FMO DATABASE

FMODB ID: ZG24N

Calculation Name: 2V3K-A-Xray549

Preferred Name:

Target Type:

Ligand Name: s-adenosylmethionine

Ligand 3-letter code: SAM

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2V3K

Chain ID: A

ChEMBL ID:

UniProt ID: Q06287

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	227
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2767753.303318
FMO2-HF: Nuclear repulsion	2678372.739906
FMO2-HF: Total energy	-89380.563412
FMO2-MP2: Total energy	-89637.925306

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:25:PRO)

Summations of interaction energy for fragment #1(A:25:PRO)

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.
-11.467	-8.189	-0.021	-1.323	-1.935	-0.005

Interaction energy analysis for fragmet #1(A:25:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.891 / q_NPA : 0.911

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	27	ALA	0	0.028	0.028	3.736	6.573	9.418	-0.019	-1.281	-1.545	-0.005
4	A	28	PRO	0	0.010	0.024	4.282	-2.029	-1.637	-0.001	-0.038	-0.354	0.000
5	A	29	PRO	0	0.000	-0.002	4.928	3.970	4.011	-0.001	-0.004	-0.036	0.000
6	A	30	VAL	0	0.007	-0.004	8.297	0.228	0.228	0.000	0.000	0.000	0.000
7	A	31	LEU	0	0.010	0.023	10.849	1.472	1.472	0.000	0.000	0.000	0.000
8	A	32	THR	0	-0.025	-0.036	13.061	1.336	1.336	0.000	0.000	0.000	0.000
9	A	33	SER	0	-0.013	-0.039	16.705	-0.241	-0.241	0.000	0.000	0.000	0.000
10	A	34	LYS	1	0.820	0.922	18.196	14.886	14.886	0.000	0.000	0.000	0.000
11	A	35	ASP	-1	-0.778	-0.841	12.987	-20.333	-20.333	0.000	0.000	0.000	0.000
12	A	36	LYS	1	0.830	0.913	16.482	13.336	13.336	0.000	0.000	0.000	0.000
13	A	37	ILE	0	0.009	0.004	14.881	0.598	0.598	0.000	0.000	0.000	0.000
14	A	38	THR	0	-0.056	-0.055	10.177	-0.744	-0.744	0.000	0.000	0.000	0.000
15	A	39	LYS	1	0.846	0.933	12.903	18.252	18.252	0.000	0.000	0.000	0.000
16	A	40	ARG	1	0.744	0.859	12.475	16.579	16.579	0.000	0.000	0.000	0.000
17	A	41	MET	0	0.060	0.045	14.577	1.102	1.102	0.000	0.000	0.000	0.000
18	A	42	ILE	0	-0.060	-0.040	16.742	-0.475	-0.475	0.000	0.000	0.000	0.000
19	A	43	VAL	0	0.033	0.019	19.528	0.539	0.539	0.000	0.000	0.000	0.000
20	A	44	VAL	0	-0.019	-0.014	22.284	-0.130	-0.130	0.000	0.000	0.000	0.000
21	A	45	LEU	0	-0.022	-0.013	25.179	0.388	0.388	0.000	0.000	0.000	0.000
22	A	46	ALA	0	0.076	0.039	27.738	0.161	0.161	0.000	0.000	0.000	0.000
23	A	47	MET	0	0.014	-0.003	31.050	0.124	0.124	0.000	0.000	0.000	0.000
24	A	48	ALA	0	0.026	0.032	30.750	0.176	0.176	0.000	0.000	0.000	0.000
