FMO DATABASE

FMODB ID: G6L21

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	OptAll
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	-2073390.035266
FMO2-HF: Nuclear repulsion	1995882.230416
FMO2-HF: Total energy	-77507.804849
FMO2-MP2: Total energy	-77738.609727

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.
-9.48	-4.068	3.858	-4.079	-5.192	-0.027

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 : -0.004 / q_NPA : -0.003

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	-0.028	-0.007	3.878	1.330	2.668	-0.017	-0.749	-0.573	0.002
4	A	139	THR	0	-0.004	-0.001	7.012	-0.546	-0.546	0.000	0.000	0.000	0.000
5	A	140	LEU	0	-0.016	0.000	8.686	-0.091	-0.091	0.000	0.000	0.000	0.000
6	A	141	PRO	0	-0.004	0.014	12.111	-0.078	-0.078	0.000	0.000	0.000	0.000
7	A	142	ASP	-1	-0.816	-0.923	15.005	0.242	0.242	0.000	0.000	0.000	0.000
8	A	143	GLY	0	0.034	0.000	16.794	0.003	0.003	0.000	0.000	0.000	0.000
9	A	144	ALA	0	0.050	0.034	18.915	-0.021	-0.021	0.000	0.000	0.000	0.000
10	A	145	ALA	0	-0.025	-0.001	14.304	-0.008	-0.008	0.000	0.000	0.000	0.000
11	A	146	ALA	0	0.018	0.000	14.381	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	147	GLU	-1	-0.850	-0.923	15.458	0.036	0.036	0.000	0.000	0.000	0.000
13	A	148	SER	0	-0.051	-0.037	15.459	-0.032	-0.032	0.000	0.000	0.000	0.000
14	A	149	LEU	0	-0.047	-0.018	9.275	-0.015	-0.015	0.000	0.000	0.000	0.000
15	A	150	VAL	0	-0.013	-0.013	13.236	-0.075	-0.075	0.000	0.000	0.000	0.000
16	A	151	GLU	-1	-0.836	-0.917	15.682	-0.064	-0.064	0.000	0.000	0.000	0.000
17	A	152	SER	0	-0.087	-0.029	13.406	0.005	0.005	0.000	0.000	0.000	0.000
18	A	153	SER	0	-0.048	-0.040	13.612	-0.025	-0.025	0.000	0.000	0.000	0.000
19	A	154	GLU	-1	-0.877	-0.934	15.707	-0.103	-0.103	0.000	0.000	0.000	0.000
20	A	155	VAL	0	-0.025	-0.015	14.373	0.011	0.011	0.000	0.000	0.000	0.000
21	A	156	ALA	0	0.032	0.039	12.205	-0.043	-0.043	0.000	0.000	0.000	0.000
22	A	157	VAL	0	0.001	0.001	9.930	0.049	0.049	0.000	0.000	0.000	0.000
23	A	158	ILE	0	-0.015	-0.002	10.188	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	159	GLY	0	0.028	0.023	9.541	-0.039	-0.039	0.000	0.000	0.000	0.000
25	A	160	PHE	0	-0.025	-0.029	10.465	0.130	0.130	0.000	0.000	0.000	0.000
26	A	161	PHE	0	0.066	0.012	9.397	-0.046	-0.046	0.000	0.000	0.000	0.000
27	A	162	LYS	1	0.786	0.893	13.216	-0.018	-0.018	0.000	0.000	0.000	0.000
28	A	163	ASP	-1	-0.862	-0.931	13.571	0.253	0.253	0.000	0.000	0.000	0.000
29	A	164	VAL	0	0.012	0.009	7.524	-0.052	-0.052	0.000	0.000	0.000	0.000
30	A	165	GLU	-1	-0.952	-0.976	8.558	0.535	0.535	0.000	0.000	0.000	0.000
