FMO DATABASE

FMODB ID: ZN25N

Calculation Name: 1UN2-A-Xray372

Preferred Name: Thiol:disulfide interchange protein DsbA

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1UN2

Chain ID: A

ChEMBL ID: CHEMBL3559645

UniProt ID: P0AEG4

Base Structure: X-ray

Registration Date: 2023-09-26

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	OptHSide
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	185
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2018645.490447
FMO2-HF: Nuclear repulsion	1945109.793761
FMO2-HF: Total energy	-73535.696686
FMO2-MP2: Total energy	-73748.469141

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:1:GLN)

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

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.
-21.498	-23.111	17.693	-6.506	-9.573	0.038

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.016 / q_NPA : 0.011

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	ILE	0	-0.011	0.006	3.738	-4.250	-2.568	0.019	-0.796	-0.905	0.002
4	A	4	ARG	1	0.887	0.925	6.107	2.921	2.921	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.050	-0.059	8.075	0.835	0.835	0.000	0.000	0.000	0.000
6	A	6	ALA	0	0.105	0.046	8.321	-0.579	-0.579	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.008	-0.001	8.368	0.076	0.076	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.773	-0.847	4.436	-5.059	-4.947	-0.001	-0.005	-0.106	0.000
9	A	9	ILE	0	-0.010	-0.009	3.869	-2.864	-2.589	0.002	-0.096	-0.182	0.000
10	A	10	ARG	1	0.811	0.880	6.167	1.695	1.695	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.898	-0.952	2.471	-4.621	-3.763	0.396	-0.444	-0.811	-0.003
12	A	12	VAL	0	-0.042	-0.015	2.400	1.836	2.599	4.305	-1.359	-3.709	0.001
13	A	13	PHE	0	0.024	-0.005	3.440	2.614	2.579	0.067	0.249	-0.281	0.001
14	A	14	ILE	0	-0.011	-0.008	5.841	0.689	0.689	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.105	-0.062	1.779	-10.163	-15.781	12.911	-3.993	-3.299	0.037
16	A	16	ALA	0	-0.011	0.008	5.046	-0.366	-0.312	-0.001	-0.001	-0.051	0.000
17	A	17	GLY	0	-0.057	-0.027	7.446	-0.625	-0.625	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.085	-0.022	9.682	-0.340	-0.340	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.913	0.936	9.937	-0.389	-0.389	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.050	0.005	10.933	-0.139	-0.139	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.914	-0.945	11.669	-0.238	-0.238	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.828	-0.913	14.442	0.306	0.306	0.000	0.000	0.000	0.000
23	A	23	TYR	0	0.016	0.011	10.275	-0.107	-0.107	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.762	-0.855	13.086	-0.787	-0.787	0.000	0.000	0.000	0.000
25	A	25	ALA	0	-0.009	0.005	15.109	-0.011	-0.011	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.002	-0.001	16.003	0.001	0.001	0.000	0.000	0.000	0.000
27	A	27	TRP	0	0.003	0.007	12.787	-0.040	-0.040	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.058	-0.046	16.537	-0.031	-0.031	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.039	-0.011	19.883	0.054	0.054	0.000	0.000	0.000	0.000
30	A	30	PHE	0	0.001	-0.016	21.980	-0.026	-0.026	0.000	0.000	0.000	0.000
31	A	31	VAL	0	0.050	0.009	22.670	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	32	VAL	0	0.043	0.041	17.839	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.972	0.986	20.940	0.302	0.302	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.072	-0.033	23.180	0.000	0.000	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.052	0.014	20.815	0.003	0.003	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.033	-0.004	19.398	-0.010	-0.010	0.000	0.000	0.000	0.000
37	A	37	ALA	0	-0.009	0.007	22.026	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	38	GLN	0	0.015	0.001	25.684	0.011	0.011	0.000	0.000	0.000	0.000