25	A	49	SER	0	0.020	0.011	32.893	0.257	0.257	0.000	0.000	0.000	0.000
26	A	50	LEU	0	-0.067	-0.035	30.008	-0.025	-0.025	0.000	0.000	0.000	0.000
27	A	51	GLU	-1	-0.749	-0.845	34.761	-7.479	-7.479	0.000	0.000	0.000	0.000
28	A	52	THR	0	-0.011	0.000	37.101	-0.050	-0.050	0.000	0.000	0.000	0.000
29	A	53	HIS	0	0.063	0.031	39.587	0.098	0.098	0.000	0.000	0.000	0.000
30	A	54	LYS	1	0.864	0.917	42.627	7.191	7.191	0.000	0.000	0.000	0.000
31	A	55	ILE	0	0.014	0.011	45.379	0.092	0.092	0.000	0.000	0.000	0.000
32	A	56	SER	0	0.012	-0.011	47.564	0.070	0.070	0.000	0.000	0.000	0.000
33	A	57	SER	0	-0.025	-0.004	43.278	0.039	0.039	0.000	0.000	0.000	0.000
34	A	58	ASN	0	-0.007	-0.017	45.217	-0.100	-0.100	0.000	0.000	0.000	0.000
35	A	59	GLY	0	0.022	0.020	46.715	0.026	0.026	0.000	0.000	0.000	0.000
36	A	60	PRO	0	0.000	-0.001	47.053	-0.051	-0.051	0.000	0.000	0.000	0.000
37	A	61	GLY	0	0.037	0.034	43.254	-0.077	-0.077	0.000	0.000	0.000	0.000
38	A	62	GLY	0	0.009	0.015	42.821	-0.142	-0.142	0.000	0.000	0.000	0.000
39	A	63	ASP	-1	-0.871	-0.950	39.331	-8.028	-8.028	0.000	0.000	0.000	0.000
40	A	64	LYS	1	0.839	0.911	41.375	7.203	7.203	0.000	0.000	0.000	0.000
41	A	65	TYR	-1	-0.857	-0.935	39.168	-7.441	-7.441	0.000	0.000	0.000	0.000
42	A	66	VAL	0	-0.033	0.002	38.404	-0.148	-0.148	0.000	0.000	0.000	0.000
43	A	67	LEU	0	0.005	0.001	33.047	0.068	0.068	0.000	0.000	0.000	0.000
44	A	68	LEU	0	-0.028	-0.013	37.777	0.110	0.110	0.000	0.000	0.000	0.000
45	A	69	ASN	0	-0.049	-0.052	38.586	-0.115	-0.115	0.000	0.000	0.000	0.000
46	A	70	CYS	0	0.008	-0.007	40.421	0.136	0.136	0.000	0.000	0.000	0.000
47	A	71	ASP	-1	-0.919	-0.938	40.274	-7.668	-7.668	0.000	0.000	0.000	0.000
48	A	72	ASP	-1	-0.861	-0.918	41.083	-7.586	-7.586	0.000	0.000	0.000	0.000
49	A	73	HIS	0	-0.014	-0.012	41.071	0.177	0.177	0.000	0.000	0.000	0.000
50	A	74	GLN	0	0.007	0.015	45.713	0.277	0.277	0.000	0.000	0.000	0.000
51	A	75	GLY	0	0.008	-0.005	47.977	0.100	0.100	0.000	0.000	0.000	0.000
52	A	76	LEU	0	-0.029	-0.018	46.046	0.127	0.127	0.000	0.000	0.000	0.000
53	A	77	LEU	0	0.037	0.001	43.700	0.070	0.070	0.000	0.000	0.000	0.000
54	A	78	LYS	1	0.959	0.983	47.865	6.215	6.215	0.000	0.000	0.000	0.000
55	A	79	LYS	1	0.908	0.957	51.343	5.916	5.916	0.000	0.000	0.000	0.000
56	A	80	MET	0	-0.056	-0.014	45.291	0.045	0.045	0.000	0.000	0.000	0.000
57	A	81	GLY	0	0.004	0.017	49.908	-0.038	-0.038	0.000	0.000	0.000	0.000
58	A	82	ARG	1	0.805	0.884	42.939	7.086	7.086	0.000	0.000	0.000	0.000
59	A	83	ASP	-1	-0.776	-0.845	45.368	-6.877	-6.877	0.000	0.000	0.000	0.000
