FMO DATABASE

FMODB ID: RY1G8

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

Total energy (hartree)

FMO2-HF: Electronic energy	-2021679.976837
FMO2-HF: Nuclear repulsion	1948143.97279
FMO2-HF: Total energy	-73536.004046
FMO2-MP2: Total energy	-73748.819759

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.
-19.157	-20.529	14.582	-5.149	-8.061	0.028

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 : 0.027 / 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	-0.025	0.005	3.865	-2.866	-1.512	-0.001	-0.580	-0.773	0.002
4	A	4	ARG	1	0.840	0.923	5.951	2.923	2.923	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.043	-0.041	7.975	0.835	0.835	0.000	0.000	0.000	0.000
6	A	6	ALA	0	0.095	0.031	7.952	-0.733	-0.733	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.022	-0.013	8.082	0.067	0.067	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.702	-0.821	4.158	-4.609	-4.467	-0.001	-0.010	-0.131	0.000
9	A	9	ILE	0	-0.021	-0.007	3.440	-4.485	-3.840	0.029	-0.306	-0.368	-0.002
10	A	10	ARG	1	0.842	0.897	5.847	1.520	1.520	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.894	-0.957	2.989	-2.820	-2.193	0.069	-0.212	-0.485	-0.002
12	A	12	VAL	0	-0.044	-0.017	2.290	2.661	2.554	4.499	-1.134	-3.259	-0.003
13	A	13	PHE	0	0.012	-0.009	3.649	2.073	2.228	0.036	0.019	-0.210	0.001
14	A	14	ILE	0	-0.026	-0.004	5.999	0.604	0.604	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.052	-0.037	1.821	-9.580	-14.122	9.956	-2.853	-2.561	0.032
16	A	16	ALA	0	0.002	0.026	5.444	-0.499	-0.478	-0.001	0.000	-0.020	0.000
17	A	17	GLY	0	-0.020	-0.015	8.010	-0.535	-0.535	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.089	-0.041	9.977	-0.285	-0.285	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.849	0.900	10.160	-0.382	-0.382	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.050	0.015	10.888	-0.153	-0.153	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.900	-0.943	11.696	-0.237	-0.237	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.803	-0.885	14.236	0.218	0.218	0.000	0.000	0.000	0.000
23	A	23	TYR	0	0.030	0.013	10.064	-0.154	-0.154	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.772	-0.866	12.892	-0.819	-0.819	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.001	0.005	14.899	-0.008	-0.008	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.007	0.007	15.627	0.003	0.003	0.000	0.000	0.000	0.000
27	A	27	TRP	0	0.015	0.011	12.516	-0.039	-0.039	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.056	-0.038	16.446	-0.025	-0.025	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.035	-0.013	19.835	0.061	0.061	0.000	0.000	0.000	0.000
30	A	30	PHE	0	-0.002	-0.019	21.919	-0.029	-0.029	0.000	0.000	0.000	0.000
31	A	31	VAL	0	0.034	0.016	22.281	-0.010	-0.010	0.000	0.000	0.000	0.000
32	A	32	VAL	0	0.052	0.034	17.544	-0.009	-0.009	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.956	0.977	20.589	0.351	0.351	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.016	-0.014	22.991	0.006	0.006	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.009	0.006	20.608	0.007	0.007	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.031	-0.001	18.926	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	37	ALA	0	-0.001	0.009	21.561	0.003	0.003	0.000	0.000	0.000	0.000
38	A	38	GLN	0	0.008	-0.004	25.192	0.018	0.018	0.000	0.000	0.000	0.000
39	A	39	GLN	0	0.009	-0.009	18.567	-0.017	-0.017	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.876	-0.923	23.522	-0.450	-0.450	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.800	0.882	25.213	0.267	0.267	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.023	0.012	26.488	0.020	0.020	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.011	0.003	25.116	0.016	0.016	0.000	0.000	0.000	0.000