31	A	166	SER	0	0.007	0.002	10.756	-0.095	-0.095	0.000	0.000	0.000	0.000
32	A	167	ASP	-1	-0.920	-0.972	11.168	-0.052	-0.052	0.000	0.000	0.000	0.000
33	A	168	SER	0	0.000	-0.002	11.345	-0.049	-0.049	0.000	0.000	0.000	0.000
34	A	169	ALA	0	0.021	0.028	8.667	-0.087	-0.087	0.000	0.000	0.000	0.000
35	A	170	LYS	1	0.873	0.934	6.914	-0.150	-0.150	0.000	0.000	0.000	0.000
36	A	171	GLN	0	0.012	0.014	6.730	-0.203	-0.203	0.000	0.000	0.000	0.000
37	A	172	PHE	0	0.030	0.001	6.338	-0.186	-0.186	0.000	0.000	0.000	0.000
38	A	173	LEU	0	-0.024	-0.010	2.524	-0.824	-0.497	1.234	-0.379	-1.183	0.000
39	A	174	GLN	0	0.026	0.004	3.350	-1.636	-0.858	0.041	-0.387	-0.432	-0.003
40	A	175	ALA	0	-0.038	-0.017	5.755	0.088	0.088	0.000	0.000	0.000	0.000
41	A	176	ALA	0	-0.003	0.000	3.339	-0.196	0.060	0.016	-0.083	-0.189	0.000
42	A	177	GLU	-1	-0.976	-1.003	2.485	-6.913	-4.403	2.582	-2.430	-2.662	-0.026
43	A	178	ALA	0	-0.069	-0.027	3.980	0.421	0.500	0.003	-0.038	-0.043	0.000
44	A	179	ILE	0	-0.039	-0.023	6.897	0.322	0.322	0.000	0.000	0.000	0.000
45	A	180	ASP	-1	-0.880	-0.941	7.890	-1.106	-1.106	0.000	0.000	0.000	0.000
46	A	181	ASP	-1	-0.905	-0.939	9.178	-0.414	-0.414	0.000	0.000	0.000	0.000
47	A	182	ILE	0	-0.033	-0.011	9.666	0.154	0.154	0.000	0.000	0.000	0.000
48	A	183	PRO	0	-0.009	0.015	7.892	-0.265	-0.265	0.000	0.000	0.000	0.000
49	A	184	PHE	0	0.051	0.020	5.325	-0.058	0.066	-0.001	-0.013	-0.110	0.000
50	A	185	GLY	0	0.002	-0.004	6.690	0.271	0.271	0.000	0.000	0.000	0.000
51	A	186	ILE	0	-0.008	-0.007	6.009	-0.212	-0.212	0.000	0.000	0.000	0.000
52	A	187	THR	0	-0.020	-0.026	8.695	0.155	0.155	0.000	0.000	0.000	0.000
53	A	188	SER	0	0.029	-0.007	12.074	-0.020	-0.020	0.000	0.000	0.000	0.000
54	A	189	ASN	0	-0.072	-0.030	14.364	-0.050	-0.050	0.000	0.000	0.000	0.000
55	A	190	SER	0	0.058	0.018	17.444	-0.019	-0.019	0.000	0.000	0.000	0.000
56	A	191	ASP	-1	-0.878	-0.922	20.512	0.140	0.140	0.000	0.000	0.000	0.000
57	A	192	VAL	0	-0.016	-0.010	15.539	-0.025	-0.025	0.000	0.000	0.000	0.000
58	A	193	PHE	0	0.001	0.001	15.340	-0.031	-0.031	0.000	0.000	0.000	0.000
59	A	194	SER	0	-0.014	-0.013	19.087	-0.026	-0.026	0.000	0.000	0.000	0.000
60	A	195	LYS	1	0.727	0.874	20.175	-0.085	-0.085	0.000	0.000	0.000	0.000
61	A	196	TYR	0	0.028	0.016	18.227	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	197	GLN	0	-0.058	-0.023	20.826	-0.027	-0.027	0.000	0.000	0.000	0.000
63	A	198	LEU	0	0.008	0.029	17.376	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	199	ASP	-1	-0.821	-0.884	20.797	0.017	0.017	0.000	0.000	0.000	0.000
