FMO DATABASE

FMODB ID: 8QNKY

Calculation Name: 2C2H-B-Xray547

Preferred Name: Ras-related C3 botulinum toxin substrate 3

Target Type: SINGLE PROTEIN

Ligand Name: guanosine-5'-diphosphate | sulfate ion | calcium ion | magnesium ion

Ligand 3-letter code: GDP | SO4 | CA | MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2C2H

Chain ID: B

ChEMBL ID: CHEMBL6087

UniProt ID: P60763

Base Structure: X-ray

Registration Date: 2025-10-05

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	177
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1871386.256818
FMO2-HF: Nuclear repulsion	1801611.62046
FMO2-HF: Total energy	-69774.636358
FMO2-MP2: Total energy	-69976.385642

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:1:MET)

Summations of interaction energy for fragment #1(A:1: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.
-58.79	-51.668	10.227	-5.278	-12.071	-0.062

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.801 / q_NPA : 0.905

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	ALA	0	0.003	-0.006	2.647	-4.551	-1.469	0.653	-1.671	-2.064	-0.016
4	A	4	ILE	0	0.031	0.020	5.249	1.309	1.356	-0.001	-0.005	-0.040	0.000
43	A	43	ASN	0	-0.053	-0.031	2.483	-9.761	-9.368	2.106	-0.892	-1.608	-0.013
44	A	44	VAL	0	0.021	0.013	4.448	3.327	3.398	-0.001	-0.005	-0.065	0.000
45	A	45	MET	0	-0.039	-0.005	5.078	-3.314	-3.253	-0.001	0.000	-0.060	0.000
50	A	50	PRO	0	-0.028	-0.002	2.148	1.365	1.369	2.444	-0.573	-1.875	0.001
51	A	51	VAL	0	0.010	-0.009	2.597	-15.259	-13.253	3.330	-1.785	-3.551	-0.026
52	A	52	ASN	0	0.020	0.007	2.750	4.421	5.775	1.678	-0.366	-2.666	-0.008
53	A	53	LEU	0	-0.004	-0.005	3.569	0.577	0.681	0.019	0.019	-0.142	0.000
5	A	5	LYS	1	0.784	0.900	8.478	18.326	18.326	0.000	0.000	0.000	0.000
6	A	6	CYS	0	-0.012	-0.006	11.669	1.426	1.426	0.000	0.000	0.000	0.000
7	A	7	VAL	0	0.001	0.008	13.996	0.095	0.095	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.002	0.003	17.342	0.426	0.426	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.022	0.032	19.799	0.358	0.358	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.083	0.026	23.556	-0.003	-0.003	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.784	-0.864	26.676	-9.307	-9.307	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.001	-0.008	28.207	-0.319	-0.319	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.012	-0.003	29.413	0.127	0.127	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.012	0.003	25.726	0.131	0.131	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.027	0.023	25.434	-0.064	-0.064	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.820	0.932	21.682	11.157	11.157	0.000	0.000	0.000	0.000
17	A	17	THR	0	0.058	0.003	20.414	-0.237	-0.237	0.000	0.000	0.000	0.000
18	A	18	CYS	0	-0.051	-0.012	20.318	-0.249	-0.249	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.011	-0.011	18.401	-0.198	-0.198	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.031	0.017	15.020	-0.508	-0.508	0.000	0.000	0.000	0.000
21	A	21	ILE	0	0.040	0.040	15.600	-0.725	-0.725	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.042	-0.005	17.028	-0.398	-0.398	0.000	0.000	0.000	0.000
23	A	23	TYR	0	-0.010	-0.009	10.106	-0.093	-0.093	0.000	0.000	0.000	0.000
24	A	24	THR	0	-0.052	-0.046	11.378	-0.608	-0.608	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.051	-0.043	12.603	-0.311	-0.311	0.000	0.000	0.000	0.000
26	A	26	ASN	0	-0.023	0.007	15.338	0.134	0.134	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.024	0.015	17.036	0.652	0.652	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.010	-0.005	20.258	-0.237	-0.237	0.000	0.000	0.000	0.000
29	A	29	PRO	0	-0.016	-0.002	21.660	0.259	0.259	0.000	0.000	0.000	0.000