39	A	39	GLN	0	0.007	-0.004	18.974	0.000	0.000	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.895	-0.934	24.054	-0.397	-0.397	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.801	0.880	25.570	0.209	0.209	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.022	0.013	26.760	0.016	0.016	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.002	0.006	25.445	0.013	0.013	0.000	0.000	0.000	0.000
44	A	44	ALA	0	-0.004	-0.008	27.586	0.014	0.014	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.837	-0.901	30.598	-0.178	-0.178	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.045	-0.012	29.346	0.016	0.016	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.097	-0.039	32.218	0.005	0.005	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.011	0.001	24.567	0.003	0.003	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.951	0.969	28.713	0.191	0.191	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.024	-0.014	25.040	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.052	0.015	20.055	0.015	0.015	0.000	0.000	0.000	0.000
52	A	52	PRO	0	0.049	-0.013	20.958	-0.016	-0.016	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.040	-0.010	22.545	0.021	0.021	0.000	0.000	0.000	0.000
54	A	54	MET	0	-0.008	0.011	24.531	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	55	PHE	0	0.033	0.011	27.000	0.008	0.008	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.023	0.016	29.494	0.002	0.002	0.000	0.000	0.000	0.000
57	A	57	ASN	0	0.033	0.002	32.137	0.002	0.002	0.000	0.000	0.000	0.000
58	A	58	GLY	0	-0.008	0.005	32.616	0.002	0.002	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.873	0.960	33.995	0.088	0.088	0.000	0.000	0.000	0.000
60	A	60	TYR	0	0.037	0.018	34.809	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	61	GLN	0	0.000	0.018	30.736	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.005	-0.013	29.348	0.011	0.011	0.000	0.000	0.000	0.000
63	A	63	ASN	0	-0.061	-0.042	30.982	-0.025	-0.025	0.000	0.000	0.000	0.000
64	A	64	PRO	0	0.045	-0.001	27.923	0.012	0.012	0.000	0.000	0.000	0.000
65	A	65	GLN	0	0.012	-0.003	30.482	0.013	0.013	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.031	0.001	33.129	0.006	0.006	0.000	0.000	0.000	0.000
67	A	67	MET	0	-0.092	-0.019	30.941	0.009	0.009	0.000	0.000	0.000	0.000
68	A	68	ASP	-1	-0.853	-0.904	34.626	-0.036	-0.036	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.008	-0.013	30.751	0.001	0.001	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.079	-0.052	33.095	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.036	-0.021	31.930	0.006	0.006	0.000	0.000	0.000	0.000
72	A	72	MET	0	0.061	0.023	24.690	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.884	-0.939	28.629	0.024	0.024	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.017	-0.020	29.979	0.000	0.000	0.000	0.000	0.000	0.000
75	A	75	PHE	0	0.000	0.012	26.152	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.005	-0.002	25.439	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	77	GLN	0	-0.023	-0.011	28.126	0.000	0.000	0.000	0.000	0.000	0.000
78	A	78	GLN	0	0.074	0.032	31.046	-0.006	-0.006	0.000	0.000	0.000	0.000
79	A	79	TYR	0	0.040	0.007	26.658	-0.011	-0.011	0.000	0.000	0.000	0.000
80	A	80	ALA	0	-0.018	-0.028	28.012	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.848	-0.896	29.573	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	THR	0	-0.043	-0.027	32.705	0.000	0.000	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.009	-0.010	28.450	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.815	0.898	31.752	0.003	0.003	0.000	0.000	0.000	0.000