65	A	200	LYS	1	0.799	0.861	20.303	0.033	0.033	0.000	0.000	0.000	0.000
66	A	201	ASP	-1	-0.770	-0.894	15.354	0.081	0.081	0.000	0.000	0.000	0.000
67	A	202	GLY	0	0.012	0.009	14.817	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	203	VAL	0	-0.026	-0.007	11.159	0.007	0.007	0.000	0.000	0.000	0.000
69	A	204	VAL	0	-0.023	-0.002	13.583	0.016	0.016	0.000	0.000	0.000	0.000
70	A	205	LEU	0	-0.002	0.024	13.969	-0.031	-0.031	0.000	0.000	0.000	0.000
71	A	206	PHE	0	-0.007	-0.025	15.155	0.058	0.058	0.000	0.000	0.000	0.000
72	A	207	LYS	1	0.842	0.906	16.688	0.145	0.145	0.000	0.000	0.000	0.000
73	A	208	LYS	1	0.777	0.887	19.131	0.088	0.088	0.000	0.000	0.000	0.000
74	A	209	PHE	0	-0.020	-0.013	19.799	0.013	0.013	0.000	0.000	0.000	0.000
75	A	210	ASP	-1	-0.820	-0.916	23.876	-0.132	-0.132	0.000	0.000	0.000	0.000
76	A	211	GLU	-1	-0.814	-0.894	23.694	-0.130	-0.130	0.000	0.000	0.000	0.000
77	A	212	GLY	0	-0.005	0.026	22.935	0.008	0.008	0.000	0.000	0.000	0.000
78	A	213	ARG	1	0.824	0.884	19.956	0.053	0.053	0.000	0.000	0.000	0.000
79	A	214	ASN	0	0.000	-0.003	18.779	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	215	ASN	0	0.011	0.008	17.859	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	216	PHE	0	-0.038	-0.008	15.263	-0.015	-0.015	0.000	0.000	0.000	0.000
82	A	217	GLU	-1	-0.897	-0.952	17.338	-0.072	-0.072	0.000	0.000	0.000	0.000
83	A	218	GLY	0	-0.013	-0.017	19.038	0.000	0.000	0.000	0.000	0.000	0.000
84	A	219	GLU	-1	-0.910	-0.937	17.349	-0.119	-0.119	0.000	0.000	0.000	0.000
85	A	220	VAL	0	-0.004	0.001	11.734	-0.030	-0.030	0.000	0.000	0.000	0.000
86	A	221	THR	0	-0.039	-0.026	12.996	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	222	LYS	1	0.877	0.918	9.360	0.637	0.637	0.000	0.000	0.000	0.000
88	A	223	GLU	-1	-0.807	-0.912	11.431	-0.533	-0.533	0.000	0.000	0.000	0.000
89	A	224	ASN	0	-0.022	-0.014	14.498	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	225	LEU	0	0.003	0.013	9.784	0.011	0.011	0.000	0.000	0.000	0.000
91	A	226	LEU	0	-0.030	-0.010	9.837	-0.021	-0.021	0.000	0.000	0.000	0.000
92	A	227	ASP	-1	-0.945	-0.959	13.227	-0.250	-0.250	0.000	0.000	0.000	0.000
93	A	228	PHE	0	-0.008	-0.006	13.683	0.016	0.016	0.000	0.000	0.000	0.000
94	A	229	ILE	0	0.004	0.004	10.477	0.019	0.019	0.000	0.000	0.000	0.000
95	A	230	LYS	1	0.828	0.904	14.388	0.488	0.488	0.000	0.000	0.000	0.000
96	A	231	HIS	0	0.028	0.012	16.691	0.027	0.027	0.000	0.000	0.000	0.000
97	A	232	ASN	0	-0.089	-0.060	17.962	0.054	0.054	0.000	0.000	0.000	0.000
98	A	233	GLN	0	-0.028	0.004	13.499	0.052	0.052	0.000	0.000	0.000	0.000
99	A	234	LEU	0	-0.014	-0.007	17.565	0.011	0.011	0.000	0.000	0.000	0.000