30	A	30	GLY	0	-0.011	-0.018	24.075	0.223	0.223	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.869	-0.927	26.506	-9.076	-9.076	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.103	-0.047	26.948	-0.311	-0.311	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.024	-0.013	23.922	-0.247	-0.247	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.017	0.011	20.333	0.285	0.285	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.009	-0.009	22.089	0.283	0.283	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.021	-0.008	23.156	-0.159	-0.159	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.058	-0.030	21.738	0.147	0.147	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.768	-0.860	18.827	-14.524	-14.524	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.055	-0.041	14.291	-0.278	-0.278	0.000	0.000	0.000	0.000
40	A	40	TYR	0	-0.034	-0.029	13.243	-0.019	-0.019	0.000	0.000	0.000	0.000
41	A	41	SER	0	-0.012	-0.011	7.665	-1.615	-1.615	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.020	0.018	8.046	1.351	1.351	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.029	0.014	7.346	2.732	2.732	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.835	-0.912	8.973	-28.328	-28.328	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.025	0.011	9.916	0.334	0.334	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.842	0.904	5.735	28.018	28.018	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.027	0.013	7.206	1.380	1.380	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.034	-0.023	9.912	0.912	0.912	0.000	0.000	0.000	0.000
56	A	56	TRP	0	0.033	0.009	12.702	0.794	0.794	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.766	-0.874	16.368	-12.511	-12.511	0.000	0.000	0.000	0.000
58	A	58	THR	0	-0.058	-0.056	19.670	0.248	0.248	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.058	0.041	23.165	0.299	0.299	0.000	0.000	0.000	0.000
60	A	60	GLY	0	-0.017	-0.005	26.796	0.004	0.004	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.004	-0.023	28.578	0.072	0.072	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.917	-0.962	31.813	-8.232	-8.232	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.928	-0.956	33.646	-8.983	-8.983	0.000	0.000	0.000	0.000
64	A	64	TYR	0	0.048	0.019	28.303	-0.253	-0.253	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.791	-0.860	29.797	-9.772	-9.772	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.855	0.919	31.306	9.144	9.144	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.036	0.022	28.021	-0.153	-0.153	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.795	0.870	25.083	10.128	10.128	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.037	0.010	24.361	-0.584	-0.584	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.005	0.000	24.141	-0.435	-0.435	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.007	0.001	20.392	-0.646	-0.646	0.000	0.000	0.000	0.000
72	A	72	TYR	0	-0.056	-0.042	19.304	-0.996	-0.996	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.018	0.026	19.493	-0.594	-0.594	0.000	0.000	0.000	0.000
74	A	74	GLN	0	-0.006	-0.012	14.670	0.158	0.158	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.008	-0.009	14.429	-1.482	-1.482	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.829	-0.899	11.331	-24.114	-24.114	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.029	-0.028	13.826	0.831	0.831	0.000	0.000	0.000	0.000
78	A	78	PHE	0	0.030	0.007	16.416	-0.179	-0.179	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.019	-0.007	16.832	0.271	0.271	0.000	0.000	0.000	0.000
80	A	80	ILE	0	0.019	0.010	20.175	0.213	0.213	0.000	0.000	0.000	0.000
81	A	81	CYS	0	-0.046	-0.011	21.860	0.028	0.028	0.000	0.000	0.000	0.000