44	A	44	ALA	0	-0.011	-0.008	27.270	0.017	0.017	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.835	-0.890	30.335	-0.224	-0.224	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.050	-0.020	28.720	0.018	0.018	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.099	-0.051	31.872	0.009	0.009	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.020	-0.005	24.290	0.003	0.003	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.954	0.970	28.062	0.220	0.220	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.024	-0.004	25.056	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.034	0.001	19.913	0.005	0.005	0.000	0.000	0.000	0.000
52	A	52	PRO	0	0.022	-0.010	20.586	-0.016	-0.016	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.033	-0.009	22.172	0.035	0.035	0.000	0.000	0.000	0.000
54	A	54	MET	0	-0.010	0.002	24.237	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	55	PHE	0	0.027	0.011	26.772	0.015	0.015	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.029	0.013	29.239	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	57	ASN	0	0.027	-0.002	31.967	0.003	0.003	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.006	0.019	32.772	0.005	0.005	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.848	0.938	34.116	0.126	0.126	0.000	0.000	0.000	0.000
60	A	60	TYR	0	0.031	0.018	34.612	0.004	0.004	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.001	0.006	30.511	-0.014	-0.014	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.000	-0.008	29.156	0.015	0.015	0.000	0.000	0.000	0.000
63	A	63	ASN	0	-0.066	-0.041	30.763	-0.027	-0.027	0.000	0.000	0.000	0.000
64	A	64	PRO	0	0.049	0.006	27.796	0.014	0.014	0.000	0.000	0.000	0.000
65	A	65	GLN	0	-0.015	-0.018	29.983	0.014	0.014	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.012	0.008	33.118	0.009	0.009	0.000	0.000	0.000	0.000
67	A	67	MET	0	-0.073	-0.007	30.614	0.007	0.007	0.000	0.000	0.000	0.000
68	A	68	ASP	-1	-0.855	-0.915	34.620	-0.068	-0.068	0.000	0.000	0.000	0.000
69	A	69	THR	0	0.002	-0.010	30.798	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.073	-0.050	32.842	0.001	0.001	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.044	-0.022	32.012	0.008	0.008	0.000	0.000	0.000	0.000
72	A	72	MET	0	0.058	0.028	24.923	-0.015	-0.015	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.870	-0.930	28.564	-0.031	-0.031	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.029	-0.021	29.789	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	75	PHE	0	0.015	0.020	25.961	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.012	-0.010	25.123	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	77	GLN	0	-0.007	-0.007	27.743	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	78	GLN	0	0.060	0.033	30.612	-0.006	-0.006	0.000	0.000	0.000	0.000
79	A	79	TYR	0	0.063	0.020	26.157	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	80	ALA	0	-0.005	-0.008	27.671	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.842	-0.889	29.316	-0.049	-0.049	0.000	0.000	0.000	0.000
82	A	82	THR	0	-0.047	-0.033	32.359	0.003	0.003	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.020	-0.023	28.015	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.790	0.892	31.275	0.051	0.051	0.000	0.000	0.000	0.000
85	A	85	TYR	0	0.003	-0.005	33.345	0.003	0.003	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.034	-0.019	33.291	0.001	0.001	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.060	-0.040	33.076	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.839	-0.884	35.234	-0.048	-0.048	0.000	0.000	0.000	0.000