100	A	235	PRO	0	-0.007	-0.011	20.876	0.011	0.011	0.000	0.000	0.000	0.000
101	A	236	LEU	0	-0.056	-0.024	24.010	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	237	VAL	0	-0.041	-0.026	27.087	0.005	0.005	0.000	0.000	0.000	0.000
103	A	238	ILE	0	-0.021	0.001	22.318	0.002	0.002	0.000	0.000	0.000	0.000
104	A	239	GLU	-1	-0.795	-0.877	26.806	-0.090	-0.090	0.000	0.000	0.000	0.000
105	A	240	PHE	0	-0.023	-0.021	26.078	-0.016	-0.016	0.000	0.000	0.000	0.000
106	A	241	THR	0	0.032	0.005	24.046	0.007	0.007	0.000	0.000	0.000	0.000
107	A	242	GLU	-1	-0.888	-0.956	23.673	-0.139	-0.139	0.000	0.000	0.000	0.000
108	A	243	GLN	0	0.012	0.012	17.240	-0.050	-0.050	0.000	0.000	0.000	0.000
109	A	244	THR	0	-0.013	-0.012	19.820	-0.031	-0.031	0.000	0.000	0.000	0.000
110	A	245	ALA	0	0.005	0.015	21.827	-0.015	-0.015	0.000	0.000	0.000	0.000
111	A	246	PRO	0	0.007	-0.001	18.673	0.002	0.002	0.000	0.000	0.000	0.000
112	A	247	LYS	1	0.883	0.936	15.389	0.365	0.365	0.000	0.000	0.000	0.000
113	A	248	ILE	0	0.003	0.006	19.628	0.004	0.004	0.000	0.000	0.000	0.000
114	A	249	PHE	0	-0.032	-0.016	23.194	0.011	0.011	0.000	0.000	0.000	0.000
115	A	250	GLY	0	0.003	0.004	19.687	0.004	0.004	0.000	0.000	0.000	0.000
116	A	251	GLY	0	0.033	0.013	20.685	0.000	0.000	0.000	0.000	0.000	0.000
117	A	252	GLU	-1	-0.861	-0.931	19.874	-0.255	-0.255	0.000	0.000	0.000	0.000
118	A	253	ILE	0	-0.011	-0.009	23.180	0.016	0.016	0.000	0.000	0.000	0.000
119	A	254	LYS	1	0.857	0.944	23.178	0.230	0.230	0.000	0.000	0.000	0.000
120	A	255	THR	0	-0.056	-0.018	27.854	0.007	0.007	0.000	0.000	0.000	0.000
121	A	256	HIS	0	0.005	-0.010	26.028	0.005	0.005	0.000	0.000	0.000	0.000
122	A	257	ILE	0	-0.026	-0.015	31.078	0.009	0.009	0.000	0.000	0.000	0.000
123	A	258	LEU	0	0.005	0.007	31.626	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	259	LEU	0	-0.027	-0.011	34.046	0.007	0.007	0.000	0.000	0.000	0.000
125	A	260	PHE	0	0.006	0.000	35.145	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	261	LEU	0	0.026	-0.008	35.857	0.006	0.006	0.000	0.000	0.000	0.000
127	A	262	PRO	0	0.000	0.008	37.228	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	263	LYS	1	0.868	0.905	31.236	0.084	0.084	0.000	0.000	0.000	0.000
129	A	264	SER	0	-0.049	-0.011	38.278	0.004	0.004	0.000	0.000	0.000	0.000
130	A	265	VAL	0	-0.078	-0.021	40.966	0.004	0.004	0.000	0.000	0.000	0.000
131	A	266	SER	0	0.006	-0.003	42.808	0.000	0.000	0.000	0.000	0.000	0.000
132	A	267	ASP	-1	-0.829	-0.929	43.098	-0.046	-0.046	0.000	0.000	0.000	0.000