85	A	85	TYR	0	-0.037	-0.026	33.716	0.002	0.002	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.011	-0.008	33.795	0.000	0.000	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.080	-0.031	33.030	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.838	-0.890	35.174	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	93	TYR	0	-0.041	-0.045	37.118	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	94	GLU	-1	-0.805	-0.879	40.398	-0.046	-0.046	0.000	0.000	0.000	0.000
91	A	95	ASP	-1	-0.817	-0.897	40.225	-0.089	-0.089	0.000	0.000	0.000	0.000
92	A	96	GLY	0	-0.025	-0.015	39.654	0.003	0.003	0.000	0.000	0.000	0.000
93	A	97	LYS	1	0.798	0.892	39.056	0.047	0.047	0.000	0.000	0.000	0.000
94	A	98	GLN	0	0.069	0.041	35.038	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	99	TYR	0	-0.044	-0.024	34.124	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	100	THR	0	-0.007	0.007	35.263	0.002	0.002	0.000	0.000	0.000	0.000
97	A	101	THR	0	-0.011	-0.037	36.612	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	102	LEU	0	-0.029	-0.010	33.493	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	103	GLU	-1	-0.912	-0.974	37.947	-0.098	-0.098	0.000	0.000	0.000	0.000
100	A	104	LYS	1	0.887	0.942	39.436	0.121	0.121	0.000	0.000	0.000	0.000
101	A	105	PRO	0	-0.045	-0.021	37.787	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	106	VAL	0	0.024	0.027	32.813	0.000	0.000	0.000	0.000	0.000	0.000
103	A	107	ALA	0	0.008	-0.004	35.558	0.005	0.005	0.000	0.000	0.000	0.000
104	A	108	GLY	0	-0.008	-0.012	35.056	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	109	ALA	0	-0.021	0.007	31.452	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	110	PRO	0	-0.007	-0.014	27.168	0.014	0.014	0.000	0.000	0.000	0.000
107	A	111	GLN	0	0.026	0.005	30.026	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	112	VAL	0	0.054	0.023	26.807	0.000	0.000	0.000	0.000	0.000	0.000
109	A	113	LEU	0	-0.060	-0.021	24.182	0.001	0.001	0.000	0.000	0.000	0.000
110	A	114	GLU	-1	-0.809	-0.882	19.756	-0.262	-0.262	0.000	0.000	0.000	0.000
111	A	115	PHE	0	-0.011	-0.010	21.819	-0.021	-0.021	0.000	0.000	0.000	0.000
112	A	116	PHE	0	0.035	-0.007	13.932	0.019	0.019	0.000	0.000	0.000	0.000
113	A	117	SER	0	0.068	0.013	16.235	-0.053	-0.053	0.000	0.000	0.000	0.000
114	A	118	PHE	0	0.043	0.017	10.673	0.027	0.027	0.000	0.000	0.000	0.000
115	A	119	PHE	0	0.037	0.019	12.044	-0.136	-0.136	0.000	0.000	0.000	0.000
116	A	120	CYS	0	-0.067	-0.004	14.349	0.155	0.155	0.000	0.000	0.000	0.000
117	A	121	PRO	0	0.060	0.027	16.045	0.008	0.008	0.000	0.000	0.000	0.000
118	A	122	HIS	0	0.030	0.007	17.077	0.021	0.021	0.000	0.000	0.000	0.000
119	A	124	TYR	0	0.055	0.029	11.130	-0.014	-0.014	0.000	0.000	0.000	0.000
120	A	125	GLN	0	0.019	0.004	15.076	0.098	0.098	0.000	0.000	0.000	0.000
121	A	126	PHE	0	-0.001	-0.015	18.085	0.053	0.053	0.000	0.000	0.000	0.000
122	A	127	GLU	-1	-0.784	-0.856	14.710	-0.123	-0.123	0.000	0.000	0.000	0.000
123	A	128	GLU	-1	-0.921	-0.972	12.543	0.131	0.131	0.000	0.000	0.000	0.000
124	A	129	VAL	0	-0.052	-0.021	15.843	0.026	0.026	0.000	0.000	0.000	0.000
125	A	130	LEU	0	-0.039	-0.034	18.740	0.032	0.032	0.000	0.000	0.000	0.000
126	A	131	HIS	0	-0.015	0.018	16.990	0.013	0.013	0.000	0.000	0.000	0.000
127	A	132	ILE	0	-0.010	-0.001	20.803	0.020	0.020	0.000	0.000	0.000	0.000
128	A	133	SER	0	0.001	-0.041	19.139	0.015	0.015	0.000	0.000	0.000	0.000
129	A	134	ASP	-1	-0.803	-0.906	20.317	0.138	0.138	0.000	0.000	0.000	0.000
130	A	135	ASN	0	-0.032	-0.025	22.107	0.023	0.023	0.000	0.000	0.000	0.000
131	A	136	VAL	0	0.006	0.003	24.857	0.005	0.005	0.000	0.000	0.000	0.000
132	A	137	LYS	1	0.869	0.941	19.008	-0.041	-0.041	0.000	0.000	0.000	0.000
133	A	138	LYS	1	0.848	0.926	22.034	-0.112	-0.112	0.000	0.000	0.000	0.000
134	A	139	LYS	1	0.805	0.911	27.617	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	140	LEU	0	-0.029	-0.001	27.579	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	141	PRO	0	-0.014	-0.002	30.665	0.011	0.011	0.000	0.000	0.000	0.000