89	A	93	TYR	0	-0.053	-0.053	36.911	0.000	0.000	0.000	0.000	0.000	0.000
90	A	94	GLU	-1	-0.807	-0.880	40.107	-0.076	-0.076	0.000	0.000	0.000	0.000
91	A	95	ASP	-1	-0.774	-0.867	39.681	-0.128	-0.128	0.000	0.000	0.000	0.000
92	A	96	GLY	0	-0.015	-0.009	39.231	0.005	0.005	0.000	0.000	0.000	0.000
93	A	97	LYS	1	0.777	0.884	38.459	0.080	0.080	0.000	0.000	0.000	0.000
94	A	98	GLN	0	0.086	0.052	34.750	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	99	TYR	0	-0.043	-0.039	33.714	-0.013	-0.013	0.000	0.000	0.000	0.000
96	A	100	THR	0	-0.032	-0.008	34.935	0.004	0.004	0.000	0.000	0.000	0.000
97	A	101	THR	0	-0.018	-0.044	36.302	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	102	LEU	0	-0.045	-0.011	33.474	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	103	GLU	-1	-0.883	-0.959	37.894	-0.124	-0.124	0.000	0.000	0.000	0.000
100	A	104	LYS	1	0.868	0.933	39.220	0.147	0.147	0.000	0.000	0.000	0.000
101	A	105	PRO	0	-0.021	-0.010	37.621	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	106	VAL	0	0.034	0.028	32.302	0.002	0.002	0.000	0.000	0.000	0.000
103	A	107	ALA	0	-0.015	-0.018	35.052	0.002	0.002	0.000	0.000	0.000	0.000
104	A	108	GLY	0	0.000	-0.001	34.852	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	109	ALA	0	-0.025	0.000	30.951	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	110	PRO	0	-0.026	-0.021	26.897	0.015	0.015	0.000	0.000	0.000	0.000
107	A	111	GLN	0	0.018	0.016	29.820	-0.007	-0.007	0.000	0.000	0.000	0.000
108	A	112	VAL	0	0.058	0.027	26.559	0.004	0.004	0.000	0.000	0.000	0.000
109	A	113	LEU	0	-0.060	-0.025	24.070	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	114	GLU	-1	-0.809	-0.889	19.572	-0.400	-0.400	0.000	0.000	0.000	0.000
111	A	115	PHE	0	0.002	-0.007	21.679	-0.026	-0.026	0.000	0.000	0.000	0.000
112	A	116	PHE	0	0.035	-0.002	13.812	0.032	0.032	0.000	0.000	0.000	0.000
113	A	117	SER	0	0.064	0.014	15.949	-0.056	-0.056	0.000	0.000	0.000	0.000
114	A	118	PHE	0	0.055	0.015	10.358	0.021	0.021	0.000	0.000	0.000	0.000
115	A	119	PHE	0	0.030	0.021	11.927	-0.114	-0.114	0.000	0.000	0.000	0.000
116	A	120	CYS	0	-0.036	0.013	13.994	0.188	0.188	0.000	0.000	0.000	0.000
117	A	121	PRO	0	0.045	0.024	15.623	0.008	0.008	0.000	0.000	0.000	0.000
118	A	122	HIS	0	0.021	0.001	16.662	0.019	0.019	0.000	0.000	0.000	0.000
119	A	124	TYR	0	0.041	0.029	11.164	-0.011	-0.011	0.000	0.000	0.000	0.000
120	A	125	GLN	0	0.012	-0.004	14.838	0.108	0.108	0.000	0.000	0.000	0.000
121	A	126	PHE	0	-0.014	-0.012	17.902	0.058	0.058	0.000	0.000	0.000	0.000
122	A	127	GLU	-1	-0.788	-0.851	14.430	-0.325	-0.325	0.000	0.000	0.000	0.000
123	A	128	GLU	-1	-0.905	-0.963	12.571	-0.079	-0.079	0.000	0.000	0.000	0.000
124	A	129	VAL	0	-0.052	-0.026	15.878	0.050	0.050	0.000	0.000	0.000	0.000
125	A	130	LEU	0	-0.022	-0.032	18.734	0.039	0.039	0.000	0.000	0.000	0.000
126	A	131	HIS	0	-0.024	0.015	16.777	0.022	0.022	0.000	0.000	0.000	0.000
127	A	132	ILE	0	0.000	0.024	20.688	0.027	0.027	0.000	0.000	0.000	0.000
128	A	133	SER	0	-0.003	-0.048	18.983	0.026	0.026	0.000	0.000	0.000	0.000
129	A	134	ASP	-1	-0.797	-0.906	19.796	0.003	0.003	0.000	0.000	0.000	0.000
130	A	135	ASN	0	-0.037	-0.027	21.819	0.044	0.044	0.000	0.000	0.000	0.000
131	A	136	VAL	0	0.024	0.001	24.474	0.011	0.011	0.000	0.000	0.000	0.000
132	A	137	LYS	1	0.844	0.935	18.510	0.108	0.108	0.000	0.000	0.000	0.000
133	A	138	LYS	1	0.835	0.914	21.961	0.001	0.001	0.000	0.000	0.000	0.000
134	A	139	LYS	1	0.786	0.893	27.579	0.061	0.061	0.000	0.000	0.000	0.000
135	A	140	LEU	0	-0.051	-0.016	27.612	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	141	PRO	0	-0.016	-0.003	30.715	0.011	0.011	0.000	0.000	0.000	0.000