60	A	84	ILE	0	-0.016	-0.029	44.875	-0.147	-0.147	0.000	0.000	0.000	0.000
61	A	85	SER	0	-0.094	-0.082	43.074	-0.186	-0.186	0.000	0.000	0.000	0.000
62	A	86	GLU	-1	-0.883	-0.953	40.742	-7.473	-7.473	0.000	0.000	0.000	0.000
63	A	87	ALA	0	-0.015	0.002	39.396	-0.225	-0.225	0.000	0.000	0.000	0.000
64	A	88	ARG	1	0.876	0.884	36.366	8.525	8.525	0.000	0.000	0.000	0.000
65	A	89	PRO	0	0.008	0.009	33.818	-0.299	-0.299	0.000	0.000	0.000	0.000
66	A	90	ASP	-1	-0.785	-0.871	32.198	-9.386	-9.386	0.000	0.000	0.000	0.000
67	A	91	ILE	0	0.034	0.034	31.366	-0.378	-0.378	0.000	0.000	0.000	0.000
68	A	92	THR	0	0.047	0.020	28.431	-0.390	-0.390	0.000	0.000	0.000	0.000
69	A	93	HIS	0	-0.106	-0.050	27.565	-0.268	-0.268	0.000	0.000	0.000	0.000
70	A	94	GLN	0	0.046	0.010	26.822	-0.743	-0.743	0.000	0.000	0.000	0.000
71	A	95	CYS	0	-0.035	0.005	25.846	-0.433	-0.433	0.000	0.000	0.000	0.000
72	A	96	LEU	0	0.007	-0.002	23.133	-0.602	-0.602	0.000	0.000	0.000	0.000
73	A	97	LEU	0	-0.065	-0.031	21.892	-0.714	-0.714	0.000	0.000	0.000	0.000
74	A	98	THR	0	-0.015	-0.023	21.562	-0.545	-0.545	0.000	0.000	0.000	0.000
75	A	99	LEU	0	0.017	0.009	19.863	-0.644	-0.644	0.000	0.000	0.000	0.000
76	A	100	LEU	0	-0.014	0.006	17.343	-0.970	-0.970	0.000	0.000	0.000	0.000
77	A	101	ASP	-1	-0.823	-0.901	16.744	-16.687	-16.687	0.000	0.000	0.000	0.000
78	A	102	SER	0	-0.007	0.006	16.385	-1.003	-1.003	0.000	0.000	0.000	0.000
79	A	103	PRO	0	0.049	0.021	12.609	-1.049	-1.049	0.000	0.000	0.000	0.000
80	A	104	ILE	0	0.043	0.021	11.401	-2.328	-2.328	0.000	0.000	0.000	0.000
81	A	105	ASN	0	-0.096	-0.063	11.930	-1.230	-1.230	0.000	0.000	0.000	0.000
82	A	106	LYS	1	0.775	0.891	11.152	18.672	18.672	0.000	0.000	0.000	0.000
83	A	107	ALA	0	0.029	0.028	7.419	-3.035	-3.035	0.000	0.000	0.000	0.000
84	A	108	GLY	0	-0.062	-0.022	7.124	-3.134	-3.134	0.000	0.000	0.000	0.000
85	A	109	LYS	1	0.932	0.953	7.398	32.231	32.231	0.000	0.000	0.000	0.000
86	A	110	LEU	0	0.014	0.023	11.196	1.778	1.778	0.000	0.000	0.000	0.000
87	A	111	GLN	0	-0.004	0.004	14.177	-0.554	-0.554	0.000	0.000	0.000	0.000
88	A	112	VAL	0	-0.011	-0.003	16.966	0.523	0.523	0.000	0.000	0.000	0.000
89	A	113	TYR	0	0.028	0.005	19.852	0.141	0.141	0.000	0.000	0.000	0.000
90	A	114	ILE	0	-0.035	-0.015	23.702	0.142	0.142	0.000	0.000	0.000	0.000
91	A	115	GLN	0	0.047	0.021	27.276	-0.040	-0.040	0.000	0.000	0.000	0.000
92	A	116	THR	0	0.010	0.000	30.597	0.166	0.166	0.000	0.000	0.000	0.000
93	A	117	SER	0	0.016	0.015	33.485	0.085	0.085	0.000	0.000	0.000	0.000