137	A	142	GLU	-1	-0.864	-0.938	32.571	0.052	0.052	0.000	0.000	0.000	0.000
138	A	143	GLY	0	-0.034	-0.013	32.764	-0.008	-0.008	0.000	0.000	0.000	0.000
139	A	144	VAL	0	-0.046	-0.011	30.401	-0.014	-0.014	0.000	0.000	0.000	0.000
140	A	145	LYS	1	0.959	0.987	24.710	0.073	0.073	0.000	0.000	0.000	0.000
141	A	146	MET	0	-0.012	-0.007	22.775	-0.004	-0.004	0.000	0.000	0.000	0.000
142	A	147	THR	0	-0.057	-0.029	22.958	0.010	0.010	0.000	0.000	0.000	0.000
143	A	148	LYS	1	0.843	0.894	17.421	0.255	0.255	0.000	0.000	0.000	0.000
144	A	149	TYR	0	-0.014	-0.008	20.144	-0.007	-0.007	0.000	0.000	0.000	0.000
145	A	150	HIS	0	0.024	0.017	14.923	-0.097	-0.097	0.000	0.000	0.000	0.000
146	A	151	VAL	0	-0.033	-0.016	18.478	0.032	0.032	0.000	0.000	0.000	0.000
147	A	152	ASN	0	-0.061	-0.040	18.870	-0.060	-0.060	0.000	0.000	0.000	0.000
148	A	153	PHE	0	0.000	0.000	20.396	-0.024	-0.024	0.000	0.000	0.000	0.000
149	A	154	MET	0	-0.017	-0.021	18.182	0.025	0.025	0.000	0.000	0.000	0.000
150	A	155	GLY	0	0.056	0.023	16.381	-0.070	-0.070	0.000	0.000	0.000	0.000
151	A	156	GLY	0	-0.009	0.001	16.535	-0.087	-0.087	0.000	0.000	0.000	0.000
152	A	157	ASP	-1	-0.860	-0.935	17.335	-0.784	-0.784	0.000	0.000	0.000	0.000
153	A	158	LEU	0	0.035	0.035	9.917	0.026	0.026	0.000	0.000	0.000	0.000
154	A	159	GLY	0	0.031	0.018	13.489	-0.111	-0.111	0.000	0.000	0.000	0.000
155	A	160	LYS	1	0.844	0.914	15.836	0.785	0.785	0.000	0.000	0.000	0.000
156	A	161	ASP	-1	-0.842	-0.919	12.494	-1.309	-1.309	0.000	0.000	0.000	0.000
157	A	162	LEU	0	-0.009	-0.004	9.544	0.005	0.005	0.000	0.000	0.000	0.000
158	A	163	THR	0	-0.023	-0.013	13.010	0.141	0.141	0.000	0.000	0.000	0.000
159	A	164	GLN	0	-0.036	-0.020	15.834	0.100	0.100	0.000	0.000	0.000	0.000
160	A	165	ALA	0	0.005	-0.003	11.100	0.094	0.094	0.000	0.000	0.000	0.000
161	A	166	TRP	0	0.003	-0.022	13.036	0.096	0.096	0.000	0.000	0.000	0.000
162	A	167	ALA	0	0.000	-0.002	15.013	0.123	0.123	0.000	0.000	0.000	0.000
163	A	168	VAL	0	0.013	0.010	13.483	0.103	0.103	0.000	0.000	0.000	0.000
164	A	169	ALA	0	-0.012	-0.002	13.290	0.112	0.112	0.000	0.000	0.000	0.000
165	A	170	MET	0	-0.035	0.001	14.915	0.102	0.102	0.000	0.000	0.000	0.000
166	A	171	ALA	0	-0.088	-0.034	18.324	0.052	0.052	0.000	0.000	0.000	0.000
167	A	172	LEU	0	-0.078	-0.047	14.251	0.040	0.040	0.000	0.000	0.000	0.000
168	A	173	GLY	0	0.013	0.031	17.974	0.068	0.068	0.000	0.000	0.000	0.000
169	A	174	VAL	0	-0.083	-0.054	13.079	0.101	0.101	0.000	0.000	0.000	0.000
170	A	175	GLU	-1	-0.806	-0.921	13.348	0.002	0.002	0.000	0.000	0.000	0.000
171	A	176	ASP	-1	-0.911	-0.950	13.557	0.132	0.132	0.000	0.000	0.000	0.000
172	A	177	LYS	1	0.878	0.957	10.809	-0.645	-0.645	0.000	0.000	0.000	0.000
173	A	178	VAL	0	0.009	-0.003	8.719	0.338	0.338	0.000	0.000	0.000	0.000
174	A	179	THR	0	0.000	-0.011	8.825	-0.428	-0.428	0.000	0.000	0.000	0.000
175	A	180	VAL	0	0.064	0.031	9.201	-0.299	-0.299	0.000	0.000	0.000	0.000
176	A	181	PRO	0	-0.002	0.003	4.764	-0.534	-0.441	-0.001	-0.003	-0.088	0.000
177	A	182	LEU	0	-0.004	0.003	4.717	-1.842	-1.778	-0.001	-0.004	-0.059	0.000
178	A	183	PHE	0	0.029	0.008	6.960	-0.432	-0.432	0.000	0.000	0.000	0.000
179	A	184	GLU	-1	-0.914	-0.952	5.992	-0.215	-0.215	0.000	0.000	0.000	0.000
180	A	185	GLY	0	0.006	0.003	4.251	-0.158	-0.158	-0.001	-0.038	0.039	0.000
181	A	186	VAL	0	-0.004	-0.001	4.824	0.100	0.120	-0.001	-0.008	-0.011	0.000
182	A	187	GLN	0	-0.040	-0.042	8.450	0.506	0.506	0.000	0.000	0.000	0.000
183	A	188	LYS	1	0.887	0.948	4.727	0.793	0.912	-0.001	-0.008	-0.110	0.000
184	A	189	THR	0	-0.031	-0.006	8.587	0.422	0.422	0.000	0.000	0.000	0.000
185	A	189	LEU	0	-0.117	-0.036	9.641	0.376	0.376	0.000	0.000	0.000	0.000

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