82	A	82	PHE	0	0.017	0.000	24.616	0.318	0.318	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.005	0.007	27.783	-0.158	-0.158	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.001	0.004	28.708	0.282	0.282	0.000	0.000	0.000	0.000
85	A	85	VAL	0	0.012	0.011	31.617	0.270	0.270	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.015	-0.015	33.237	0.239	0.239	0.000	0.000	0.000	0.000
87	A	87	PRO	0	0.062	0.030	34.095	-0.197	-0.197	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.011	0.021	36.245	-0.018	-0.018	0.000	0.000	0.000	0.000
89	A	89	SER	0	0.016	-0.001	30.835	-0.184	-0.184	0.000	0.000	0.000	0.000
90	A	90	PHE	0	-0.005	-0.009	31.524	-0.238	-0.238	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.822	-0.911	32.902	-8.130	-8.130	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.028	-0.028	32.390	0.080	0.080	0.000	0.000	0.000	0.000
93	A	93	VAL	0	-0.056	-0.021	28.656	-0.265	-0.265	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.779	0.841	30.895	8.087	8.087	0.000	0.000	0.000	0.000
95	A	95	ALA	0	-0.036	-0.021	33.803	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.852	0.916	31.173	9.421	9.421	0.000	0.000	0.000	0.000
97	A	97	TRP	0	-0.032	-0.034	27.293	-0.304	-0.304	0.000	0.000	0.000	0.000
98	A	98	TYR	0	0.046	0.024	27.782	-0.435	-0.435	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.008	0.006	29.050	-0.238	-0.238	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.815	-0.884	28.119	-10.757	-10.757	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.021	0.010	23.384	-0.171	-0.171	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.835	0.910	23.485	12.022	12.022	0.000	0.000	0.000	0.000
103	A	103	HIS	0	-0.015	0.002	27.333	0.026	0.026	0.000	0.000	0.000	0.000
104	A	104	HIS	0	-0.058	-0.040	25.758	0.087	0.087	0.000	0.000	0.000	0.000
105	A	105	CYS	0	-0.068	-0.023	22.215	-0.710	-0.710	0.000	0.000	0.000	0.000
106	A	106	PRO	0	0.011	0.017	24.126	-0.062	-0.062	0.000	0.000	0.000	0.000
107	A	107	HIS	0	0.012	-0.013	22.627	0.161	0.161	0.000	0.000	0.000	0.000
108	A	108	THR	0	0.006	0.035	18.028	-0.023	-0.023	0.000	0.000	0.000	0.000
109	A	109	PRO	0	0.041	0.032	17.465	0.998	0.998	0.000	0.000	0.000	0.000
110	A	110	ILE	0	0.030	0.004	19.880	-0.286	-0.286	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.008	0.013	17.981	0.329	0.329	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.057	-0.016	21.678	0.161	0.161	0.000	0.000	0.000	0.000
113	A	113	VAL	0	0.024	-0.011	20.483	0.029	0.029	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.038	0.026	23.925	0.233	0.233	0.000	0.000	0.000	0.000
115	A	115	THR	0	-0.017	-0.048	23.846	-0.080	-0.080	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.907	0.943	26.281	9.738	9.738	0.000	0.000	0.000	0.000
117	A	117	LEU	0	0.004	0.007	26.658	0.341	0.341	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.878	-0.928	28.109	-9.546	-9.546	0.000	0.000	0.000	0.000
119	A	119	LEU	0	0.032	0.017	30.515	0.205	0.205	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.749	0.836	30.958	9.161	9.161	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.892	-0.957	34.217	-8.046	-8.046	0.000	0.000	0.000	0.000
122	A	122	ASP	-1	-0.823	-0.878	35.986	-7.403	-7.403	0.000	0.000	0.000	0.000
123	A	123	LYS	1	0.837	0.915	37.697	6.618	6.618	0.000	0.000	0.000	0.000
124	A	124	ASP	-1	-0.843	-0.924	40.507	-6.714	-6.714	0.000	0.000	0.000	0.000
125	A	125	THR	0	-0.067	-0.063	35.695	0.022	0.022	0.000	0.000	0.000	0.000
126	A	126	ILE	0	-0.038	-0.020	38.980	0.051	0.051	0.000	0.000	0.000	0.000
127	A	127	GLU	-1	-0.912	-0.946	40.849	-6.230	-6.230	0.000	0.000	0.000	0.000
128	A	128	ARG	1	0.980	0.977	39.454	7.277	7.277	0.000	0.000	0.000	0.000