94	A	118	ARG	1	0.841	0.904	36.511	7.929	7.929	0.000	0.000	0.000	0.000
95	A	119	GLY	0	0.049	0.034	35.309	0.097	0.097	0.000	0.000	0.000	0.000
96	A	120	ILE	0	-0.052	-0.023	31.684	-0.145	-0.145	0.000	0.000	0.000	0.000
97	A	121	LEU	0	0.019	0.025	27.059	-0.176	-0.176	0.000	0.000	0.000	0.000
98	A	122	ILE	0	-0.032	-0.028	25.094	0.064	0.064	0.000	0.000	0.000	0.000
99	A	123	GLU	-1	-0.736	-0.839	19.626	-14.662	-14.662	0.000	0.000	0.000	0.000
100	A	124	VAL	0	-0.050	-0.037	19.990	0.358	0.358	0.000	0.000	0.000	0.000
101	A	125	ASN	0	0.010	0.026	16.020	-1.501	-1.501	0.000	0.000	0.000	0.000
102	A	126	PRO	0	0.068	0.028	13.210	0.480	0.480	0.000	0.000	0.000	0.000
103	A	127	THR	0	-0.010	-0.010	12.925	-0.085	-0.085	0.000	0.000	0.000	0.000
104	A	128	VAL	0	-0.043	-0.005	15.387	0.570	0.570	0.000	0.000	0.000	0.000
105	A	129	ARG	1	0.988	0.992	19.212	13.154	13.154	0.000	0.000	0.000	0.000
106	A	130	ILE	0	0.023	0.013	21.077	0.825	0.825	0.000	0.000	0.000	0.000
107	A	131	PRO	0	-0.074	-0.044	23.896	-0.091	-0.091	0.000	0.000	0.000	0.000
108	A	132	ARG	1	0.914	0.932	21.915	13.881	13.881	0.000	0.000	0.000	0.000
109	A	133	THR	0	0.011	0.010	27.953	0.200	0.200	0.000	0.000	0.000	0.000
110	A	134	PHE	0	0.130	0.055	31.495	-0.168	-0.168	0.000	0.000	0.000	0.000
111	A	135	LYS	1	0.936	0.976	33.161	8.236	8.236	0.000	0.000	0.000	0.000
112	A	136	ARG	1	0.949	0.964	30.634	9.991	9.991	0.000	0.000	0.000	0.000
113	A	137	PHE	0	0.027	0.019	27.536	-0.149	-0.149	0.000	0.000	0.000	0.000
114	A	138	SER	0	0.041	0.011	30.366	0.008	0.008	0.000	0.000	0.000	0.000
115	A	139	GLY	0	0.008	0.005	33.693	0.095	0.095	0.000	0.000	0.000	0.000
116	A	140	LEU	0	-0.011	-0.003	25.574	0.047	0.047	0.000	0.000	0.000	0.000
117	A	141	MET	0	0.008	0.006	26.886	-0.109	-0.109	0.000	0.000	0.000	0.000
118	A	142	VAL	0	0.013	0.009	31.218	0.129	0.129	0.000	0.000	0.000	0.000
119	A	143	GLN	0	-0.042	-0.017	30.755	-0.065	-0.065	0.000	0.000	0.000	0.000
120	A	144	LEU	0	-0.017	-0.007	27.256	0.038	0.038	0.000	0.000	0.000	0.000
121	A	145	LEU	0	-0.009	-0.011	30.540	0.023	0.023	0.000	0.000	0.000	0.000
122	A	146	HIS	0	0.034	0.023	33.567	0.045	0.045	0.000	0.000	0.000	0.000
123	A	147	LYS	1	0.880	0.940	31.940	8.909	8.909	0.000	0.000	0.000	0.000
124	A	148	LEU	0	0.021	0.021	31.441	-0.161	-0.161	0.000	0.000	0.000	0.000
125	A	149	SER	0	-0.051	-0.041	26.553	-0.400	-0.400	0.000	0.000	0.000	0.000
126	A	150	ILE	0	-0.015	0.008	25.200	0.366	0.366	0.000	0.000	0.000	0.000
127	A	151	ARG	1	0.838	0.901	24.040	10.325	10.325	0.000	0.000	0.000	0.000