133	A	268	TYR	0	0.080	0.045	33.464	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	269	ASP	-1	-0.820	-0.911	35.538	-0.064	-0.064	0.000	0.000	0.000	0.000
135	A	270	GLY	0	0.064	0.040	38.191	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	271	LYS	1	0.781	0.887	40.484	0.044	0.044	0.000	0.000	0.000	0.000
137	A	272	LEU	0	0.051	0.032	32.686	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	273	SER	0	-0.014	-0.013	35.770	-0.005	-0.005	0.000	0.000	0.000	0.000
139	A	274	ASN	0	-0.079	-0.035	37.413	0.000	0.000	0.000	0.000	0.000	0.000
140	A	275	PHE	0	0.011	0.006	32.403	0.000	0.000	0.000	0.000	0.000	0.000
141	A	276	LYS	1	0.896	0.935	32.334	0.065	0.065	0.000	0.000	0.000	0.000
142	A	277	THR	0	-0.030	-0.027	34.322	-0.001	-0.001	0.000	0.000	0.000	0.000
143	A	278	ALA	0	-0.037	-0.019	37.122	0.000	0.000	0.000	0.000	0.000	0.000
144	A	279	ALA	0	0.032	0.014	31.488	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	280	GLU	-1	-0.867	-0.943	31.813	-0.095	-0.095	0.000	0.000	0.000	0.000
146	A	281	SER	0	-0.053	-0.020	33.320	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	282	PHE	0	-0.067	-0.034	33.217	0.001	0.001	0.000	0.000	0.000	0.000
148	A	283	LYS	1	0.977	1.001	26.771	0.108	0.108	0.000	0.000	0.000	0.000
149	A	284	GLY	0	0.015	0.005	27.017	0.005	0.005	0.000	0.000	0.000	0.000
150	A	285	LYS	1	0.754	0.876	28.045	0.101	0.101	0.000	0.000	0.000	0.000
151	A	286	ILE	0	-0.003	-0.008	30.755	0.002	0.002	0.000	0.000	0.000	0.000
152	A	287	LEU	0	0.026	0.025	24.960	0.000	0.000	0.000	0.000	0.000	0.000
153	A	288	PHE	0	0.002	-0.006	28.621	0.008	0.008	0.000	0.000	0.000	0.000
154	A	289	ILE	0	0.011	0.018	27.626	-0.004	-0.004	0.000	0.000	0.000	0.000
155	A	290	PHE	0	-0.024	-0.018	29.441	0.010	0.010	0.000	0.000	0.000	0.000
156	A	291	ILE	0	0.017	0.004	30.721	-0.007	-0.007	0.000	0.000	0.000	0.000
157	A	292	ASP	-1	-0.758	-0.877	32.987	-0.062	-0.062	0.000	0.000	0.000	0.000
158	A	293	SER	0	0.023	-0.022	35.050	-0.002	-0.002	0.000	0.000	0.000	0.000
159	A	294	ASP	-1	-0.846	-0.922	38.151	-0.049	-0.049	0.000	0.000	0.000	0.000
160	A	295	HIS	0	-0.002	0.019	32.580	0.009	0.009	0.000	0.000	0.000	0.000
161	A	296	THR	0	-0.004	-0.020	36.054	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	297	ASP	-1	-0.883	-0.938	32.269	-0.085	-0.085	0.000	0.000	0.000	0.000
163	A	298	ASN	0	0.036	0.000	32.223	-0.009	-0.009	0.000	0.000	0.000	0.000
164	A	299	GLN	0	-0.007	0.005	34.574	0.000	0.000	0.000	0.000	0.000	0.000
165	A	300	ARG	1	0.861	0.922	35.053	0.075	0.075	0.000	0.000	0.000	0.000
166	A	301	ILE	0	0.008	0.003	31.227	-0.001	-0.001	0.000	0.000	0.000	0.000
167	A	302	LEU	0	-0.012	-0.008	35.433	0.000	0.000	0.000	0.000	0.000	0.000