137	A	142	GLU	-1	-0.853	-0.923	32.482	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	143	GLY	0	-0.045	-0.023	33.198	-0.005	-0.005	0.000	0.000	0.000	0.000
139	A	144	VAL	0	-0.056	-0.023	30.402	-0.013	-0.013	0.000	0.000	0.000	0.000
140	A	145	LYS	1	0.949	0.983	23.574	0.189	0.189	0.000	0.000	0.000	0.000
141	A	146	MET	0	-0.001	0.007	21.741	-0.003	-0.003	0.000	0.000	0.000	0.000
142	A	147	THR	0	-0.046	-0.025	22.821	0.005	0.005	0.000	0.000	0.000	0.000
143	A	148	LYS	1	0.824	0.882	17.373	0.428	0.428	0.000	0.000	0.000	0.000
144	A	149	TYR	0	-0.010	-0.002	20.121	-0.005	-0.005	0.000	0.000	0.000	0.000
145	A	150	HIS	0	0.018	0.023	14.569	-0.119	-0.119	0.000	0.000	0.000	0.000
146	A	151	VAL	0	-0.040	-0.025	18.180	0.044	0.044	0.000	0.000	0.000	0.000
147	A	152	ASN	0	-0.051	-0.036	18.547	-0.069	-0.069	0.000	0.000	0.000	0.000
148	A	153	PHE	0	-0.007	0.000	19.702	-0.032	-0.032	0.000	0.000	0.000	0.000
149	A	154	MET	0	-0.010	-0.009	17.718	0.023	0.023	0.000	0.000	0.000	0.000
150	A	155	GLY	0	0.063	0.022	15.766	-0.095	-0.095	0.000	0.000	0.000	0.000
151	A	156	GLY	0	-0.011	0.000	16.022	-0.092	-0.092	0.000	0.000	0.000	0.000
152	A	157	ASP	-1	-0.839	-0.907	17.182	-0.768	-0.768	0.000	0.000	0.000	0.000
153	A	158	LEU	0	0.045	0.042	9.592	0.015	0.015	0.000	0.000	0.000	0.000
154	A	159	GLY	0	0.030	0.014	13.036	-0.147	-0.147	0.000	0.000	0.000	0.000
155	A	160	LYS	1	0.810	0.890	15.447	0.829	0.829	0.000	0.000	0.000	0.000
156	A	161	ASP	-1	-0.856	-0.930	11.886	-1.479	-1.479	0.000	0.000	0.000	0.000
157	A	162	LEU	0	-0.004	-0.011	9.078	-0.020	-0.020	0.000	0.000	0.000	0.000
158	A	163	THR	0	-0.027	-0.012	12.465	0.138	0.138	0.000	0.000	0.000	0.000
159	A	164	GLN	0	-0.030	-0.019	15.345	0.117	0.117	0.000	0.000	0.000	0.000
160	A	165	ALA	0	0.010	0.005	10.663	0.095	0.095	0.000	0.000	0.000	0.000
161	A	166	TRP	0	0.001	-0.024	12.756	0.093	0.093	0.000	0.000	0.000	0.000
162	A	167	ALA	0	-0.022	-0.009	14.776	0.131	0.131	0.000	0.000	0.000	0.000
163	A	168	VAL	0	0.007	-0.004	13.052	0.111	0.111	0.000	0.000	0.000	0.000
164	A	169	ALA	0	-0.021	-0.013	13.483	0.112	0.112	0.000	0.000	0.000	0.000
165	A	170	MET	0	-0.026	-0.004	14.980	0.123	0.123	0.000	0.000	0.000	0.000
166	A	171	ALA	0	-0.070	-0.030	18.315	0.061	0.061	0.000	0.000	0.000	0.000
167	A	172	LEU	0	-0.067	-0.030	14.334	0.049	0.049	0.000	0.000	0.000	0.000
168	A	173	GLY	0	-0.002	0.029	17.997	0.070	0.070	0.000	0.000	0.000	0.000
169	A	174	VAL	0	-0.048	-0.030	13.222	0.084	0.084	0.000	0.000	0.000	0.000
170	A	175	GLU	-1	-0.825	-0.929	13.827	-0.250	-0.250	0.000	0.000	0.000	0.000
171	A	176	ASP	-1	-0.890	-0.943	13.568	-0.161	-0.161	0.000	0.000	0.000	0.000
172	A	177	LYS	1	0.818	0.927	11.196	-0.570	-0.570	0.000	0.000	0.000	0.000
173	A	178	VAL	0	0.003	-0.003	8.901	0.155	0.155	0.000	0.000	0.000	0.000
174	A	179	THR	0	-0.024	-0.030	8.765	-0.459	-0.459	0.000	0.000	0.000	0.000
175	A	180	VAL	0	0.063	0.036	9.271	-0.288	-0.288	0.000	0.000	0.000	0.000
176	A	181	PRO	0	0.013	0.005	4.772	-0.444	-0.362	-0.001	-0.003	-0.078	0.000
177	A	182	LEU	0	0.003	0.008	4.803	-1.785	-1.722	-0.001	-0.003	-0.058	0.000
178	A	183	PHE	0	0.020	0.009	6.916	-0.371	-0.371	0.000	0.000	0.000	0.000
179	A	184	GLU	-1	-0.877	-0.923	5.706	-0.310	-0.310	0.000	0.000	0.000	0.000
180	A	185	GLY	0	-0.004	0.001	4.137	-0.032	-0.019	0.000	-0.047	0.034	0.000
181	A	186	VAL	0	0.002	-0.005	4.672	0.542	0.578	-0.001	-0.010	-0.025	0.000
182	A	187	GLN	0	-0.035	-0.038	8.329	0.613	0.613	0.000	0.000	0.000	0.000
183	A	188	LYS	1	0.847	0.915	4.585	0.864	1.003	-0.001	-0.010	-0.127	0.000
184	A	189	THR	0	-0.043	-0.034	8.308	0.472	0.472	0.000	0.000	0.000	0.000
185	A	189	LEU	0	-0.099	-0.036	9.607	0.414	0.414	0.000	0.000	0.000	0.000

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