128	A	152	SER	0	-0.019	-0.012	19.870	0.095	0.095	0.000	0.000	0.000	0.000
129	A	153	VAL	0	-0.008	-0.013	22.199	0.161	0.161	0.000	0.000	0.000	0.000
130	A	154	ASN	0	0.002	-0.004	22.275	0.838	0.838	0.000	0.000	0.000	0.000
131	A	155	SER	0	-0.037	-0.035	19.712	0.124	0.124	0.000	0.000	0.000	0.000
132	A	156	GLU	-1	-0.820	-0.894	21.916	-11.305	-11.305	0.000	0.000	0.000	0.000
133	A	157	GLU	-1	-0.804	-0.852	17.960	-15.533	-15.533	0.000	0.000	0.000	0.000
134	A	158	LYS	1	0.862	0.912	21.305	11.547	11.547	0.000	0.000	0.000	0.000
135	A	159	LEU	0	0.015	0.011	18.837	-0.590	-0.590	0.000	0.000	0.000	0.000
136	A	160	LEU	0	0.023	0.007	21.080	-0.184	-0.184	0.000	0.000	0.000	0.000
137	A	161	LYS	1	0.915	0.954	23.777	11.905	11.905	0.000	0.000	0.000	0.000
138	A	162	VAL	0	0.041	0.036	25.790	-0.155	-0.155	0.000	0.000	0.000	0.000
139	A	163	ILE	0	-0.067	-0.040	24.963	-0.012	-0.012	0.000	0.000	0.000	0.000
140	A	164	LYS	1	0.963	0.978	28.869	9.076	9.076	0.000	0.000	0.000	0.000
141	A	165	ASN	0	0.018	0.028	29.885	-0.514	-0.514	0.000	0.000	0.000	0.000
142	A	166	PRO	0	0.039	0.027	30.993	0.218	0.218	0.000	0.000	0.000	0.000
143	A	167	ILE	0	0.031	-0.004	24.395	-0.231	-0.231	0.000	0.000	0.000	0.000
144	A	168	THR	0	0.026	0.000	26.073	-0.415	-0.415	0.000	0.000	0.000	0.000
145	A	169	ASP	-1	-0.878	-0.919	26.507	-10.360	-10.360	0.000	0.000	0.000	0.000
146	A	170	HIS	0	-0.120	-0.078	23.258	-0.734	-0.734	0.000	0.000	0.000	0.000
147	A	171	LEU	0	0.004	-0.006	21.543	-0.681	-0.681	0.000	0.000	0.000	0.000
148	A	172	PRO	0	0.025	0.003	17.996	0.277	0.277	0.000	0.000	0.000	0.000
149	A	173	THR	0	-0.008	-0.002	20.343	0.390	0.390	0.000	0.000	0.000	0.000
150	A	174	LYS	1	0.789	0.893	20.493	14.121	14.121	0.000	0.000	0.000	0.000
151	A	175	CYS	0	-0.054	-0.023	20.482	-0.929	-0.929	0.000	0.000	0.000	0.000
152	A	176	ARG	1	0.905	0.957	22.418	12.941	12.941	0.000	0.000	0.000	0.000
153	A	177	LYS	1	0.877	0.929	24.048	11.091	11.091	0.000	0.000	0.000	0.000
154	A	178	VAL	0	0.069	0.045	26.124	0.378	0.378	0.000	0.000	0.000	0.000
155	A	179	THR	0	-0.020	-0.005	27.872	-0.361	-0.361	0.000	0.000	0.000	0.000
156	A	180	LEU	0	-0.029	-0.015	25.884	0.084	0.084	0.000	0.000	0.000	0.000
157	A	181	SER	0	-0.057	-0.069	30.119	0.268	0.268	0.000	0.000	0.000	0.000
158	A	182	PHE	0	-0.045	-0.031	33.697	-0.112	-0.112	0.000	0.000	0.000	0.000
159	A	183	ASP	-1	-0.933	-0.958	35.888	-7.892	-7.892	0.000	0.000	0.000	0.000
160	A	184	ALA	0	-0.031	0.001	33.979	0.126	0.126	0.000	0.000	0.000	0.000
161	A	185	PRO	0	0.005	0.002	34.050	-0.018	-0.018	0.000	0.000	0.000	0.000