168	A	303	GLU	-1	-0.846	-0.914	38.822	-0.066	-0.066	0.000	0.000	0.000	0.000
169	A	304	PHE	0	-0.065	-0.020	34.956	0.001	0.001	0.000	0.000	0.000	0.000
170	A	305	PHE	0	0.000	-0.002	33.657	0.000	0.000	0.000	0.000	0.000	0.000
171	A	306	GLY	0	-0.025	0.001	39.199	0.003	0.003	0.000	0.000	0.000	0.000
172	A	307	LEU	0	-0.053	-0.025	39.816	0.002	0.002	0.000	0.000	0.000	0.000
173	A	308	LYS	1	0.864	0.931	42.832	0.044	0.044	0.000	0.000	0.000	0.000
174	A	309	LYS	1	0.824	0.892	41.461	0.052	0.052	0.000	0.000	0.000	0.000
175	A	310	GLU	-1	-0.847	-0.925	44.037	-0.045	-0.045	0.000	0.000	0.000	0.000
176	A	311	GLU	-1	-0.966	-0.977	45.519	-0.050	-0.050	0.000	0.000	0.000	0.000
177	A	312	CYS	0	-0.031	0.015	41.586	-0.004	-0.004	0.000	0.000	0.000	0.000
178	A	313	PRO	0	-0.021	-0.028	41.165	0.003	0.003	0.000	0.000	0.000	0.000
179	A	314	ALA	0	-0.027	0.001	40.718	0.003	0.003	0.000	0.000	0.000	0.000
180	A	315	VAL	0	0.012	0.004	37.673	-0.003	-0.003	0.000	0.000	0.000	0.000
181	A	316	ARG	1	0.830	0.925	36.798	0.074	0.074	0.000	0.000	0.000	0.000
182	A	317	LEU	0	0.019	0.006	35.625	-0.003	-0.003	0.000	0.000	0.000	0.000
183	A	318	ILE	0	-0.017	-0.006	32.116	0.004	0.004	0.000	0.000	0.000	0.000
184	A	319	THR	0	0.037	0.023	32.062	-0.003	-0.003	0.000	0.000	0.000	0.000
185	A	320	LEU	0	-0.024	0.005	26.846	0.004	0.004	0.000	0.000	0.000	0.000
186	A	321	GLU	-1	-0.819	-0.894	30.206	-0.108	-0.108	0.000	0.000	0.000	0.000
187	A	322	GLU	-1	-0.992	-0.988	27.013	-0.168	-0.168	0.000	0.000	0.000	0.000
188	A	335	THR	0	0.013	-0.018	37.224	-0.002	-0.002	0.000	0.000	0.000	0.000
189	A	336	ALA	0	0.021	0.003	39.095	-0.003	-0.003	0.000	0.000	0.000	0.000
190	A	337	GLU	-1	-0.830	-0.888	41.465	-0.072	-0.072	0.000	0.000	0.000	0.000
191	A	338	ARG	1	0.826	0.880	34.374	0.096	0.096	0.000	0.000	0.000	0.000
192	A	339	ILE	0	0.028	0.012	37.000	-0.004	-0.004	0.000	0.000	0.000	0.000
193	A	340	THR	0	-0.021	-0.019	38.408	0.000	0.000	0.000	0.000	0.000	0.000
194	A	341	GLU	-1	-0.851	-0.908	38.725	-0.085	-0.085	0.000	0.000	0.000	0.000
195	A	342	PHE	0	-0.020	0.002	31.774	0.000	0.000	0.000	0.000	0.000	0.000
196	A	343	CYS	0	-0.041	-0.031	36.777	-0.002	-0.002	0.000	0.000	0.000	0.000
197	A	344	HIS	0	-0.027	-0.013	39.410	0.001	0.001	0.000	0.000	0.000	0.000
198	A	345	ARG	1	0.801	0.890	35.002	0.108	0.108	0.000	0.000	0.000	0.000
199	A	346	PHE	0	-0.019	-0.008	38.389	-0.001	-0.001	0.000	0.000	0.000	0.000
200	A	347	LEU	0	-0.041	-0.005	39.736	0.001	0.001	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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