129	A	129	LEU	0	-0.062	-0.017	37.336	0.011	0.011	0.000	0.000	0.000	0.000
130	A	130	ARG	1	0.976	0.988	41.980	6.183	6.183	0.000	0.000	0.000	0.000
131	A	131	ASP	-1	-0.938	-0.955	45.309	-6.121	-6.121	0.000	0.000	0.000	0.000
132	A	132	LYS	1	0.909	0.955	42.170	7.053	7.053	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.937	0.973	45.402	6.177	6.177	0.000	0.000	0.000	0.000
134	A	134	LEU	0	-0.078	-0.042	40.249	-0.088	-0.088	0.000	0.000	0.000	0.000
135	A	135	ALA	0	0.027	0.006	40.691	0.117	0.117	0.000	0.000	0.000	0.000
136	A	136	PRO	0	0.005	-0.002	35.509	-0.112	-0.112	0.000	0.000	0.000	0.000
137	A	137	ILE	0	-0.053	-0.001	32.891	0.110	0.110	0.000	0.000	0.000	0.000
138	A	138	THR	0	0.017	-0.012	33.803	-0.197	-0.197	0.000	0.000	0.000	0.000
139	A	139	TYR	0	0.057	0.024	28.029	-0.130	-0.130	0.000	0.000	0.000	0.000
140	A	140	PRO	0	0.004	-0.017	32.442	-0.166	-0.166	0.000	0.000	0.000	0.000
141	A	141	GLN	0	0.052	0.055	34.996	-0.018	-0.018	0.000	0.000	0.000	0.000
142	A	142	GLY	0	0.060	0.030	30.834	-0.051	-0.051	0.000	0.000	0.000	0.000
143	A	143	LEU	0	-0.008	-0.005	29.468	-0.220	-0.220	0.000	0.000	0.000	0.000
144	A	144	ALA	0	-0.056	-0.030	31.287	-0.074	-0.074	0.000	0.000	0.000	0.000
145	A	145	MET	0	0.018	0.021	30.900	-0.071	-0.071	0.000	0.000	0.000	0.000
146	A	146	ALA	0	-0.010	-0.017	27.813	-0.149	-0.149	0.000	0.000	0.000	0.000
147	A	147	ARG	1	0.927	0.969	29.306	8.742	8.742	0.000	0.000	0.000	0.000
148	A	148	GLU	-1	-0.828	-0.871	31.808	-8.493	-8.493	0.000	0.000	0.000	0.000
149	A	149	ILE	0	-0.036	-0.027	27.613	0.009	0.009	0.000	0.000	0.000	0.000
150	A	150	GLY	0	-0.008	0.014	28.789	-0.263	-0.263	0.000	0.000	0.000	0.000
151	A	151	SER	0	-0.059	-0.029	24.989	-0.607	-0.607	0.000	0.000	0.000	0.000
152	A	152	VAL	0	-0.007	-0.011	20.263	0.218	0.218	0.000	0.000	0.000	0.000
153	A	153	LYS	1	0.818	0.898	21.117	13.091	13.091	0.000	0.000	0.000	0.000
154	A	154	TYR	0	-0.041	-0.030	23.328	0.009	0.009	0.000	0.000	0.000	0.000
155	A	155	LEU	0	-0.009	-0.002	19.689	-0.119	-0.119	0.000	0.000	0.000	0.000
156	A	156	GLU	-1	-0.755	-0.822	23.937	-9.267	-9.267	0.000	0.000	0.000	0.000
157	A	157	CYS	0	-0.044	-0.018	21.979	-0.280	-0.280	0.000	0.000	0.000	0.000
158	A	158	SER	0	-0.049	-0.044	23.694	0.353	0.353	0.000	0.000	0.000	0.000
159	A	159	ALA	0	0.035	0.012	21.660	-0.269	-0.269	0.000	0.000	0.000	0.000
160	A	160	LEU	0	0.008	0.029	22.477	-0.268	-0.268	0.000	0.000	0.000	0.000
161	A	161	THR	0	0.005	-0.029	25.287	0.063	0.063	0.000	0.000	0.000	0.000
162	A	162	GLN	0	-0.001	-0.013	18.510	-0.179	-0.179	0.000	0.000	0.000	0.000
163	A	163	ARG	1	0.948	0.986	21.035	9.389	9.389	0.000	0.000	0.000	0.000
164	A	164	GLY	0	0.039	0.011	21.607	0.123	0.123	0.000	0.000	0.000	0.000
165	A	165	LEU	0	-0.047	-0.013	17.199	-0.375	-0.375	0.000	0.000	0.000	0.000
166	A	166	LYS	1	0.859	0.905	11.976	18.174	18.174	0.000	0.000	0.000	0.000
167	A	167	THR	0	0.021	0.005	14.937	-0.874	-0.874	0.000	0.000	0.000	0.000
168	A	168	VAL	0	0.008	0.001	16.767	-0.329	-0.329	0.000	0.000	0.000	0.000
169	A	169	PHE	0	0.025	-0.001	11.879	-0.188	-0.188	0.000	0.000	0.000	0.000
170	A	170	ASP	-1	-0.809	-0.880	12.031	-20.198	-20.198	0.000	0.000	0.000	0.000
171	A	171	GLU	-1	-0.860	-0.928	13.357	-14.715	-14.715	0.000	0.000	0.000	0.000
172	A	172	ALA	0	-0.008	-0.002	13.729	-0.006	-0.006	0.000	0.000	0.000	0.000
173	A	173	ILE	0	0.013	0.001	8.112	-0.524	-0.524	0.000	0.000	0.000	0.000
174	A	174	ARG	1	0.857	0.904	11.967	16.635	16.635	0.000	0.000	0.000	0.000
175	A	175	ALA	0	-0.046	-0.023	14.840	0.725	0.725	0.000	0.000	0.000	0.000
176	A	176	VAL	0	-0.056	-0.025	11.441	0.461	0.461	0.000	0.000	0.000	0.000
177	A	177	LEU	-1	-0.886	-0.906	9.253	-20.346	-20.346	0.000	0.000	0.000	0.000

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