0.081	0.081	0.000	0.000	0.000	0.000
166	A	301	ILE	0	0.031	0.016	30.886	0.000	0.000	0.000	0.000	0.000	0.000
167	A	302	LEU	0	0.000	0.001	35.408	0.000	0.000	0.000	0.000	0.000	0.000
168	A	303	GLU	-1	-0.910	-0.956	38.692	-0.067	-0.067	0.000	0.000	0.000	0.000
169	A	304	PHE	0	-0.069	-0.024	35.611	0.001	0.001	0.000	0.000	0.000	0.000
170	A	305	PHE	0	-0.056	-0.028	34.062	0.000	0.000	0.000	0.000	0.000	0.000
171	A	306	GLY	0	-0.040	-0.013	39.614	0.003	0.003	0.000	0.000	0.000	0.000
172	A	307	LEU	0	-0.037	-0.016	39.897	0.003	0.003	0.000	0.000	0.000	0.000
173	A	308	LYS	1	0.865	0.923	42.743	0.046	0.046	0.000	0.000	0.000	0.000
174	A	309	LYS	1	0.992	0.975	42.063	0.052	0.052	0.000	0.000	0.000	0.000
175	A	310	GLU	-1	-0.863	-0.932	43.871	-0.048	-0.048	0.000	0.000	0.000	0.000
176	A	311	GLU	-1	-0.956	-0.961	45.426	-0.054	-0.054	0.000	0.000	0.000	0.000
177	A	312	CYS	0	-0.026	0.046	41.478	-0.004	-0.004	0.000	0.000	0.000	0.000
178	A	313	PRO	0	-0.004	-0.027	41.297	0.003	0.003	0.000	0.000	0.000	0.000
179	A	314	ALA	0	-0.015	0.011	40.734	0.003	0.003	0.000	0.000	0.000	0.000
180	A	315	VAL	0	0.021	0.008	37.931	-0.004	-0.004	0.000	0.000	0.000	0.000
181	A	316	ARG	1	0.908	0.962	37.169	0.077	0.077	0.000	0.000	0.000	0.000
182	A	317	LEU	0	-0.005	0.009	35.620	-0.004	-0.004	0.000	0.000	0.000	0.000
183	A	318	ILE	0	-0.017	-0.009	32.398	0.004	0.004	0.000	0.000	0.000	0.000
184	A	319	THR	0	0.016	0.016	32.911	-0.004	-0.004	0.000	0.000	0.000	0.000
185	A	320	LEU	0	-0.038	-0.009	27.227	0.003	0.003	0.000	0.000	0.000	0.000
186	A	321	GLU	-1	-0.860	-0.933	30.905	-0.110	-0.110	0.000	0.000	0.000	0.000
187	A	322	GLU	-1	-0.989	-0.990	28.014	-0.166	-0.166	0.000	0.000	0.000	0.000
188	A	335	THR	0	-0.001	-0.027	37.438	-0.002	-0.002	0.000	0.000	0.000	0.000
189	A	336	ALA	0	0.018	-0.003	39.310	-0.003	-0.003	0.000	0.000	0.000	0.000
190	A	337	GLU	-1	-0.837	-0.911	41.909	-0.074	-0.074	0.000	0.000	0.000	0.000
191	A	338	ARG	1	0.828	0.879	34.602	0.096	0.096	0.000	0.000	0.000	0.000
192	A	339	ILE	0	0.025	0.015	37.467	-0.003	-0.003	0.000	0.000	0.000	0.000
193	A	340	THR	0	-0.008	-0.003	38.777	0.000	0.000	0.000	0.000	0.000	0.000
194	A	341	GLU	-1	-0.846	-0.896	39.160	-0.085	-0.085	0.000	0.000	0.000	0.000
195	A	342	PHE	0	-0.034	-0.002	32.780	0.000	0.000	0.000	0.000	0.000	0.000
196	A	343	CYS	0	-0.009	-0.015	37.111	-0.002	-0.002	0.000	0.000	0.000	0.000
197	A	344	HIS	0	-0.070	-0.006	39.496	0.002	0.002	0.000	0.000	0.000	0.000
198	A	345	ARG	1	0.851	0.914	35.300	0.108	0.108	0.000	0.000	0.000	0.000
199	A	346	PHE	0	-0.027	-0.011	38.929	-0.001	-0.001	0.000	0.000	0.000	0.000
200	A	347	LEU	0	-0.012	-0.001	40.145	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:136:ALA)