162	A	186	VAL	0	-0.021	-0.014	31.499	-0.319	-0.319	0.000	0.000	0.000	0.000
163	A	187	ILE	0	-0.016	0.000	25.990	0.077	0.077	0.000	0.000	0.000	0.000
164	A	188	ARG	1	0.856	0.935	22.480	12.940	12.940	0.000	0.000	0.000	0.000
165	A	189	VAL	0	-0.015	-0.010	20.977	-0.006	-0.006	0.000	0.000	0.000	0.000
166	A	190	GLN	0	-0.036	-0.033	20.032	0.346	0.346	0.000	0.000	0.000	0.000
167	A	191	ASP	-1	-0.801	-0.904	21.426	-12.270	-12.270	0.000	0.000	0.000	0.000
168	A	192	TYR	0	-0.102	-0.083	22.942	-0.134	-0.134	0.000	0.000	0.000	0.000
169	A	193	ILE	0	-0.014	-0.013	17.231	-0.068	-0.068	0.000	0.000	0.000	0.000
170	A	194	GLU	-1	-0.934	-0.974	19.056	-15.243	-15.243	0.000	0.000	0.000	0.000
171	A	195	LYS	1	0.865	0.935	20.462	12.293	12.293	0.000	0.000	0.000	0.000
172	A	196	LEU	0	-0.028	0.004	18.968	0.461	0.461	0.000	0.000	0.000	0.000
173	A	197	ASP	-1	-0.773	-0.869	19.318	-13.610	-13.610	0.000	0.000	0.000	0.000
174	A	198	ASP	-1	-0.920	-0.952	15.149	-18.191	-18.191	0.000	0.000	0.000	0.000
175	A	199	ASP	-1	-0.887	-0.938	14.886	-15.836	-15.836	0.000	0.000	0.000	0.000
176	A	200	GLU	-1	-0.840	-0.902	17.079	-12.632	-12.632	0.000	0.000	0.000	0.000
177	A	201	SER	0	0.005	-0.007	17.163	-1.069	-1.069	0.000	0.000	0.000	0.000
178	A	202	ILE	0	0.006	0.007	18.444	0.811	0.811	0.000	0.000	0.000	0.000
179	A	203	CYS	0	-0.069	-0.032	20.246	-0.419	-0.419	0.000	0.000	0.000	0.000
180	A	204	VAL	0	0.034	0.025	22.545	0.532	0.532	0.000	0.000	0.000	0.000
181	A	205	PHE	0	0.018	-0.003	24.784	-0.149	-0.149	0.000	0.000	0.000	0.000
182	A	206	VAL	0	0.019	-0.006	26.377	0.191	0.191	0.000	0.000	0.000	0.000
183	A	207	GLY	0	0.061	0.041	29.178	0.008	0.008	0.000	0.000	0.000	0.000
184	A	208	ALA	0	-0.061	-0.037	29.961	-0.040	-0.040	0.000	0.000	0.000	0.000
185	A	209	MET	0	-0.042	-0.023	31.918	0.127	0.127	0.000	0.000	0.000	0.000
186	A	210	ALA	0	0.005	-0.008	35.690	-0.072	-0.072	0.000	0.000	0.000	0.000
187	A	211	ARG	1	0.900	0.950	38.191	7.337	7.337	0.000	0.000	0.000	0.000
188	A	212	GLY	0	0.023	0.010	39.572	0.009	0.009	0.000	0.000	0.000	0.000
189	A	213	LYS	1	0.974	0.996	40.023	7.129	7.129	0.000	0.000	0.000	0.000
190	A	214	ASP	-1	-0.739	-0.840	34.918	-9.009	-9.009	0.000	0.000	0.000	0.000
191	A	215	ASN	0	-0.033	-0.032	36.117	-0.131	-0.131	0.000	0.000	0.000	0.000
192	A	216	PHE	0	-0.049	-0.025	31.407	0.070	0.070	0.000	0.000	0.000	0.000
193	A	217	ALA	0	0.020	0.009	31.254	-0.162	-0.162	0.000	0.000	0.000	0.000
194	A	218	ASP	-1	-0.773	-0.866	33.070	-8.768	-8.768	0.000	0.000	0.000	0.000
195	A	219	GLU	-1	-0.889	-0.947	34.181	-8.746	-8.746	0.000	0.000	0.000	0.000
196	A	220	TYR	0	-0.107	-0.065	29.821	-0.179	-0.179	0.000	0.000	0.000	0.000
197	A	221	VAL	0	-0.068	-0.033	29.328	-0.375	-0.375	0.000	0.000	0.000	0.000
198	A	222	ASP	-1	-0.898	-0.937	30.519	-9.816	-9.816	0.000	0.000	0.000	0.000
199	A	223	GLU	-1	-0.844	-0.889	28.441	-10.672	-10.672	0.000	0.000	0.000	0.000
200	A	224	LYS	1	0.783	0.841	31.446	8.588	8.588	0.000	0.000	0.000	0.000
201	A	225	VAL	0	0.006	0.012	27.632	0.107	0.107	0.000	0.000	0.000	0.000
202	A	226	GLY	0	0.073	0.043	30.864	-0.062	-0.062	0.000	0.000	0.000	0.000
203	A	227	LEU	0	-0.027	-0.024	25.874	-0.243	-0.243	0.000	0.000	0.000	0.000
204	A	228	SER	0	-0.068	-0.059	29.558	-0.149	-0.149	0.000	0.000	0.000	0.000
205	A	229	ASN	0	0.057	0.034	32.535	0.092	0.092	0.000	0.000	0.000	0.000
206	A	230	TYR	0	-0.026	-0.001	34.685	0.217	0.217	0.000	0.000	0.000	0.000
207	A	231	PRO	0	0.044	0.026	34.936	-0.301	-0.301	0.000	0.000	0.000	0.000
208	A	232	LEU	0	-0.013	-0.003	29.601	-0.115	-0.115	0.000	0.000	0.000	0.000
209	A	233	SER	0	0.009	0.008	31.850	0.174	0.174	0.000	0.000	0.000	0.000
210	A	234	ALA	0	0.075	0.031	29.620	-0.303	-0.303	0.000	0.000	0.000	0.000
211	A	235	SER	0	0.046	0.018	26.640	-0.287	-0.287	0.000	0.000	0.000	0.000
212	A	236	VAL	0	0.007	0.000	25.823	-0.507	-0.507	0.000	0.000	0.000	0.000
213	A	237	ALA	0	0.006	0.009	26.476	-0.274	-0.274	0.000	0.000	0.000	0.000
214	A	238	CYS	0	-0.006	-0.012	23.153	-0.363	-0.363	0.000	0.000	0.000	0.000
215	A	239	SER	0	-0.010	-0.002	21.953	-0.777	-0.777	0.000	0.000	0.000	0.000
216	A	240	LYS	1	0.951	0.976	21.625	10.660	10.660	0.000	0.000	0.000	0.000
217	A	241	PHE	0	0.053	0.017	20.532	-0.213	-0.213	0.000	0.000	0.000	0.000
218	A	242	CYS	0	-0.081	-0.034	17.703	-0.578	-0.578	0.000	0.000	0.000	0.000
219	A	243	HIS	0	0.042	0.028	17.413	-0.295	-0.295	0.000	0.000	0.000	0.000
220	A	244	GLY	0	0.024	0.005	18.316	-0.426	-0.426	0.000	0.000	0.000	0.000
221	A	245	ALA	0	0.032	0.002	16.271	-0.097	-0.097	0.000	0.000	0.000	0.000
222	A	246	GLU	-1	-0.851	-0.943	13.633	-20.063	-20.063	0.000	0.000	0.000	0.000
223	A	247	ASP	-1	-0.858	-0.915	13.982	-16.701	-16.701	0.000	0.000	0.000	0.000
224	A	248	ALA	0	0.030	0.017	15.869	-0.404	-0.404	0.000	0.000	0.000	0.000
225	A	249	TRP	0	-0.104	-0.056	11.591	-0.514	-0.514	0.000	0.000	0.000	0.000
226	A	250	ASN	0	-0.089	-0.032	10.848	-1.197	-1.197	0.000	0.000	0.000	0.000
227	A	251	ILE	-1	-0.961	-0.971	9.296	-28.569	-28.569	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:25:PRO)